CNRS Nantes University UFIP UFIP
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***  TRANSCRIPTION 29-NOV-17 6F44  ***

elNémo ID: 20011910031388361

Job options:

ID        	=	 20011910031388361
JOBID     	=	 TRANSCRIPTION 29-NOV-17 6F44
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSCRIPTION                           29-NOV-17   6F44              
TITLE     RNA POLYMERASE III CLOSED COMPLEX CC2.                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1;              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: RNA POLYMERASE III SUBUNIT C1,DNA-DIRECTED RNA POLYMERASE   
COMPND   5 III LARGEST SUBUNIT,RNA POLYMERASE III SUBUNIT C160;                 
COMPND   6 EC: 2.7.7.6;                                                         
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC2;              
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: RNA POLYMERASE III SUBUNIT C2,C128,DNA-DIRECTED RNA         
COMPND  11 POLYMERASE III 130 KDA POLYPEPTIDE;                                  
COMPND  12 EC: 2.7.7.6;                                                         
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA-DIRECTED RNA POLYMERASES I AND III SUBUNIT RPAC1;      
COMPND  15 CHAIN: C;                                                            
COMPND  16 SYNONYM: RNA POLYMERASES I AND III SUBUNIT AC1,C37,DNA-DIRECTED RNA  
COMPND  17 POLYMERASES I AND III 40 KDA POLYPEPTIDE,C40;                        
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC9;              
COMPND  20 CHAIN: D;                                                            
COMPND  21 SYNONYM: RNA POLYMERASE III SUBUNIT C9,RNA POLYMERASE III SUBUNIT    
COMPND  22 C17;                                                                 
COMPND  23 MOL_ID: 5;                                                           
COMPND  24 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC1;
COMPND  25 CHAIN: E;                                                            
COMPND  26 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC1,ABC27,DNA-DIRECTED
COMPND  27 RNA POLYMERASES I,AND III 27 KDA POLYPEPTIDE;                        
COMPND  28 MOL_ID: 6;                                                           
COMPND  29 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC2;
COMPND  30 CHAIN: F;                                                            
COMPND  31 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC2,ABC23,DNA-DIRECTED
COMPND  32 RNA POLYMERASES I,AND III 23 KDA POLYPEPTIDE;                        
COMPND  33 MOL_ID: 7;                                                           
COMPND  34 MOLECULE: DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC8;              
COMPND  35 CHAIN: G;                                                            
COMPND  36 SYNONYM: RNA POLYMERASE III SUBUNIT C8,DNA-DIRECTED RNA POLYMERASE   
COMPND  37 III 25 KDA POLYPEPTIDE,RNA POLYMERASE III SUBUNIT C25;               
COMPND  38 MOL_ID: 8;                                                           
COMPND  39 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC3;
COMPND  40 CHAIN: H;                                                            
COMPND  41 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC3,ABC14.4,ABC14.5,  
COMPND  42 DNA-DIRECTED RNA POLYMERASES I,AND III 14.5 KDA POLYPEPTIDE;         
COMPND  43 MOL_ID: 9;                                                           
COMPND  44 MOLECULE: DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC10;             
COMPND  45 CHAIN: I;                                                            
COMPND  46 SYNONYM: RNA POLYMERASE III SUBUNIT C10,DNA-DIRECTED RNA POLYMERASES 
COMPND  47 III 12.5 KDA POLYPEPTIDE,RNA POLYMERASE III SUBUNIT C11;             
COMPND  48 MOL_ID: 10;                                                          
COMPND  49 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5;
COMPND  50 CHAIN: J;                                                            
COMPND  51 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC5,ABC10-BETA,ABC8,  
COMPND  52 DNA-DIRECTED RNA POLYMERASES I,AND III 8.3 KDA POLYPEPTIDE;          
COMPND  53 MOL_ID: 11;                                                          
COMPND  54 MOLECULE: DNA-DIRECTED RNA POLYMERASES I AND III SUBUNIT RPAC2;      
COMPND  55 CHAIN: K;                                                            
COMPND  56 SYNONYM: RNA POLYMERASES I AND III SUBUNIT AC2,AC19,DNA-DIRECTED RNA 
COMPND  57 POLYMERASES I AND III 16 KDA POLYPEPTIDE,RPA19;                      
COMPND  58 MOL_ID: 12;                                                          
COMPND  59 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC4;
COMPND  60 CHAIN: L;                                                            
COMPND  61 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC4,ABC10-ALPHA;      
COMPND  62 MOL_ID: 13;                                                          
COMPND  63 MOLECULE: DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC5;              
COMPND  64 CHAIN: M;                                                            
COMPND  65 SYNONYM: RNA POLYMERASE III SUBUNIT C5,DNA-DIRECTED RNA POLYMERASE   
COMPND  66 III 37 KDA POLYPEPTIDE,RNA POLYMERASE III SUBUNIT C37;               
COMPND  67 MOL_ID: 14;                                                          
COMPND  68 MOLECULE: DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC4;              
COMPND  69 CHAIN: N;                                                            
COMPND  70 SYNONYM: RNA POLYMERASE III SUBUNIT C4,C53,DNA-DIRECTED RNA          
COMPND  71 POLYMERASE III 47 KDA POLYPEPTIDE;                                   
COMPND  72 MOL_ID: 15;                                                          
COMPND  73 MOLECULE: DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC3;              
COMPND  74 CHAIN: O;                                                            
COMPND  75 SYNONYM: RNA POLYMERASE III SUBUNIT C3,C82,DNA-DIRECTED III 74 KDA   
COMPND  76 POLYPEPTIDE,C74;                                                     
COMPND  77 MOL_ID: 16;                                                          
COMPND  78 MOLECULE: DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC6;              
COMPND  79 CHAIN: P;                                                            
COMPND  80 SYNONYM: RNA POLYMERASE III SUBUNIT C6,C34,DNA-DIRECTED RNA          
COMPND  81 POLYMERASE III 36 KDA POLYPEPTIDE;                                   
COMPND  82 MOL_ID: 17;                                                          
COMPND  83 MOLECULE: DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC7;              
COMPND  84 CHAIN: Q;                                                            
COMPND  85 SYNONYM: RNA POLYMERASE III SUBUNIT C7,DNA-DIRECTED RNA POLYMERASE   
COMPND  86 III 31 KDA POLYPEPTIDE,C31;                                          
COMPND  87 MOL_ID: 18;                                                          
COMPND  88 MOLECULE: TATA-BOX-BINDING PROTEIN;                                  
COMPND  89 CHAIN: U;                                                            
COMPND  90 SYNONYM: TATA SEQUENCE-BINDING PROTEIN,TBP,TATA-BINDING FACTOR,TATA- 
COMPND  91 BOX FACTOR,TRANSCRIPTION FACTOR D,TRANSCRIPTION INITIATION FACTOR    
COMPND  92 TFIID TBP SUBUNIT;                                                   
COMPND  93 ENGINEERED: YES;                                                     
COMPND  94 MOL_ID: 19;                                                          
COMPND  95 MOLECULE: TRANSCRIPTION FACTOR IIIB 70 KDA SUBUNIT;                  
COMPND  96 CHAIN: V;                                                            
COMPND  97 SYNONYM: TFIIIB,B-RELATED FACTOR 1,BRF-1;                            
COMPND  98 ENGINEERED: YES;                                                     
COMPND  99 MOL_ID: 20;                                                          
COMPND 100 MOLECULE: TRANSCRIPTION FACTOR TFIIIB COMPONENT B'';                 
COMPND 101 CHAIN: W;                                                            
COMPND 102 SYNONYM: TFIIIB90;                                                   
COMPND 103 ENGINEERED: YES;                                                     
COMPND 104 MOL_ID: 21;                                                          
COMPND 105 MOLECULE: NON-TEMPLATE DNA;                                          
COMPND 106 CHAIN: X;                                                            
COMPND 107 ENGINEERED: YES;                                                     
COMPND 108 MOL_ID: 22;                                                          
COMPND 109 MOLECULE: TEMPLATE DNA;                                              
COMPND 110 CHAIN: Y;                                                            
COMPND 111 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   3 S288C);                                                              
SOURCE   4 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 559292;                                              
SOURCE   6 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   9 S288C);                                                              
SOURCE  10 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  11 ORGANISM_TAXID: 559292;                                              
SOURCE  12 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  15 S288C);                                                              
SOURCE  16 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  17 ORGANISM_TAXID: 559292;                                              
SOURCE  18 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  19 MOL_ID: 4;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  21 S288C);                                                              
SOURCE  22 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  23 ORGANISM_TAXID: 559292;                                              
SOURCE  24 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  25 MOL_ID: 5;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  27 S288C);                                                              
SOURCE  28 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  29 ORGANISM_TAXID: 559292;                                              
SOURCE  30 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  31 MOL_ID: 6;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  33 S288C);                                                              
SOURCE  34 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  35 ORGANISM_TAXID: 559292;                                              
SOURCE  36 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  37 MOL_ID: 7;                                                           
SOURCE  38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  39 S288C);                                                              
SOURCE  40 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  41 ORGANISM_TAXID: 559292;                                              
SOURCE  42 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  43 MOL_ID: 8;                                                           
SOURCE  44 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  45 S288C);                                                              
SOURCE  46 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  47 ORGANISM_TAXID: 559292;                                              
SOURCE  48 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  49 MOL_ID: 9;                                                           
SOURCE  50 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  51 S288C);                                                              
SOURCE  52 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  53 ORGANISM_TAXID: 559292;                                              
SOURCE  54 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  55 MOL_ID: 10;                                                          
SOURCE  56 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  57 S288C);                                                              
SOURCE  58 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  59 ORGANISM_TAXID: 559292;                                              
SOURCE  60 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  61 MOL_ID: 11;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  63 S288C);                                                              
SOURCE  64 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  65 ORGANISM_TAXID: 559292;                                              
SOURCE  66 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  67 MOL_ID: 12;                                                          
SOURCE  68 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  69 S288C);                                                              
SOURCE  70 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  71 ORGANISM_TAXID: 559292;                                              
SOURCE  72 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  73 MOL_ID: 13;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  75 S288C);                                                              
SOURCE  76 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  77 ORGANISM_TAXID: 559292;                                              
SOURCE  78 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  79 MOL_ID: 14;                                                          
SOURCE  80 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  81 S288C);                                                              
SOURCE  82 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  83 ORGANISM_TAXID: 559292;                                              
SOURCE  84 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  85 MOL_ID: 15;                                                          
SOURCE  86 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  87 S288C);                                                              
SOURCE  88 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  89 ORGANISM_TAXID: 559292;                                              
SOURCE  90 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  91 MOL_ID: 16;                                                          
SOURCE  92 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  93 S288C);                                                              
SOURCE  94 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  95 ORGANISM_TAXID: 559292;                                              
SOURCE  96 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  97 MOL_ID: 17;                                                          
SOURCE  98 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  99 S288C);                                                              
SOURCE 100 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE 101 ORGANISM_TAXID: 559292;                                              
SOURCE 102 STRAIN: ATCC 204508 / S288C;                                         
SOURCE 103 MOL_ID: 18;                                                          
SOURCE 104 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE 105 S288C);                                                              
SOURCE 106 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE 107 ORGANISM_TAXID: 559292;                                              
SOURCE 108 STRAIN: ATCC 204508 / S288C;                                         
SOURCE 109 GENE: SPT15, BTF1, TBP1, YER148W;                                    
SOURCE 110 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE 111 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE 112 MOL_ID: 19;                                                          
SOURCE 113 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE 114 S288C);                                                              
SOURCE 115 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE 116 ORGANISM_TAXID: 559292;                                              
SOURCE 117 STRAIN: ATCC 204508 / S288C;                                         
SOURCE 118 GENE: BRF1, PCF4, TDS4, YGR246C;                                     
SOURCE 119 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE 120 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE 121 MOL_ID: 20;                                                          
SOURCE 122 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE 123 S288C);                                                              
SOURCE 124 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE 125 ORGANISM_TAXID: 559292;                                              
SOURCE 126 STRAIN: ATCC 204508 / S288C;                                         
SOURCE 127 GENE: BDP1, TFC5, YNL039W, N2682;                                    
SOURCE 128 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE 129 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE 130 MOL_ID: 21;                                                          
SOURCE 131 SYNTHETIC: YES;                                                      
SOURCE 132 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE 133 ORGANISM_TAXID: 559292;                                              
SOURCE 134 MOL_ID: 22;                                                          
SOURCE 135 SYNTHETIC: YES;                                                      
SOURCE 136 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE 137 ORGANISM_TAXID: 559292                                               
KEYWDS    TRANSCRIPTION, RNA POLYMERASE III, TFIIIB, PRE-INITIATION COMPLEX,    
KEYWDS   2 BRF1, BDP1, TBP, POL III, ENZYME                                     
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    M.K.VORLAENDER,H.KHATTER,R.WETZEL,W.J.H.HAGEN,C.W.MUELLER             
REVDAT   4   11-DEC-19 6F44    1       SCALE                                    
REVDAT   3   31-JAN-18 6F44    1       JRNL   REMARK                            
REVDAT   2   24-JAN-18 6F44    1       TITLE                                    
REVDAT   1   17-JAN-18 6F44    0                                                
JRNL        AUTH   M.K.VORLANDER,H.KHATTER,R.WETZEL,W.J.H.HAGEN,C.W.MULLER      
JRNL        TITL   MOLECULAR MECHANISM OF PROMOTER OPENING BY RNA POLYMERASE    
JRNL        TITL 2 III.                                                         
JRNL        REF    NATURE                        V. 553   295 2018              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   29345638                                                     
JRNL        DOI    10.1038/NATURE25440                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : SERIALEM, COOT, RELION, PHENIX            
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : AB INITIO MODEL                     
REMARK   3   REFINEMENT TARGET            : CROSS-CORRELATION COEFFICIENT       
REMARK   3   OVERALL ANISOTROPIC B VALUE  : 90.000                              
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 4.200                          
REMARK   3   NUMBER OF PARTICLES               : 34176                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6F44 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007643.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : RNA POLYMERASE III CLOSED         
REMARK 245                                    COMPLEX CC2; RNA POLYMERASE III;  
REMARK 245                                    TRANSCRIPTION FACTOR IIIB;        
REMARK 245                                    NUCLEIC ACIDS                     
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.02                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 60.90                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 22-MERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 22-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 106830 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 263310 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -577.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O, P, Q, U, V,            
REMARK 350                    AND CHAINS: W, X, Y                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A   169                                                      
REMARK 465     GLY A   170                                                      
REMARK 465     ALA A   171                                                      
REMARK 465     GLY A   172                                                      
REMARK 465     SER A   173                                                      
REMARK 465     ALA A   174                                                      
REMARK 465     ALA A   335                                                      
REMARK 465     MET A   336                                                      
REMARK 465     LEU A   337                                                      
REMARK 465     PRO A   338                                                      
REMARK 465     GLY A   339                                                      
REMARK 465     SER A   340                                                      
REMARK 465     SER A   341                                                      
REMARK 465     ASN A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     GLY A   344                                                      
REMARK 465     GLY A   345                                                      
REMARK 465     LYS A   346                                                      
REMARK 465     VAL A   347                                                      
REMARK 465     GLY A  1101                                                      
REMARK 465     THR A  1102                                                      
REMARK 465     GLN A  1103                                                      
REMARK 465     MET A  1104                                                      
REMARK 465     THR A  1105                                                      
REMARK 465     LEU A  1106                                                      
REMARK 465     LYS A  1107                                                      
REMARK 465     THR A  1108                                                      
REMARK 465     PHE A  1109                                                      
REMARK 465     HIS A  1110                                                      
REMARK 465     PHE A  1111                                                      
REMARK 465     ALA A  1112                                                      
REMARK 465     GLY A  1113                                                      
REMARK 465     VAL A  1114                                                      
REMARK 465     ALA A  1115                                                      
REMARK 465     SER A  1116                                                      
REMARK 465     GLU A  1237                                                      
REMARK 465     GLY A  1238                                                      
REMARK 465     TYR A  1239                                                      
REMARK 465     LYS A  1240                                                      
REMARK 465     ALA A  1241                                                      
REMARK 465     LYS A  1242                                                      
REMARK 465     SER A  1243                                                      
REMARK 465     ILE A  1244                                                      
REMARK 465     SER A  1245                                                      
REMARK 465     THR A  1246                                                      
REMARK 465     SER A  1247                                                      
REMARK 465     ALA A  1248                                                      
REMARK 465     LYS A  1249                                                      
REMARK 465     GLU A  1250                                                      
REMARK 465     PRO A  1251                                                      
REMARK 465     LEU A  1451                                                      
REMARK 465     SER A  1452                                                      
REMARK 465     ASN A  1453                                                      
REMARK 465     GLU A  1454                                                      
REMARK 465     ALA A  1455                                                      
REMARK 465     ALA A  1456                                                      
REMARK 465     LEU A  1457                                                      
REMARK 465     LYS A  1458                                                      
REMARK 465     ALA A  1459                                                      
REMARK 465     ASN A  1460                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     THR B    10                                                      
REMARK 465     HIS B    11                                                      
REMARK 465     ILE B    12                                                      
REMARK 465     HIS B    13                                                      
REMARK 465     LYS B    14                                                      
REMARK 465     HIS B    15                                                      
REMARK 465     VAL B    16                                                      
REMARK 465     LYS B    17                                                      
REMARK 465     ASP B    18                                                      
REMARK 465     GLU B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     PHE B    21                                                      
REMARK 465     ASP B    22                                                      
REMARK 465     ASP B    23                                                      
REMARK 465     LEU B    24                                                      
REMARK 465     LEU B    25                                                      
REMARK 465     LYS B    26                                                      
REMARK 465     PRO B    27                                                      
REMARK 465     VAL B    28                                                      
REMARK 465     TYR B    29                                                      
REMARK 465     LYS B    30                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     LYS B    32                                                      
REMARK 465     LYS B    33                                                      
REMARK 465     LEU B    34                                                      
REMARK 465     THR B    35                                                      
REMARK 465     ALA D    36                                                      
REMARK 465     LEU D    37                                                      
REMARK 465     LYS D    38                                                      
REMARK 465     LYS D    39                                                      
REMARK 465     SER D    40                                                      
REMARK 465     ARG D    41                                                      
REMARK 465     SER D    42                                                      
REMARK 465     LYS D    43                                                      
REMARK 465     GLY D    44                                                      
REMARK 465     LYS D    45                                                      
REMARK 465     GLN D    46                                                      
REMARK 465     ASN D    47                                                      
REMARK 465     ARG D    48                                                      
REMARK 465     PRO D    49                                                      
REMARK 465     TYR D    50                                                      
REMARK 465     ASN D    51                                                      
REMARK 465     HIS D    52                                                      
REMARK 465     ILE D    73                                                      
REMARK 465     ASN D    74                                                      
REMARK 465     GLN D    75                                                      
REMARK 465     GLU D    76                                                      
REMARK 465     ASP D    77                                                      
REMARK 465     GLU D    78                                                      
REMARK 465     GLY D    79                                                      
REMARK 465     GLU D    80                                                      
REMARK 465     GLU D    81                                                      
REMARK 465     ARG D    82                                                      
REMARK 465     GLU D    83                                                      
REMARK 465     SER D    84                                                      
REMARK 465     SER D    85                                                      
REMARK 465     GLY D    86                                                      
REMARK 465     ALA D    87                                                      
REMARK 465     LYS D    88                                                      
REMARK 465     ASP D    89                                                      
REMARK 465     ALA D    90                                                      
REMARK 465     GLU D    91                                                      
REMARK 465     LYS D    92                                                      
REMARK 465     SER D    93                                                      
REMARK 465     GLY D    94                                                      
REMARK 465     ILE D    95                                                      
REMARK 465     SER D    96                                                      
REMARK 465     LYS D    97                                                      
REMARK 465     MET E     1                                                      
REMARK 465     MET F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     ASP F     3                                                      
REMARK 465     TYR F     4                                                      
REMARK 465     GLU F     5                                                      
REMARK 465     GLU F     6                                                      
REMARK 465     ALA F     7                                                      
REMARK 465     PHE F     8                                                      
REMARK 465     ASN F     9                                                      
REMARK 465     ASP F    10                                                      
REMARK 465     GLY F    11                                                      
REMARK 465     ASN F    12                                                      
REMARK 465     GLU F    13                                                      
REMARK 465     ASN F    14                                                      
REMARK 465     PHE F    15                                                      
REMARK 465     GLU F    16                                                      
REMARK 465     ASP F    17                                                      
REMARK 465     PHE F    18                                                      
REMARK 465     ASP F    19                                                      
REMARK 465     VAL F    20                                                      
REMARK 465     GLU F    21                                                      
REMARK 465     HIS F    22                                                      
REMARK 465     PHE F    23                                                      
REMARK 465     SER F    24                                                      
REMARK 465     ASP F    25                                                      
REMARK 465     GLU F    26                                                      
REMARK 465     GLU F    27                                                      
REMARK 465     THR F    28                                                      
REMARK 465     TYR F    29                                                      
REMARK 465     GLU F    30                                                      
REMARK 465     GLU F    31                                                      
REMARK 465     LYS F    32                                                      
REMARK 465     PRO F    33                                                      
REMARK 465     GLN F    34                                                      
REMARK 465     PHE F    35                                                      
REMARK 465     LYS F    36                                                      
REMARK 465     ASP F    37                                                      
REMARK 465     GLY F    38                                                      
REMARK 465     GLU F    39                                                      
REMARK 465     THR F    40                                                      
REMARK 465     THR F    41                                                      
REMARK 465     ASP F    42                                                      
REMARK 465     ALA F    43                                                      
REMARK 465     ASN F    44                                                      
REMARK 465     GLY F    45                                                      
REMARK 465     LYS F    46                                                      
REMARK 465     THR F    47                                                      
REMARK 465     ILE F    48                                                      
REMARK 465     VAL F    49                                                      
REMARK 465     THR F    50                                                      
REMARK 465     GLY F    51                                                      
REMARK 465     GLY F    52                                                      
REMARK 465     ASN F    53                                                      
REMARK 465     GLY F    54                                                      
REMARK 465     PRO F    55                                                      
REMARK 465     GLU F    56                                                      
REMARK 465     ASP F    57                                                      
REMARK 465     PHE F    58                                                      
REMARK 465     GLN F    59                                                      
REMARK 465     GLN F    60                                                      
REMARK 465     HIS F    61                                                      
REMARK 465     GLU F    62                                                      
REMARK 465     GLN F    63                                                      
REMARK 465     ILE F    64                                                      
REMARK 465     ARG F    65                                                      
REMARK 465     ARG F    66                                                      
REMARK 465     LYS F    67                                                      
REMARK 465     THR F    68                                                      
REMARK 465     LEU F    69                                                      
REMARK 465     LYS F    70                                                      
REMARK 465     ASP F   154                                                      
REMARK 465     LEU F   155                                                      
REMARK 465     MET G     1                                                      
REMARK 465     MET G   132                                                      
REMARK 465     ASP G   133                                                      
REMARK 465     GLU G   134                                                      
REMARK 465     GLU G   135                                                      
REMARK 465     THR G   136                                                      
REMARK 465     PRO G   163                                                      
REMARK 465     LYS G   164                                                      
REMARK 465     GLU G   165                                                      
REMARK 465     ARG G   166                                                      
REMARK 465     GLU G   167                                                      
REMARK 465     LEU G   168                                                      
REMARK 465     GLU G   169                                                      
REMARK 465     GLU G   170                                                      
REMARK 465     ARG G   171                                                      
REMARK 465     ALA G   172                                                      
REMARK 465     GLN G   173                                                      
REMARK 465     LEU G   174                                                      
REMARK 465     GLU G   175                                                      
REMARK 465     ASN G   176                                                      
REMARK 465     GLU G   177                                                      
REMARK 465     ILE G   178                                                      
REMARK 465     GLU G   179                                                      
REMARK 465     GLY G   180                                                      
REMARK 465     LYS G   181                                                      
REMARK 465     ASN G   182                                                      
REMARK 465     GLU G   183                                                      
REMARK 465     GLU G   184                                                      
REMARK 465     THR G   185                                                      
REMARK 465     PRO G   186                                                      
REMARK 465     GLN G   187                                                      
REMARK 465     ASN G   188                                                      
REMARK 465     THR H    68                                                      
REMARK 465     PRO H    69                                                      
REMARK 465     ALA H    70                                                      
REMARK 465     ASN H    71                                                      
REMARK 465     ASP H    72                                                      
REMARK 465     SER H    73                                                      
REMARK 465     ILE I    35                                                      
REMARK 465     GLU I    36                                                      
REMARK 465     GLY I    37                                                      
REMARK 465     ILE I    38                                                      
REMARK 465     GLU I    39                                                      
REMARK 465     ILE I    40                                                      
REMARK 465     TYR I    41                                                      
REMARK 465     ASP I    42                                                      
REMARK 465     ARG I    43                                                      
REMARK 465     LYS I    44                                                      
REMARK 465     LYS I    45                                                      
REMARK 465     LEU I    46                                                      
REMARK 465     PRO I    47                                                      
REMARK 465     ARG I    48                                                      
REMARK 465     LYS I    49                                                      
REMARK 465     GLU I    50                                                      
REMARK 465     VAL I    51                                                      
REMARK 465     ASP I    52                                                      
REMARK 465     ASP I    53                                                      
REMARK 465     VAL I    54                                                      
REMARK 465     LEU I    55                                                      
REMARK 465     GLY I    56                                                      
REMARK 465     GLY I    57                                                      
REMARK 465     GLY I    58                                                      
REMARK 465     TRP I    59                                                      
REMARK 465     ASP I    60                                                      
REMARK 465     ASN I    61                                                      
REMARK 465     VAL I    62                                                      
REMARK 465     ASP I    63                                                      
REMARK 465     GLN I    64                                                      
REMARK 465     THR I    65                                                      
REMARK 465     LYS I    66                                                      
REMARK 465     THR I    67                                                      
REMARK 465     GLN I    68                                                      
REMARK 465     CYS I    69                                                      
REMARK 465     PRO I    70                                                      
REMARK 465     ASN I    71                                                      
REMARK 465     TYR I    72                                                      
REMARK 465     ASP I    73                                                      
REMARK 465     THR I    74                                                      
REMARK 465     CYS I    75                                                      
REMARK 465     GLY I    76                                                      
REMARK 465     GLY I    77                                                      
REMARK 465     GLU I    78                                                      
REMARK 465     SER I    79                                                      
REMARK 465     ALA I    80                                                      
REMARK 465     TYR I    81                                                      
REMARK 465     PHE I    82                                                      
REMARK 465     PHE I    83                                                      
REMARK 465     GLN I    84                                                      
REMARK 465     LEU I    85                                                      
REMARK 465     GLN I    86                                                      
REMARK 465     ILE I    87                                                      
REMARK 465     ARG I    88                                                      
REMARK 465     SER I    89                                                      
REMARK 465     ALA I    90                                                      
REMARK 465     ASP I    91                                                      
REMARK 465     GLU I    92                                                      
REMARK 465     PRO I    93                                                      
REMARK 465     MET I    94                                                      
REMARK 465     THR I    95                                                      
REMARK 465     THR I    96                                                      
REMARK 465     PHE I    97                                                      
REMARK 465     TYR I    98                                                      
REMARK 465     LYS I    99                                                      
REMARK 465     CYS I   100                                                      
REMARK 465     VAL I   101                                                      
REMARK 465     ASN I   102                                                      
REMARK 465     CYS I   103                                                      
REMARK 465     GLY I   104                                                      
REMARK 465     HIS I   105                                                      
REMARK 465     ARG I   106                                                      
REMARK 465     TRP I   107                                                      
REMARK 465     LYS I   108                                                      
REMARK 465     GLU I   109                                                      
REMARK 465     ASN I   110                                                      
REMARK 465     LYS J    68                                                      
REMARK 465     ARG J    69                                                      
REMARK 465     ASP J    70                                                      
REMARK 465     MET K     1                                                      
REMARK 465     THR K     2                                                      
REMARK 465     GLU K     3                                                      
REMARK 465     ASP K     4                                                      
REMARK 465     ILE K     5                                                      
REMARK 465     GLU K     6                                                      
REMARK 465     GLN K     7                                                      
REMARK 465     LYS K     8                                                      
REMARK 465     LYS K     9                                                      
REMARK 465     THR K    10                                                      
REMARK 465     ALA K    11                                                      
REMARK 465     THR K    12                                                      
REMARK 465     GLU K    13                                                      
REMARK 465     VAL K    14                                                      
REMARK 465     THR K    15                                                      
REMARK 465     PRO K    16                                                      
REMARK 465     GLN K    17                                                      
REMARK 465     GLU K    18                                                      
REMARK 465     PRO K    19                                                      
REMARK 465     LYS K    20                                                      
REMARK 465     HIS K    21                                                      
REMARK 465     ILE K    22                                                      
REMARK 465     GLN K    23                                                      
REMARK 465     GLU K    24                                                      
REMARK 465     GLU K    25                                                      
REMARK 465     GLU K    26                                                      
REMARK 465     GLU K    27                                                      
REMARK 465     GLN K    28                                                      
REMARK 465     ASP K    29                                                      
REMARK 465     VAL K    30                                                      
REMARK 465     ASP K    31                                                      
REMARK 465     MET K    32                                                      
REMARK 465     THR K    33                                                      
REMARK 465     GLY K    34                                                      
REMARK 465     ASP K    35                                                      
REMARK 465     GLU K    36                                                      
REMARK 465     GLU K    37                                                      
REMARK 465     GLN K    38                                                      
REMARK 465     GLU K    39                                                      
REMARK 465     GLU K    40                                                      
REMARK 465     GLU K    41                                                      
REMARK 465     MET L     1                                                      
REMARK 465     SER L     2                                                      
REMARK 465     ARG L     3                                                      
REMARK 465     GLU L     4                                                      
REMARK 465     GLY L     5                                                      
REMARK 465     PHE L     6                                                      
REMARK 465     GLN L     7                                                      
REMARK 465     ILE L     8                                                      
REMARK 465     PRO L     9                                                      
REMARK 465     THR L    10                                                      
REMARK 465     ASN L    11                                                      
REMARK 465     LEU L    12                                                      
REMARK 465     ASP L    13                                                      
REMARK 465     ALA L    14                                                      
REMARK 465     ALA L    15                                                      
REMARK 465     ALA L    16                                                      
REMARK 465     ALA L    17                                                      
REMARK 465     GLY L    18                                                      
REMARK 465     THR L    19                                                      
REMARK 465     SER L    20                                                      
REMARK 465     GLN L    21                                                      
REMARK 465     ALA L    22                                                      
REMARK 465     ARG L    23                                                      
REMARK 465     THR L    24                                                      
REMARK 465     ALA L    25                                                      
REMARK 465     MET M     1                                                      
REMARK 465     SER M     2                                                      
REMARK 465     ILE M     3                                                      
REMARK 465     ASP M     4                                                      
REMARK 465     ASN M     5                                                      
REMARK 465     LYS M     6                                                      
REMARK 465     LEU M     7                                                      
REMARK 465     PHE M     8                                                      
REMARK 465     VAL M     9                                                      
REMARK 465     THR M    10                                                      
REMARK 465     GLU M    11                                                      
REMARK 465     GLU M    12                                                      
REMARK 465     ASP M    13                                                      
REMARK 465     GLU M    14                                                      
REMARK 465     GLU M    15                                                      
REMARK 465     ASP M    16                                                      
REMARK 465     ARG M    17                                                      
REMARK 465     THR M    18                                                      
REMARK 465     GLN M    19                                                      
REMARK 465     ASP M    20                                                      
REMARK 465     ARG M    21                                                      
REMARK 465     ALA M    22                                                      
REMARK 465     ASP M    23                                                      
REMARK 465     VAL M    24                                                      
REMARK 465     GLU M    25                                                      
REMARK 465     ASP M    26                                                      
REMARK 465     GLU M    27                                                      
REMARK 465     SER M    28                                                      
REMARK 465     ASN M    29                                                      
REMARK 465     ASP M    30                                                      
REMARK 465     ILE M    31                                                      
REMARK 465     ASP M    32                                                      
REMARK 465     MET M    33                                                      
REMARK 465     ILE M    34                                                      
REMARK 465     ALA M    35                                                      
REMARK 465     ASP M    36                                                      
REMARK 465     GLU M    37                                                      
REMARK 465     ASN M    38                                                      
REMARK 465     GLY M    39                                                      
REMARK 465     THR M    40                                                      
REMARK 465     ASN M    41                                                      
REMARK 465     SER M    42                                                      
REMARK 465     ALA M    43                                                      
REMARK 465     ILE M    44                                                      
REMARK 465     ALA M    45                                                      
REMARK 465     ASN M    46                                                      
REMARK 465     GLU M    47                                                      
REMARK 465     GLN M    48                                                      
REMARK 465     GLU M    49                                                      
REMARK 465     GLU M    50                                                      
REMARK 465     LYS M    51                                                      
REMARK 465     SER M    52                                                      
REMARK 465     GLU M    53                                                      
REMARK 465     GLU M    54                                                      
REMARK 465     VAL M    55                                                      
REMARK 465     LYS M    56                                                      
REMARK 465     ALA M    57                                                      
REMARK 465     GLU M    58                                                      
REMARK 465     ASP M    59                                                      
REMARK 465     ASP M    60                                                      
REMARK 465     THR M    61                                                      
REMARK 465     GLY M    62                                                      
REMARK 465     GLU M    63                                                      
REMARK 465     GLU M    64                                                      
REMARK 465     GLU M    65                                                      
REMARK 465     GLU M    66                                                      
REMARK 465     ASP M    67                                                      
REMARK 465     ASP M    68                                                      
REMARK 465     PRO M    69                                                      
REMARK 465     VAL M    70                                                      
REMARK 465     SER M   205                                                      
REMARK 465     SER M   206                                                      
REMARK 465     GLN M   207                                                      
REMARK 465     ARG M   208                                                      
REMARK 465     ALA M   209                                                      
REMARK 465     GLN M   210                                                      
REMARK 465     VAL M   211                                                      
REMARK 465     VAL M   212                                                      
REMARK 465     THR M   213                                                      
REMARK 465     MET M   214                                                      
REMARK 465     SER M   215                                                      
REMARK 465     VAL M   216                                                      
REMARK 465     LYS M   217                                                      
REMARK 465     SER M   218                                                      
REMARK 465     VAL M   219                                                      
REMARK 465     ASN M   220                                                      
REMARK 465     ASP M   221                                                      
REMARK 465     PRO M   222                                                      
REMARK 465     SER M   223                                                      
REMARK 465     GLN M   224                                                      
REMARK 465     ASN M   225                                                      
REMARK 465     ALA M   263                                                      
REMARK 465     GLU M   264                                                      
REMARK 465     ASP M   265                                                      
REMARK 465     LYS M   266                                                      
REMARK 465     THR M   267                                                      
REMARK 465     LEU M   268                                                      
REMARK 465     VAL M   269                                                      
REMARK 465     ALA M   270                                                      
REMARK 465     LEU M   271                                                      
REMARK 465     GLU M   272                                                      
REMARK 465     LYS M   273                                                      
REMARK 465     GLN M   274                                                      
REMARK 465     GLU M   275                                                      
REMARK 465     ASP M   276                                                      
REMARK 465     TYR M   277                                                      
REMARK 465     ILE M   278                                                      
REMARK 465     ASP M   279                                                      
REMARK 465     ASN M   280                                                      
REMARK 465     LEU M   281                                                      
REMARK 465     VAL M   282                                                      
REMARK 465     MET N     1                                                      
REMARK 465     SER N     2                                                      
REMARK 465     SER N     3                                                      
REMARK 465     ASN N     4                                                      
REMARK 465     LYS N     5                                                      
REMARK 465     GLY N     6                                                      
REMARK 465     ASN N     7                                                      
REMARK 465     GLY N     8                                                      
REMARK 465     ARG N     9                                                      
REMARK 465     LEU N    10                                                      
REMARK 465     PRO N    11                                                      
REMARK 465     SER N    12                                                      
REMARK 465     LEU N    13                                                      
REMARK 465     LYS N    14                                                      
REMARK 465     ASP N    15                                                      
REMARK 465     SER N    16                                                      
REMARK 465     SER N    17                                                      
REMARK 465     SER N    18                                                      
REMARK 465     ASN N    19                                                      
REMARK 465     GLY N    20                                                      
REMARK 465     GLY N    21                                                      
REMARK 465     GLY N    22                                                      
REMARK 465     SER N    23                                                      
REMARK 465     ALA N    24                                                      
REMARK 465     LYS N    25                                                      
REMARK 465     PRO N    26                                                      
REMARK 465     SER N    27                                                      
REMARK 465     LEU N    28                                                      
REMARK 465     LYS N    29                                                      
REMARK 465     PHE N    30                                                      
REMARK 465     LYS N    31                                                      
REMARK 465     PRO N    32                                                      
REMARK 465     LYS N    33                                                      
REMARK 465     ALA N    34                                                      
REMARK 465     VAL N    35                                                      
REMARK 465     ALA N    36                                                      
REMARK 465     ARG N    37                                                      
REMARK 465     LYS N    38                                                      
REMARK 465     SER N    39                                                      
REMARK 465     LYS N    40                                                      
REMARK 465     GLU N    41                                                      
REMARK 465     GLU N    42                                                      
REMARK 465     ARG N    43                                                      
REMARK 465     GLU N    44                                                      
REMARK 465     ALA N    45                                                      
REMARK 465     ALA N    46                                                      
REMARK 465     ALA N    47                                                      
REMARK 465     SER N    48                                                      
REMARK 465     LYS N    49                                                      
REMARK 465     VAL N    50                                                      
REMARK 465     LYS N    51                                                      
REMARK 465     LEU N    52                                                      
REMARK 465     GLU N    53                                                      
REMARK 465     GLU N    54                                                      
REMARK 465     GLU N    55                                                      
REMARK 465     SER N    56                                                      
REMARK 465     LYS N    57                                                      
REMARK 465     ARG N    58                                                      
REMARK 465     GLY N    59                                                      
REMARK 465     ASN N    60                                                      
REMARK 465     ASP N    61                                                      
REMARK 465     LYS N    62                                                      
REMARK 465     LYS N    63                                                      
REMARK 465     HIS N    64                                                      
REMARK 465     PHE N    65                                                      
REMARK 465     ASN N    66                                                      
REMARK 465     ASN N    67                                                      
REMARK 465     LYS N    68                                                      
REMARK 465     ASN N    69                                                      
REMARK 465     LYS N    70                                                      
REMARK 465     ARG N    71                                                      
REMARK 465     VAL N    72                                                      
REMARK 465     THR N    73                                                      
REMARK 465     GLY N    74                                                      
REMARK 465     ALA N    75                                                      
REMARK 465     GLY N    76                                                      
REMARK 465     GLY N    77                                                      
REMARK 465     GLN N    78                                                      
REMARK 465     GLN N    79                                                      
REMARK 465     ARG N    80                                                      
REMARK 465     ARG N    81                                                      
REMARK 465     MET N    82                                                      
REMARK 465     ALA N    83                                                      
REMARK 465     LYS N    84                                                      
REMARK 465     TYR N    85                                                      
REMARK 465     LEU N    86                                                      
REMARK 465     ASN N    87                                                      
REMARK 465     ASN N    88                                                      
REMARK 465     THR N    89                                                      
REMARK 465     HIS N    90                                                      
REMARK 465     VAL N    91                                                      
REMARK 465     ILE N    92                                                      
REMARK 465     SER N    93                                                      
REMARK 465     SER N    94                                                      
REMARK 465     GLY N    95                                                      
REMARK 465     PRO N    96                                                      
REMARK 465     LEU N    97                                                      
REMARK 465     ALA N    98                                                      
REMARK 465     ALA N    99                                                      
REMARK 465     GLY N   100                                                      
REMARK 465     ASN N   101                                                      
REMARK 465     PHE N   102                                                      
REMARK 465     VAL N   103                                                      
REMARK 465     SER N   104                                                      
REMARK 465     GLU N   105                                                      
REMARK 465     LYS N   106                                                      
REMARK 465     GLY N   107                                                      
REMARK 465     ASP N   108                                                      
REMARK 465     LEU N   109                                                      
REMARK 465     ARG N   110                                                      
REMARK 465     ARG N   111                                                      
REMARK 465     GLY N   112                                                      
REMARK 465     PHE N   113                                                      
REMARK 465     ILE N   114                                                      
REMARK 465     LYS N   115                                                      
REMARK 465     SER N   116                                                      
REMARK 465     GLU N   117                                                      
REMARK 465     GLY N   118                                                      
REMARK 465     SER N   119                                                      
REMARK 465     GLY N   120                                                      
REMARK 465     SER N   121                                                      
REMARK 465     SER N   122                                                      
REMARK 465     LEU N   123                                                      
REMARK 465     VAL N   124                                                      
REMARK 465     GLN N   125                                                      
REMARK 465     LYS N   126                                                      
REMARK 465     GLY N   127                                                      
REMARK 465     LEU N   128                                                      
REMARK 465     GLU N   129                                                      
REMARK 465     THR N   130                                                      
REMARK 465     ILE N   131                                                      
REMARK 465     ASP N   132                                                      
REMARK 465     ASN N   133                                                      
REMARK 465     GLY N   134                                                      
REMARK 465     ALA N   135                                                      
REMARK 465     GLU N   136                                                      
REMARK 465     SER N   137                                                      
REMARK 465     SER N   138                                                      
REMARK 465     GLU N   139                                                      
REMARK 465     ASN N   140                                                      
REMARK 465     GLU N   141                                                      
REMARK 465     ALA N   142                                                      
REMARK 465     GLU N   143                                                      
REMARK 465     ASP N   144                                                      
REMARK 465     ASP N   145                                                      
REMARK 465     ASP N   146                                                      
REMARK 465     ASN N   147                                                      
REMARK 465     GLU N   148                                                      
REMARK 465     GLY N   149                                                      
REMARK 465     VAL N   150                                                      
REMARK 465     ALA N   151                                                      
REMARK 465     SER N   152                                                      
REMARK 465     LYS N   153                                                      
REMARK 465     SER N   154                                                      
REMARK 465     LYS N   155                                                      
REMARK 465     LYS N   156                                                      
REMARK 465     LYS N   157                                                      
REMARK 465     PHE N   158                                                      
REMARK 465     ASN N   159                                                      
REMARK 465     MET N   160                                                      
REMARK 465     GLY N   161                                                      
REMARK 465     LYS N   162                                                      
REMARK 465     GLU N   163                                                      
REMARK 465     PHE N   164                                                      
REMARK 465     GLU N   165                                                      
REMARK 465     ALA N   166                                                      
REMARK 465     ARG N   167                                                      
REMARK 465     ASN N   168                                                      
REMARK 465     LEU N   169                                                      
REMARK 465     ILE N   170                                                      
REMARK 465     GLU N   171                                                      
REMARK 465     ASP N   172                                                      
REMARK 465     GLU N   173                                                      
REMARK 465     ASP N   174                                                      
REMARK 465     ASP N   175                                                      
REMARK 465     GLY N   176                                                      
REMARK 465     GLU N   177                                                      
REMARK 465     SER N   178                                                      
REMARK 465     GLU N   179                                                      
REMARK 465     LYS N   180                                                      
REMARK 465     SER N   181                                                      
REMARK 465     SER N   182                                                      
REMARK 465     ASP N   183                                                      
REMARK 465     VAL N   184                                                      
REMARK 465     ASP N   185                                                      
REMARK 465     MET N   186                                                      
REMARK 465     ASP N   187                                                      
REMARK 465     ASP N   188                                                      
REMARK 465     GLU N   189                                                      
REMARK 465     GLU N   190                                                      
REMARK 465     TRP N   191                                                      
REMARK 465     ARG N   192                                                      
REMARK 465     SER N   193                                                      
REMARK 465     LYS N   194                                                      
REMARK 465     ARG N   195                                                      
REMARK 465     ILE N   196                                                      
REMARK 465     GLU N   197                                                      
REMARK 465     GLN N   198                                                      
REMARK 465     LEU N   199                                                      
REMARK 465     PHE N   200                                                      
REMARK 465     PRO N   201                                                      
REMARK 465     VAL N   202                                                      
REMARK 465     ARG N   203                                                      
REMARK 465     PRO N   204                                                      
REMARK 465     VAL N   205                                                      
REMARK 465     ARG N   206                                                      
REMARK 465     VAL N   207                                                      
REMARK 465     ARG N   208                                                      
REMARK 465     HIS N   209                                                      
REMARK 465     GLU N   210                                                      
REMARK 465     ASP N   211                                                      
REMARK 465     VAL N   212                                                      
REMARK 465     GLU N   213                                                      
REMARK 465     THR N   214                                                      
REMARK 465     VAL N   215                                                      
REMARK 465     LYS N   216                                                      
REMARK 465     ARG N   217                                                      
REMARK 465     GLU N   218                                                      
REMARK 465     ILE N   219                                                      
REMARK 465     GLN N   220                                                      
REMARK 465     GLU N   221                                                      
REMARK 465     ALA N   222                                                      
REMARK 465     LEU N   223                                                      
REMARK 465     SER N   224                                                      
REMARK 465     GLU N   225                                                      
REMARK 465     LYS N   226                                                      
REMARK 465     PRO N   227                                                      
REMARK 465     THR N   228                                                      
REMARK 465     ARG N   229                                                      
REMARK 465     GLU N   230                                                      
REMARK 465     PRO N   231                                                      
REMARK 465     THR N   232                                                      
REMARK 465     PRO N   233                                                      
REMARK 465     SER N   234                                                      
REMARK 465     VAL N   235                                                      
REMARK 465     LYS N   236                                                      
REMARK 465     THR N   237                                                      
REMARK 465     GLU N   238                                                      
REMARK 465     PRO N   239                                                      
REMARK 465     VAL N   240                                                      
REMARK 465     GLY N   241                                                      
REMARK 465     THR N   242                                                      
REMARK 465     GLY N   243                                                      
REMARK 465     LEU N   244                                                      
REMARK 465     GLN N   245                                                      
REMARK 465     SER N   246                                                      
REMARK 465     TYR N   247                                                      
REMARK 465     LEU N   248                                                      
REMARK 465     GLU N   249                                                      
REMARK 465     GLU N   250                                                      
REMARK 465     ARG N   251                                                      
REMARK 465     GLU N   252                                                      
REMARK 465     ARG N   253                                                      
REMARK 465     GLN N   254                                                      
REMARK 465     VAL N   255                                                      
REMARK 465     ASN N   256                                                      
REMARK 465     GLU N   257                                                      
REMARK 465     LYS N   258                                                      
REMARK 465     LEU N   259                                                      
REMARK 465     ALA N   260                                                      
REMARK 465     ASP N   261                                                      
REMARK 465     LEU N   262                                                      
REMARK 465     GLY N   263                                                      
REMARK 465     LEU N   264                                                      
REMARK 465     GLU N   265                                                      
REMARK 465     LYS N   266                                                      
REMARK 465     GLU N   267                                                      
REMARK 465     PHE N   268                                                      
REMARK 465     GLN N   269                                                      
REMARK 465     SER N   270                                                      
REMARK 465     VAL N   271                                                      
REMARK 465     ASP N   272                                                      
REMARK 465     GLY N   273                                                      
REMARK 465     ALA N   315                                                      
REMARK 465     PHE N   316                                                      
REMARK 465     GLU N   317                                                      
REMARK 465     ARG N   318                                                      
REMARK 465     PRO N   319                                                      
REMARK 465     ALA N   320                                                      
REMARK 465     VAL N   321                                                      
REMARK 465     LYS N   322                                                      
REMARK 465     GLU N   323                                                      
REMARK 465     GLU N   324                                                      
REMARK 465     LYS N   325                                                      
REMARK 465     GLU N   326                                                      
REMARK 465     ASP N   327                                                      
REMARK 465     MET N   328                                                      
REMARK 465     GLU N   329                                                      
REMARK 465     THR N   330                                                      
REMARK 465     GLN N   331                                                      
REMARK 465     ALA N   332                                                      
REMARK 465     SER N   333                                                      
REMARK 465     ASP N   334                                                      
REMARK 465     PRO N   335                                                      
REMARK 465     SER N   336                                                      
REMARK 465     LYS N   337                                                      
REMARK 465     LYS N   338                                                      
REMARK 465     LYS N   339                                                      
REMARK 465     LYS N   340                                                      
REMARK 465     ASN N   341                                                      
REMARK 465     ILE N   342                                                      
REMARK 465     LYS N   343                                                      
REMARK 465     LYS N   344                                                      
REMARK 465     LYS N   345                                                      
REMARK 465     ASP N   346                                                      
REMARK 465     THR N   347                                                      
REMARK 465     LYS N   348                                                      
REMARK 465     ASP N   349                                                      
REMARK 465     ALA N   350                                                      
REMARK 465     LEU N   351                                                      
REMARK 465     SER N   352                                                      
REMARK 465     THR N   353                                                      
REMARK 465     ARG N   354                                                      
REMARK 465     GLU N   355                                                      
REMARK 465     LEU N   356                                                      
REMARK 465     ALA N   357                                                      
REMARK 465     GLY N   358                                                      
REMARK 465     LYS N   359                                                      
REMARK 465     MET O     1                                                      
REMARK 465     ASP O     2                                                      
REMARK 465     GLU O     3                                                      
REMARK 465     LEU O     4                                                      
REMARK 465     LEU O     5                                                      
REMARK 465     GLY O     6                                                      
REMARK 465     GLU O     7                                                      
REMARK 465     ALA O     8                                                      
REMARK 465     LEU O     9                                                      
REMARK 465     SER O    10                                                      
REMARK 465     ALA O    11                                                      
REMARK 465     GLU O    12                                                      
REMARK 465     ASN O    13                                                      
REMARK 465     GLN O    14                                                      
REMARK 465     THR O    15                                                      
REMARK 465     GLY O    16                                                      
REMARK 465     GLU O    17                                                      
REMARK 465     SER O    18                                                      
REMARK 465     THR O    19                                                      
REMARK 465     VAL O    20                                                      
REMARK 465     GLU O    21                                                      
REMARK 465     SER O    22                                                      
REMARK 465     GLU O    23                                                      
REMARK 465     LYS O    24                                                      
REMARK 465     LEU O    25                                                      
REMARK 465     VAL O    26                                                      
REMARK 465     THR O    27                                                      
REMARK 465     PRO O    28                                                      
REMARK 465     GLU O    29                                                      
REMARK 465     ASP O    30                                                      
REMARK 465     VAL O    31                                                      
REMARK 465     MET O    32                                                      
REMARK 465     THR O    33                                                      
REMARK 465     ILE O    34                                                      
REMARK 465     SER O    35                                                      
REMARK 465     ALA O   372                                                      
REMARK 465     GLU O   373                                                      
REMARK 465     LEU O   374                                                      
REMARK 465     ASP O   375                                                      
REMARK 465     LEU O   376                                                      
REMARK 465     ARG O   377                                                      
REMARK 465     GLY O   378                                                      
REMARK 465     SER O   379                                                      
REMARK 465     LEU O   380                                                      
REMARK 465     LEU O   381                                                      
REMARK 465     SER O   382                                                      
REMARK 465     ARG O   383                                                      
REMARK 465     LYS O   384                                                      
REMARK 465     PRO O   385                                                      
REMARK 465     SER O   386                                                      
REMARK 465     ASP O   387                                                      
REMARK 465     ASN O   388                                                      
REMARK 465     LYS O   389                                                      
REMARK 465     LYS O   390                                                      
REMARK 465     ARG O   391                                                      
REMARK 465     SER O   392                                                      
REMARK 465     GLY O   393                                                      
REMARK 465     SER O   394                                                      
REMARK 465     ASN O   395                                                      
REMARK 465     ALA O   396                                                      
REMARK 465     ALA O   397                                                      
REMARK 465     ALA O   398                                                      
REMARK 465     SER O   399                                                      
REMARK 465     LEU O   400                                                      
REMARK 465     PRO O   401                                                      
REMARK 465     SER O   402                                                      
REMARK 465     LYS O   403                                                      
REMARK 465     LYS O   404                                                      
REMARK 465     LEU O   405                                                      
REMARK 465     LYS O   406                                                      
REMARK 465     THR O   407                                                      
REMARK 465     GLU O   408                                                      
REMARK 465     ASP O   409                                                      
REMARK 465     GLY O   410                                                      
REMARK 465     PHE O   411                                                      
REMARK 465     VAL O   412                                                      
REMARK 465     ILE O   413                                                      
REMARK 465     PRO O   414                                                      
REMARK 465     ALA O   415                                                      
REMARK 465     LEU O   416                                                      
REMARK 465     PRO O   417                                                      
REMARK 465     ALA O   418                                                      
REMARK 465     ALA O   419                                                      
REMARK 465     VAL O   420                                                      
REMARK 465     SER O   421                                                      
REMARK 465     LYS O   422                                                      
REMARK 465     SER O   423                                                      
REMARK 465     LEU O   424                                                      
REMARK 465     GLN O   425                                                      
REMARK 465     GLU O   426                                                      
REMARK 465     SER O   427                                                      
REMARK 465     GLY O   428                                                      
REMARK 465     ASP O   429                                                      
REMARK 465     THR O   430                                                      
REMARK 465     GLN O   431                                                      
REMARK 465     GLU O   432                                                      
REMARK 465     GLU O   433                                                      
REMARK 465     ASP O   434                                                      
REMARK 465     GLU O   435                                                      
REMARK 465     GLU O   436                                                      
REMARK 465     GLU O   437                                                      
REMARK 465     GLU O   438                                                      
REMARK 465     ASP O   439                                                      
REMARK 465     LEU O   440                                                      
REMARK 465     ASP O   441                                                      
REMARK 465     ALA O   442                                                      
REMARK 465     ASP O   443                                                      
REMARK 465     THR O   444                                                      
REMARK 465     GLU O   445                                                      
REMARK 465     ASP O   446                                                      
REMARK 465     PRO O   447                                                      
REMARK 465     HIS O   448                                                      
REMARK 465     VAL O   611                                                      
REMARK 465     LYS O   612                                                      
REMARK 465     GLY O   613                                                      
REMARK 465     ARG O   614                                                      
REMARK 465     GLU O   615                                                      
REMARK 465     ASN O   616                                                      
REMARK 465     GLU O   617                                                      
REMARK 465     LEU O   618                                                      
REMARK 465     MET P     1                                                      
REMARK 465     SER P     2                                                      
REMARK 465     GLY P     3                                                      
REMARK 465     MET P     4                                                      
REMARK 465     ILE P     5                                                      
REMARK 465     GLU P     6                                                      
REMARK 465     ASN P     7                                                      
REMARK 465     GLY P     8                                                      
REMARK 465     LEU P     9                                                      
REMARK 465     GLN P    10                                                      
REMARK 465     LEU P    11                                                      
REMARK 465     SER P    12                                                      
REMARK 465     ASP P    13                                                      
REMARK 465     ASN P    14                                                      
REMARK 465     ALA P    15                                                      
REMARK 465     LYS P    16                                                      
REMARK 465     THR P    17                                                      
REMARK 465     LEU P    18                                                      
REMARK 465     HIS P    19                                                      
REMARK 465     SER P    20                                                      
REMARK 465     GLN P    21                                                      
REMARK 465     MET P    22                                                      
REMARK 465     MET P    23                                                      
REMARK 465     SER P    24                                                      
REMARK 465     LYS P    25                                                      
REMARK 465     GLY P    26                                                      
REMARK 465     ILE P    27                                                      
REMARK 465     GLY P    28                                                      
REMARK 465     ALA P    29                                                      
REMARK 465     LEU P    30                                                      
REMARK 465     PHE P    31                                                      
REMARK 465     THR P    32                                                      
REMARK 465     GLN P    33                                                      
REMARK 465     GLN P    34                                                      
REMARK 465     GLU P    35                                                      
REMARK 465     LEU P    36                                                      
REMARK 465     GLN P    37                                                      
REMARK 465     LYS P    38                                                      
REMARK 465     GLN P    39                                                      
REMARK 465     MET P    40                                                      
REMARK 465     GLY P    41                                                      
REMARK 465     ILE P    42                                                      
REMARK 465     GLY P    43                                                      
REMARK 465     SER P    44                                                      
REMARK 465     LEU P    45                                                      
REMARK 465     THR P    46                                                      
REMARK 465     ASP P    47                                                      
REMARK 465     LEU P    48                                                      
REMARK 465     MET P    49                                                      
REMARK 465     SER P    50                                                      
REMARK 465     ILE P    51                                                      
REMARK 465     VAL P    52                                                      
REMARK 465     GLN P    53                                                      
REMARK 465     GLU P    54                                                      
REMARK 465     LEU P    55                                                      
REMARK 465     LEU P    56                                                      
REMARK 465     ASP P    57                                                      
REMARK 465     LYS P    58                                                      
REMARK 465     ASN P    59                                                      
REMARK 465     LEU P    60                                                      
REMARK 465     ILE P    61                                                      
REMARK 465     LYS P    62                                                      
REMARK 465     LEU P    63                                                      
REMARK 465     VAL P    64                                                      
REMARK 465     LYS P    65                                                      
REMARK 465     GLN P    66                                                      
REMARK 465     ASN P    67                                                      
REMARK 465     ASP P    68                                                      
REMARK 465     GLU P    69                                                      
REMARK 465     LEU P    70                                                      
REMARK 465     LYS P    71                                                      
REMARK 465     PHE P    72                                                      
REMARK 465     GLN P    73                                                      
REMARK 465     GLY P    74                                                      
REMARK 465     VAL P    75                                                      
REMARK 465     LEU P    76                                                      
REMARK 465     GLU P    77                                                      
REMARK 465     SER P    78                                                      
REMARK 465     GLU P    79                                                      
REMARK 465     ALA P    80                                                      
REMARK 465     GLN P    81                                                      
REMARK 465     LYS P    82                                                      
REMARK 465     LYS P    83                                                      
REMARK 465     ALA P    84                                                      
REMARK 465     THR P    85                                                      
REMARK 465     MET P    86                                                      
REMARK 465     SER P    87                                                      
REMARK 465     ALA P    88                                                      
REMARK 465     GLU P    89                                                      
REMARK 465     GLU P    90                                                      
REMARK 465     ALA P    91                                                      
REMARK 465     LEU P    92                                                      
REMARK 465     VAL P    93                                                      
REMARK 465     TYR P    94                                                      
REMARK 465     SER P    95                                                      
REMARK 465     TYR P    96                                                      
REMARK 465     ILE P    97                                                      
REMARK 465     GLU P    98                                                      
REMARK 465     ALA P    99                                                      
REMARK 465     SER P   100                                                      
REMARK 465     GLY P   101                                                      
REMARK 465     ARG P   102                                                      
REMARK 465     GLU P   103                                                      
REMARK 465     GLY P   104                                                      
REMARK 465     ILE P   105                                                      
REMARK 465     TRP P   106                                                      
REMARK 465     SER P   107                                                      
REMARK 465     LYS P   108                                                      
REMARK 465     THR P   109                                                      
REMARK 465     ILE P   110                                                      
REMARK 465     LYS P   111                                                      
REMARK 465     ALA P   112                                                      
REMARK 465     ARG P   113                                                      
REMARK 465     THR P   114                                                      
REMARK 465     ASN P   115                                                      
REMARK 465     LEU P   116                                                      
REMARK 465     HIS P   117                                                      
REMARK 465     GLN P   118                                                      
REMARK 465     HIS P   119                                                      
REMARK 465     VAL P   120                                                      
REMARK 465     VAL P   121                                                      
REMARK 465     LEU P   122                                                      
REMARK 465     LYS P   123                                                      
REMARK 465     CYS P   124                                                      
REMARK 465     LEU P   125                                                      
REMARK 465     LYS P   126                                                      
REMARK 465     SER P   127                                                      
REMARK 465     LEU P   128                                                      
REMARK 465     GLU P   129                                                      
REMARK 465     SER P   130                                                      
REMARK 465     GLN P   131                                                      
REMARK 465     ARG P   132                                                      
REMARK 465     TYR P   133                                                      
REMARK 465     VAL P   134                                                      
REMARK 465     LYS P   135                                                      
REMARK 465     SER P   136                                                      
REMARK 465     VAL P   137                                                      
REMARK 465     LYS P   138                                                      
REMARK 465     SER P   139                                                      
REMARK 465     VAL P   140                                                      
REMARK 465     LYS P   141                                                      
REMARK 465     PHE P   142                                                      
REMARK 465     PRO P   143                                                      
REMARK 465     THR P   144                                                      
REMARK 465     ARG P   145                                                      
REMARK 465     LYS P   146                                                      
REMARK 465     ILE P   147                                                      
REMARK 465     TYR P   148                                                      
REMARK 465     MET P   149                                                      
REMARK 465     LEU P   150                                                      
REMARK 465     TYR P   151                                                      
REMARK 465     SER P   152                                                      
REMARK 465     LEU P   153                                                      
REMARK 465     GLN P   154                                                      
REMARK 465     PRO P   155                                                      
REMARK 465     SER P   156                                                      
REMARK 465     VAL P   157                                                      
REMARK 465     ASP P   158                                                      
REMARK 465     ILE P   159                                                      
REMARK 465     THR P   160                                                      
REMARK 465     GLY P   161                                                      
REMARK 465     GLY P   162                                                      
REMARK 465     PRO P   163                                                      
REMARK 465     TRP P   164                                                      
REMARK 465     PHE P   165                                                      
REMARK 465     THR P   166                                                      
REMARK 465     ASP P   167                                                      
REMARK 465     GLY P   168                                                      
REMARK 465     THR P   190                                                      
REMARK 465     PHE P   191                                                      
REMARK 465     PRO P   192                                                      
REMARK 465     ASN P   193                                                      
REMARK 465     GLY P   194                                                      
REMARK 465     PHE P   195                                                      
REMARK 465     LYS P   196                                                      
REMARK 465     ASN P   197                                                      
REMARK 465     PHE P   198                                                      
REMARK 465     GLU P   199                                                      
REMARK 465     ASN P   200                                                      
REMARK 465     GLY P   201                                                      
REMARK 465     PRO P   202                                                      
REMARK 465     LYS P   203                                                      
REMARK 465     LYS P   204                                                      
REMARK 465     ASN P   205                                                      
REMARK 465     VAL P   206                                                      
REMARK 465     PHE P   207                                                      
REMARK 465     TYR P   208                                                      
REMARK 465     ALA P   209                                                      
REMARK 465     PRO P   210                                                      
REMARK 465     ASN P   211                                                      
REMARK 465     VAL P   212                                                      
REMARK 465     LYS P   213                                                      
REMARK 465     ASN P   214                                                      
REMARK 465     TYR P   215                                                      
REMARK 465     SER P   216                                                      
REMARK 465     THR P   217                                                      
REMARK 465     ASN P   272                                                      
REMARK 465     GLN P   273                                                      
REMARK 465     GLY P   274                                                      
REMARK 465     GLU P   275                                                      
REMARK 465     GLY P   276                                                      
REMARK 465     GLU P   277                                                      
REMARK 465     PRO P   278                                                      
REMARK 465     GLU P   279                                                      
REMARK 465     ALA P   280                                                      
REMARK 465     GLY P   281                                                      
REMARK 465     ASN P   282                                                      
REMARK 465     LYS P   283                                                      
REMARK 465     ALA P   284                                                      
REMARK 465     LEU P   285                                                      
REMARK 465     GLU P   286                                                      
REMARK 465     ASP P   287                                                      
REMARK 465     GLU P   288                                                      
REMARK 465     GLU P   289                                                      
REMARK 465     GLU P   290                                                      
REMARK 465     PHE P   291                                                      
REMARK 465     SER P   292                                                      
REMARK 465     ILE P   317                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     SER Q     2                                                      
REMARK 465     SER Q     3                                                      
REMARK 465     TYR Q     4                                                      
REMARK 465     ARG Q     5                                                      
REMARK 465     GLY Q     6                                                      
REMARK 465     GLY Q     7                                                      
REMARK 465     SER Q     8                                                      
REMARK 465     ARG Q     9                                                      
REMARK 465     GLY Q    10                                                      
REMARK 465     GLY Q    11                                                      
REMARK 465     GLY Q    12                                                      
REMARK 465     SER Q    13                                                      
REMARK 465     ASN Q    14                                                      
REMARK 465     TYR Q    15                                                      
REMARK 465     MET Q    16                                                      
REMARK 465     SER Q    17                                                      
REMARK 465     ASN Q    18                                                      
REMARK 465     LEU Q    19                                                      
REMARK 465     PRO Q    20                                                      
REMARK 465     PHE Q    21                                                      
REMARK 465     GLY Q    22                                                      
REMARK 465     LEU Q    23                                                      
REMARK 465     GLY Q    24                                                      
REMARK 465     TYR Q    25                                                      
REMARK 465     GLY Q    26                                                      
REMARK 465     ASP Q    27                                                      
REMARK 465     VAL Q    28                                                      
REMARK 465     GLY Q    29                                                      
REMARK 465     LYS Q    30                                                      
REMARK 465     ASN Q    31                                                      
REMARK 465     HIS Q    32                                                      
REMARK 465     ILE Q    33                                                      
REMARK 465     THR Q    34                                                      
REMARK 465     GLU Q    35                                                      
REMARK 465     TYR Q    71                                                      
REMARK 465     THR Q    72                                                      
REMARK 465     GLY Q    73                                                      
REMARK 465     SER Q    74                                                      
REMARK 465     MET Q    75                                                      
REMARK 465     SER Q    76                                                      
REMARK 465     LEU Q    77                                                      
REMARK 465     ILE Q    78                                                      
REMARK 465     ILE Q    79                                                      
REMARK 465     ASP Q    80                                                      
REMARK 465     GLN Q    81                                                      
REMARK 465     GLN Q    82                                                      
REMARK 465     GLU Q    83                                                      
REMARK 465     ASN Q    84                                                      
REMARK 465     SER Q    85                                                      
REMARK 465     LYS Q    86                                                      
REMARK 465     SER Q    87                                                      
REMARK 465     GLY Q    88                                                      
REMARK 465     LYS Q    89                                                      
REMARK 465     ARG Q    90                                                      
REMARK 465     LYS Q    91                                                      
REMARK 465     PRO Q    92                                                      
REMARK 465     ASN Q    93                                                      
REMARK 465     ILE Q    94                                                      
REMARK 465     ILE Q    95                                                      
REMARK 465     LEU Q    96                                                      
REMARK 465     ASP Q    97                                                      
REMARK 465     GLU Q    98                                                      
REMARK 465     ASP Q    99                                                      
REMARK 465     ASP Q   100                                                      
REMARK 465     THR Q   101                                                      
REMARK 465     ASN Q   102                                                      
REMARK 465     ASP Q   103                                                      
REMARK 465     GLY Q   104                                                      
REMARK 465     ILE Q   105                                                      
REMARK 465     GLU Q   106                                                      
REMARK 465     ARG Q   107                                                      
REMARK 465     TYR Q   108                                                      
REMARK 465     SER Q   109                                                      
REMARK 465     ASP Q   110                                                      
REMARK 465     LYS Q   111                                                      
REMARK 465     TYR Q   112                                                      
REMARK 465     LEU Q   113                                                      
REMARK 465     LYS Q   114                                                      
REMARK 465     LYS Q   115                                                      
REMARK 465     ARG Q   116                                                      
REMARK 465     LYS Q   117                                                      
REMARK 465     ILE Q   118                                                      
REMARK 465     GLY Q   119                                                      
REMARK 465     ILE Q   120                                                      
REMARK 465     SER Q   121                                                      
REMARK 465     ILE Q   122                                                      
REMARK 465     ASP Q   123                                                      
REMARK 465     ASP Q   124                                                      
REMARK 465     HIS Q   125                                                      
REMARK 465     PRO Q   126                                                      
REMARK 465     TYR Q   127                                                      
REMARK 465     ASN Q   128                                                      
REMARK 465     LEU Q   129                                                      
REMARK 465     ASN Q   130                                                      
REMARK 465     LEU Q   131                                                      
REMARK 465     PHE Q   132                                                      
REMARK 465     PRO Q   133                                                      
REMARK 465     ASN Q   134                                                      
REMARK 465     GLU Q   135                                                      
REMARK 465     LEU Q   136                                                      
REMARK 465     TYR Q   137                                                      
REMARK 465     ASN Q   138                                                      
REMARK 465     VAL Q   139                                                      
REMARK 465     MET Q   140                                                      
REMARK 465     GLY Q   141                                                      
REMARK 465     ILE Q   142                                                      
REMARK 465     ASN Q   143                                                      
REMARK 465     LYS Q   144                                                      
REMARK 465     LYS Q   145                                                      
REMARK 465     LYS Q   146                                                      
REMARK 465     LEU Q   147                                                      
REMARK 465     LEU Q   148                                                      
REMARK 465     ALA Q   149                                                      
REMARK 465     ILE Q   150                                                      
REMARK 465     SER Q   151                                                      
REMARK 465     LYS Q   152                                                      
REMARK 465     PHE Q   153                                                      
REMARK 465     ASN Q   154                                                      
REMARK 465     ASN Q   155                                                      
REMARK 465     ALA Q   156                                                      
REMARK 465     ASP Q   157                                                      
REMARK 465     ASP Q   158                                                      
REMARK 465     VAL Q   159                                                      
REMARK 465     PHE Q   160                                                      
REMARK 465     THR Q   161                                                      
REMARK 465     GLY Q   162                                                      
REMARK 465     THR Q   163                                                      
REMARK 465     GLY Q   164                                                      
REMARK 465     LEU Q   165                                                      
REMARK 465     GLN Q   166                                                      
REMARK 465     ASP Q   167                                                      
REMARK 465     GLU Q   168                                                      
REMARK 465     ASN Q   169                                                      
REMARK 465     ILE Q   170                                                      
REMARK 465     GLY Q   171                                                      
REMARK 465     LEU Q   172                                                      
REMARK 465     SER Q   173                                                      
REMARK 465     MET Q   174                                                      
REMARK 465     LEU Q   175                                                      
REMARK 465     ALA Q   176                                                      
REMARK 465     LYS Q   177                                                      
REMARK 465     LEU Q   178                                                      
REMARK 465     LYS Q   179                                                      
REMARK 465     GLU Q   180                                                      
REMARK 465     LEU Q   181                                                      
REMARK 465     ALA Q   182                                                      
REMARK 465     GLU Q   183                                                      
REMARK 465     ASP Q   184                                                      
REMARK 465     VAL Q   185                                                      
REMARK 465     ASP Q   186                                                      
REMARK 465     ASP Q   187                                                      
REMARK 465     ALA Q   188                                                      
REMARK 465     SER Q   189                                                      
REMARK 465     THR Q   190                                                      
REMARK 465     GLY Q   191                                                      
REMARK 465     ASP Q   192                                                      
REMARK 465     GLY Q   193                                                      
REMARK 465     ALA Q   194                                                      
REMARK 465     ALA Q   195                                                      
REMARK 465     LYS Q   196                                                      
REMARK 465     GLY Q   197                                                      
REMARK 465     SER Q   198                                                      
REMARK 465     LYS Q   199                                                      
REMARK 465     THR Q   200                                                      
REMARK 465     GLY Q   201                                                      
REMARK 465     GLU Q   202                                                      
REMARK 465     GLY Q   203                                                      
REMARK 465     GLU Q   204                                                      
REMARK 465     ASP Q   205                                                      
REMARK 465     ASP Q   206                                                      
REMARK 465     ASP Q   207                                                      
REMARK 465     LEU Q   208                                                      
REMARK 465     ALA Q   209                                                      
REMARK 465     ASP Q   210                                                      
REMARK 465     ASP Q   211                                                      
REMARK 465     ASP Q   212                                                      
REMARK 465     PHE Q   213                                                      
REMARK 465     GLU Q   214                                                      
REMARK 465     GLU Q   215                                                      
REMARK 465     ASP Q   216                                                      
REMARK 465     GLU Q   217                                                      
REMARK 465     ASP Q   218                                                      
REMARK 465     GLU Q   219                                                      
REMARK 465     GLU Q   220                                                      
REMARK 465     ASP Q   221                                                      
REMARK 465     ASP Q   222                                                      
REMARK 465     ASP Q   223                                                      
REMARK 465     ASP Q   224                                                      
REMARK 465     TYR Q   225                                                      
REMARK 465     ASN Q   226                                                      
REMARK 465     ALA Q   227                                                      
REMARK 465     GLU Q   228                                                      
REMARK 465     LYS Q   229                                                      
REMARK 465     TYR Q   230                                                      
REMARK 465     PHE Q   231                                                      
REMARK 465     ASN Q   232                                                      
REMARK 465     ASN Q   233                                                      
REMARK 465     GLY Q   234                                                      
REMARK 465     ASP Q   235                                                      
REMARK 465     ASP Q   236                                                      
REMARK 465     ASP Q   237                                                      
REMARK 465     ASP Q   238                                                      
REMARK 465     TYR Q   239                                                      
REMARK 465     GLY Q   240                                                      
REMARK 465     ASP Q   241                                                      
REMARK 465     GLU Q   242                                                      
REMARK 465     GLU Q   243                                                      
REMARK 465     ASP Q   244                                                      
REMARK 465     PRO Q   245                                                      
REMARK 465     ASN Q   246                                                      
REMARK 465     GLU Q   247                                                      
REMARK 465     GLU Q   248                                                      
REMARK 465     ALA Q   249                                                      
REMARK 465     ALA Q   250                                                      
REMARK 465     PHE Q   251                                                      
REMARK 465     MET U     1                                                      
REMARK 465     ALA U     2                                                      
REMARK 465     ASP U     3                                                      
REMARK 465     GLU U     4                                                      
REMARK 465     GLU U     5                                                      
REMARK 465     ARG U     6                                                      
REMARK 465     LEU U     7                                                      
REMARK 465     LYS U     8                                                      
REMARK 465     GLU U     9                                                      
REMARK 465     PHE U    10                                                      
REMARK 465     LYS U    11                                                      
REMARK 465     GLU U    12                                                      
REMARK 465     ALA U    13                                                      
REMARK 465     ASN U    14                                                      
REMARK 465     LYS U    15                                                      
REMARK 465     ILE U    16                                                      
REMARK 465     VAL U    17                                                      
REMARK 465     PHE U    18                                                      
REMARK 465     ASP U    19                                                      
REMARK 465     PRO U    20                                                      
REMARK 465     ASN U    21                                                      
REMARK 465     THR U    22                                                      
REMARK 465     ARG U    23                                                      
REMARK 465     GLN U    24                                                      
REMARK 465     VAL U    25                                                      
REMARK 465     TRP U    26                                                      
REMARK 465     GLU U    27                                                      
REMARK 465     ASN U    28                                                      
REMARK 465     GLN U    29                                                      
REMARK 465     ASN U    30                                                      
REMARK 465     ARG U    31                                                      
REMARK 465     ASP U    32                                                      
REMARK 465     GLY U    33                                                      
REMARK 465     THR U    34                                                      
REMARK 465     LYS U    35                                                      
REMARK 465     PRO U    36                                                      
REMARK 465     ALA U    37                                                      
REMARK 465     THR U    38                                                      
REMARK 465     THR U    39                                                      
REMARK 465     PHE U    40                                                      
REMARK 465     GLN U    41                                                      
REMARK 465     SER U    42                                                      
REMARK 465     GLU U    43                                                      
REMARK 465     GLU U    44                                                      
REMARK 465     ASP U    45                                                      
REMARK 465     ILE U    46                                                      
REMARK 465     LYS U    47                                                      
REMARK 465     ARG U    48                                                      
REMARK 465     ALA U    49                                                      
REMARK 465     ALA U    50                                                      
REMARK 465     PRO U    51                                                      
REMARK 465     GLU U    52                                                      
REMARK 465     SER U    53                                                      
REMARK 465     GLU U    54                                                      
REMARK 465     LYS U    55                                                      
REMARK 465     ASP U    56                                                      
REMARK 465     THR U    57                                                      
REMARK 465     SER U    58                                                      
REMARK 465     ALA U    59                                                      
REMARK 465     THR U    60                                                      
REMARK 465     MET V     1                                                      
REMARK 465     VAL V    41                                                      
REMARK 465     THR V    42                                                      
REMARK 465     PHE V    43                                                      
REMARK 465     GLY V    44                                                      
REMARK 465     GLU V    45                                                      
REMARK 465     THR V    46                                                      
REMARK 465     SER V    47                                                      
REMARK 465     ALA V    48                                                      
REMARK 465     GLY V    49                                                      
REMARK 465     ALA V    50                                                      
REMARK 465     ALA V    51                                                      
REMARK 465     VAL V    52                                                      
REMARK 465     VAL V    53                                                      
REMARK 465     GLN V    54                                                      
REMARK 465     GLY V    55                                                      
REMARK 465     SER V    56                                                      
REMARK 465     PHE V    57                                                      
REMARK 465     ILE V    58                                                      
REMARK 465     GLY V    59                                                      
REMARK 465     ALA V    60                                                      
REMARK 465     GLY V    61                                                      
REMARK 465     GLN V    62                                                      
REMARK 465     SER V    63                                                      
REMARK 465     HIS V    64                                                      
REMARK 465     ALA V    65                                                      
REMARK 465     ALA V    66                                                      
REMARK 465     PHE V    67                                                      
REMARK 465     GLY V    68                                                      
REMARK 465     GLY V    69                                                      
REMARK 465     SER V    70                                                      
REMARK 465     SER V    71                                                      
REMARK 465     ALA V    72                                                      
REMARK 465     ARG V   298                                                      
REMARK 465     LYS V   299                                                      
REMARK 465     ILE V   300                                                      
REMARK 465     LYS V   301                                                      
REMARK 465     ASP V   302                                                      
REMARK 465     SER V   303                                                      
REMARK 465     LEU V   304                                                      
REMARK 465     ASP V   305                                                      
REMARK 465     LYS V   306                                                      
REMARK 465     GLU V   307                                                      
REMARK 465     GLU V   308                                                      
REMARK 465     MET V   309                                                      
REMARK 465     PHE V   310                                                      
REMARK 465     GLN V   311                                                      
REMARK 465     THR V   312                                                      
REMARK 465     SER V   313                                                      
REMARK 465     GLU V   314                                                      
REMARK 465     GLU V   315                                                      
REMARK 465     ALA V   316                                                      
REMARK 465     LEU V   317                                                      
REMARK 465     ASN V   318                                                      
REMARK 465     LYS V   319                                                      
REMARK 465     ASN V   320                                                      
REMARK 465     PRO V   321                                                      
REMARK 465     ILE V   322                                                      
REMARK 465     LEU V   323                                                      
REMARK 465     THR V   324                                                      
REMARK 465     GLN V   325                                                      
REMARK 465     VAL V   326                                                      
REMARK 465     LEU V   327                                                      
REMARK 465     GLY V   328                                                      
REMARK 465     GLU V   329                                                      
REMARK 465     GLN V   330                                                      
REMARK 465     GLU V   331                                                      
REMARK 465     LEU V   332                                                      
REMARK 465     SER V   333                                                      
REMARK 465     SER V   334                                                      
REMARK 465     LYS V   335                                                      
REMARK 465     GLU V   336                                                      
REMARK 465     VAL V   337                                                      
REMARK 465     LEU V   338                                                      
REMARK 465     PHE V   339                                                      
REMARK 465     TYR V   340                                                      
REMARK 465     LEU V   341                                                      
REMARK 465     LYS V   342                                                      
REMARK 465     GLN V   343                                                      
REMARK 465     PHE V   344                                                      
REMARK 465     SER V   345                                                      
REMARK 465     GLU V   346                                                      
REMARK 465     ARG V   347                                                      
REMARK 465     ARG V   348                                                      
REMARK 465     ALA V   349                                                      
REMARK 465     ARG V   350                                                      
REMARK 465     VAL V   351                                                      
REMARK 465     VAL V   352                                                      
REMARK 465     GLU V   353                                                      
REMARK 465     ARG V   354                                                      
REMARK 465     ILE V   355                                                      
REMARK 465     LYS V   356                                                      
REMARK 465     ALA V   357                                                      
REMARK 465     THR V   358                                                      
REMARK 465     ASN V   359                                                      
REMARK 465     GLY V   360                                                      
REMARK 465     ILE V   361                                                      
REMARK 465     ASP V   362                                                      
REMARK 465     GLY V   363                                                      
REMARK 465     GLU V   364                                                      
REMARK 465     ASN V   365                                                      
REMARK 465     ILE V   366                                                      
REMARK 465     TYR V   367                                                      
REMARK 465     HIS V   368                                                      
REMARK 465     GLU V   369                                                      
REMARK 465     GLY V   370                                                      
REMARK 465     SER V   371                                                      
REMARK 465     GLU V   372                                                      
REMARK 465     ASN V   373                                                      
REMARK 465     GLU V   374                                                      
REMARK 465     THR V   375                                                      
REMARK 465     ARG V   376                                                      
REMARK 465     LYS V   377                                                      
REMARK 465     ARG V   378                                                      
REMARK 465     LYS V   379                                                      
REMARK 465     LEU V   380                                                      
REMARK 465     SER V   381                                                      
REMARK 465     GLU V   382                                                      
REMARK 465     VAL V   383                                                      
REMARK 465     SER V   384                                                      
REMARK 465     ILE V   385                                                      
REMARK 465     GLN V   386                                                      
REMARK 465     ASN V   387                                                      
REMARK 465     GLU V   388                                                      
REMARK 465     HIS V   389                                                      
REMARK 465     VAL V   390                                                      
REMARK 465     GLU V   391                                                      
REMARK 465     GLY V   392                                                      
REMARK 465     GLU V   393                                                      
REMARK 465     ASP V   394                                                      
REMARK 465     LYS V   395                                                      
REMARK 465     GLU V   396                                                      
REMARK 465     THR V   397                                                      
REMARK 465     GLU V   398                                                      
REMARK 465     GLY V   399                                                      
REMARK 465     THR V   400                                                      
REMARK 465     GLU V   401                                                      
REMARK 465     GLU V   402                                                      
REMARK 465     LYS V   403                                                      
REMARK 465     VAL V   404                                                      
REMARK 465     LYS V   405                                                      
REMARK 465     LYS V   406                                                      
REMARK 465     VAL V   407                                                      
REMARK 465     LYS V   408                                                      
REMARK 465     THR V   409                                                      
REMARK 465     LYS V   410                                                      
REMARK 465     THR V   411                                                      
REMARK 465     SER V   412                                                      
REMARK 465     GLU V   413                                                      
REMARK 465     GLU V   414                                                      
REMARK 465     LYS V   415                                                      
REMARK 465     LYS V   416                                                      
REMARK 465     GLU V   417                                                      
REMARK 465     ASN V   418                                                      
REMARK 465     GLU V   419                                                      
REMARK 465     SER V   420                                                      
REMARK 465     GLY V   421                                                      
REMARK 465     HIS V   422                                                      
REMARK 465     PHE V   423                                                      
REMARK 465     GLN V   424                                                      
REMARK 465     ASP V   425                                                      
REMARK 465     ALA V   426                                                      
REMARK 465     ILE V   427                                                      
REMARK 465     ASP V   428                                                      
REMARK 465     GLY V   429                                                      
REMARK 465     TYR V   430                                                      
REMARK 465     SER V   431                                                      
REMARK 465     LEU V   432                                                      
REMARK 465     GLU V   433                                                      
REMARK 465     THR V   434                                                      
REMARK 465     ASP V   435                                                      
REMARK 465     PRO V   436                                                      
REMARK 465     TYR V   437                                                      
REMARK 465     THR V   511                                                      
REMARK 465     GLY V   512                                                      
REMARK 465     ASN V   513                                                      
REMARK 465     THR V   514                                                      
REMARK 465     SER V   515                                                      
REMARK 465     VAL V   516                                                      
REMARK 465     LYS V   517                                                      
REMARK 465     LYS V   518                                                      
REMARK 465     LYS V   519                                                      
REMARK 465     ARG V   520                                                      
REMARK 465     THR V   521                                                      
REMARK 465     ARG V   522                                                      
REMARK 465     ARG V   523                                                      
REMARK 465     ARG V   524                                                      
REMARK 465     ASN V   525                                                      
REMARK 465     ASN V   526                                                      
REMARK 465     THR V   527                                                      
REMARK 465     ARG V   528                                                      
REMARK 465     SER V   529                                                      
REMARK 465     ASP V   530                                                      
REMARK 465     GLU V   531                                                      
REMARK 465     PRO V   532                                                      
REMARK 465     THR V   533                                                      
REMARK 465     LYS V   534                                                      
REMARK 465     THR V   535                                                      
REMARK 465     VAL V   536                                                      
REMARK 465     ASP V   537                                                      
REMARK 465     ALA V   538                                                      
REMARK 465     ALA V   539                                                      
REMARK 465     ALA V   540                                                      
REMARK 465     ALA V   541                                                      
REMARK 465     ILE V   542                                                      
REMARK 465     GLY V   543                                                      
REMARK 465     LEU V   544                                                      
REMARK 465     MET V   545                                                      
REMARK 465     SER V   546                                                      
REMARK 465     ASP V   547                                                      
REMARK 465     LEU V   548                                                      
REMARK 465     GLN V   549                                                      
REMARK 465     ASP V   550                                                      
REMARK 465     LYS V   551                                                      
REMARK 465     SER V   552                                                      
REMARK 465     GLY V   553                                                      
REMARK 465     LEU V   554                                                      
REMARK 465     HIS V   555                                                      
REMARK 465     ALA V   556                                                      
REMARK 465     ALA V   557                                                      
REMARK 465     LEU V   558                                                      
REMARK 465     LYS V   559                                                      
REMARK 465     ALA V   560                                                      
REMARK 465     ALA V   561                                                      
REMARK 465     GLU V   562                                                      
REMARK 465     GLU V   563                                                      
REMARK 465     SER V   564                                                      
REMARK 465     GLY V   565                                                      
REMARK 465     ASP V   566                                                      
REMARK 465     PHE V   567                                                      
REMARK 465     THR V   568                                                      
REMARK 465     THR V   569                                                      
REMARK 465     ALA V   570                                                      
REMARK 465     ASP V   571                                                      
REMARK 465     SER V   572                                                      
REMARK 465     VAL V   573                                                      
REMARK 465     LYS V   574                                                      
REMARK 465     ASN V   575                                                      
REMARK 465     MET V   576                                                      
REMARK 465     LEU V   577                                                      
REMARK 465     GLN V   578                                                      
REMARK 465     LYS V   579                                                      
REMARK 465     ALA V   580                                                      
REMARK 465     SER V   581                                                      
REMARK 465     PHE V   582                                                      
REMARK 465     SER V   583                                                      
REMARK 465     LYS V   584                                                      
REMARK 465     LYS V   585                                                      
REMARK 465     ILE V   586                                                      
REMARK 465     ASN V   587                                                      
REMARK 465     TYR V   588                                                      
REMARK 465     ASP V   589                                                      
REMARK 465     ALA V   590                                                      
REMARK 465     ILE V   591                                                      
REMARK 465     ASP V   592                                                      
REMARK 465     GLY V   593                                                      
REMARK 465     LEU V   594                                                      
REMARK 465     PHE V   595                                                      
REMARK 465     ARG V   596                                                      
REMARK 465     MET W     1                                                      
REMARK 465     SER W     2                                                      
REMARK 465     SER W     3                                                      
REMARK 465     ILE W     4                                                      
REMARK 465     VAL W     5                                                      
REMARK 465     ASN W     6                                                      
REMARK 465     LYS W     7                                                      
REMARK 465     SER W     8                                                      
REMARK 465     GLY W     9                                                      
REMARK 465     THR W    10                                                      
REMARK 465     ARG W    11                                                      
REMARK 465     PHE W    12                                                      
REMARK 465     ALA W    13                                                      
REMARK 465     PRO W    14                                                      
REMARK 465     LYS W    15                                                      
REMARK 465     VAL W    16                                                      
REMARK 465     ARG W    17                                                      
REMARK 465     GLN W    18                                                      
REMARK 465     ARG W    19                                                      
REMARK 465     ARG W    20                                                      
REMARK 465     ALA W    21                                                      
REMARK 465     ALA W    22                                                      
REMARK 465     THR W    23                                                      
REMARK 465     GLY W    24                                                      
REMARK 465     GLY W    25                                                      
REMARK 465     THR W    26                                                      
REMARK 465     PRO W    27                                                      
REMARK 465     THR W    28                                                      
REMARK 465     PRO W    29                                                      
REMARK 465     LYS W    30                                                      
REMARK 465     PRO W    31                                                      
REMARK 465     ARG W    32                                                      
REMARK 465     THR W    33                                                      
REMARK 465     PRO W    34                                                      
REMARK 465     GLN W    35                                                      
REMARK 465     LEU W    36                                                      
REMARK 465     PHE W    37                                                      
REMARK 465     ILE W    38                                                      
REMARK 465     PRO W    39                                                      
REMARK 465     GLU W    40                                                      
REMARK 465     SER W    41                                                      
REMARK 465     LYS W    42                                                      
REMARK 465     GLU W    43                                                      
REMARK 465     ILE W    44                                                      
REMARK 465     GLU W    45                                                      
REMARK 465     GLU W    46                                                      
REMARK 465     ASP W    47                                                      
REMARK 465     ASN W    48                                                      
REMARK 465     SER W    49                                                      
REMARK 465     ASP W    50                                                      
REMARK 465     ASN W    51                                                      
REMARK 465     ASP W    52                                                      
REMARK 465     LYS W    53                                                      
REMARK 465     GLY W    54                                                      
REMARK 465     VAL W    55                                                      
REMARK 465     ASP W    56                                                      
REMARK 465     GLU W    57                                                      
REMARK 465     ASN W    58                                                      
REMARK 465     GLU W    59                                                      
REMARK 465     THR W    60                                                      
REMARK 465     ALA W    61                                                      
REMARK 465     ILE W    62                                                      
REMARK 465     VAL W    63                                                      
REMARK 465     GLU W    64                                                      
REMARK 465     LYS W    65                                                      
REMARK 465     PRO W    66                                                      
REMARK 465     SER W    67                                                      
REMARK 465     LEU W    68                                                      
REMARK 465     VAL W    69                                                      
REMARK 465     GLY W    70                                                      
REMARK 465     GLU W    71                                                      
REMARK 465     ARG W    72                                                      
REMARK 465     SER W    73                                                      
REMARK 465     LEU W    74                                                      
REMARK 465     GLU W    75                                                      
REMARK 465     GLY W    76                                                      
REMARK 465     PHE W    77                                                      
REMARK 465     THR W    78                                                      
REMARK 465     LEU W    79                                                      
REMARK 465     THR W    80                                                      
REMARK 465     GLY W    81                                                      
REMARK 465     THR W    82                                                      
REMARK 465     ASN W    83                                                      
REMARK 465     GLY W    84                                                      
REMARK 465     HIS W    85                                                      
REMARK 465     ASP W    86                                                      
REMARK 465     ASN W    87                                                      
REMARK 465     GLU W    88                                                      
REMARK 465     ILE W    89                                                      
REMARK 465     GLY W    90                                                      
REMARK 465     ASP W    91                                                      
REMARK 465     GLU W    92                                                      
REMARK 465     GLY W    93                                                      
REMARK 465     PRO W    94                                                      
REMARK 465     ILE W    95                                                      
REMARK 465     ASP W    96                                                      
REMARK 465     ALA W    97                                                      
REMARK 465     SER W    98                                                      
REMARK 465     THR W    99                                                      
REMARK 465     GLN W   100                                                      
REMARK 465     ASN W   101                                                      
REMARK 465     PRO W   102                                                      
REMARK 465     LYS W   103                                                      
REMARK 465     ALA W   104                                                      
REMARK 465     ASP W   105                                                      
REMARK 465     VAL W   106                                                      
REMARK 465     ILE W   107                                                      
REMARK 465     GLU W   108                                                      
REMARK 465     ASP W   109                                                      
REMARK 465     ASN W   110                                                      
REMARK 465     VAL W   111                                                      
REMARK 465     THR W   112                                                      
REMARK 465     LEU W   113                                                      
REMARK 465     LYS W   114                                                      
REMARK 465     PRO W   115                                                      
REMARK 465     ALA W   116                                                      
REMARK 465     PRO W   117                                                      
REMARK 465     LEU W   118                                                      
REMARK 465     GLN W   119                                                      
REMARK 465     THR W   120                                                      
REMARK 465     HIS W   121                                                      
REMARK 465     ARG W   122                                                      
REMARK 465     ASP W   123                                                      
REMARK 465     GLN W   124                                                      
REMARK 465     LYS W   125                                                      
REMARK 465     VAL W   126                                                      
REMARK 465     PRO W   127                                                      
REMARK 465     ARG W   128                                                      
REMARK 465     SER W   129                                                      
REMARK 465     SER W   130                                                      
REMARK 465     ARG W   131                                                      
REMARK 465     LEU W   132                                                      
REMARK 465     ALA W   133                                                      
REMARK 465     SER W   134                                                      
REMARK 465     LEU W   135                                                      
REMARK 465     SER W   136                                                      
REMARK 465     LYS W   137                                                      
REMARK 465     ASP W   138                                                      
REMARK 465     ASN W   139                                                      
REMARK 465     GLU W   140                                                      
REMARK 465     SER W   141                                                      
REMARK 465     ARG W   142                                                      
REMARK 465     PRO W   143                                                      
REMARK 465     SER W   144                                                      
REMARK 465     PHE W   145                                                      
REMARK 465     LYS W   146                                                      
REMARK 465     PRO W   147                                                      
REMARK 465     SER W   148                                                      
REMARK 465     PHE W   149                                                      
REMARK 465     LEU W   150                                                      
REMARK 465     ASP W   151                                                      
REMARK 465     SER W   152                                                      
REMARK 465     SER W   153                                                      
REMARK 465     SER W   154                                                      
REMARK 465     ASN W   155                                                      
REMARK 465     SER W   156                                                      
REMARK 465     ASN W   157                                                      
REMARK 465     GLY W   158                                                      
REMARK 465     THR W   159                                                      
REMARK 465     ALA W   160                                                      
REMARK 465     ARG W   161                                                      
REMARK 465     ARG W   162                                                      
REMARK 465     LEU W   163                                                      
REMARK 465     SER W   164                                                      
REMARK 465     THR W   165                                                      
REMARK 465     ILE W   166                                                      
REMARK 465     SER W   167                                                      
REMARK 465     ASN W   168                                                      
REMARK 465     LYS W   169                                                      
REMARK 465     LEU W   170                                                      
REMARK 465     PRO W   171                                                      
REMARK 465     LYS W   172                                                      
REMARK 465     LYS W   173                                                      
REMARK 465     ILE W   174                                                      
REMARK 465     ARG W   175                                                      
REMARK 465     LEU W   176                                                      
REMARK 465     GLY W   177                                                      
REMARK 465     SER W   178                                                      
REMARK 465     ILE W   179                                                      
REMARK 465     THR W   180                                                      
REMARK 465     GLU W   181                                                      
REMARK 465     ASN W   182                                                      
REMARK 465     ASP W   183                                                      
REMARK 465     MET W   184                                                      
REMARK 465     ASN W   185                                                      
REMARK 465     LEU W   186                                                      
REMARK 465     LYS W   187                                                      
REMARK 465     THR W   188                                                      
REMARK 465     PHE W   189                                                      
REMARK 465     LYS W   190                                                      
REMARK 465     ARG W   191                                                      
REMARK 465     HIS W   192                                                      
REMARK 465     ARG W   193                                                      
REMARK 465     VAL W   194                                                      
REMARK 465     LEU W   195                                                      
REMARK 465     GLY W   196                                                      
REMARK 465     LYS W   197                                                      
REMARK 465     PRO W   198                                                      
REMARK 465     SER W   199                                                      
REMARK 465     SER W   200                                                      
REMARK 465     ALA W   201                                                      
REMARK 465     LYS W   202                                                      
REMARK 465     LYS W   203                                                      
REMARK 465     PRO W   204                                                      
REMARK 465     ALA W   205                                                      
REMARK 465     GLY W   206                                                      
REMARK 465     ALA W   207                                                      
REMARK 465     HIS W   208                                                      
REMARK 465     ARG W   209                                                      
REMARK 465     ILE W   210                                                      
REMARK 465     SER W   211                                                      
REMARK 465     ILE W   212                                                      
REMARK 465     VAL W   213                                                      
REMARK 465     SER W   214                                                      
REMARK 465     LYS W   215                                                      
REMARK 465     ILE W   216                                                      
REMARK 465     SER W   217                                                      
REMARK 465     PRO W   218                                                      
REMARK 465     PRO W   219                                                      
REMARK 465     THR W   220                                                      
REMARK 465     ALA W   221                                                      
REMARK 465     MET W   222                                                      
REMARK 465     THR W   223                                                      
REMARK 465     ASP W   224                                                      
REMARK 465     SER W   225                                                      
REMARK 465     LEU W   226                                                      
REMARK 465     ASP W   227                                                      
REMARK 465     ARG W   228                                                      
REMARK 465     ASN W   229                                                      
REMARK 465     GLU W   230                                                      
REMARK 465     PHE W   231                                                      
REMARK 465     SER W   232                                                      
REMARK 465     SER W   233                                                      
REMARK 465     GLU W   234                                                      
REMARK 465     THR W   235                                                      
REMARK 465     SER W   236                                                      
REMARK 465     THR W   237                                                      
REMARK 465     SER W   238                                                      
REMARK 465     ARG W   239                                                      
REMARK 465     GLU W   240                                                      
REMARK 465     ALA W   241                                                      
REMARK 465     ASP W   242                                                      
REMARK 465     GLU W   243                                                      
REMARK 465     ASN W   244                                                      
REMARK 465     GLU W   245                                                      
REMARK 465     ASN W   246                                                      
REMARK 465     TYR W   247                                                      
REMARK 465     VAL W   248                                                      
REMARK 465     ILE W   249                                                      
REMARK 465     SER W   250                                                      
REMARK 465     LYS W   251                                                      
REMARK 465     VAL W   252                                                      
REMARK 465     LYS W   253                                                      
REMARK 465     ASP W   254                                                      
REMARK 465     ILE W   255                                                      
REMARK 465     PRO W   256                                                      
REMARK 465     LYS W   257                                                      
REMARK 465     LYS W   258                                                      
REMARK 465     VAL W   259                                                      
REMARK 465     ARG W   260                                                      
REMARK 465     ASP W   261                                                      
REMARK 465     GLY W   262                                                      
REMARK 465     GLU W   263                                                      
REMARK 465     SER W   264                                                      
REMARK 465     ALA W   265                                                      
REMARK 465     LYS W   266                                                      
REMARK 465     TYR W   267                                                      
REMARK 465     PHE W   268                                                      
REMARK 465     ILE W   269                                                      
REMARK 465     ASP W   270                                                      
REMARK 465     GLU W   271                                                      
REMARK 465     GLU W   272                                                      
REMARK 465     ASN W   273                                                      
REMARK 465     PHE W   274                                                      
REMARK 465     THR W   275                                                      
REMARK 465     MET W   276                                                      
REMARK 465     ALA W   277                                                      
REMARK 465     GLU W   278                                                      
REMARK 465     LEU W   279                                                      
REMARK 465     GLU W   320                                                      
REMARK 465     PHE W   321                                                      
REMARK 465     LYS W   322                                                      
REMARK 465     PRO W   323                                                      
REMARK 465     LEU W   324                                                      
REMARK 465     HIS W   325                                                      
REMARK 465     SER W   326                                                      
REMARK 465     LEU W   327                                                      
REMARK 465     THR W   328                                                      
REMARK 465     LYS W   329                                                      
REMARK 465     GLU W   330                                                      
REMARK 465     GLU W   331                                                      
REMARK 465     GLN W   332                                                      
REMARK 465     GLU W   333                                                      
REMARK 465     GLU W   334                                                      
REMARK 465     GLU W   335                                                      
REMARK 465     GLU W   336                                                      
REMARK 465     GLU W   337                                                      
REMARK 465     LYS W   338                                                      
REMARK 465     ARG W   339                                                      
REMARK 465     LYS W   340                                                      
REMARK 465     GLU W   341                                                      
REMARK 465     GLU W   342                                                      
REMARK 465     ARG W   343                                                      
REMARK 465     ASP W   344                                                      
REMARK 465     LYS W   345                                                      
REMARK 465     LEU W   346                                                      
REMARK 465     LEU W   347                                                      
REMARK 465     ASN W   348                                                      
REMARK 465     ALA W   349                                                      
REMARK 465     ASP W   350                                                      
REMARK 465     ILE W   351                                                      
REMARK 465     PRO W   352                                                      
REMARK 465     GLU W   353                                                      
REMARK 465     SER W   354                                                      
REMARK 465     ASP W   355                                                      
REMARK 465     ARG W   356                                                      
REMARK 465     LYS W   357                                                      
REMARK 465     ALA W   358                                                      
REMARK 465     HIS W   359                                                      
REMARK 465     THR W   360                                                      
REMARK 465     ALA W   361                                                      
REMARK 465     ILE W   362                                                      
REMARK 465     GLN W   363                                                      
REMARK 465     LEU W   364                                                      
REMARK 465     LYS W   365                                                      
REMARK 465     LEU W   366                                                      
REMARK 465     ASN W   367                                                      
REMARK 465     PRO W   368                                                      
REMARK 465     ASP W   369                                                      
REMARK 465     GLY W   370                                                      
REMARK 465     THR W   371                                                      
REMARK 465     MET W   372                                                      
REMARK 465     ALA W   373                                                      
REMARK 465     ILE W   374                                                      
REMARK 465     ASP W   375                                                      
REMARK 465     GLU W   376                                                      
REMARK 465     GLU W   377                                                      
REMARK 465     THR W   378                                                      
REMARK 465     MET W   379                                                      
REMARK 465     VAL W   380                                                      
REMARK 465     VAL W   381                                                      
REMARK 465     ASP W   382                                                      
REMARK 465     ARG W   383                                                      
REMARK 465     HIS W   384                                                      
REMARK 465     GLU W   517                                                      
REMARK 465     GLU W   518                                                      
REMARK 465     ALA W   519                                                      
REMARK 465     LYS W   520                                                      
REMARK 465     ASN W   521                                                      
REMARK 465     THR W   522                                                      
REMARK 465     ALA W   523                                                      
REMARK 465     LYS W   524                                                      
REMARK 465     GLU W   525                                                      
REMARK 465     GLU W   526                                                      
REMARK 465     ASP W   527                                                      
REMARK 465     GLN W   528                                                      
REMARK 465     THR W   529                                                      
REMARK 465     ALA W   530                                                      
REMARK 465     GLN W   531                                                      
REMARK 465     ARG W   532                                                      
REMARK 465     LEU W   533                                                      
REMARK 465     ASN W   534                                                      
REMARK 465     ASP W   535                                                      
REMARK 465     ALA W   536                                                      
REMARK 465     ASN W   537                                                      
REMARK 465     LEU W   538                                                      
REMARK 465     ASN W   539                                                      
REMARK 465     LYS W   540                                                      
REMARK 465     LYS W   541                                                      
REMARK 465     GLY W   542                                                      
REMARK 465     SER W   543                                                      
REMARK 465     GLY W   544                                                      
REMARK 465     GLY W   545                                                      
REMARK 465     ILE W   546                                                      
REMARK 465     MET W   547                                                      
REMARK 465     THR W   548                                                      
REMARK 465     ASN W   549                                                      
REMARK 465     ASP W   550                                                      
REMARK 465     LEU W   551                                                      
REMARK 465     LYS W   552                                                      
REMARK 465     VAL W   553                                                      
REMARK 465     TYR W   554                                                      
REMARK 465     ARG W   555                                                      
REMARK 465     LYS W   556                                                      
REMARK 465     THR W   557                                                      
REMARK 465     GLU W   558                                                      
REMARK 465     VAL W   559                                                      
REMARK 465     VAL W   560                                                      
REMARK 465     LEU W   561                                                      
REMARK 465     GLY W   562                                                      
REMARK 465     THR W   563                                                      
REMARK 465     ILE W   564                                                      
REMARK 465     ASP W   565                                                      
REMARK 465     ASP W   566                                                      
REMARK 465     LEU W   567                                                      
REMARK 465     LYS W   568                                                      
REMARK 465     ARG W   569                                                      
REMARK 465     LYS W   570                                                      
REMARK 465     LYS W   571                                                      
REMARK 465     LEU W   572                                                      
REMARK 465     LYS W   573                                                      
REMARK 465     GLU W   574                                                      
REMARK 465     ARG W   575                                                      
REMARK 465     ASN W   576                                                      
REMARK 465     ASN W   577                                                      
REMARK 465     ASP W   578                                                      
REMARK 465     ASP W   579                                                      
REMARK 465     ASN W   580                                                      
REMARK 465     GLU W   581                                                      
REMARK 465     ASP W   582                                                      
REMARK 465     ASN W   583                                                      
REMARK 465     GLU W   584                                                      
REMARK 465     GLY W   585                                                      
REMARK 465     SER W   586                                                      
REMARK 465     GLU W   587                                                      
REMARK 465     GLU W   588                                                      
REMARK 465     GLU W   589                                                      
REMARK 465     PRO W   590                                                      
REMARK 465     GLU W   591                                                      
REMARK 465     ILE W   592                                                      
REMARK 465     ASP W   593                                                      
REMARK 465     GLN W   594                                                      
REMARK 465      DC X     1                                                      
REMARK 465      DG X     2                                                      
REMARK 465      DT X     3                                                      
REMARK 465      DC X     4                                                      
REMARK 465      DG X    49                                                      
REMARK 465      DT X    50                                                      
REMARK 465      DG X    51                                                      
REMARK 465      DT X    52                                                      
REMARK 465      DT X    53                                                      
REMARK 465      DC X    54                                                      
REMARK 465      DG X    55                                                      
REMARK 465      DC X    56                                                      
REMARK 465      DG X    57                                                      
REMARK 465      DA X    58                                                      
REMARK 465      DA X    59                                                      
REMARK 465      DG X    60                                                      
REMARK 465      DT X    61                                                      
REMARK 465      DA X    62                                                      
REMARK 465      DA X    63                                                      
REMARK 465      DC X    64                                                      
REMARK 465      DC X    65                                                      
REMARK 465      DC X    66                                                      
REMARK 465      DT X    67                                                      
REMARK 465      DT X    68                                                      
REMARK 465      DC X    69                                                      
REMARK 465      DG X    70                                                      
REMARK 465      DT X    71                                                      
REMARK 465      DG X    72                                                      
REMARK 465      DG X    73                                                      
REMARK 465      DA X    74                                                      
REMARK 465      DC X    75                                                      
REMARK 465      DA X    76                                                      
REMARK 465      DT X    77                                                      
REMARK 465      DT X    78                                                      
REMARK 465      DT X    79                                                      
REMARK 465      DG X    80                                                      
REMARK 465      DG X    81                                                      
REMARK 465      DC Y     1                                                      
REMARK 465      DC Y     2                                                      
REMARK 465      DA Y     3                                                      
REMARK 465      DA Y     4                                                      
REMARK 465      DA Y     5                                                      
REMARK 465      DT Y     6                                                      
REMARK 465      DG Y     7                                                      
REMARK 465      DT Y     8                                                      
REMARK 465      DC Y     9                                                      
REMARK 465      DC Y    10                                                      
REMARK 465      DA Y    11                                                      
REMARK 465      DC Y    12                                                      
REMARK 465      DG Y    13                                                      
REMARK 465      DA Y    14                                                      
REMARK 465      DA Y    15                                                      
REMARK 465      DG Y    16                                                      
REMARK 465      DG Y    17                                                      
REMARK 465      DG Y    18                                                      
REMARK 465      DT Y    19                                                      
REMARK 465      DT Y    20                                                      
REMARK 465      DA Y    21                                                      
REMARK 465      DC Y    22                                                      
REMARK 465      DT Y    23                                                      
REMARK 465      DT Y    24                                                      
REMARK 465      DC Y    25                                                      
REMARK 465      DG Y    26                                                      
REMARK 465      DC Y    27                                                      
REMARK 465      DG Y    28                                                      
REMARK 465      DA Y    29                                                      
REMARK 465      DA Y    30                                                      
REMARK 465      DC Y    31                                                      
REMARK 465      DA Y    32                                                      
REMARK 465      DC Y    33                                                      
REMARK 465      DG Y    78                                                      
REMARK 465      DA Y    79                                                      
REMARK 465      DC Y    80                                                      
REMARK 465      DG Y    81                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   2    N                                                   
REMARK 470     LYS A 216    CG   CD   CE   NZ                                   
REMARK 470     LEU B 320    CG   CD1  CD2                                       
REMARK 470     SER B 585    OG                                                  
REMARK 470     PRO M 202    CG   CD                                             
REMARK 470     ASN M 203    CG   OD1  ND2                                       
REMARK 470     PRO M 204    CG   CD                                             
REMARK 470     ASP O 181    CG   OD1  OD2                                       
REMARK 470     GLU V  40    CG   CD   OE1  OE2                                  
REMARK 470     GLU V 284    CB   CG   CD   OE1  OE2                             
REMARK 470     ALA V 285    CB                                                  
REMARK 470     ARG V 286    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     CYS W 280    SG                                                  
REMARK 470     SER W 475    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS J    46    ZN     ZN J  2000              1.04            
REMARK 500   CB   CYS A   107    ZN     ZN A  1502              1.09            
REMARK 500   SG   CYS A    70    ZN     ZN A  1501              1.24            
REMARK 500   N    CYS V    28    ZN     ZN V  1001              1.30            
REMARK 500   CA   CYS A   107    ZN     ZN A  1502              1.53            
REMARK 500   O    VAL O   352     OG1  THR O   356              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DA Y  46   O4' -  C1' -  N9  ANGL. DEV. =   2.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  47       68.01   -119.39                                   
REMARK 500    ASN A  51      -37.96   -133.95                                   
REMARK 500    ALA A  53     -157.16   -146.92                                   
REMARK 500    CYS A  70      -71.02    -92.50                                   
REMARK 500    HIS A  71      177.53    170.24                                   
REMARK 500    ASN A  73      -62.22    -90.42                                   
REMARK 500    LEU A  74      -38.11   -134.03                                   
REMARK 500    VAL A 186      -61.60   -109.00                                   
REMARK 500    LYS A 188       73.22   -103.82                                   
REMARK 500    ASN A 208       77.31     52.21                                   
REMARK 500    PRO A 224        5.48    -67.16                                   
REMARK 500    LEU A 242       28.16   -140.10                                   
REMARK 500    THR A 247       -7.45     73.67                                   
REMARK 500    ASN A 333       72.92     47.41                                   
REMARK 500    PHE A 364       -6.12     66.28                                   
REMARK 500    ASN A 367      -30.25   -130.90                                   
REMARK 500    ASP A 390       -3.60     86.93                                   
REMARK 500    VAL A 401      -51.52   -122.26                                   
REMARK 500    PRO A 424       49.31    -87.65                                   
REMARK 500    ASN A 455      -75.73    -82.01                                   
REMARK 500    ASN A 509       46.72     32.63                                   
REMARK 500    ASP A 568       37.99    -99.73                                   
REMARK 500    VAL A 632      -66.03    -97.00                                   
REMARK 500    PHE A 633       70.53     54.96                                   
REMARK 500    PRO A 636     -167.64    -72.52                                   
REMARK 500    SER A 638       -7.47     77.01                                   
REMARK 500    LYS A 666       -9.57     75.79                                   
REMARK 500    ASP A 721       -7.78     73.46                                   
REMARK 500    LEU A 744       49.29    -91.98                                   
REMARK 500    GLU A 759       62.33     63.03                                   
REMARK 500    VAL A 823       81.21     55.26                                   
REMARK 500    ASN A 838       46.06     33.52                                   
REMARK 500    LYS A 840       57.09    -94.60                                   
REMARK 500    GLN A 843       -4.54     81.62                                   
REMARK 500    LYS A 845      -63.85    -95.17                                   
REMARK 500    LEU A 893       11.02   -140.68                                   
REMARK 500    PRO A 932       45.40    -86.12                                   
REMARK 500    VAL A 933      -59.51   -128.20                                   
REMARK 500    CYS A 982     -163.50    -79.78                                   
REMARK 500    ALA A1036     -169.75    -77.98                                   
REMARK 500    GLU A1038     -158.59   -137.43                                   
REMARK 500    ASP A1043       78.53     54.58                                   
REMARK 500    LEU A1121       -0.62   -141.30                                   
REMARK 500    THR A1138       71.47     50.76                                   
REMARK 500    LYS A1178      -69.05    -96.49                                   
REMARK 500    ASP A1179      -27.48   -142.44                                   
REMARK 500    ASN A1180       24.24   -142.94                                   
REMARK 500    PRO A1268       47.58    -79.42                                   
REMARK 500    ASP A1269       26.15   -144.33                                   
REMARK 500    ASN A1317     -169.17   -117.50                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     199 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A   44     ASP A   45                  149.81                    
REMARK 500 CYS A   70     HIS A   71                  140.44                    
REMARK 500 PRO A  842     GLN A  843                 -149.84                    
REMARK 500 TYR B 1103     SER B 1104                 -149.90                    
REMARK 500 GLU P  234     LEU P  235                  147.38                    
REMARK 500 PHE W  284     PRO W  285                  145.22                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 107   N                                                      
REMARK 620 2 CYS A 107   O    75.8                                              
REMARK 620 3 CYS A 107   SG  124.6 105.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1095   O                                                      
REMARK 620 2 CYS B1095   SG  107.6                                              
REMARK 620 3 LYS B1097   O   130.0  97.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I2000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS I   5   SG                                                     
REMARK 620 2 CYS I   8   SG   95.3                                              
REMARK 620 3 CYS I  26   SG   82.5 142.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L2000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS L  34   SG                                                     
REMARK 620 2 CYS L  48   SG  171.2                                              
REMARK 620 3 LYS L  49   O    93.6  86.9                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 2000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 2000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 2000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 2000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN V 1001                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-4183   RELATED DB: EMDB                              
REMARK 900 RNA POLYMERASE III CLOSED COMPLEX CC2                                
REMARK 900 RELATED ID: EMD-4180   RELATED DB: EMDB                              
REMARK 900 RNA POLYMERASE III OPEN COMPLEX                                      
REMARK 900 RELATED ID: EMD-4181   RELATED DB: EMDB                              
REMARK 900 RNA POLYMERASE III INITIALLY TRANSCRIBING COMPLEX                    
REMARK 900 RELATED ID: EMD-4182   RELATED DB: EMDB                              
REMARK 900 RNA POLYMERASE III CLOSED COMPLEX CC1                                
REMARK 900 RELATED ID: EMD-4184   RELATED DB: EMDB                              
REMARK 900 RNA POLYMERASE III PRE-INITIATION COMPLEX AT HIGHER RESOLUTION       
REMARK 900 RELATED ID: 6F40   RELATED DB: PDB                                   
REMARK 900 RNA POLYMERASE III OPEN COMPLEX                                      
REMARK 900 RELATED ID: 6F41   RELATED DB: PDB                                   
REMARK 900 RNA POLYMERASE III INITIALLY TRANSCRIBING COMPLEX                    
REMARK 900 RELATED ID: 6F42   RELATED DB: PDB                                   
REMARK 900 RNA POLYMERASE III CLOSED COMPLEX CC1                                
DBREF  6F44 A    1  1460  UNP    P04051   RPC1_YEAST       1   1460             
DBREF  6F44 B    1  1149  UNP    P22276   RPC2_YEAST       1   1149             
DBREF  6F44 C    1   335  UNP    P07703   RPAC1_YEAST      1    335             
DBREF  6F44 D    1   161  UNP    P47076   RPC9_YEAST       1    161             
DBREF  6F44 E    1   215  UNP    P20434   RPAB1_YEAST      1    215             
DBREF  6F44 F    1   155  UNP    P20435   RPAB2_YEAST      1    155             
DBREF  6F44 G    1   212  UNP    P35718   RPC8_YEAST       1    212             
DBREF  6F44 H    1   146  UNP    P20436   RPAB3_YEAST      1    146             
DBREF  6F44 I    1   110  UNP    Q04307   RPC10_YEAST      1    110             
DBREF  6F44 J    1    70  UNP    P22139   RPAB5_YEAST      1     70             
DBREF  6F44 K    1   142  UNP    P28000   RPAC2_YEAST      1    142             
DBREF  6F44 L    1    70  UNP    P40422   RPAB4_YEAST      1     70             
DBREF  6F44 M    1   282  UNP    P36121   RPC5_YEAST       1    282             
DBREF  6F44 N    1   422  UNP    P25441   RPC4_YEAST       1    422             
DBREF  6F44 O    1   654  UNP    P32349   RPC3_YEAST       1    654             
DBREF  6F44 P    1   317  UNP    P32910   RPC6_YEAST       1    317             
DBREF  6F44 Q    1   251  UNP    P17890   RPC7_YEAST       1    251             
DBREF  6F44 U    1   240  UNP    P13393   TBP_YEAST        1    240             
DBREF  6F44 V    1   596  UNP    P29056   TF3B_YEAST       1    596             
DBREF  6F44 W    1   594  UNP    P46678   TFC5_YEAST       1    594             
DBREF  6F44 X    1    81  PDB    6F44     6F44             1     81             
DBREF  6F44 Y    1    81  PDB    6F44     6F44             1     81             
SEQADV 6F44 PRO M  201  UNP  P36121    ASN   201 CONFLICT                       
SEQRES   1 A 1460  MET LYS GLU VAL VAL VAL SER GLU THR PRO LYS ARG ILE          
SEQRES   2 A 1460  LYS GLY LEU GLU PHE SER ALA LEU SER ALA ALA ASP ILE          
SEQRES   3 A 1460  VAL ALA GLN SER GLU VAL GLU VAL SER THR ARG ASP LEU          
SEQRES   4 A 1460  PHE ASP LEU GLU LYS ASP ARG ALA PRO LYS ALA ASN GLY          
SEQRES   5 A 1460  ALA LEU ASP PRO LYS MET GLY VAL SER SER SER SER LEU          
SEQRES   6 A 1460  GLU CYS ALA THR CYS HIS GLY ASN LEU ALA SER CYS HIS          
SEQRES   7 A 1460  GLY HIS PHE GLY HIS LEU LYS LEU ALA LEU PRO VAL PHE          
SEQRES   8 A 1460  HIS ILE GLY TYR PHE LYS ALA THR ILE GLN ILE LEU GLN          
SEQRES   9 A 1460  GLY ILE CYS LYS ASN CYS SER ALA ILE LEU LEU SER GLU          
SEQRES  10 A 1460  THR ASP LYS ARG GLN PHE LEU HIS GLU LEU ARG ARG PRO          
SEQRES  11 A 1460  GLY VAL ASP ASN LEU ARG ARG MET GLY ILE LEU LYS LYS          
SEQRES  12 A 1460  ILE LEU ASP GLN CYS LYS LYS GLN ARG ARG CYS LEU HIS          
SEQRES  13 A 1460  CYS GLY ALA LEU ASN GLY VAL VAL LYS LYS ALA ALA ALA          
SEQRES  14 A 1460  GLY ALA GLY SER ALA ALA LEU LYS ILE ILE HIS ASP THR          
SEQRES  15 A 1460  PHE ARG TRP VAL GLY LYS LYS SER ALA PRO GLU LYS ASP          
SEQRES  16 A 1460  ILE TRP VAL GLY GLU TRP LYS GLU VAL LEU ALA HIS ASN          
SEQRES  17 A 1460  PRO GLU LEU GLU ARG TYR VAL LYS ARG CYS MET ASP ASP          
SEQRES  18 A 1460  LEU ASN PRO LEU LYS THR LEU ASN LEU PHE LYS GLN ILE          
SEQRES  19 A 1460  LYS SER ALA ASP CYS GLU LEU LEU GLY ILE ASP ALA THR          
SEQRES  20 A 1460  VAL PRO SER GLY ARG PRO GLU THR TYR ILE TRP ARG TYR          
SEQRES  21 A 1460  LEU PRO ALA PRO PRO VAL CYS ILE ARG PRO SER VAL MET          
SEQRES  22 A 1460  MET GLN ASP SER PRO ALA SER ASN GLU ASP ASP LEU THR          
SEQRES  23 A 1460  VAL LYS LEU THR GLU ILE VAL TRP THR SER SER LEU ILE          
SEQRES  24 A 1460  LYS ALA GLY LEU ASP LYS GLY ILE SER ILE ASN ASN MET          
SEQRES  25 A 1460  MET GLU HIS TRP ASP TYR LEU GLN LEU THR VAL ALA MET          
SEQRES  26 A 1460  TYR ILE ASN SER ASP SER VAL ASN PRO ALA MET LEU PRO          
SEQRES  27 A 1460  GLY SER SER ASN GLY GLY GLY LYS VAL LYS PRO ILE ARG          
SEQRES  28 A 1460  GLY PHE CYS GLN ARG LEU LYS GLY LYS GLN GLY ARG PHE          
SEQRES  29 A 1460  ARG GLY ASN LEU SER GLY LYS ARG VAL ASP PHE SER GLY          
SEQRES  30 A 1460  ARG THR VAL ILE SER PRO ASP PRO ASN LEU SER ILE ASP          
SEQRES  31 A 1460  GLU VAL ALA VAL PRO ASP ARG VAL ALA LYS VAL LEU THR          
SEQRES  32 A 1460  TYR PRO GLU LYS VAL THR ARG TYR ASN ARG HIS LYS LEU          
SEQRES  33 A 1460  GLN GLU LEU ILE VAL ASN GLY PRO ASN VAL HIS PRO GLY          
SEQRES  34 A 1460  ALA ASN TYR LEU LEU LYS ARG ASN GLU ASP ALA ARG ARG          
SEQRES  35 A 1460  ASN LEU ARG TYR GLY ASP ARG MET LYS LEU ALA LYS ASN          
SEQRES  36 A 1460  LEU GLN ILE GLY ASP VAL VAL GLU ARG HIS LEU GLU ASP          
SEQRES  37 A 1460  GLY ASP VAL VAL LEU PHE ASN ARG GLN PRO SER LEU HIS          
SEQRES  38 A 1460  ARG LEU SER ILE LEU SER HIS TYR ALA LYS ILE ARG PRO          
SEQRES  39 A 1460  TRP ARG THR PHE ARG LEU ASN GLU CYS VAL CYS THR PRO          
SEQRES  40 A 1460  TYR ASN ALA ASP PHE ASP GLY ASP GLU MET ASN LEU HIS          
SEQRES  41 A 1460  VAL PRO GLN THR GLU GLU ALA ARG ALA GLU ALA ILE ASN          
SEQRES  42 A 1460  LEU MET GLY VAL LYS ASN ASN LEU LEU THR PRO LYS SER          
SEQRES  43 A 1460  GLY GLU PRO ILE ILE ALA ALA THR GLN ASP PHE ILE THR          
SEQRES  44 A 1460  GLY SER TYR LEU ILE SER HIS LYS ASP SER PHE TYR ASP          
SEQRES  45 A 1460  ARG ALA THR LEU THR GLN LEU LEU SER MET MET SER ASP          
SEQRES  46 A 1460  GLY ILE GLU HIS PHE ASP ILE PRO PRO PRO ALA ILE MET          
SEQRES  47 A 1460  LYS PRO TYR TYR LEU TRP THR GLY LYS GLN VAL PHE SER          
SEQRES  48 A 1460  LEU LEU ILE LYS PRO ASN HIS ASN SER PRO VAL VAL ILE          
SEQRES  49 A 1460  ASN LEU ASP ALA LYS ASN LYS VAL PHE VAL PRO PRO LYS          
SEQRES  50 A 1460  SER LYS SER LEU PRO ASN GLU MET SER GLN ASN ASP GLY          
SEQRES  51 A 1460  PHE VAL ILE ILE ARG GLY SER GLN ILE LEU SER GLY VAL          
SEQRES  52 A 1460  MET ASP LYS SER VAL LEU GLY ASP GLY LYS LYS HIS SER          
SEQRES  53 A 1460  VAL PHE TYR THR ILE LEU ARG ASP TYR GLY PRO GLN GLU          
SEQRES  54 A 1460  ALA ALA ASN ALA MET ASN ARG MET ALA LYS LEU CYS ALA          
SEQRES  55 A 1460  ARG PHE LEU GLY ASN ARG GLY PHE SER ILE GLY ILE ASN          
SEQRES  56 A 1460  ASP VAL THR PRO ALA ASP ASP LEU LYS GLN LYS LYS GLU          
SEQRES  57 A 1460  GLU LEU VAL GLU ILE ALA TYR HIS LYS CYS ASP GLU LEU          
SEQRES  58 A 1460  ILE THR LEU PHE ASN LYS GLY GLU LEU GLU THR GLN PRO          
SEQRES  59 A 1460  GLY CYS ASN GLU GLU GLN THR LEU GLU ALA LYS ILE GLY          
SEQRES  60 A 1460  GLY LEU LEU SER LYS VAL ARG GLU GLU VAL GLY ASP VAL          
SEQRES  61 A 1460  CYS ILE ASN GLU LEU ASP ASN TRP ASN ALA PRO LEU ILE          
SEQRES  62 A 1460  MET ALA THR CYS GLY SER LYS GLY SER THR LEU ASN VAL          
SEQRES  63 A 1460  SER GLN MET VAL ALA VAL VAL GLY GLN GLN ILE ILE SER          
SEQRES  64 A 1460  GLY ASN ARG VAL PRO ASP GLY PHE GLN ASP ARG SER LEU          
SEQRES  65 A 1460  PRO HIS PHE PRO LYS ASN SER LYS THR PRO GLN SER LYS          
SEQRES  66 A 1460  GLY PHE VAL ARG ASN SER PHE PHE SER GLY LEU SER PRO          
SEQRES  67 A 1460  PRO GLU PHE LEU PHE HIS ALA ILE SER GLY ARG GLU GLY          
SEQRES  68 A 1460  LEU VAL ASP THR ALA VAL LYS THR ALA GLU THR GLY TYR          
SEQRES  69 A 1460  MET SER ARG ARG LEU MET LYS SER LEU GLU ASP LEU SER          
SEQRES  70 A 1460  CYS GLN TYR ASP ASN THR VAL ARG THR SER ALA ASN GLY          
SEQRES  71 A 1460  ILE VAL GLN PHE THR TYR GLY GLY ASP GLY LEU ASP PRO          
SEQRES  72 A 1460  LEU GLU MET GLU GLY ASN ALA GLN PRO VAL ASN PHE ASN          
SEQRES  73 A 1460  ARG SER TRP ASP HIS ALA TYR ASN ILE THR PHE ASN ASN          
SEQRES  74 A 1460  GLN ASP LYS GLY LEU LEU PRO TYR ALA ILE MET GLU THR          
SEQRES  75 A 1460  ALA ASN GLU ILE LEU GLY PRO LEU GLU GLU ARG LEU VAL          
SEQRES  76 A 1460  ARG TYR ASP ASN SER GLY CYS LEU VAL LYS ARG GLU ASP          
SEQRES  77 A 1460  LEU ASN LYS ALA GLU TYR VAL ASP GLN TYR ASP ALA GLU          
SEQRES  78 A 1460  ARG ASP PHE TYR HIS SER LEU ARG GLU TYR ILE ASN GLY          
SEQRES  79 A 1460  LYS ALA THR ALA LEU ALA ASN LEU ARG LYS SER ARG GLY          
SEQRES  80 A 1460  MET LEU GLY LEU LEU GLU PRO PRO ALA LYS GLU LEU GLN          
SEQRES  81 A 1460  GLY ILE ASP PRO ASP GLU THR VAL PRO ASP ASN VAL LYS          
SEQRES  82 A 1460  THR SER VAL SER GLN LEU TYR ARG ILE SER GLU LYS SER          
SEQRES  83 A 1460  VAL ARG LYS PHE LEU GLU ILE ALA LEU PHE LYS TYR ARG          
SEQRES  84 A 1460  LYS ALA ARG LEU GLU PRO GLY THR ALA ILE GLY ALA ILE          
SEQRES  85 A 1460  GLY ALA GLN SER ILE GLY GLU PRO GLY THR GLN MET THR          
SEQRES  86 A 1460  LEU LYS THR PHE HIS PHE ALA GLY VAL ALA SER MET ASN          
SEQRES  87 A 1460  VAL THR LEU GLY VAL PRO ARG ILE LYS GLU ILE ILE ASN          
SEQRES  88 A 1460  ALA SER LYS VAL ILE SER THR PRO ILE ILE ASN ALA VAL          
SEQRES  89 A 1460  LEU VAL ASN ASP ASN ASP GLU ARG ALA ALA ARG VAL VAL          
SEQRES  90 A 1460  LYS GLY ARG VAL GLU LYS THR LEU LEU SER ASP VAL ALA          
SEQRES  91 A 1460  PHE TYR VAL GLN ASP VAL TYR LYS ASP ASN LEU SER PHE          
SEQRES  92 A 1460  ILE GLN VAL ARG ILE ASP LEU GLY THR ILE ASP LYS LEU          
SEQRES  93 A 1460  GLN LEU GLU LEU THR ILE GLU ASP ILE ALA VAL ALA ILE          
SEQRES  94 A 1460  THR ARG ALA SER LYS LEU LYS ILE GLN ALA SER ASP VAL          
SEQRES  95 A 1460  ASN ILE ILE GLY LYS ASP ARG ILE ALA ILE ASN VAL PHE          
SEQRES  96 A 1460  PRO GLU GLY TYR LYS ALA LYS SER ILE SER THR SER ALA          
SEQRES  97 A 1460  LYS GLU PRO SER GLU ASN ASP VAL PHE TYR ARG MET GLN          
SEQRES  98 A 1460  GLN LEU ARG ARG ALA LEU PRO ASP VAL VAL VAL LYS GLY          
SEQRES  99 A 1460  LEU PRO ASP ILE SER ARG ALA VAL ILE ASN ILE ARG ASP          
SEQRES 100 A 1460  ASP GLY LYS ARG GLU LEU LEU VAL GLU GLY TYR GLY LEU          
SEQRES 101 A 1460  ARG ASP VAL MET CYS THR ASP GLY VAL ILE GLY SER ARG          
SEQRES 102 A 1460  THR THR THR ASN HIS VAL LEU GLU VAL PHE SER VAL LEU          
SEQRES 103 A 1460  GLY ILE GLU ALA ALA ARG TYR SER ILE ILE ARG GLU ILE          
SEQRES 104 A 1460  ASN TYR THR MET SER ASN HIS GLY MET SER VAL ASP PRO          
SEQRES 105 A 1460  ARG HIS ILE GLN LEU LEU GLY ASP VAL MET THR TYR LYS          
SEQRES 106 A 1460  GLY GLU VAL LEU GLY ILE THR ARG PHE GLY LEU SER LYS          
SEQRES 107 A 1460  MET ARG ASP SER VAL LEU GLN LEU ALA SER PHE GLU LYS          
SEQRES 108 A 1460  THR THR ASP HIS LEU PHE ASP ALA ALA PHE TYR MET LYS          
SEQRES 109 A 1460  LYS ASP ALA VAL GLU GLY VAL SER GLU CYS ILE ILE LEU          
SEQRES 110 A 1460  GLY GLN THR MET SER ILE GLY THR GLY SER PHE LYS VAL          
SEQRES 111 A 1460  VAL LYS GLY THR ASN ILE SER GLU LYS ASP LEU VAL PRO          
SEQRES 112 A 1460  LYS ARG CYS LEU PHE GLU SER LEU SER ASN GLU ALA ALA          
SEQRES 113 A 1460  LEU LYS ALA ASN                                              
SEQRES   1 B 1149  MET VAL ALA ALA THR LYS ARG ARG LYS THR HIS ILE HIS          
SEQRES   2 B 1149  LYS HIS VAL LYS ASP GLU ALA PHE ASP ASP LEU LEU LYS          
SEQRES   3 B 1149  PRO VAL TYR LYS GLY LYS LYS LEU THR ASP GLU ILE ASN          
SEQRES   4 B 1149  THR ALA GLN ASP LYS TRP HIS LEU LEU PRO ALA PHE LEU          
SEQRES   5 B 1149  LYS VAL LYS GLY LEU VAL LYS GLN HIS LEU ASP SER PHE          
SEQRES   6 B 1149  ASN TYR PHE VAL ASP THR ASP LEU LYS LYS ILE ILE LYS          
SEQRES   7 B 1149  ALA ASN GLN LEU ILE LEU SER ASP VAL ASP PRO GLU PHE          
SEQRES   8 B 1149  TYR LEU LYS TYR VAL ASP ILE ARG VAL GLY LYS LYS SER          
SEQRES   9 B 1149  SER SER SER THR LYS ASP TYR LEU THR PRO PRO HIS GLU          
SEQRES  10 B 1149  CYS ARG LEU ARG ASP MET THR TYR SER ALA PRO ILE TYR          
SEQRES  11 B 1149  VAL ASP ILE GLU TYR THR ARG GLY ARG ASN ILE ILE MET          
SEQRES  12 B 1149  HIS LYS ASP VAL GLU ILE GLY ARG MET PRO ILE MET LEU          
SEQRES  13 B 1149  ARG SER ASN LYS CYS ILE LEU TYR ASP ALA ASP GLU SER          
SEQRES  14 B 1149  LYS MET ALA LYS LEU ASN GLU CYS PRO LEU ASP PRO GLY          
SEQRES  15 B 1149  GLY TYR PHE ILE VAL ASN GLY THR GLU LYS VAL ILE LEU          
SEQRES  16 B 1149  VAL GLN GLU GLN LEU SER LYS ASN ARG ILE ILE VAL GLU          
SEQRES  17 B 1149  ALA ASP GLU LYS LYS GLY ILE VAL GLN ALA SER VAL THR          
SEQRES  18 B 1149  SER SER THR HIS GLU ARG LYS SER LYS THR TYR VAL ILE          
SEQRES  19 B 1149  THR LYS ASN GLY LYS ILE TYR LEU LYS HIS ASN SER ILE          
SEQRES  20 B 1149  ALA GLU GLU ILE PRO ILE ALA ILE VAL LEU LYS ALA CYS          
SEQRES  21 B 1149  GLY ILE LEU SER ASP LEU GLU ILE MET GLN LEU VAL CYS          
SEQRES  22 B 1149  GLY ASN ASP SER SER TYR GLN ASP ILE PHE ALA VAL ASN          
SEQRES  23 B 1149  LEU GLU GLU SER SER LYS LEU ASP ILE TYR THR GLN GLN          
SEQRES  24 B 1149  GLN ALA LEU GLU TYR ILE GLY ALA LYS VAL LYS THR MET          
SEQRES  25 B 1149  ARG ARG GLN LYS LEU THR ILE LEU GLN GLU GLY ILE GLU          
SEQRES  26 B 1149  ALA ILE ALA THR THR VAL ILE ALA HIS LEU THR VAL GLU          
SEQRES  27 B 1149  ALA LEU ASP PHE ARG GLU LYS ALA LEU TYR ILE ALA MET          
SEQRES  28 B 1149  MET THR ARG ARG VAL VAL MET ALA MET TYR ASN PRO LYS          
SEQRES  29 B 1149  MET ILE ASP ASP ARG ASP TYR VAL GLY ASN LYS ARG LEU          
SEQRES  30 B 1149  GLU LEU ALA GLY GLN LEU ILE SER LEU LEU PHE GLU ASP          
SEQRES  31 B 1149  LEU PHE LYS LYS PHE ASN ASN ASP PHE LYS LEU SER ILE          
SEQRES  32 B 1149  ASP LYS VAL LEU LYS LYS PRO ASN ARG ALA MET GLU TYR          
SEQRES  33 B 1149  ASP ALA LEU LEU SER ILE ASN VAL HIS SER ASN ASN ILE          
SEQRES  34 B 1149  THR SER GLY LEU ASN ARG ALA ILE SER THR GLY ASN TRP          
SEQRES  35 B 1149  SER LEU LYS ARG PHE LYS MET GLU ARG ALA GLY VAL THR          
SEQRES  36 B 1149  HIS VAL LEU SER ARG LEU SER TYR ILE SER ALA LEU GLY          
SEQRES  37 B 1149  MET MET THR ARG ILE SER SER GLN PHE GLU LYS SER ARG          
SEQRES  38 B 1149  LYS VAL SER GLY PRO ARG ALA LEU GLN PRO SER GLN PHE          
SEQRES  39 B 1149  GLY MET LEU CYS THR ALA ASP THR PRO GLU GLY GLU ALA          
SEQRES  40 B 1149  CYS GLY LEU VAL LYS ASN LEU ALA LEU MET THR HIS ILE          
SEQRES  41 B 1149  THR THR ASP ASP GLU GLU GLU PRO ILE LYS LYS LEU CYS          
SEQRES  42 B 1149  TYR VAL LEU GLY VAL GLU ASP ILE THR LEU ILE ASP SER          
SEQRES  43 B 1149  ALA SER LEU HIS LEU ASN TYR GLY VAL TYR LEU ASN GLY          
SEQRES  44 B 1149  THR LEU ILE GLY SER ILE ARG PHE PRO THR LYS PHE VAL          
SEQRES  45 B 1149  THR GLN PHE ARG HIS LEU ARG ARG THR GLY LYS VAL SER          
SEQRES  46 B 1149  GLU PHE ILE SER ILE TYR SER ASN SER HIS GLN MET ALA          
SEQRES  47 B 1149  VAL HIS ILE ALA THR ASP GLY GLY ARG ILE CYS ARG PRO          
SEQRES  48 B 1149  LEU ILE ILE VAL SER ASP GLY GLN SER ARG VAL LYS ASP          
SEQRES  49 B 1149  ILE HIS LEU ARG LYS LEU LEU ASP GLY GLU LEU ASP PHE          
SEQRES  50 B 1149  ASP ASP PHE LEU LYS LEU GLY LEU VAL GLU TYR LEU ASP          
SEQRES  51 B 1149  VAL ASN GLU GLU ASN ASP SER TYR ILE ALA LEU TYR GLU          
SEQRES  52 B 1149  LYS ASP ILE VAL PRO SER MET THR HIS LEU GLU ILE GLU          
SEQRES  53 B 1149  PRO PHE THR ILE LEU GLY ALA VAL ALA GLY LEU ILE PRO          
SEQRES  54 B 1149  TYR PRO HIS HIS ASN GLN SER PRO ARG ASN THR TYR GLN          
SEQRES  55 B 1149  CYS ALA MET GLY LYS GLN ALA ILE GLY ALA ILE ALA TYR          
SEQRES  56 B 1149  ASN GLN PHE LYS ARG ILE ASP THR LEU LEU TYR LEU MET          
SEQRES  57 B 1149  THR TYR PRO GLN GLN PRO MET VAL LYS THR LYS THR ILE          
SEQRES  58 B 1149  GLU LEU ILE ASP TYR ASP LYS LEU PRO ALA GLY GLN ASN          
SEQRES  59 B 1149  ALA THR VAL ALA VAL MET SER TYR SER GLY TYR ASP ILE          
SEQRES  60 B 1149  GLU ASP ALA LEU VAL LEU ASN LYS SER SER ILE ASP ARG          
SEQRES  61 B 1149  GLY PHE GLY ARG CYS GLU THR ARG ARG LYS THR THR THR          
SEQRES  62 B 1149  VAL LEU LYS ARG TYR ALA ASN HIS THR GLN ASP ILE ILE          
SEQRES  63 B 1149  GLY GLY MET ARG VAL ASP GLU ASN GLY ASP PRO ILE TRP          
SEQRES  64 B 1149  GLN HIS GLN SER LEU GLY PRO ASP GLY LEU GLY GLU VAL          
SEQRES  65 B 1149  GLY MET LYS VAL GLN SER GLY GLN ILE TYR ILE ASN LYS          
SEQRES  66 B 1149  SER VAL PRO THR ASN SER ALA ASP ALA PRO ASN PRO ASN          
SEQRES  67 B 1149  ASN VAL ASN VAL GLN THR GLN TYR ARG GLU ALA PRO VAL          
SEQRES  68 B 1149  ILE TYR ARG GLY PRO GLU PRO SER HIS ILE ASP GLN VAL          
SEQRES  69 B 1149  MET MET SER VAL SER ASP ASN ASP GLN ALA LEU ILE LYS          
SEQRES  70 B 1149  VAL LEU LEU ARG GLN ASN ARG ARG PRO GLU LEU GLY ASP          
SEQRES  71 B 1149  LYS PHE SER SER ARG HIS GLY GLN LYS GLY VAL CYS GLY          
SEQRES  72 B 1149  ILE ILE VAL LYS GLN GLU ASP MET PRO PHE ASN ASP GLN          
SEQRES  73 B 1149  GLY ILE VAL PRO ASP ILE ILE MET ASN PRO HIS GLY PHE          
SEQRES  74 B 1149  PRO SER ARG MET THR VAL GLY LYS MET ILE GLU LEU ILE          
SEQRES  75 B 1149  SER GLY LYS ALA GLY VAL LEU ASN GLY THR LEU GLU TYR          
SEQRES  76 B 1149  GLY THR CYS PHE GLY GLY SER LYS LEU GLU ASP MET SER          
SEQRES  77 B 1149  LYS ILE LEU VAL ASP GLN GLY PHE ASN TYR SER GLY LYS          
SEQRES  78 B 1149  ASP MET LEU TYR SER GLY ILE THR GLY GLU CYS LEU GLN          
SEQRES  79 B 1149  ALA TYR ILE PHE PHE GLY PRO ILE TYR TYR GLN LYS LEU          
SEQRES  80 B 1149  LYS HIS MET VAL LEU ASP LYS MET HIS ALA ARG ALA ARG          
SEQRES  81 B 1149  GLY PRO ARG ALA VAL LEU THR ARG GLN PRO THR GLU GLY          
SEQRES  82 B 1149  ARG SER ARG ASP GLY GLY LEU ARG LEU GLY GLU MET GLU          
SEQRES  83 B 1149  ARG ASP CYS VAL ILE ALA TYR GLY ALA SER GLN LEU LEU          
SEQRES  84 B 1149  LEU GLU ARG LEU MET ILE SER SER ASP ALA PHE GLU VAL          
SEQRES  85 B 1149  ASP VAL CYS ASP LYS CYS GLY LEU MET GLY TYR SER GLY          
SEQRES  86 B 1149  TRP CYS THR THR CYS LYS SER ALA GLU ASN ILE ILE LYS          
SEQRES  87 B 1149  MET THR ILE PRO TYR ALA ALA LYS LEU LEU PHE GLN GLU          
SEQRES  88 B 1149  LEU LEU SER MET ASN ILE ALA PRO ARG LEU ARG LEU GLU          
SEQRES  89 B 1149  ASP ILE PHE GLN GLN                                          
SEQRES   1 C  335  MET SER ASN ILE VAL GLY ILE GLU TYR ASN ARG VAL THR          
SEQRES   2 C  335  ASN THR THR SER THR ASP PHE PRO GLY PHE SER LYS ASP          
SEQRES   3 C  335  ALA GLU ASN GLU TRP ASN VAL GLU LYS PHE LYS LYS ASP          
SEQRES   4 C  335  PHE GLU VAL ASN ILE SER SER LEU ASP ALA ARG GLU ALA          
SEQRES   5 C  335  ASN PHE ASP LEU ILE ASN ILE ASP THR SER ILE ALA ASN          
SEQRES   6 C  335  ALA PHE ARG ARG ILE MET ILE SER GLU VAL PRO SER VAL          
SEQRES   7 C  335  ALA ALA GLU TYR VAL TYR PHE PHE ASN ASN THR SER VAL          
SEQRES   8 C  335  ILE GLN ASP GLU VAL LEU ALA HIS ARG ILE GLY LEU VAL          
SEQRES   9 C  335  PRO LEU LYS VAL ASP PRO ASP MET LEU THR TRP VAL ASP          
SEQRES  10 C  335  SER ASN LEU PRO ASP ASP GLU LYS PHE THR ASP GLU ASN          
SEQRES  11 C  335  THR ILE VAL LEU SER LEU ASN VAL LYS CYS THR ARG ASN          
SEQRES  12 C  335  PRO ASP ALA PRO LYS GLY SER THR ASP PRO LYS GLU LEU          
SEQRES  13 C  335  TYR ASN ASN ALA HIS VAL TYR ALA ARG ASP LEU LYS PHE          
SEQRES  14 C  335  GLU PRO GLN GLY ARG GLN SER THR THR PHE ALA ASP CYS          
SEQRES  15 C  335  PRO VAL VAL PRO ALA ASP PRO ASP ILE LEU LEU ALA LYS          
SEQRES  16 C  335  LEU ARG PRO GLY GLN GLU ILE SER LEU LYS ALA HIS CYS          
SEQRES  17 C  335  ILE LEU GLY ILE GLY GLY ASP HIS ALA LYS PHE SER PRO          
SEQRES  18 C  335  VAL SER THR ALA SER TYR ARG LEU LEU PRO GLN ILE ASN          
SEQRES  19 C  335  ILE LEU GLN PRO ILE LYS GLY GLU SER ALA ARG ARG PHE          
SEQRES  20 C  335  GLN LYS CYS PHE PRO PRO GLY VAL ILE GLY ILE ASP GLU          
SEQRES  21 C  335  GLY SER ASP GLU ALA TYR VAL LYS ASP ALA ARG LYS ASP          
SEQRES  22 C  335  THR VAL SER ARG GLU VAL LEU ARG TYR GLU GLU PHE ALA          
SEQRES  23 C  335  ASP LYS VAL LYS LEU GLY ARG VAL ARG ASN HIS PHE ILE          
SEQRES  24 C  335  PHE ASN VAL GLU SER ALA GLY ALA MET THR PRO GLU GLU          
SEQRES  25 C  335  ILE PHE PHE LYS SER VAL ARG ILE LEU LYS ASN LYS ALA          
SEQRES  26 C  335  GLU TYR LEU LYS ASN CYS PRO ILE THR GLN                      
SEQRES   1 D  161  MET LYS VAL LEU GLU GLU ARG ASN ALA PHE LEU SER ASP          
SEQRES   2 D  161  TYR GLU VAL LEU LYS PHE LEU THR ASP LEU GLU LYS LYS          
SEQRES   3 D  161  HIS LEU TRP ASP GLN LYS SER LEU ALA ALA LEU LYS LYS          
SEQRES   4 D  161  SER ARG SER LYS GLY LYS GLN ASN ARG PRO TYR ASN HIS          
SEQRES   5 D  161  PRO GLU LEU GLN GLY ILE THR ARG ASN VAL VAL ASN TYR          
SEQRES   6 D  161  LEU SER ILE ASN LYS ASN PHE ILE ASN GLN GLU ASP GLU          
SEQRES   7 D  161  GLY GLU GLU ARG GLU SER SER GLY ALA LYS ASP ALA GLU          
SEQRES   8 D  161  LYS SER GLY ILE SER LYS MET SER ASP GLU SER PHE ALA          
SEQRES   9 D  161  GLU LEU MET THR LYS LEU ASN SER PHE LYS LEU PHE LYS          
SEQRES  10 D  161  ALA GLU LYS LEU GLN ILE VAL ASN GLN LEU PRO ALA ASN          
SEQRES  11 D  161  MET VAL HIS LEU TYR SER ILE VAL GLU GLU CYS ASP ALA          
SEQRES  12 D  161  ARG PHE ASP GLU LYS THR ILE GLU GLU MET LEU GLU ILE          
SEQRES  13 D  161  ILE SER GLY TYR ALA                                          
SEQRES   1 E  215  MET ASP GLN GLU ASN GLU ARG ASN ILE SER ARG LEU TRP          
SEQRES   2 E  215  ARG ALA PHE ARG THR VAL LYS GLU MET VAL LYS ASP ARG          
SEQRES   3 E  215  GLY TYR PHE ILE THR GLN GLU GLU VAL GLU LEU PRO LEU          
SEQRES   4 E  215  GLU ASP PHE LYS ALA LYS TYR CYS ASP SER MET GLY ARG          
SEQRES   5 E  215  PRO GLN ARG LYS MET MET SER PHE GLN ALA ASN PRO THR          
SEQRES   6 E  215  GLU GLU SER ILE SER LYS PHE PRO ASP MET GLY SER LEU          
SEQRES   7 E  215  TRP VAL GLU PHE CYS ASP GLU PRO SER VAL GLY VAL LYS          
SEQRES   8 E  215  THR MET LYS THR PHE VAL ILE HIS ILE GLN GLU LYS ASN          
SEQRES   9 E  215  PHE GLN THR GLY ILE PHE VAL TYR GLN ASN ASN ILE THR          
SEQRES  10 E  215  PRO SER ALA MET LYS LEU VAL PRO SER ILE PRO PRO ALA          
SEQRES  11 E  215  THR ILE GLU THR PHE ASN GLU ALA ALA LEU VAL VAL ASN          
SEQRES  12 E  215  ILE THR HIS HIS GLU LEU VAL PRO LYS HIS ILE ARG LEU          
SEQRES  13 E  215  SER SER ASP GLU LYS ARG GLU LEU LEU LYS ARG TYR ARG          
SEQRES  14 E  215  LEU LYS GLU SER GLN LEU PRO ARG ILE GLN ARG ALA ASP          
SEQRES  15 E  215  PRO VAL ALA LEU TYR LEU GLY LEU LYS ARG GLY GLU VAL          
SEQRES  16 E  215  VAL LYS ILE ILE ARG LYS SER GLU THR SER GLY ARG TYR          
SEQRES  17 E  215  ALA SER TYR ARG ILE CYS MET                                  
SEQRES   1 F  155  MET SER ASP TYR GLU GLU ALA PHE ASN ASP GLY ASN GLU          
SEQRES   2 F  155  ASN PHE GLU ASP PHE ASP VAL GLU HIS PHE SER ASP GLU          
SEQRES   3 F  155  GLU THR TYR GLU GLU LYS PRO GLN PHE LYS ASP GLY GLU          
SEQRES   4 F  155  THR THR ASP ALA ASN GLY LYS THR ILE VAL THR GLY GLY          
SEQRES   5 F  155  ASN GLY PRO GLU ASP PHE GLN GLN HIS GLU GLN ILE ARG          
SEQRES   6 F  155  ARG LYS THR LEU LYS GLU LYS ALA ILE PRO LYS ASP GLN          
SEQRES   7 F  155  ARG ALA THR THR PRO TYR MET THR LYS TYR GLU ARG ALA          
SEQRES   8 F  155  ARG ILE LEU GLY THR ARG ALA LEU GLN ILE SER MET ASN          
SEQRES   9 F  155  ALA PRO VAL PHE VAL ASP LEU GLU GLY GLU THR ASP PRO          
SEQRES  10 F  155  LEU ARG ILE ALA MET LYS GLU LEU ALA GLU LYS LYS ILE          
SEQRES  11 F  155  PRO LEU VAL ILE ARG ARG TYR LEU PRO ASP GLY SER PHE          
SEQRES  12 F  155  GLU ASP TRP SER VAL GLU GLU LEU ILE VAL ASP LEU              
SEQRES   1 G  212  MET PHE ILE LEU SER LYS ILE ALA ASP LEU VAL ARG ILE          
SEQRES   2 G  212  PRO PRO ASP GLN PHE HIS ARG ASP THR ILE SER ALA ILE          
SEQRES   3 G  212  THR HIS GLN LEU ASN ASN LYS PHE ALA ASN LYS ILE ILE          
SEQRES   4 G  212  PRO ASN VAL GLY LEU CYS ILE THR ILE TYR ASP LEU LEU          
SEQRES   5 G  212  THR VAL GLU GLU GLY GLN LEU LYS PRO GLY ASP GLY SER          
SEQRES   6 G  212  SER TYR ILE ASN VAL THR PHE ARG ALA VAL VAL PHE LYS          
SEQRES   7 G  212  PRO PHE LEU GLY GLU ILE VAL THR GLY TRP ILE SER LYS          
SEQRES   8 G  212  CYS THR ALA GLU GLY ILE LYS VAL SER LEU LEU GLY ILE          
SEQRES   9 G  212  PHE ASP ASP ILE PHE ILE PRO GLN ASN MET LEU PHE GLU          
SEQRES  10 G  212  GLY CYS TYR TYR THR PRO GLU GLU SER ALA TRP ILE TRP          
SEQRES  11 G  212  PRO MET ASP GLU GLU THR LYS LEU TYR PHE ASP VAL ASN          
SEQRES  12 G  212  GLU LYS ILE ARG PHE ARG ILE GLU ARG GLU VAL PHE VAL          
SEQRES  13 G  212  ASP VAL LYS PRO LYS SER PRO LYS GLU ARG GLU LEU GLU          
SEQRES  14 G  212  GLU ARG ALA GLN LEU GLU ASN GLU ILE GLU GLY LYS ASN          
SEQRES  15 G  212  GLU GLU THR PRO GLN ASN GLU LYS PRO PRO ALA TYR ALA          
SEQRES  16 G  212  LEU LEU GLY SER CYS GLN THR ASP GLY MET GLY LEU VAL          
SEQRES  17 G  212  SER TRP TRP GLU                                              
SEQRES   1 H  146  MET SER ASN THR LEU PHE ASP ASP ILE PHE GLN VAL SER          
SEQRES   2 H  146  GLU VAL ASP PRO GLY ARG TYR ASN LYS VAL CYS ARG ILE          
SEQRES   3 H  146  GLU ALA ALA SER THR THR GLN ASP GLN CYS LYS LEU THR          
SEQRES   4 H  146  LEU ASP ILE ASN VAL GLU LEU PHE PRO VAL ALA ALA GLN          
SEQRES   5 H  146  ASP SER LEU THR VAL THR ILE ALA SER SER LEU ASN LEU          
SEQRES   6 H  146  GLU ASP THR PRO ALA ASN ASP SER SER ALA THR ARG SER          
SEQRES   7 H  146  TRP ARG PRO PRO GLN ALA GLY ASP ARG SER LEU ALA ASP          
SEQRES   8 H  146  ASP TYR ASP TYR VAL MET TYR GLY THR ALA TYR LYS PHE          
SEQRES   9 H  146  GLU GLU VAL SER LYS ASP LEU ILE ALA VAL TYR TYR SER          
SEQRES  10 H  146  PHE GLY GLY LEU LEU MET ARG LEU GLU GLY ASN TYR ARG          
SEQRES  11 H  146  ASN LEU ASN ASN LEU LYS GLN GLU ASN ALA TYR LEU LEU          
SEQRES  12 H  146  ILE ARG ARG                                                  
SEQRES   1 I  110  MET LEU SER PHE CYS PRO SER CYS ASN ASN MET LEU LEU          
SEQRES   2 I  110  ILE THR SER GLY ASP SER GLY VAL TYR THR LEU ALA CYS          
SEQRES   3 I  110  ARG SER CYS PRO TYR GLU PHE PRO ILE GLU GLY ILE GLU          
SEQRES   4 I  110  ILE TYR ASP ARG LYS LYS LEU PRO ARG LYS GLU VAL ASP          
SEQRES   5 I  110  ASP VAL LEU GLY GLY GLY TRP ASP ASN VAL ASP GLN THR          
SEQRES   6 I  110  LYS THR GLN CYS PRO ASN TYR ASP THR CYS GLY GLY GLU          
SEQRES   7 I  110  SER ALA TYR PHE PHE GLN LEU GLN ILE ARG SER ALA ASP          
SEQRES   8 I  110  GLU PRO MET THR THR PHE TYR LYS CYS VAL ASN CYS GLY          
SEQRES   9 I  110  HIS ARG TRP LYS GLU ASN                                      
SEQRES   1 J   70  MET ILE VAL PRO VAL ARG CYS PHE SER CYS GLY LYS VAL          
SEQRES   2 J   70  VAL GLY ASP LYS TRP GLU SER TYR LEU ASN LEU LEU GLN          
SEQRES   3 J   70  GLU ASP GLU LEU ASP GLU GLY THR ALA LEU SER ARG LEU          
SEQRES   4 J   70  GLY LEU LYS ARG TYR CYS CYS ARG ARG MET ILE LEU THR          
SEQRES   5 J   70  HIS VAL ASP LEU ILE GLU LYS PHE LEU ARG TYR ASN PRO          
SEQRES   6 J   70  LEU GLU LYS ARG ASP                                          
SEQRES   1 K  142  MET THR GLU ASP ILE GLU GLN LYS LYS THR ALA THR GLU          
SEQRES   2 K  142  VAL THR PRO GLN GLU PRO LYS HIS ILE GLN GLU GLU GLU          
SEQRES   3 K  142  GLU GLN ASP VAL ASP MET THR GLY ASP GLU GLU GLN GLU          
SEQRES   4 K  142  GLU GLU PRO ASP ARG GLU LYS ILE LYS LEU LEU THR GLN          
SEQRES   5 K  142  ALA THR SER GLU ASP GLY THR SER ALA SER PHE GLN ILE          
SEQRES   6 K  142  VAL GLU GLU ASP HIS THR LEU GLY ASN ALA LEU ARG TYR          
SEQRES   7 K  142  VAL ILE MET LYS ASN PRO ASP VAL GLU PHE CYS GLY TYR          
SEQRES   8 K  142  SER ILE PRO HIS PRO SER GLU ASN LEU LEU ASN ILE ARG          
SEQRES   9 K  142  ILE GLN THR TYR GLY GLU THR THR ALA VAL ASP ALA LEU          
SEQRES  10 K  142  GLN LYS GLY LEU LYS ASP LEU MET ASP LEU CYS ASP VAL          
SEQRES  11 K  142  VAL GLU SER LYS PHE THR GLU LYS ILE LYS SER MET              
SEQRES   1 L   70  MET SER ARG GLU GLY PHE GLN ILE PRO THR ASN LEU ASP          
SEQRES   2 L   70  ALA ALA ALA ALA GLY THR SER GLN ALA ARG THR ALA THR          
SEQRES   3 L   70  LEU LYS TYR ILE CYS ALA GLU CYS SER SER LYS LEU SER          
SEQRES   4 L   70  LEU SER ARG THR ASP ALA VAL ARG CYS LYS ASP CYS GLY          
SEQRES   5 L   70  HIS ARG ILE LEU LEU LYS ALA ARG THR LYS ARG LEU VAL          
SEQRES   6 L   70  GLN PHE GLU ALA ARG                                          
SEQRES   1 M  282  MET SER ILE ASP ASN LYS LEU PHE VAL THR GLU GLU ASP          
SEQRES   2 M  282  GLU GLU ASP ARG THR GLN ASP ARG ALA ASP VAL GLU ASP          
SEQRES   3 M  282  GLU SER ASN ASP ILE ASP MET ILE ALA ASP GLU ASN GLY          
SEQRES   4 M  282  THR ASN SER ALA ILE ALA ASN GLU GLN GLU GLU LYS SER          
SEQRES   5 M  282  GLU GLU VAL LYS ALA GLU ASP ASP THR GLY GLU GLU GLU          
SEQRES   6 M  282  GLU ASP ASP PRO VAL ILE GLU GLU PHE PRO LEU LYS ILE          
SEQRES   7 M  282  SER GLY GLU GLU GLU SER LEU HIS VAL PHE GLN TYR ALA          
SEQRES   8 M  282  ASN ARG PRO ARG LEU VAL GLY ARG LYS PRO ALA GLU HIS          
SEQRES   9 M  282  PRO PHE ILE SER ALA ALA ARG TYR LYS PRO LYS SER HIS          
SEQRES  10 M  282  LEU TRP GLU ILE ASP ILE PRO LEU ASP GLU GLN ALA PHE          
SEQRES  11 M  282  TYR ASN LYS ASP LYS ALA GLU SER GLU TRP ASN GLY VAL          
SEQRES  12 M  282  ASN VAL GLN THR LEU LYS GLY VAL GLY VAL GLU ASN ASN          
SEQRES  13 M  282  GLY GLN TYR ALA ALA PHE VAL LYS ASP MET GLN VAL TYR          
SEQRES  14 M  282  LEU VAL PRO ILE GLU ARG VAL ALA GLN LEU LYS PRO PHE          
SEQRES  15 M  282  PHE LYS TYR ILE ASP ASP ALA ASN VAL THR ARG LYS GLN          
SEQRES  16 M  282  GLU ASP ALA ARG ARG PRO PRO ASN PRO SER SER GLN ARG          
SEQRES  17 M  282  ALA GLN VAL VAL THR MET SER VAL LYS SER VAL ASN ASP          
SEQRES  18 M  282  PRO SER GLN ASN ARG LEU THR GLY SER LEU LEU ALA HIS          
SEQRES  19 M  282  LYS VAL ALA ASP GLU GLU ALA ASN ILE GLU LEU THR TRP          
SEQRES  20 M  282  ALA GLU GLY THR PHE GLU GLN PHE LYS ASP THR ILE VAL          
SEQRES  21 M  282  LYS GLU ALA GLU ASP LYS THR LEU VAL ALA LEU GLU LYS          
SEQRES  22 M  282  GLN GLU ASP TYR ILE ASP ASN LEU VAL                          
SEQRES   1 N  422  MET SER SER ASN LYS GLY ASN GLY ARG LEU PRO SER LEU          
SEQRES   2 N  422  LYS ASP SER SER SER ASN GLY GLY GLY SER ALA LYS PRO          
SEQRES   3 N  422  SER LEU LYS PHE LYS PRO LYS ALA VAL ALA ARG LYS SER          
SEQRES   4 N  422  LYS GLU GLU ARG GLU ALA ALA ALA SER LYS VAL LYS LEU          
SEQRES   5 N  422  GLU GLU GLU SER LYS ARG GLY ASN ASP LYS LYS HIS PHE          
SEQRES   6 N  422  ASN ASN LYS ASN LYS ARG VAL THR GLY ALA GLY GLY GLN          
SEQRES   7 N  422  GLN ARG ARG MET ALA LYS TYR LEU ASN ASN THR HIS VAL          
SEQRES   8 N  422  ILE SER SER GLY PRO LEU ALA ALA GLY ASN PHE VAL SER          
SEQRES   9 N  422  GLU LYS GLY ASP LEU ARG ARG GLY PHE ILE LYS SER GLU          
SEQRES  10 N  422  GLY SER GLY SER SER LEU VAL GLN LYS GLY LEU GLU THR          
SEQRES  11 N  422  ILE ASP ASN GLY ALA GLU SER SER GLU ASN GLU ALA GLU          
SEQRES  12 N  422  ASP ASP ASP ASN GLU GLY VAL ALA SER LYS SER LYS LYS          
SEQRES  13 N  422  LYS PHE ASN MET GLY LYS GLU PHE GLU ALA ARG ASN LEU          
SEQRES  14 N  422  ILE GLU ASP GLU ASP ASP GLY GLU SER GLU LYS SER SER          
SEQRES  15 N  422  ASP VAL ASP MET ASP ASP GLU GLU TRP ARG SER LYS ARG          
SEQRES  16 N  422  ILE GLU GLN LEU PHE PRO VAL ARG PRO VAL ARG VAL ARG          
SEQRES  17 N  422  HIS GLU ASP VAL GLU THR VAL LYS ARG GLU ILE GLN GLU          
SEQRES  18 N  422  ALA LEU SER GLU LYS PRO THR ARG GLU PRO THR PRO SER          
SEQRES  19 N  422  VAL LYS THR GLU PRO VAL GLY THR GLY LEU GLN SER TYR          
SEQRES  20 N  422  LEU GLU GLU ARG GLU ARG GLN VAL ASN GLU LYS LEU ALA          
SEQRES  21 N  422  ASP LEU GLY LEU GLU LYS GLU PHE GLN SER VAL ASP GLY          
SEQRES  22 N  422  LYS GLU ALA ALA ALA GLU LEU GLU LEU LEU ASN ALA ASP          
SEQRES  23 N  422  HIS GLN HIS ILE LEU ARG LYS LEU LYS LYS MET ASN ASN          
SEQRES  24 N  422  LYS PRO GLU ARG PHE MET VAL PHE GLN LEU PRO THR ARG          
SEQRES  25 N  422  LEU PRO ALA PHE GLU ARG PRO ALA VAL LYS GLU GLU LYS          
SEQRES  26 N  422  GLU ASP MET GLU THR GLN ALA SER ASP PRO SER LYS LYS          
SEQRES  27 N  422  LYS LYS ASN ILE LYS LYS LYS ASP THR LYS ASP ALA LEU          
SEQRES  28 N  422  SER THR ARG GLU LEU ALA GLY LYS VAL GLY SER ILE ARG          
SEQRES  29 N  422  VAL HIS LYS SER GLY LYS LEU SER VAL LYS ILE GLY ASN          
SEQRES  30 N  422  VAL VAL MET ASP ILE GLY LYS GLY ALA GLU THR THR PHE          
SEQRES  31 N  422  LEU GLN ASP VAL ILE ALA LEU SER ILE ALA ASP ASP ALA          
SEQRES  32 N  422  SER SER ALA GLU LEU LEU GLY ARG VAL ASP GLY LYS ILE          
SEQRES  33 N  422  VAL VAL THR PRO GLN ILE                                      
SEQRES   1 O  654  MET ASP GLU LEU LEU GLY GLU ALA LEU SER ALA GLU ASN          
SEQRES   2 O  654  GLN THR GLY GLU SER THR VAL GLU SER GLU LYS LEU VAL          
SEQRES   3 O  654  THR PRO GLU ASP VAL MET THR ILE SER SER LEU GLU GLN          
SEQRES   4 O  654  ARG THR LEU ASN PRO ASP LEU PHE LEU TYR LYS GLU LEU          
SEQRES   5 O  654  VAL LYS ALA HIS LEU GLY GLU ARG ALA ALA SER VAL ILE          
SEQRES   6 O  654  GLY MET LEU VAL ALA LEU GLY ARG LEU SER VAL ARG GLU          
SEQRES   7 O  654  LEU VAL GLU LYS ILE ASP GLY MET ASP VAL ASP SER VAL          
SEQRES   8 O  654  LYS THR THR LEU VAL SER LEU THR GLN LEU ARG CYS VAL          
SEQRES   9 O  654  LYS TYR LEU GLN GLU THR ALA ILE SER GLY LYS LYS THR          
SEQRES  10 O  654  THR TYR TYR TYR TYR ASN GLU GLU GLY ILE HIS ILE LEU          
SEQRES  11 O  654  LEU TYR SER GLY LEU ILE ILE ASP GLU ILE ILE THR GLN          
SEQRES  12 O  654  MET ARG VAL ASN ASP GLU GLU GLU HIS LYS GLN LEU VAL          
SEQRES  13 O  654  ALA GLU ILE VAL GLN ASN VAL ILE SER LEU GLY SER LEU          
SEQRES  14 O  654  THR VAL GLU ASP TYR LEU SER SER VAL THR SER ASP SER          
SEQRES  15 O  654  MET LYS TYR THR ILE SER SER LEU PHE VAL GLN LEU CYS          
SEQRES  16 O  654  GLU MET GLY TYR LEU ILE GLN ILE SER LYS LEU HIS TYR          
SEQRES  17 O  654  THR PRO ILE GLU ASP LEU TRP GLN PHE LEU TYR GLU LYS          
SEQRES  18 O  654  HIS TYR LYS ASN ILE PRO ARG ASN SER PRO LEU SER ASP          
SEQRES  19 O  654  LEU LYS LYS ARG SER GLN ALA LYS MET ASN ALA LYS THR          
SEQRES  20 O  654  ASP PHE ALA LYS ILE ILE ASN LYS PRO ASN GLU LEU SER          
SEQRES  21 O  654  GLN ILE LEU THR VAL ASP PRO LYS THR SER LEU ARG ILE          
SEQRES  22 O  654  VAL LYS PRO THR VAL SER LEU THR ILE ASN LEU ASP ARG          
SEQRES  23 O  654  PHE MET LYS GLY ARG ARG SER LYS GLN LEU ILE ASN LEU          
SEQRES  24 O  654  ALA LYS THR ARG VAL GLY SER VAL THR ALA GLN VAL TYR          
SEQRES  25 O  654  LYS ILE ALA LEU ARG LEU THR GLU GLN LYS SER PRO LYS          
SEQRES  26 O  654  ILE ARG ASP PRO LEU THR GLN THR GLY LEU LEU GLN ASP          
SEQRES  27 O  654  LEU GLU GLU ALA LYS SER PHE GLN ASP GLU ALA GLU LEU          
SEQRES  28 O  654  VAL GLU GLU LYS THR PRO GLY LEU THR PHE ASN ALA ILE          
SEQRES  29 O  654  ASP LEU ALA ARG HIS LEU PRO ALA GLU LEU ASP LEU ARG          
SEQRES  30 O  654  GLY SER LEU LEU SER ARG LYS PRO SER ASP ASN LYS LYS          
SEQRES  31 O  654  ARG SER GLY SER ASN ALA ALA ALA SER LEU PRO SER LYS          
SEQRES  32 O  654  LYS LEU LYS THR GLU ASP GLY PHE VAL ILE PRO ALA LEU          
SEQRES  33 O  654  PRO ALA ALA VAL SER LYS SER LEU GLN GLU SER GLY ASP          
SEQRES  34 O  654  THR GLN GLU GLU ASP GLU GLU GLU GLU ASP LEU ASP ALA          
SEQRES  35 O  654  ASP THR GLU ASP PRO HIS SER ALA SER LEU ILE ASN SER          
SEQRES  36 O  654  HIS LEU LYS ILE LEU ALA SER SER ASN PHE PRO PHE LEU          
SEQRES  37 O  654  ASN GLU THR LYS PRO GLY VAL TYR TYR VAL PRO TYR SER          
SEQRES  38 O  654  LYS LEU MET PRO VAL LEU LYS SER SER VAL TYR GLU TYR          
SEQRES  39 O  654  VAL ILE ALA SER THR LEU GLY PRO SER ALA MET ARG LEU          
SEQRES  40 O  654  SER ARG CYS ILE ARG ASP ASN LYS LEU VAL SER GLU LYS          
SEQRES  41 O  654  ILE ILE ASN SER THR ALA LEU MET LYS GLU LYS ASP ILE          
SEQRES  42 O  654  ARG SER THR LEU ALA SER LEU ILE ARG TYR ASN SER VAL          
SEQRES  43 O  654  GLU ILE GLN GLU VAL PRO ARG THR ALA ASP ARG SER ALA          
SEQRES  44 O  654  SER ARG ALA VAL PHE LEU PHE ARG CYS LYS GLU THR HIS          
SEQRES  45 O  654  SER TYR ASN PHE MET ARG GLN ASN LEU GLU TRP ASN MET          
SEQRES  46 O  654  ALA ASN LEU LEU PHE LYS LYS GLU LYS LEU LYS GLN GLU          
SEQRES  47 O  654  ASN SER THR LEU LEU LYS LYS ALA ASN ARG ASP ASP VAL          
SEQRES  48 O  654  LYS GLY ARG GLU ASN GLU LEU LEU LEU PRO SER GLU LEU          
SEQRES  49 O  654  ASN GLN LEU LYS MET VAL ASN GLU ARG GLU LEU ASN VAL          
SEQRES  50 O  654  PHE ALA ARG LEU SER ARG LEU LEU SER LEU TRP GLU VAL          
SEQRES  51 O  654  PHE GLN MET ALA                                              
SEQRES   1 P  317  MET SER GLY MET ILE GLU ASN GLY LEU GLN LEU SER ASP          
SEQRES   2 P  317  ASN ALA LYS THR LEU HIS SER GLN MET MET SER LYS GLY          
SEQRES   3 P  317  ILE GLY ALA LEU PHE THR GLN GLN GLU LEU GLN LYS GLN          
SEQRES   4 P  317  MET GLY ILE GLY SER LEU THR ASP LEU MET SER ILE VAL          
SEQRES   5 P  317  GLN GLU LEU LEU ASP LYS ASN LEU ILE LYS LEU VAL LYS          
SEQRES   6 P  317  GLN ASN ASP GLU LEU LYS PHE GLN GLY VAL LEU GLU SER          
SEQRES   7 P  317  GLU ALA GLN LYS LYS ALA THR MET SER ALA GLU GLU ALA          
SEQRES   8 P  317  LEU VAL TYR SER TYR ILE GLU ALA SER GLY ARG GLU GLY          
SEQRES   9 P  317  ILE TRP SER LYS THR ILE LYS ALA ARG THR ASN LEU HIS          
SEQRES  10 P  317  GLN HIS VAL VAL LEU LYS CYS LEU LYS SER LEU GLU SER          
SEQRES  11 P  317  GLN ARG TYR VAL LYS SER VAL LYS SER VAL LYS PHE PRO          
SEQRES  12 P  317  THR ARG LYS ILE TYR MET LEU TYR SER LEU GLN PRO SER          
SEQRES  13 P  317  VAL ASP ILE THR GLY GLY PRO TRP PHE THR ASP GLY GLU          
SEQRES  14 P  317  LEU ASP ILE GLU PHE ILE ASN SER LEU LEU THR ILE VAL          
SEQRES  15 P  317  TRP ARG PHE ILE SER GLU ASN THR PHE PRO ASN GLY PHE          
SEQRES  16 P  317  LYS ASN PHE GLU ASN GLY PRO LYS LYS ASN VAL PHE TYR          
SEQRES  17 P  317  ALA PRO ASN VAL LYS ASN TYR SER THR THR GLN GLU ILE          
SEQRES  18 P  317  LEU GLU PHE ILE THR ALA ALA GLN VAL ALA ASN VAL GLU          
SEQRES  19 P  317  LEU THR PRO SER ASN ILE ARG SER LEU CYS GLU VAL LEU          
SEQRES  20 P  317  VAL TYR ASP ASP LYS LEU GLU LYS VAL THR HIS ASP CYS          
SEQRES  21 P  317  TYR ARG VAL THR LEU GLU SER ILE LEU GLN MET ASN GLN          
SEQRES  22 P  317  GLY GLU GLY GLU PRO GLU ALA GLY ASN LYS ALA LEU GLU          
SEQRES  23 P  317  ASP GLU GLU GLU PHE SER ILE PHE ASN TYR PHE LYS MET          
SEQRES  24 P  317  PHE PRO ALA SER LYS HIS ASP LYS GLU VAL VAL TYR PHE          
SEQRES  25 P  317  ASP GLU TRP THR ILE                                          
SEQRES   1 Q  251  MET SER SER TYR ARG GLY GLY SER ARG GLY GLY GLY SER          
SEQRES   2 Q  251  ASN TYR MET SER ASN LEU PRO PHE GLY LEU GLY TYR GLY          
SEQRES   3 Q  251  ASP VAL GLY LYS ASN HIS ILE THR GLU PHE PRO SER ILE          
SEQRES   4 Q  251  PRO LEU PRO ILE ASN GLY PRO ILE THR ASN LYS GLU ARG          
SEQRES   5 Q  251  SER LEU ALA VAL LYS TYR ILE ASN PHE GLY LYS THR VAL          
SEQRES   6 Q  251  LYS ASP GLY PRO PHE TYR THR GLY SER MET SER LEU ILE          
SEQRES   7 Q  251  ILE ASP GLN GLN GLU ASN SER LYS SER GLY LYS ARG LYS          
SEQRES   8 Q  251  PRO ASN ILE ILE LEU ASP GLU ASP ASP THR ASN ASP GLY          
SEQRES   9 Q  251  ILE GLU ARG TYR SER ASP LYS TYR LEU LYS LYS ARG LYS          
SEQRES  10 Q  251  ILE GLY ILE SER ILE ASP ASP HIS PRO TYR ASN LEU ASN          
SEQRES  11 Q  251  LEU PHE PRO ASN GLU LEU TYR ASN VAL MET GLY ILE ASN          
SEQRES  12 Q  251  LYS LYS LYS LEU LEU ALA ILE SER LYS PHE ASN ASN ALA          
SEQRES  13 Q  251  ASP ASP VAL PHE THR GLY THR GLY LEU GLN ASP GLU ASN          
SEQRES  14 Q  251  ILE GLY LEU SER MET LEU ALA LYS LEU LYS GLU LEU ALA          
SEQRES  15 Q  251  GLU ASP VAL ASP ASP ALA SER THR GLY ASP GLY ALA ALA          
SEQRES  16 Q  251  LYS GLY SER LYS THR GLY GLU GLY GLU ASP ASP ASP LEU          
SEQRES  17 Q  251  ALA ASP ASP ASP PHE GLU GLU ASP GLU ASP GLU GLU ASP          
SEQRES  18 Q  251  ASP ASP ASP TYR ASN ALA GLU LYS TYR PHE ASN ASN GLY          
SEQRES  19 Q  251  ASP ASP ASP ASP TYR GLY ASP GLU GLU ASP PRO ASN GLU          
SEQRES  20 Q  251  GLU ALA ALA PHE                                              
SEQRES   1 U  240  MET ALA ASP GLU GLU ARG LEU LYS GLU PHE LYS GLU ALA          
SEQRES   2 U  240  ASN LYS ILE VAL PHE ASP PRO ASN THR ARG GLN VAL TRP          
SEQRES   3 U  240  GLU ASN GLN ASN ARG ASP GLY THR LYS PRO ALA THR THR          
SEQRES   4 U  240  PHE GLN SER GLU GLU ASP ILE LYS ARG ALA ALA PRO GLU          
SEQRES   5 U  240  SER GLU LYS ASP THR SER ALA THR SER GLY ILE VAL PRO          
SEQRES   6 U  240  THR LEU GLN ASN ILE VAL ALA THR VAL THR LEU GLY CYS          
SEQRES   7 U  240  ARG LEU ASP LEU LYS THR VAL ALA LEU HIS ALA ARG ASN          
SEQRES   8 U  240  ALA GLU TYR ASN PRO LYS ARG PHE ALA ALA VAL ILE MET          
SEQRES   9 U  240  ARG ILE ARG GLU PRO LYS THR THR ALA LEU ILE PHE ALA          
SEQRES  10 U  240  SER GLY LYS MET VAL VAL THR GLY ALA LYS SER GLU ASP          
SEQRES  11 U  240  ASP SER LYS LEU ALA SER ARG LYS TYR ALA ARG ILE ILE          
SEQRES  12 U  240  GLN LYS ILE GLY PHE ALA ALA LYS PHE THR ASP PHE LYS          
SEQRES  13 U  240  ILE GLN ASN ILE VAL GLY SER CYS ASP VAL LYS PHE PRO          
SEQRES  14 U  240  ILE ARG LEU GLU GLY LEU ALA PHE SER HIS GLY THR PHE          
SEQRES  15 U  240  SER SER TYR GLU PRO GLU LEU PHE PRO GLY LEU ILE TYR          
SEQRES  16 U  240  ARG MET VAL LYS PRO LYS ILE VAL LEU LEU ILE PHE VAL          
SEQRES  17 U  240  SER GLY LYS ILE VAL LEU THR GLY ALA LYS GLN ARG GLU          
SEQRES  18 U  240  GLU ILE TYR GLN ALA PHE GLU ALA ILE TYR PRO VAL LEU          
SEQRES  19 U  240  SER GLU PHE ARG LYS MET                                      
SEQRES   1 V  596  MET PRO VAL CYS LYS ASN CYS HIS GLY THR GLU PHE GLU          
SEQRES   2 V  596  ARG ASP LEU SER ASN ALA ASN ASN ASP LEU VAL CYS LYS          
SEQRES   3 V  596  ALA CYS GLY VAL VAL SER GLU ASP ASN PRO ILE VAL SER          
SEQRES   4 V  596  GLU VAL THR PHE GLY GLU THR SER ALA GLY ALA ALA VAL          
SEQRES   5 V  596  VAL GLN GLY SER PHE ILE GLY ALA GLY GLN SER HIS ALA          
SEQRES   6 V  596  ALA PHE GLY GLY SER SER ALA LEU GLU SER ARG GLU ALA          
SEQRES   7 V  596  THR LEU ASN ASN ALA ARG ARG LYS LEU ARG ALA VAL SER          
SEQRES   8 V  596  TYR ALA LEU HIS ILE PRO GLU TYR ILE THR ASP ALA ALA          
SEQRES   9 V  596  PHE GLN TRP TYR LYS LEU ALA LEU ALA ASN ASN PHE VAL          
SEQRES  10 V  596  GLN GLY ARG ARG SER GLN ASN VAL ILE ALA SER CYS LEU          
SEQRES  11 V  596  TYR VAL ALA CYS ARG LYS GLU LYS THR HIS HIS MET LEU          
SEQRES  12 V  596  ILE ASP PHE SER SER ARG LEU GLN VAL SER VAL TYR SER          
SEQRES  13 V  596  ILE GLY ALA THR PHE LEU LYS MET VAL LYS LYS LEU HIS          
SEQRES  14 V  596  ILE THR GLU LEU PRO LEU ALA ASP PRO SER LEU PHE ILE          
SEQRES  15 V  596  GLN HIS PHE ALA GLU LYS LEU ASP LEU ALA ASP LYS LYS          
SEQRES  16 V  596  ILE LYS VAL VAL LYS ASP ALA VAL LYS LEU ALA GLN ARG          
SEQRES  17 V  596  MET SER LYS ASP TRP MET PHE GLU GLY ARG ARG PRO ALA          
SEQRES  18 V  596  GLY ILE ALA GLY ALA CYS ILE LEU LEU ALA CYS ARG MET          
SEQRES  19 V  596  ASN ASN LEU ARG ARG THR HIS THR GLU ILE VAL ALA VAL          
SEQRES  20 V  596  SER HIS VAL ALA GLU GLU THR LEU GLN GLN ARG LEU ASN          
SEQRES  21 V  596  GLU PHE LYS ASN THR LYS ALA ALA LYS LEU SER VAL GLN          
SEQRES  22 V  596  LYS PHE ARG GLU ASN ASP VAL GLU ASP GLY GLU ALA ARG          
SEQRES  23 V  596  PRO PRO SER PHE VAL LYS ASN ARG LYS LYS GLU ARG LYS          
SEQRES  24 V  596  ILE LYS ASP SER LEU ASP LYS GLU GLU MET PHE GLN THR          
SEQRES  25 V  596  SER GLU GLU ALA LEU ASN LYS ASN PRO ILE LEU THR GLN          
SEQRES  26 V  596  VAL LEU GLY GLU GLN GLU LEU SER SER LYS GLU VAL LEU          
SEQRES  27 V  596  PHE TYR LEU LYS GLN PHE SER GLU ARG ARG ALA ARG VAL          
SEQRES  28 V  596  VAL GLU ARG ILE LYS ALA THR ASN GLY ILE ASP GLY GLU          
SEQRES  29 V  596  ASN ILE TYR HIS GLU GLY SER GLU ASN GLU THR ARG LYS          
SEQRES  30 V  596  ARG LYS LEU SER GLU VAL SER ILE GLN ASN GLU HIS VAL          
SEQRES  31 V  596  GLU GLY GLU ASP LYS GLU THR GLU GLY THR GLU GLU LYS          
SEQRES  32 V  596  VAL LYS LYS VAL LYS THR LYS THR SER GLU GLU LYS LYS          
SEQRES  33 V  596  GLU ASN GLU SER GLY HIS PHE GLN ASP ALA ILE ASP GLY          
SEQRES  34 V  596  TYR SER LEU GLU THR ASP PRO TYR CYS PRO ARG ASN LEU          
SEQRES  35 V  596  HIS LEU LEU PRO THR THR ASP THR TYR LEU SER LYS VAL          
SEQRES  36 V  596  SER ASP ASP PRO ASP ASN LEU GLU ASP VAL ASP ASP GLU          
SEQRES  37 V  596  GLU LEU ASN ALA HIS LEU LEU ASN GLU GLU ALA SER LYS          
SEQRES  38 V  596  LEU LYS GLU ARG ILE TRP ILE GLY LEU ASN ALA ASP PHE          
SEQRES  39 V  596  LEU LEU GLU GLN GLU SER LYS ARG LEU LYS GLN GLU ALA          
SEQRES  40 V  596  ASP ILE ALA THR GLY ASN THR SER VAL LYS LYS LYS ARG          
SEQRES  41 V  596  THR ARG ARG ARG ASN ASN THR ARG SER ASP GLU PRO THR          
SEQRES  42 V  596  LYS THR VAL ASP ALA ALA ALA ALA ILE GLY LEU MET SER          
SEQRES  43 V  596  ASP LEU GLN ASP LYS SER GLY LEU HIS ALA ALA LEU LYS          
SEQRES  44 V  596  ALA ALA GLU GLU SER GLY ASP PHE THR THR ALA ASP SER          
SEQRES  45 V  596  VAL LYS ASN MET LEU GLN LYS ALA SER PHE SER LYS LYS          
SEQRES  46 V  596  ILE ASN TYR ASP ALA ILE ASP GLY LEU PHE ARG                  
SEQRES   1 W  594  MET SER SER ILE VAL ASN LYS SER GLY THR ARG PHE ALA          
SEQRES   2 W  594  PRO LYS VAL ARG GLN ARG ARG ALA ALA THR GLY GLY THR          
SEQRES   3 W  594  PRO THR PRO LYS PRO ARG THR PRO GLN LEU PHE ILE PRO          
SEQRES   4 W  594  GLU SER LYS GLU ILE GLU GLU ASP ASN SER ASP ASN ASP          
SEQRES   5 W  594  LYS GLY VAL ASP GLU ASN GLU THR ALA ILE VAL GLU LYS          
SEQRES   6 W  594  PRO SER LEU VAL GLY GLU ARG SER LEU GLU GLY PHE THR          
SEQRES   7 W  594  LEU THR GLY THR ASN GLY HIS ASP ASN GLU ILE GLY ASP          
SEQRES   8 W  594  GLU GLY PRO ILE ASP ALA SER THR GLN ASN PRO LYS ALA          
SEQRES   9 W  594  ASP VAL ILE GLU ASP ASN VAL THR LEU LYS PRO ALA PRO          
SEQRES  10 W  594  LEU GLN THR HIS ARG ASP GLN LYS VAL PRO ARG SER SER          
SEQRES  11 W  594  ARG LEU ALA SER LEU SER LYS ASP ASN GLU SER ARG PRO          
SEQRES  12 W  594  SER PHE LYS PRO SER PHE LEU ASP SER SER SER ASN SER          
SEQRES  13 W  594  ASN GLY THR ALA ARG ARG LEU SER THR ILE SER ASN LYS          
SEQRES  14 W  594  LEU PRO LYS LYS ILE ARG LEU GLY SER ILE THR GLU ASN          
SEQRES  15 W  594  ASP MET ASN LEU LYS THR PHE LYS ARG HIS ARG VAL LEU          
SEQRES  16 W  594  GLY LYS PRO SER SER ALA LYS LYS PRO ALA GLY ALA HIS          
SEQRES  17 W  594  ARG ILE SER ILE VAL SER LYS ILE SER PRO PRO THR ALA          
SEQRES  18 W  594  MET THR ASP SER LEU ASP ARG ASN GLU PHE SER SER GLU          
SEQRES  19 W  594  THR SER THR SER ARG GLU ALA ASP GLU ASN GLU ASN TYR          
SEQRES  20 W  594  VAL ILE SER LYS VAL LYS ASP ILE PRO LYS LYS VAL ARG          
SEQRES  21 W  594  ASP GLY GLU SER ALA LYS TYR PHE ILE ASP GLU GLU ASN          
SEQRES  22 W  594  PHE THR MET ALA GLU LEU CYS LYS PRO ASN PHE PRO ILE          
SEQRES  23 W  594  GLY GLN ILE SER GLU ASN PHE GLU LYS SER LYS MET ALA          
SEQRES  24 W  594  LYS LYS ALA LYS LEU GLU LYS ARG ARG HIS LEU ARG GLU          
SEQRES  25 W  594  LEU ARG MET ARG ALA ARG GLN GLU PHE LYS PRO LEU HIS          
SEQRES  26 W  594  SER LEU THR LYS GLU GLU GLN GLU GLU GLU GLU GLU LYS          
SEQRES  27 W  594  ARG LYS GLU GLU ARG ASP LYS LEU LEU ASN ALA ASP ILE          
SEQRES  28 W  594  PRO GLU SER ASP ARG LYS ALA HIS THR ALA ILE GLN LEU          
SEQRES  29 W  594  LYS LEU ASN PRO ASP GLY THR MET ALA ILE ASP GLU GLU          
SEQRES  30 W  594  THR MET VAL VAL ASP ARG HIS LYS ASN ALA SER ILE GLU          
SEQRES  31 W  594  ASN GLU TYR LYS GLU LYS VAL ASP GLU ASN PRO PHE ALA          
SEQRES  32 W  594  ASN LEU TYR ASN TYR GLY SER TYR GLY ARG GLY SER TYR          
SEQRES  33 W  594  THR ASP PRO TRP THR VAL GLU GLU MET ILE LYS PHE TYR          
SEQRES  34 W  594  LYS ALA LEU SER MET TRP GLY THR ASP PHE ASN LEU ILE          
SEQRES  35 W  594  SER GLN LEU TYR PRO TYR ARG SER ARG LYS GLN VAL LYS          
SEQRES  36 W  594  ALA LYS PHE VAL ASN GLU GLU LYS LYS ARG PRO ILE LEU          
SEQRES  37 W  594  ILE GLU LEU ALA LEU ARG SER LYS LEU PRO PRO ASN PHE          
SEQRES  38 W  594  ASP GLU TYR CYS CYS GLU ILE LYS LYS ASN ILE GLY THR          
SEQRES  39 W  594  VAL ALA ASP PHE ASN GLU LYS LEU ILE GLU LEU GLN ASN          
SEQRES  40 W  594  GLU HIS LYS HIS HIS MET LYS GLU ILE GLU GLU ALA LYS          
SEQRES  41 W  594  ASN THR ALA LYS GLU GLU ASP GLN THR ALA GLN ARG LEU          
SEQRES  42 W  594  ASN ASP ALA ASN LEU ASN LYS LYS GLY SER GLY GLY ILE          
SEQRES  43 W  594  MET THR ASN ASP LEU LYS VAL TYR ARG LYS THR GLU VAL          
SEQRES  44 W  594  VAL LEU GLY THR ILE ASP ASP LEU LYS ARG LYS LYS LEU          
SEQRES  45 W  594  LYS GLU ARG ASN ASN ASP ASP ASN GLU ASP ASN GLU GLY          
SEQRES  46 W  594  SER GLU GLU GLU PRO GLU ILE ASP GLN                          
SEQRES   1 X   81   DC  DG  DT  DC  DC  DA  DC  DT  DA  DT  DT  DT  DT          
SEQRES   2 X   81   DC  DG  DG  DC  DT  DA  DC  DT  DA  DT  DA  DA  DA          
SEQRES   3 X   81   DT  DA  DA  DA  DT  DG  DT  DT  DT  DT  DT  DT  DT          
SEQRES   4 X   81   DC  DG  DC  DA  DA  DT  DA  DG  DT  DG  DT  DG  DT          
SEQRES   5 X   81   DT  DC  DG  DC  DG  DA  DA  DG  DT  DA  DA  DC  DC          
SEQRES   6 X   81   DC  DT  DT  DC  DG  DT  DG  DG  DA  DC  DA  DT  DT          
SEQRES   7 X   81   DT  DG  DG                                                  
SEQRES   1 Y   81   DC  DC  DA  DA  DA  DT  DG  DT  DC  DC  DA  DC  DG          
SEQRES   2 Y   81   DA  DA  DG  DG  DG  DT  DT  DA  DC  DT  DT  DC  DG          
SEQRES   3 Y   81   DC  DG  DA  DA  DC  DA  DC  DA  DC  DT  DA  DT  DT          
SEQRES   4 Y   81   DG  DC  DG  DA  DA  DA  DA  DA  DA  DA  DC  DA  DT          
SEQRES   5 Y   81   DT  DT  DA  DT  DT  DT  DA  DT  DA  DG  DT  DA  DG          
SEQRES   6 Y   81   DC  DC  DG  DA  DA  DA  DA  DT  DA  DG  DT  DG  DG          
SEQRES   7 Y   81   DA  DC  DG                                                  
HET     ZN  A1501       1                                                       
HET     ZN  A1502       1                                                       
HET     ZN  B2000       1                                                       
HET     ZN  I2000       1                                                       
HET     ZN  J2000       1                                                       
HET     ZN  L2000       1                                                       
HET     ZN  V1001       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  23   ZN    7(ZN 2+)                                                     
HELIX    1 AA1 ASP A   25  SER A   30  1                                   6    
HELIX    2 AA2 ILE A  100  GLY A  105  1                                   6    
HELIX    3 AA3 SER A  116  LEU A  124  1                                   9    
HELIX    4 AA4 LEU A  124  ARG A  129  1                                   6    
HELIX    5 AA5 ASP A  133  LYS A  149  1                                  17    
HELIX    6 AA6 GLU A  193  HIS A  207  1                                  15    
HELIX    7 AA7 THR A  227  LYS A  232  1                                   6    
HELIX    8 AA8 LYS A  235  GLY A  243  5                                   9    
HELIX    9 AA9 VAL A  248  ILE A  257  5                                  10    
HELIX   10 AB1 LEU A  285  GLY A  306  1                                  22    
HELIX   11 AB2 SER A  308  ILE A  327  1                                  20    
HELIX   12 AB3 ASN A  328  VAL A  332  5                                   5    
HELIX   13 AB4 PHE A  353  LYS A  358  1                                   6    
HELIX   14 AB5 ASP A  396  LYS A  400  1                                   5    
HELIX   15 AB6 ASN A  412  VAL A  421  1                                  10    
HELIX   16 AB7 ARG A  449  LYS A  454  1                                   6    
HELIX   17 AB8 HIS A  481  LEU A  483  5                                   3    
HELIX   18 AB9 VAL A  504  ASN A  509  1                                   6    
HELIX   19 AC1 GLU A  526  GLY A  536  1                                  11    
HELIX   20 AC2 VAL A  537  ASN A  540  5                                   4    
HELIX   21 AC3 ASP A  556  SER A  565  1                                  10    
HELIX   22 AC4 ASP A  572  SER A  581  1                                  10    
HELIX   23 AC5 LYS A  607  LYS A  615  1                                   9    
HELIX   24 AC6 SER A  676  TYR A  685  1                                  10    
HELIX   25 AC7 TYR A  685  GLY A  709  1                                  25    
HELIX   26 AC8 ASP A  721  THR A  743  1                                  23    
HELIX   27 AC9 GLN A  760  LYS A  765  1                                   6    
HELIX   28 AD1 LYS A  765  GLU A  784  1                                  20    
HELIX   29 AD2 ASN A  789  CYS A  797  1                                   9    
HELIX   30 AD3 LEU A  804  ALA A  811  1                                   8    
HELIX   31 AD4 SER A  857  ASP A  874  1                                  18    
HELIX   32 AD5 ASP A  874  SER A  892  1                                  19    
HELIX   33 AD6 GLU A  927  GLN A  931  5                                   5    
HELIX   34 AD7 ASN A  934  THR A  946  1                                  13    
HELIX   35 AD8 LEU A  955  GLU A  965  1                                  11    
HELIX   36 AD9 ILE A  966  ARG A  973  1                                   8    
HELIX   37 AE1 ASP A  999  ARG A 1026  1                                  28    
HELIX   38 AE2 PRO A 1049  TYR A 1060  1                                  12    
HELIX   39 AE3 GLU A 1064  LYS A 1069  1                                   6    
HELIX   40 AE4 LYS A 1069  ALA A 1081  1                                  13    
HELIX   41 AE5 ALA A 1088  GLY A 1098  1                                  11    
HELIX   42 AE6 GLY A 1122  ALA A 1132  1                                  11    
HELIX   43 AE7 ARG A 1155  GLU A 1162  1                                   8    
HELIX   44 AE8 LEU A 1166  VAL A 1169  1                                   4    
HELIX   45 AE9 ASP A 1189  LEU A 1196  1                                   8    
HELIX   46 AF1 ILE A 1202  ARG A 1211  1                                  10    
HELIX   47 AF2 ASN A 1254  LEU A 1267  1                                  14    
HELIX   48 AF3 LEU A 1300  THR A 1306  1                                   7    
HELIX   49 AF4 HIS A 1318  LEU A 1326  1                                   9    
HELIX   50 AF5 ILE A 1328  ASN A 1345  1                                  18    
HELIX   51 AF6 PRO A 1352  THR A 1363  1                                  12    
HELIX   52 AF7 THR A 1372  ARG A 1380  1                                   9    
HELIX   53 AF8 SER A 1382  SER A 1388  1                                   7    
HELIX   54 AF9 THR A 1393  TYR A 1402  1                                  10    
HELIX   55 AG1 GLY A 1410  GLY A 1418  1                                   9    
HELIX   56 AG2 ILE A 1423  SER A 1427  5                                   5    
HELIX   57 AG3 SER A 1437  LEU A 1441  5                                   5    
HELIX   58 AG4 LYS B   44  HIS B   46  5                                   3    
HELIX   59 AG5 LEU B   47  LYS B   55  1                                   9    
HELIX   60 AG6 VAL B   58  THR B   71  1                                  14    
HELIX   61 AG7 THR B   71  LYS B   78  1                                   8    
HELIX   62 AG8 PRO B  114  ARG B  119  1                                   6    
HELIX   63 AG9 SER B  169  LEU B  174  1                                   6    
HELIX   64 AH1 PRO B  252  LEU B  257  1                                   6    
HELIX   65 AH2 LEU B  266  CYS B  273  1                                   8    
HELIX   66 AH3 SER B  278  ALA B  284  1                                   7    
HELIX   67 AH4 LEU B  287  ASP B  294  1                                   8    
HELIX   68 AH5 LEU B  302  ALA B  307  1                                   6    
HELIX   69 AH6 ARG B  343  ASN B  362  1                                  20    
HELIX   70 AH7 PRO B  363  ILE B  366  5                                   4    
HELIX   71 AH8 TYR B  371  GLY B  373  5                                   3    
HELIX   72 AH9 ALA B  380  LEU B  401  1                                  22    
HELIX   73 AI1 ILE B  403  LYS B  408  1                                   6    
HELIX   74 AI2 ALA B  418  ILE B  422  5                                   5    
HELIX   75 AI3 HIS B  425  ASN B  428  5                                   4    
HELIX   76 AI4 ILE B  429  THR B  439  1                                  11    
HELIX   77 AI5 SER B  462  MET B  469  1                                   8    
HELIX   78 AI6 GLU B  526  LEU B  536  1                                  11    
HELIX   79 AI7 ASP B  545  ASN B  552  1                                   8    
HELIX   80 AI8 PHE B  567  THR B  581  1                                  15    
HELIX   81 AI9 LYS B  623  GLY B  633  1                                  11    
HELIX   82 AJ1 PHE B  637  GLY B  644  1                                   8    
HELIX   83 AJ2 ASN B  652  SER B  657  1                                   6    
HELIX   84 AJ3 TYR B  662  ILE B  666  5                                   5    
HELIX   85 AJ4 TYR B  690  ASN B  694  5                                   5    
HELIX   86 AJ5 SER B  696  LYS B  707  1                                  12    
HELIX   87 AJ6 LYS B  775  ARG B  780  1                                   6    
HELIX   88 AJ7 ASN B  945  HIS B  947  5                                   3    
HELIX   89 AJ8 GLY B  948  MET B  953  1                                   6    
HELIX   90 AJ9 THR B  954  ASN B  970  1                                  17    
HELIX   91 AK1 LEU B  984  GLY B  995  1                                  12    
HELIX   92 AK2 MET B 1030  LYS B 1034  5                                   5    
HELIX   93 AK3 GLY B 1063  TYR B 1073  1                                  11    
HELIX   94 AK4 GLN B 1077  ARG B 1082  1                                   6    
HELIX   95 AK5 TYR B 1123  LEU B 1127  1                                   5    
HELIX   96 AK6 LEU B 1127  MET B 1135  1                                   9    
HELIX   97 AK7 ASN C   32  LYS C   38  1                                   7    
HELIX   98 AK8 ASP C   60  ILE C   72  1                                  13    
HELIX   99 AK9 GLN C   93  LEU C  103  1                                  11    
HELIX  100 AL1 ARG C  165  LEU C  167  5                                   3    
HELIX  101 AL2 GLU C  242  LYS C  249  1                                   8    
HELIX  102 AL3 ARG C  277  ARG C  281  5                                   5    
HELIX  103 AL4 THR C  309  LEU C  328  1                                  20    
HELIX  104 AL5 LYS C  329  CYS C  331  5                                   3    
HELIX  105 AL6 SER D   12  LYS D   26  1                                  15    
HELIX  106 AL7 GLU D   54  ASN D   64  1                                  11    
HELIX  107 AL8 SER D   67  PHE D   72  1                                   6    
HELIX  108 AL9 SER D   99  ALA D  104  1                                   6    
HELIX  109 AM1 LYS D  117  LEU D  121  5                                   5    
HELIX  110 AM2 HIS D  133  VAL D  138  1                                   6    
HELIX  111 AM3 LYS D  148  SER D  158  1                                  11    
HELIX  112 AM4 ASP E    2  GLU E    6  5                                   5    
HELIX  113 AM5 ARG E    7  GLY E   27  1                                  21    
HELIX  114 AM6 THR E   31  GLU E   36  1                                   6    
HELIX  115 AM7 PRO E   38  TYR E   46  1                                   9    
HELIX  116 AM8 THR E   65  PHE E   72  1                                   8    
HELIX  117 AM9 GLY E   89  GLN E  101  1                                  13    
HELIX  118 AN1 THR E  117  LYS E  122  5                                   6    
HELIX  119 AN2 SER E  157  LEU E  165  1                                   9    
HELIX  120 AN3 VAL E  184  GLY E  189  1                                   6    
HELIX  121 AN4 THR F   86  SER F  102  1                                  17    
HELIX  122 AN5 ASP F  116  GLU F  127  1                                  12    
HELIX  123 AN6 PRO G   14  PHE G   18  5                                   5    
HELIX  124 AN7 ASP G   21  ALA G   35  1                                  15    
HELIX  125 AN8 LEU G  207  TRP G  211  5                                   5    
HELIX  126 AN9 ASP I   18  GLY I   20  5                                   3    
HELIX  127 AO1 LYS J   17  GLU J   27  1                                  11    
HELIX  128 AO2 ASP J   31  GLY J   40  1                                  10    
HELIX  129 AO3 ARG J   43  THR J   52  1                                  10    
HELIX  130 AO4 LEU J   56  LEU J   61  1                                   6    
HELIX  131 AO5 ARG J   62  ASN J   64  5                                   3    
HELIX  132 AO6 LEU K   50  THR K   54  5                                   5    
HELIX  133 AO7 ASP K   69  LYS K   82  1                                  14    
HELIX  134 AO8 THR K  112  MET K  142  1                                  31    
HELIX  135 AO9 GLU M  127  TYR M  131  5                                   5    
HELIX  136 AP1 ASN M  132  TRP M  140  1                                   9    
HELIX  137 AP2 LYS M  184  ALA M  198  1                                  15    
HELIX  138 AP3 LEU M  231  VAL M  236  1                                   6    
HELIX  139 AP4 THR M  251  LYS M  261  1                                  11    
HELIX  140 AP5 LYS N  274  ALA N  278  5                                   5    
HELIX  141 AP6 GLU N  279  MET N  297  1                                  19    
HELIX  142 AP7 LEU O   37  THR O   41  1                                   5    
HELIX  143 AP8 ASP O   45  HIS O   56  1                                  12    
HELIX  144 AP9 GLY O   58  ARG O   60  5                                   3    
HELIX  145 AQ1 ALA O   61  ALA O   70  1                                  10    
HELIX  146 AQ2 SER O   75  ILE O   83  1                                   9    
HELIX  147 AQ3 ASP O   87  LEU O  101  1                                  15    
HELIX  148 AQ4 GLU O  125  SER O  133  1                                   9    
HELIX  149 AQ5 ILE O  136  MET O  144  1                                   9    
HELIX  150 AQ6 HIS O  152  ILE O  164  1                                  13    
HELIX  151 AQ7 VAL O  171  SER O  176  1                                   6    
HELIX  152 AQ8 LYS O  184  MET O  197  1                                  14    
HELIX  153 AQ9 GLU O  212  GLU O  220  1                                   9    
HELIX  154 AR1 SER O  233  LYS O  237  5                                   5    
HELIX  155 AR2 ARG O  238  ILE O  253  1                                  16    
HELIX  156 AR3 ILE O  253  GLU O  258  1                                   6    
HELIX  157 AR4 LEU O  284  ILE O  297  1                                  14    
HELIX  158 AR5 ILE O  297  VAL O  304  1                                   8    
HELIX  159 AR6 SER O  306  LEU O  318  1                                  13    
HELIX  160 AR7 ASP O  328  GLN O  332  5                                   5    
HELIX  161 AR8 ASP O  338  GLU O  348  1                                  11    
HELIX  162 AR9 GLU O  348  LYS O  355  1                                   8    
HELIX  163 AS1 LEU O  366  LEU O  370  5                                   5    
HELIX  164 AS2 ALA O  450  LEU O  457  1                                   8    
HELIX  165 AS3 LEU O  457  SER O  463  1                                   7    
HELIX  166 AS4 LEU O  483  LEU O  500  1                                  18    
HELIX  167 AS5 PRO O  502  ASN O  514  1                                  13    
HELIX  168 AS6 ILE O  521  ALA O  526  1                                   6    
HELIX  169 AS7 ASP O  532  ARG O  542  1                                  11    
HELIX  170 AS8 THR O  554  SER O  558  5                                   5    
HELIX  171 AS9 THR O  571  GLU O  598  1                                  28    
HELIX  172 AT1 ASN O  599  ALA O  606  1                                   8    
HELIX  173 AT2 LEU O  624  GLU O  649  1                                  26    
HELIX  174 AT3 VAL O  650  MET O  653  5                                   4    
HELIX  175 AT4 ILE P  175  GLU P  188  1                                  14    
HELIX  176 AT5 GLN P  219  THR P  226  1                                   8    
HELIX  177 AT6 THR P  236  ASP P  250  1                                  15    
HELIX  178 AT7 GLU P  266  MET P  271  1                                   6    
HELIX  179 AT8 THR Q   48  ASP Q   67  1                                  20    
HELIX  180 AT9 LEU U   82  LEU U   87  1                                   6    
HELIX  181 AU1 GLU U  129  GLN U  144  1                                  16    
HELIX  182 AU2 LEU U  172  HIS U  179  1                                   8    
HELIX  183 AU3 GLU U  221  SER U  235  1                                  15    
HELIX  184 AU4 GLU V   74  LEU V   94  1                                  21    
HELIX  185 AU5 PRO V   97  ASN V  114  1                                  18    
HELIX  186 AU6 ARG V  121  GLU V  137  1                                  17    
HELIX  187 AU7 SER V  153  LEU V  168  1                                  16    
HELIX  188 AU8 PRO V  178  ALA V  186  1                                   9    
HELIX  189 AU9 LYS V  195  ASP V  212  1                                  18    
HELIX  190 AV1 ARG V  219  ALA V  224  1                                   6    
HELIX  191 AV2 ALA V  226  MET V  234  1                                   9    
HELIX  192 AV3 ILE V  244  HIS V  249  1                                   6    
HELIX  193 AV4 ALA V  251  PHE V  262  1                                  12    
HELIX  194 AV5 LYS V  263  THR V  265  5                                   3    
HELIX  195 AV6 ALA V  267  VAL V  272  1                                   6    
HELIX  196 AV7 SER V  289  GLU V  297  1                                   9    
HELIX  197 AV8 THR V  448  SER V  453  1                                   6    
HELIX  198 AV9 GLU V  468  HIS V  473  1                                   6    
HELIX  199 AW1 ALA V  479  LEU V  490  1                                  12    
HELIX  200 AW2 ALA V  492  ALA V  510  1                                  19    
HELIX  201 AW3 PHE W  293  GLN W  319  1                                  27    
HELIX  202 AW4 ASN W  386  LYS W  394  1                                   9    
HELIX  203 AW5 THR W  421  TRP W  435  1                                  15    
HELIX  204 AW6 ASP W  438  TYR W  446  1                                   9    
HELIX  205 AW7 SER W  450  ARG W  465  1                                  16    
HELIX  206 AW8 ILE W  467  SER W  475  1                                   9    
HELIX  207 AW9 ASP W  482  LYS W  490  1                                   9    
HELIX  208 AX1 GLU W  500  ILE W  516  1                                  17    
SHEET    1 AA1 2 LYS A  11  ILE A  13  0                                        
SHEET    2 AA1 2 LEU B1143  ASP B1145 -1  O  GLU B1144   N  ARG A  12           
SHEET    1 AA2 2 GLU A  17  SER A  19  0                                        
SHEET    2 AA2 2 ALA B1138  ARG B1140 -1  O  ALA B1138   N  SER A  19           
SHEET    1 AA3 3 VAL A  32  GLU A  33  0                                        
SHEET    2 AA3 3 GLY A  82  HIS A  83  1  O  HIS A  83   N  VAL A  32           
SHEET    3 AA3 3 PRO A 262  ALA A 263 -1  O  ALA A 263   N  GLY A  82           
SHEET    1 AA4 2 VAL A 163  LYS A 166  0                                        
SHEET    2 AA4 2 ILE A 178  ASP A 181 -1  O  ILE A 179   N  LYS A 165           
SHEET    1 AA5 8 ALA B1037  ARG B1038  0                                        
SHEET    2 AA5 8 SER A 376  PRO A 383 -1  N  SER A 376   O  ARG B1038           
SHEET    3 AA5 8 GLU A 516  HIS A 520 -1  O  MET A 517   N  THR A 379           
SHEET    4 AA5 8 VAL A 471  ASN A 475 -1  N  LEU A 473   O  HIS A 520           
SHEET    5 AA5 8 ILE A 485  ARG A 493 -1  O  HIS A 488   N  VAL A 472           
SHEET    6 AA5 8 GLU A 391  PRO A 395  1  N  VAL A 392   O  TYR A 489           
SHEET    7 AA5 8 PHE A 498  LEU A 500 -1  O  ARG A 499   N  ALA A 393           
SHEET    8 AA5 8 SER A 376  PRO A 383  1  N  SER A 382   O  PHE A 498           
SHEET    1 AA6 4 THR A 403  LYS A 407  0                                        
SHEET    2 AA6 4 VAL A 461  HIS A 465 -1  O  VAL A 462   N  GLU A 406           
SHEET    3 AA6 4 ALA A 430  LEU A 434 -1  N  LEU A 434   O  VAL A 461           
SHEET    4 AA6 4 ARG A 442  ASN A 443 -1  O  ARG A 442   N  LEU A 433           
SHEET    1 AA7 2 PHE A 570  TYR A 571  0                                        
SHEET    2 AA7 2 TRP A 604  THR A 605 -1  O  TRP A 604   N  TYR A 571           
SHEET    1 AA8 2 ASN A 625  ALA A 628  0                                        
SHEET    2 AA8 2 VAL A 652  ARG A 655 -1  O  VAL A 652   N  ALA A 628           
SHEET    1 AA9 3 LEU A 896  GLN A 899  0                                        
SHEET    2 AA9 3 THR A 903  THR A 906 -1  O  THR A 903   N  GLN A 899           
SHEET    3 AA9 3 ILE A 911  GLN A 913 -1  O  VAL A 912   N  VAL A 904           
SHEET    1 AB1 3 ILE A1140  VAL A1144  0                                        
SHEET    2 AB1 3 ARG A1291  GLU A1296 -1  O  VAL A1295   N  ILE A1141           
SHEET    3 AB1 3 ALA A1281  ILE A1285 -1  N  VAL A1282   O  LEU A1294           
SHEET    1 AB2 2 THR A1164  LEU A1165  0                                        
SHEET    2 AB2 2 VAL A1271  LYS A1273 -1  O  LYS A1273   N  THR A1164           
SHEET    1 AB3 4 ALA A1170  VAL A1176  0                                        
SHEET    2 AB3 4 PHE A1183  ILE A1188 -1  O  GLN A1185   N  GLN A1174           
SHEET    3 AB3 4 ARG A1229  ASN A1233 -1  O  ILE A1230   N  VAL A1186           
SHEET    4 AB3 4 VAL A1222  ILE A1225 -1  N  ASN A1223   O  ALA A1231           
SHEET    1 AB4 4 ASP F 145  SER F 147  0                                        
SHEET    2 AB4 4 LEU F 132  ARG F 135 -1  N  ILE F 134   O  TRP F 146           
SHEET    3 AB4 4 LYS A1429  LYS A1432 -1  N  VAL A1431   O  VAL F 133           
SHEET    4 AB4 4 GLY G  57  GLN G  58 -1  O  GLY G  57   N  LYS A1432           
SHEET    1 AB5 5 ILE B  83  LEU B  84  0                                        
SHEET    2 AB5 5 TYR B  92  VAL B 100 -1  O  LEU B  93   N  ILE B  83           
SHEET    3 AB5 5 SER B 126  THR B 136 -1  O  TYR B 130   N  ARG B  99           
SHEET    4 AB5 5 ILE B 141  PRO B 153 -1  O  MET B 152   N  ALA B 127           
SHEET    5 AB5 5 LYS W 396  ASP W 398  1  O  VAL W 397   N  MET B 143           
SHEET    1 AB6 2 LYS B 192  ILE B 194  0                                        
SHEET    2 AB6 2 THR B 455  VAL B 457 -1  O  HIS B 456   N  VAL B 193           
SHEET    1 AB7 4 LYS B 375  GLU B 378  0                                        
SHEET    2 AB7 4 VAL B 196  LEU B 200 -1  N  GLN B 199   O  ARG B 376           
SHEET    3 AB7 4 ILE B 473  SER B 474  1  O  SER B 474   N  VAL B 196           
SHEET    4 AB7 4 VAL B 511  LYS B 512 -1  O  LYS B 512   N  ILE B 473           
SHEET    1 AB8 4 ILE B 205  VAL B 207  0                                        
SHEET    2 AB8 4 VAL B 216  THR B 221 -1  O  ALA B 218   N  ILE B 206           
SHEET    3 AB8 4 SER B 229  LYS B 236 -1  O  SER B 229   N  THR B 221           
SHEET    4 AB8 4 LYS B 239  HIS B 244 -1  O  LYS B 239   N  LYS B 236           
SHEET    1 AB9 3 HIS B 519  ILE B 520  0                                        
SHEET    2 AB9 3 ILE B 608  ILE B 613 -1  O  CYS B 609   N  HIS B 519           
SHEET    3 AB9 3 VAL B 646  ASP B 650 -1  O  LEU B 649   N  ARG B 610           
SHEET    1 AC1 3 THR B 560  LEU B 561  0                                        
SHEET    2 AC1 3 VAL B 555  LEU B 557 -1  N  LEU B 557   O  THR B 560           
SHEET    3 AC1 3 VAL B 599  ILE B 601  1  O  ILE B 601   N  TYR B 556           
SHEET    1 AC2 5 LEU B 724  MET B 728  0                                        
SHEET    2 AC2 5 CYS B 785  VAL B 794 -1  O  ARG B 788   N  LEU B 725           
SHEET    3 AC2 5 ALA B 894  ASN B 903 -1  O  GLN B 902   N  THR B 787           
SHEET    4 AC2 5 SER B 879  VAL B 888 -1  N  HIS B 880   O  ARG B 901           
SHEET    5 AC2 5 LYS B 835  VAL B 836 -1  N  VAL B 836   O  SER B 879           
SHEET    1 AC3 6 LEU B 724  MET B 728  0                                        
SHEET    2 AC3 6 CYS B 785  VAL B 794 -1  O  ARG B 788   N  LEU B 725           
SHEET    3 AC3 6 ALA B 894  ASN B 903 -1  O  GLN B 902   N  THR B 787           
SHEET    4 AC3 6 SER B 879  VAL B 888 -1  N  HIS B 880   O  ARG B 901           
SHEET    5 AC3 6 ILE L  55  LEU L  57 -1  O  LEU L  56   N  MET B 886           
SHEET    6 AC3 6 ILE L  30  CYS L  31 -1  N  ILE L  30   O  LEU L  57           
SHEET    1 AC4 2 VAL B 736  LYS B 737  0                                        
SHEET    2 AC4 2 GLU B 974  TYR B 975  1  O  GLU B 974   N  LYS B 737           
SHEET    1 AC5 2 GLN B 753  VAL B 759  0                                        
SHEET    2 AC5 2 PHE B1018  TYR B1024 -1  O  ILE B1022   N  ALA B 755           
SHEET    1 AC6 4 LYS B 911  PHE B 912  0                                        
SHEET    2 AC6 4 GLY B 920  VAL B 926 -1  O  GLY B 920   N  PHE B 912           
SHEET    3 AC6 4 ALA B 770  ASN B 774  1  N  LEU B 771   O  GLY B 923           
SHEET    4 AC6 4 ILE B 942  ILE B 943 -1  O  ILE B 943   N  VAL B 772           
SHEET    1 AC7 2 GLY B 839  ILE B 843  0                                        
SHEET    2 AC7 2 VAL B 871  TYR B 873 -1  O  VAL B 871   N  ILE B 843           
SHEET    1 AC8 2 SER B 846  PRO B 848  0                                        
SHEET    2 AC8 2 TYR B 866  GLU B 868 -1  O  ARG B 867   N  VAL B 847           
SHEET    1 AC9 2 ALA B1089  CYS B1095  0                                        
SHEET    2 AC9 2 ILE B1116  PRO B1122 -1  O  ILE B1117   N  VAL B1094           
SHEET    1 AD1 3 ILE C   4  VAL C   5  0                                        
SHEET    2 AD1 3 VAL C 289  VAL C 294 -1  O  ARG C 293   N  VAL C   5           
SHEET    3 AD1 3 PRO C 231  ILE C 235 -1  N  GLN C 232   O  GLY C 292           
SHEET    1 AD2 4 GLU C  41  ILE C  44  0                                        
SHEET    2 AD2 4 GLU C  51  ILE C  57 -1  O  ASP C  55   N  ASN C  43           
SHEET    3 AD2 4 HIS C 297  GLU C 303 -1  O  VAL C 302   N  ALA C  52           
SHEET    4 AD2 4 SER C 226  ARG C 228 -1  N  ARG C 228   O  ILE C 299           
SHEET    1 AD3 5 LYS C 168  GLU C 170  0                                        
SHEET    2 AD3 5 THR C 131  LYS C 139 -1  N  SER C 135   O  LYS C 168           
SHEET    3 AD3 5 GLU C 201  GLY C 211 -1  O  ALA C 206   N  LEU C 134           
SHEET    4 AD3 5 SER C  77  ASN C  88 -1  N  TYR C  84   O  LYS C 205           
SHEET    5 AD3 5 VAL L  65  GLU L  68 -1  O  VAL L  65   N  PHE C  85           
SHEET    1 AD4 2 THR C 141  ARG C 142  0                                        
SHEET    2 AD4 2 TYR C 157  ASN C 158 -1  O  ASN C 158   N  THR C 141           
SHEET    1 AD5 2 HIS C 161  TYR C 163  0                                        
SHEET    2 AD5 2 LEU C 192  LYS C 195 -1  O  ALA C 194   N  VAL C 162           
SHEET    1 AD6 2 ILE C 256  ASP C 259  0                                        
SHEET    2 AD6 2 GLU C 264  VAL C 267 -1  O  GLU C 264   N  ASP C 259           
SHEET    1 AD7 5 LYS D   2  VAL D   3  0                                        
SHEET    2 AD7 5 ILE G   3  ILE G  13 -1  O  ALA G   8   N  LYS D   2           
SHEET    3 AD7 5 SER G  66  VAL G  76 -1  O  ILE G  68   N  VAL G  11           
SHEET    4 AD7 5 GLY G  43  ILE G  48 -1  N  THR G  47   O  VAL G  75           
SHEET    5 AD7 5 LYS G  37  ILE G  39 -1  N  ILE G  39   O  GLY G  43           
SHEET    1 AD8 4 ALA D   9  PHE D  10  0                                        
SHEET    2 AD8 4 ILE G   3  ILE G  13 -1  O  LEU G   4   N  ALA D   9           
SHEET    3 AD8 4 SER G  66  VAL G  76 -1  O  ILE G  68   N  VAL G  11           
SHEET    4 AD8 4 THR G  53  VAL G  54 -1  N  THR G  53   O  THR G  71           
SHEET    1 AD9 4 PHE E  60  ALA E  62  0                                        
SHEET    2 AD9 4 SER E  77  GLU E  81 -1  O  LEU E  78   N  ALA E  62           
SHEET    3 AD9 4 PHE E 105  TYR E 112  1  O  ILE E 109   N  TRP E  79           
SHEET    4 AD9 4 GLU E 133  ASN E 136  1  O  GLU E 133   N  PHE E 110           
SHEET    1 AE1 4 HIS E 153  ARG E 155  0                                        
SHEET    2 AE1 4 VAL E 195  LYS E 201 -1  O  LYS E 197   N  ILE E 154           
SHEET    3 AE1 4 ARG E 207  MET E 215 -1  O  SER E 210   N  ILE E 198           
SHEET    4 AE1 4 ARG E 177  GLN E 179  1  N  ILE E 178   O  ILE E 213           
SHEET    1 AE2 3 ILE G  84  GLY G  87  0                                        
SHEET    2 AE2 3 ILE G 146  VAL G 154 -1  O  PHE G 148   N  VAL G  85           
SHEET    3 AE2 3 ALA G 195  SER G 199 -1  O  LEU G 197   N  ARG G 152           
SHEET    1 AE3 9 TYR H  95  VAL H  96  0                                        
SHEET    2 AE3 9 TYR H 141  ILE H 144 -1  O  ILE H 144   N  TYR H  95           
SHEET    3 AE3 9 SER H  54  ALA H  60 -1  N  ALA H  60   O  TYR H 141           
SHEET    4 AE3 9 THR H   4  ASP H  16 -1  N  ASP H   8   O  VAL H  57           
SHEET    5 AE3 9 VAL H  23  SER H  30 -1  O  ALA H  29   N  GLN H  11           
SHEET    6 AE3 9 LYS H  37  ASN H  43 -1  O  LEU H  40   N  ILE H  26           
SHEET    7 AE3 9 LEU H 122  GLY H 127 -1  O  GLU H 126   N  LYS H  37           
SHEET    8 AE3 9 LEU H 111  SER H 117 -1  N  VAL H 114   O  LEU H 125           
SHEET    9 AE3 9 THR H 100  SER H 108 -1  N  GLU H 105   O  ALA H 113           
SHEET    1 AE4 2 ILE I  14  SER I  16  0                                        
SHEET    2 AE4 2 TYR I  22  LEU I  24 -1  O  THR I  23   N  THR I  15           
SHEET    1 AE5 3 SER K  60  VAL K  66  0                                        
SHEET    2 AE5 3 LEU K 100  THR K 107 -1  O  LEU K 101   N  ILE K  65           
SHEET    3 AE5 3 VAL K  86  PHE K  88 -1  N  PHE K  88   O  GLN K 106           
SHEET    1 AE6 3 SER K  60  VAL K  66  0                                        
SHEET    2 AE6 3 LEU K 100  THR K 107 -1  O  LEU K 101   N  ILE K  65           
SHEET    3 AE6 3 TYR K  91  SER K  92 -1  N  SER K  92   O  ASN K 102           
SHEET    1 AE711 GLY M 152  GLU M 154  0                                        
SHEET    2 AE711 ARG M 175  ALA M 177 -1  O  VAL M 176   N  VAL M 153           
SHEET    3 AE711 SER M  84  TYR M  90  1  N  VAL M  87   O  ALA M 177           
SHEET    4 AE711 ASP N 393  ILE N 399 -1  O  ASP N 393   N  TYR M  90           
SHEET    5 AE711 ALA N 406  THR N 419 -1  O  LEU N 409   N  ALA N 396           
SHEET    6 AE711 PHE N 304  GLN N 308  1  N  PHE N 304   O  ASP N 413           
SHEET    7 AE711 TYR M 159  VAL M 163 -1  N  TYR M 159   O  PHE N 307           
SHEET    8 AE711 VAL M 168  PRO M 172 -1  O  VAL M 171   N  ALA M 160           
SHEET    9 AE711 GLU M  73  ILE M  78  1  N  LYS M  77   O  LEU M 170           
SHEET   10 AE711 SER N 362  VAL N 365 -1  O  ILE N 363   N  PHE M  74           
SHEET   11 AE711 LEU N 371  SER N 372 -1  O  SER N 372   N  ARG N 364           
SHEET    1 AE8 3 TRP M 247  ALA M 248  0                                        
SHEET    2 AE8 3 ALA N 406  THR N 419  1  O  ALA N 406   N  ALA M 248           
SHEET    3 AE8 3 GLY N 383  LYS N 384 -1  N  GLY N 383   O  THR N 419           
SHEET    1 AE9 2 ALA M 110  TYR M 112  0                                        
SHEET    2 AE9 2 ILE M 243  LEU M 245 -1  O  ILE M 243   N  TYR M 112           
SHEET    1 AF1 3 GLU M 120  ILE M 121  0                                        
SHEET    2 AF1 3 LEU M 148  LYS M 149 -1  O  LEU M 148   N  ILE M 121           
SHEET    3 AF1 3 LYS M 180  PRO M 181 -1  O  LYS M 180   N  LYS M 149           
SHEET    1 AF2 2 VAL O 104  TYR O 106  0                                        
SHEET    2 AF2 2 TYR O 120  TYR O 122 -1  O  TYR O 121   N  LYS O 105           
SHEET    1 AF3 2 GLU O 109  THR O 110  0                                        
SHEET    2 AF3 2 LYS O 116  THR O 117 -1  O  THR O 117   N  GLU O 109           
SHEET    1 AF4 2 LEU O 169  THR O 170  0                                        
SHEET    2 AF4 2 SER O 279  LEU O 280 -1  O  LEU O 280   N  LEU O 169           
SHEET    1 AF5 2 THR O 264  VAL O 265  0                                        
SHEET    2 AF5 2 ARG O 272  ILE O 273 -1  O  ILE O 273   N  THR O 264           
SHEET    1 AF6 2 GLN O 549  PRO O 552  0                                        
SHEET    2 AF6 2 ALA O 562  LEU O 565 -1  O  VAL O 563   N  VAL O 551           
SHEET    1 AF7 2 LEU P 253  VAL P 256  0                                        
SHEET    2 AF7 2 CYS P 260  VAL P 263 -1  O  ARG P 262   N  GLU P 254           
SHEET    1 AF8 6 ILE U 103  ARG U 105  0                                        
SHEET    2 AF8 6 THR U 112  ILE U 115 -1  O  ALA U 113   N  MET U 104           
SHEET    3 AF8 6 MET U 121  ALA U 126 -1  O  THR U 124   N  THR U 112           
SHEET    4 AF8 6 THR U  66  VAL U  74 -1  N  ALA U  72   O  VAL U 123           
SHEET    5 AF8 6 LYS U 156  SER U 163 -1  O  SER U 163   N  THR U  66           
SHEET    6 AF8 6 VAL U 213  ALA U 217 -1  O  LEU U 214   N  GLY U 162           
SHEET    1 AF9 2 LEU U 193  MET U 197  0                                        
SHEET    2 AF9 2 ILE U 202  ILE U 206 -1  O  ILE U 202   N  MET U 197           
SHEET    1 AG1 3 PHE V  12  ARG V  14  0                                        
SHEET    2 AG1 3 LEU V  23  CYS V  25 -1  O  VAL V  24   N  GLU V  13           
SHEET    3 AG1 3 VAL V  31  GLU V  33 -1  O  SER V  32   N  LEU V  23           
LINK         NE2 HIS A  80                ZN    ZN A1501     1555   1555  2.41  
LINK         N   CYS A 107                ZN    ZN A1502     1555   1555  2.08  
LINK         O   CYS A 107                ZN    ZN A1502     1555   1555  2.44  
LINK         SG  CYS A 107                ZN    ZN A1502     1555   1555  2.54  
LINK         O   CYS B1095                ZN    ZN B2000     1555   1555  2.70  
LINK         SG  CYS B1095                ZN    ZN B2000     1555   1555  2.43  
LINK         O   LYS B1097                ZN    ZN B2000     1555   1555  1.78  
LINK         SG  CYS I   5                ZN    ZN I2000     1555   1555  2.56  
LINK         SG  CYS I   8                ZN    ZN I2000     1555   1555  2.24  
LINK         SG  CYS I  26                ZN    ZN I2000     1555   1555  2.83  
LINK         SG  CYS J  10                ZN    ZN J2000     1555   1555  2.75  
LINK         SG  CYS L  34                ZN    ZN L2000     1555   1555  2.58  
LINK         SG  CYS L  48                ZN    ZN L2000     1555   1555  2.37  
LINK         O   LYS L  49                ZN    ZN L2000     1555   1555  2.60  
LINK         SG  CYS V  28                ZN    ZN V1001     1555   1555  2.79  
CISPEP   1 GLU U  108    PRO U  109          0        -2.43                     
SITE     1 AC1  4 CYS A  67  CYS A  70  HIS A  71  HIS A  80                    
SITE     1 AC2  5 ILE A 106  CYS A 107  LYS A 108  SER A 111                    
SITE     2 AC2  5 ALA A 112                                                     
SITE     1 AC3  5 CYS B1095  ASP B1096  LYS B1097  CYS B1098                    
SITE     2 AC3  5 GLY B1099                                                     
SITE     1 AC4  4 CYS I   5  CYS I   8  MET I  11  CYS I  26                    
SITE     1 AC5  3 CYS J  10  CYS J  45  CYS J  46                               
SITE     1 AC6  5 CYS L  31  CYS L  34  CYS L  48  LYS L  49                    
SITE     2 AC6  5 CYS L  51                                                     
SITE     1 AC7  5 CYS V   7  CYS V  25  ALA V  27  CYS V  28                    
SITE     2 AC7  5 GLY V  29                                                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  CA  LYS A   2     160.578 154.343 105.760  1.00174.97           C  
ATOM      2  C   LYS A   2     161.037 155.378 104.735  1.00174.97           C  
ATOM      3  O   LYS A   2     160.348 156.371 104.503  1.00174.97           O  
ATOM      4  CB  LYS A   2     160.149 153.053 105.059  1.00174.97           C  
ATOM      5  CG  LYS A   2     158.643 152.853 104.997  1.00174.97           C  
ATOM      6  CD  LYS A   2     158.261 151.856 103.915  1.00174.97           C  
ATOM      7  CE  LYS A   2     156.989 152.280 103.198  1.00174.97           C  
ATOM      8  NZ  LYS A   2     155.776 152.005 104.016  1.00174.97           N  
ATOM      9  N   GLU A   3     162.217 155.135 104.156  1.00176.08           N  
ATOM     10  CA  GLU A   3     162.916 156.039 103.241  1.00176.08           C  
ATOM     11  C   GLU A   3     162.898 157.488 103.723  1.00176.08           C  
ATOM     12  O   GLU A   3     162.853 158.419 102.911  1.00176.08           O  
ATOM     13  CB  GLU A   3     162.368 155.933 101.805  1.00176.08           C  
ATOM     14  CG  GLU A   3     160.933 156.388 101.557  1.00176.08           C  
ATOM     15  CD  GLU A   3     159.934 155.250 101.639  1.00176.08           C  
ATOM     16  OE1 GLU A   3     160.315 154.152 102.096  1.00176.08           O  
ATOM     17  OE2 GLU A   3     158.766 155.453 101.247  1.00176.08           O  
ATOM     18  N   VAL A   4     162.951 157.690 105.038  1.00172.11           N  
ATOM     19  CA  VAL A   4     162.873 159.019 105.630  1.00172.11           C  
ATOM     20  C   VAL A   4     164.109 159.228 106.494  1.00172.11           C  
ATOM     21  O   VAL A   4     164.711 158.271 106.993  1.00172.11           O  
ATOM     22  CB  VAL A   4     161.575 159.200 106.453  1.00172.11           C  
ATOM     23  CG1 VAL A   4     161.612 158.351 107.716  1.00172.11           C  
ATOM     24  CG2 VAL A   4     161.331 160.669 106.783  1.00172.11           C  
ATOM     25  N   VAL A   5     164.495 160.491 106.663  1.00174.15           N  
ATOM     26  CA  VAL A   5     165.701 160.845 107.399  1.00174.15           C  
ATOM     27  C   VAL A   5     165.315 161.450 108.742  1.00174.15           C  
ATOM     28  O   VAL A   5     164.241 162.042 108.899  1.00174.15           O  
ATOM     29  CB  VAL A   5     166.585 161.815 106.583  1.00174.15           C  
ATOM     30  CG1 VAL A   5     165.965 163.206 106.540  1.00174.15           C  
ATOM     31  CG2 VAL A   5     167.997 161.867 107.147  1.00174.15           C  
ATOM     32  N   VAL A   6     166.200 161.283 109.723  1.00174.71           N  
ATOM     33  CA  VAL A   6     166.068 161.911 111.032  1.00174.71           C  
ATOM     34  C   VAL A   6     167.389 162.588 111.369  1.00174.71           C  
ATOM     35  O   VAL A   6     168.464 162.043 111.093  1.00174.71           O  
ATOM     36  CB  VAL A   6     165.667 160.888 112.119  1.00174.71           C  
ATOM     37  CG1 VAL A   6     166.670 159.743 112.187  1.00174.71           C  
ATOM     38  CG2 VAL A   6     165.523 161.567 113.474  1.00174.71           C  
ATOM     39  N   SER A   7     167.313 163.786 111.947  1.00165.09           N  
ATOM     40  CA  SER A   7     168.509 164.546 112.307  1.00165.09           C  
ATOM     41  C   SER A   7     168.239 165.297 113.603  1.00165.09           C  
ATOM     42  O   SER A   7     167.417 166.218 113.627  1.00165.09           O  
ATOM     43  CB  SER A   7     168.906 165.512 111.190  1.00165.09           C  
ATOM     44  OG  SER A   7     170.058 166.256 111.547  1.00165.09           O  
ATOM     45  N   GLU A   8     168.924 164.905 114.675  1.00153.42           N  
ATOM     46  CA  GLU A   8     168.724 165.502 115.986  1.00153.42           C  
ATOM     47  C   GLU A   8     170.055 166.004 116.528  1.00153.42           C  
ATOM     48  O   GLU A   8     171.111 165.423 116.263  1.00153.42           O  
ATOM     49  CB  GLU A   8     168.090 164.501 116.969  1.00153.42           C  
ATOM     50  CG  GLU A   8     168.902 163.233 117.200  1.00153.42           C  
ATOM     51  CD  GLU A   8     169.874 163.360 118.358  1.00153.42           C  
ATOM     52  OE1 GLU A   8     169.670 164.248 119.212  1.00153.42           O  
ATOM     53  OE2 GLU A   8     170.840 162.571 118.414  1.00153.42           O  
ATOM     54  N   THR A   9     169.996 167.099 117.288  1.00143.73           N  
ATOM     55  CA  THR A   9     171.197 167.665 117.878  1.00143.73           C  
ATOM     56  C   THR A   9     171.211 167.436 119.388  1.00143.73           C  
ATOM     57  O   THR A   9     170.151 167.323 120.012  1.00143.73           O  
ATOM     58  CB  THR A   9     171.301 169.170 117.591  1.00143.73           C  
ATOM     59  OG1 THR A   9     172.490 169.699 118.192  1.00143.73           O  
ATOM     60  CG2 THR A   9     170.086 169.909 118.138  1.00143.73           C  
ATOM     61  N   PRO A  10     172.388 167.354 120.005  1.00134.60           N  
ATOM     62  CA  PRO A  10     172.449 167.440 121.469  1.00134.60           C  
ATOM     63  C   PRO A  10     172.106 168.843 121.941  1.00134.60           C  
ATOM     64  O   PRO A  10     172.510 169.837 121.332  1.00134.60           O  
ATOM     65  CB  PRO A  10     173.905 167.079 121.788  1.00134.60           C  
ATOM     66  CG  PRO A  10     174.651 167.364 120.521  1.00134.60           C  
ATOM     67  CD  PRO A  10     173.697 167.023 119.417  1.00134.60           C  
ATOM     68  N   LYS A  11     171.354 168.922 123.036  1.00122.75           N  
ATOM     69  CA  LYS A  11     170.833 170.194 123.509  1.00122.75           C  
ATOM     70  C   LYS A  11     171.129 170.377 124.991  1.00122.75           C  
ATOM     71  O   LYS A  11     171.435 169.425 125.714  1.00122.75           O  
ATOM     72  CB  LYS A  11     169.322 170.311 123.261  1.00122.75           C  
ATOM     73  CG  LYS A  11     168.952 170.568 121.810  1.00122.75           C  
ATOM     74  CD  LYS A  11     167.458 170.794 121.650  1.00122.75           C  
ATOM     75  CE  LYS A  11     167.093 171.050 120.198  1.00122.75           C  
ATOM     76  NZ  LYS A  11     167.628 172.354 119.717  1.00122.75           N  
ATOM     77  N   ARG A  12     171.031 171.629 125.429  1.00117.95           N  
ATOM     78  CA  ARG A  12     171.394 172.054 126.771  1.00117.95           C  
ATOM     79  C   ARG A  12     170.202 172.794 127.368  1.00117.95           C  
ATOM     80  O   ARG A  12     169.263 173.169 126.660  1.00117.95           O  
ATOM     81  CB  ARG A  12     172.657 172.934 126.748  1.00117.95           C  
ATOM     82  CG  ARG A  12     173.230 173.300 128.112  1.00117.95           C  
ATOM     83  CD  ARG A  12     174.401 174.260 127.986  1.00117.95           C  
ATOM     84  NE  ARG A  12     174.860 174.731 129.290  1.00117.95           N  
ATOM     85  CZ  ARG A  12     175.815 174.144 130.003  1.00117.95           C  
ATOM     86  NH1 ARG A  12     176.424 173.062 129.536  1.00117.95           N  
ATOM     87  NH2 ARG A  12     176.168 174.642 131.180  1.00117.95           N  
ATOM     88  N   ILE A  13     170.233 173.007 128.680  1.00109.40           N  
ATOM     89  CA  ILE A  13     169.221 173.801 129.367  1.00109.40           C  
ATOM     90  C   ILE A  13     169.825 175.162 129.683  1.00109.40           C  
ATOM     91  O   ILE A  13     170.798 175.259 130.441  1.00109.40           O  
ATOM     92  CB  ILE A  13     168.728 173.105 130.645  1.00109.40           C  
ATOM     93  CG1 ILE A  13     168.087 171.757 130.305  1.00109.40           C  
ATOM     94  CG2 ILE A  13     167.745 173.993 131.390  1.00109.40           C  
ATOM     95  CD1 ILE A  13     167.837 170.878 131.511  1.00109.40           C  
ATOM     96  N   LYS A  14     169.248 176.217 129.103  1.00116.00           N  
ATOM     97  CA  LYS A  14     169.781 177.561 129.280  1.00116.00           C  
ATOM     98  C   LYS A  14     169.381 178.181 130.611  1.00116.00           C  
ATOM     99  O   LYS A  14     170.003 179.161 131.035  1.00116.00           O  
ATOM    100  CB  LYS A  14     169.319 178.465 128.135  1.00116.00           C  
ATOM    101  CG  LYS A  14     167.830 178.775 128.155  1.00116.00           C  
ATOM    102  CD  LYS A  14     167.436 179.688 127.006  1.00116.00           C  
ATOM    103  CE  LYS A  14     167.953 181.100 127.222  1.00116.00           C  
ATOM    104  NZ  LYS A  14     167.285 181.764 128.375  1.00116.00           N  
ATOM    105  N   GLY A  15     168.364 177.638 131.272  1.00115.75           N  
ATOM    106  CA  GLY A  15     167.870 178.208 132.509  1.00115.75           C  
ATOM    107  C   GLY A  15     166.386 177.986 132.704  1.00115.75           C  
ATOM    108  O   GLY A  15     165.605 178.077 131.751  1.00115.75           O  
ATOM    109  N   LEU A  16     165.984 177.694 133.936  1.00112.56           N  
ATOM    110  CA  LEU A  16     164.582 177.466 134.238  1.00112.56           C  
ATOM    111  C   LEU A  16     163.818 178.787 134.271  1.00112.56           C  
ATOM    112  O   LEU A  16     164.383 179.860 134.496  1.00112.56           O  
ATOM    113  CB  LEU A  16     164.427 176.737 135.574  1.00112.56           C  
ATOM    114  CG  LEU A  16     164.434 175.205 135.555  1.00112.56           C  
ATOM    115  CD1 LEU A  16     163.272 174.672 134.728  1.00112.56           C  
ATOM    116  CD2 LEU A  16     165.760 174.652 135.048  1.00112.56           C  
ATOM    117  N   GLU A  17     162.513 178.697 134.031  1.00115.82           N  
ATOM    118  CA  GLU A  17     161.594 179.773 134.367  1.00115.82           C  
ATOM    119  C   GLU A  17     160.351 179.170 135.001  1.00115.82           C  
ATOM    120  O   GLU A  17     159.930 178.065 134.650  1.00115.82           O  
ATOM    121  CB  GLU A  17     161.219 180.616 133.138  1.00115.82           C  
ATOM    122  CG  GLU A  17     160.423 179.876 132.077  1.00115.82           C  
ATOM    123  CD  GLU A  17     160.127 180.742 130.869  1.00115.82           C  
ATOM    124  OE1 GLU A  17     160.581 181.905 130.845  1.00115.82           O  
ATOM    125  OE2 GLU A  17     159.434 180.264 129.947  1.00115.82           O  
ATOM    126  N   PHE A  18     159.770 179.901 135.945  1.00118.43           N  
ATOM    127  CA  PHE A  18     158.651 179.393 136.721  1.00118.43           C  
ATOM    128  C   PHE A  18     157.335 180.013 136.268  1.00118.43           C  
ATOM    129  O   PHE A  18     157.297 181.041 135.586  1.00118.43           O  
ATOM    130  CB  PHE A  18     158.862 179.638 138.217  1.00118.43           C  
ATOM    131  CG  PHE A  18     159.734 178.610 138.879  1.00118.43           C  
ATOM    132  CD1 PHE A  18     160.014 177.411 138.244  1.00118.43           C  
ATOM    133  CD2 PHE A  18     160.257 178.831 140.141  1.00118.43           C  
ATOM    134  CE1 PHE A  18     160.810 176.457 138.849  1.00118.43           C  
ATOM    135  CE2 PHE A  18     161.052 177.879 140.753  1.00118.43           C  
ATOM    136  CZ  PHE A  18     161.330 176.692 140.105  1.00118.43           C  
ATOM    137  N   SER A  19     156.250 179.362 136.671  1.00125.24           N  
ATOM    138  CA  SER A  19     154.886 179.781 136.387  1.00125.24           C  
ATOM    139  C   SER A  19     153.967 178.952 137.270  1.00125.24           C  
ATOM    140  O   SER A  19     154.332 177.861 137.714  1.00125.24           O  
ATOM    141  CB  SER A  19     154.528 179.604 134.908  1.00125.24           C  
ATOM    142  OG  SER A  19     153.160 179.893 134.675  1.00125.24           O  
ATOM    143  N   ALA A  20     152.777 179.482 137.527  1.00133.77           N  
ATOM    144  CA  ALA A  20     151.669 178.665 137.999  1.00133.77           C  
ATOM    145  C   ALA A  20     150.769 178.337 136.816  1.00133.77           C  
ATOM    146  O   ALA A  20     150.228 179.241 136.170  1.00133.77           O  
ATOM    147  CB  ALA A  20     150.883 179.385 139.095  1.00133.77           C  
ATOM    148  N   LEU A  21     150.618 177.045 136.538  1.00132.39           N  
ATOM    149  CA  LEU A  21     149.811 176.593 135.418  1.00132.39           C  
ATOM    150  C   LEU A  21     148.337 176.917 135.642  1.00132.39           C  
ATOM    151  O   LEU A  21     147.868 177.086 136.771  1.00132.39           O  
ATOM    152  CB  LEU A  21     150.014 175.093 135.187  1.00132.39           C  
ATOM    153  CG  LEU A  21     149.878 174.138 136.377  1.00132.39           C  
ATOM    154  CD1 LEU A  21     148.442 173.683 136.573  1.00132.39           C  
ATOM    155  CD2 LEU A  21     150.803 172.940 136.206  1.00132.39           C  
ATOM    156  N   SER A  22     147.604 177.002 134.536  1.00135.57           N  
ATOM    157  CA  SER A  22     146.258 177.548 134.536  1.00135.57           C  
ATOM    158  C   SER A  22     145.270 176.516 135.079  1.00135.57           C  
ATOM    159  O   SER A  22     145.629 175.386 135.421  1.00135.57           O  
ATOM    160  CB  SER A  22     145.869 178.000 133.131  1.00135.57           C  
ATOM    161  OG  SER A  22     145.706 176.891 132.264  1.00135.57           O  
ATOM    162  N   ALA A  23     144.001 176.912 135.156  1.00133.60           N  
ATOM    163  CA  ALA A  23     142.925 175.980 135.462  1.00133.60           C  
ATOM    164  C   ALA A  23     142.471 175.189 134.244  1.00133.60           C  
ATOM    165  O   ALA A  23     141.603 174.319 134.376  1.00133.60           O  
ATOM    166  CB  ALA A  23     141.735 176.729 136.067  1.00133.60           C  
ATOM    167  N   ALA A  24     143.034 175.469 133.069  1.00127.79           N  
ATOM    168  CA  ALA A  24     142.831 174.646 131.886  1.00127.79           C  
ATOM    169  C   ALA A  24     144.008 173.726 131.597  1.00127.79           C  
ATOM    170  O   ALA A  24     143.825 172.701 130.931  1.00127.79           O  
ATOM    171  CB  ALA A  24     142.570 175.529 130.659  1.00127.79           C  
ATOM    172  N   ASP A  25     145.204 174.069 132.080  1.00131.06           N  
ATOM    173  CA  ASP A  25     146.364 173.197 131.936  1.00131.06           C  
ATOM    174  C   ASP A  25     146.268 171.943 132.796  1.00131.06           C  
ATOM    175  O   ASP A  25     147.003 170.983 132.545  1.00131.06           O  
ATOM    176  CB  ASP A  25     147.643 173.963 132.277  1.00131.06           C  
ATOM    177  CG  ASP A  25     147.998 175.000 131.229  1.00131.06           C  
ATOM    178  OD1 ASP A  25     147.651 174.794 130.047  1.00131.06           O  
ATOM    179  OD2 ASP A  25     148.624 176.020 131.587  1.00131.06           O  
ATOM    180  N   ILE A  26     145.389 171.926 133.800  1.00124.25           N  
ATOM    181  CA  ILE A  26     145.344 170.796 134.725  1.00124.25           C  
ATOM    182  C   ILE A  26     144.805 169.556 134.021  1.00124.25           C  
ATOM    183  O   ILE A  26     145.355 168.456 134.155  1.00124.25           O  
ATOM    184  CB  ILE A  26     144.501 171.151 135.963  1.00124.25           C  
ATOM    185  CG1 ILE A  26     145.116 172.339 136.704  1.00124.25           C  
ATOM    186  CG2 ILE A  26     144.379 169.950 136.889  1.00124.25           C  
ATOM    187  CD1 ILE A  26     144.192 172.972 137.720  1.00124.25           C  
ATOM    188  N   VAL A  27     143.722 169.715 133.253  1.00124.91           N  
ATOM    189  CA  VAL A  27     143.135 168.594 132.521  1.00124.91           C  
ATOM    190  C   VAL A  27     143.830 168.339 131.196  1.00124.91           C  
ATOM    191  O   VAL A  27     143.433 167.422 130.465  1.00124.91           O  
ATOM    192  CB  VAL A  27     141.631 168.823 132.266  1.00124.91           C  
ATOM    193  CG1 VAL A  27     140.870 168.862 133.582  1.00124.91           C  
ATOM    194  CG2 VAL A  27     141.416 170.106 131.478  1.00124.91           C  
ATOM    195  N   ALA A  28     144.856 169.124 130.861  1.00127.92           N  
ATOM    196  CA  ALA A  28     145.579 168.930 129.609  1.00127.92           C  
ATOM    197  C   ALA A  28     146.411 167.652 129.634  1.00127.92           C  
ATOM    198  O   ALA A  28     146.231 166.764 128.793  1.00127.92           O  
ATOM    199  CB  ALA A  28     146.462 170.145 129.323  1.00127.92           C  
ATOM    200  N   GLN A  29     147.328 167.536 130.597  1.00138.26           N  
ATOM    201  CA  GLN A  29     148.137 166.329 130.714  1.00138.26           C  
ATOM    202  C   GLN A  29     147.473 165.224 131.522  1.00138.26           C  
ATOM    203  O   GLN A  29     147.914 164.071 131.441  1.00138.26           O  
ATOM    204  CB  GLN A  29     149.499 166.655 131.339  1.00138.26           C  
ATOM    205  CG  GLN A  29     149.445 167.005 132.817  1.00138.26           C  
ATOM    206  CD  GLN A  29     149.341 168.497 133.055  1.00138.26           C  
ATOM    207  OE1 GLN A  29     149.117 169.269 132.124  1.00138.26           O  
ATOM    208  NE2 GLN A  29     149.505 168.910 134.306  1.00138.26           N  
ATOM    209  N   SER A  30     146.435 165.533 132.293  1.00135.00           N  
ATOM    210  CA  SER A  30     145.694 164.486 132.979  1.00135.00           C  
ATOM    211  C   SER A  30     144.912 163.645 131.975  1.00135.00           C  
ATOM    212  O   SER A  30     144.495 164.126 130.918  1.00135.00           O  
ATOM    213  CB  SER A  30     144.743 165.093 134.010  1.00135.00           C  
ATOM    214  OG  SER A  30     143.917 164.098 134.589  1.00135.00           O  
ATOM    215  N   GLU A  31     144.715 162.371 132.315  1.00141.58           N  
ATOM    216  CA  GLU A  31     144.030 161.443 131.422  1.00141.58           C  
ATOM    217  C   GLU A  31     142.985 160.570 132.100  1.00141.58           C  
ATOM    218  O   GLU A  31     142.095 160.067 131.404  1.00141.58           O  
ATOM    219  CB  GLU A  31     145.047 160.534 130.715  1.00141.58           C  
ATOM    220  CG  GLU A  31     145.869 159.672 131.658  1.00141.58           C  
ATOM    221  CD  GLU A  31     147.000 158.952 130.953  1.00141.58           C  
ATOM    222  OE1 GLU A  31     147.188 159.180 129.739  1.00141.58           O  
ATOM    223  OE2 GLU A  31     147.705 158.160 131.613  1.00141.58           O  
ATOM    224  N   VAL A  32     143.053 160.370 133.412  1.00140.73           N  
ATOM    225  CA  VAL A  32     142.021 159.652 134.144  1.00140.73           C  
ATOM    226  C   VAL A  32     141.326 160.629 135.087  1.00140.73           C  
ATOM    227  O   VAL A  32     141.802 161.737 135.333  1.00140.73           O  
ATOM    228  CB  VAL A  32     142.590 158.444 134.912  1.00140.73           C  
ATOM    229  CG1 VAL A  32     143.250 157.468 133.954  1.00140.73           C  
ATOM    230  CG2 VAL A  32     143.577 158.908 135.961  1.00140.73           C  
ATOM    231  N   GLU A  33     140.182 160.206 135.620  1.00152.77           N  
ATOM    232  CA  GLU A  33     139.444 161.013 136.578  1.00152.77           C  
ATOM    233  C   GLU A  33     139.006 160.140 137.748  1.00152.77           C  
ATOM    234  O   GLU A  33     138.710 158.953 137.582  1.00152.77           O  
ATOM    235  CB  GLU A  33     138.240 161.689 135.901  1.00152.77           C  
ATOM    236  CG  GLU A  33     137.587 162.799 136.706  1.00152.77           C  
ATOM    237  CD  GLU A  33     136.515 162.293 137.636  1.00152.77           C  
ATOM    238  OE1 GLU A  33     135.870 161.279 137.296  1.00152.77           O  
ATOM    239  OE2 GLU A  33     136.311 162.915 138.699  1.00152.77           O  
ATOM    240  N   VAL A  34     138.974 160.741 138.937  1.00153.35           N  
ATOM    241  CA  VAL A  34     138.967 160.000 140.197  1.00153.35           C  
ATOM    242  C   VAL A  34     137.696 160.297 140.988  1.00153.35           C  
ATOM    243  O   VAL A  34     137.741 160.459 142.213  1.00153.35           O  
ATOM    244  CB  VAL A  34     140.230 160.307 141.024  1.00153.35           C  
ATOM    245  CG1 VAL A  34     141.439 159.628 140.402  1.00153.35           C  
ATOM    246  CG2 VAL A  34     140.463 161.800 141.093  1.00153.35           C  
ATOM    247  N   SER A  35     136.560 160.380 140.288  1.00158.36           N  
ATOM    248  CA  SER A  35     135.314 160.834 140.907  1.00158.36           C  
ATOM    249  C   SER A  35     134.913 159.983 142.108  1.00158.36           C  
ATOM    250  O   SER A  35     134.365 160.505 143.086  1.00158.36           O  
ATOM    251  CB  SER A  35     134.187 160.840 139.874  1.00158.36           C  
ATOM    252  OG  SER A  35     133.868 159.524 139.458  1.00158.36           O  
ATOM    253  N   THR A  36     135.165 158.678 142.061  1.00155.17           N  
ATOM    254  CA  THR A  36     134.719 157.843 143.165  1.00155.17           C  
ATOM    255  C   THR A  36     135.737 157.848 144.304  1.00155.17           C  
ATOM    256  O   THR A  36     136.830 158.411 144.205  1.00155.17           O  
ATOM    257  CB  THR A  36     134.470 156.412 142.690  1.00155.17           C  
ATOM    258  OG1 THR A  36     133.848 155.660 143.739  1.00155.17           O  
ATOM    259  CG2 THR A  36     135.781 155.744 142.309  1.00155.17           C  
ATOM    260  N   ARG A  37     135.355 157.203 145.405  1.00153.90           N  
ATOM    261  CA  ARG A  37     136.096 157.249 146.661  1.00153.90           C  
ATOM    262  C   ARG A  37     136.855 155.967 146.958  1.00153.90           C  
ATOM    263  O   ARG A  37     137.998 156.025 147.417  1.00153.90           O  
ATOM    264  CB  ARG A  37     135.140 157.556 147.824  1.00153.90           C  
ATOM    265  CG  ARG A  37     135.821 157.818 149.169  1.00153.90           C  
ATOM    266  CD  ARG A  37     135.904 156.567 150.039  1.00153.90           C  
ATOM    267  NE  ARG A  37     134.607 155.921 150.215  1.00153.90           N  
ATOM    268  CZ  ARG A  37     133.735 156.244 151.166  1.00153.90           C  
ATOM    269  NH1 ARG A  37     134.029 157.194 152.043  1.00153.90           N  
ATOM    270  NH2 ARG A  37     132.577 155.604 151.252  1.00153.90           N  
ATOM    271  N   ASP A  38     136.242 154.812 146.712  1.00169.85           N  
ATOM    272  CA  ASP A  38     136.745 153.557 147.255  1.00169.85           C  
ATOM    273  C   ASP A  38     138.028 153.144 146.546  1.00169.85           C  
ATOM    274  O   ASP A  38     138.074 153.061 145.315  1.00169.85           O  
ATOM    275  CB  ASP A  38     135.685 152.465 147.118  1.00169.85           C  
ATOM    276  CG  ASP A  38     135.979 151.253 147.981  1.00169.85           C  
ATOM    277  OD1 ASP A  38     137.001 151.261 148.698  1.00169.85           O  
ATOM    278  OD2 ASP A  38     135.184 150.290 147.943  1.00169.85           O  
ATOM    279  N   LEU A  39     139.075 152.886 147.332  1.00173.35           N  
ATOM    280  CA  LEU A  39     140.327 152.392 146.767  1.00173.35           C  
ATOM    281  C   LEU A  39     140.173 150.962 146.267  1.00173.35           C  
ATOM    282  O   LEU A  39     140.292 150.693 145.066  1.00173.35           O  
ATOM    283  CB  LEU A  39     141.449 152.482 147.804  1.00173.35           C  
ATOM    284  CG  LEU A  39     142.229 153.796 147.890  1.00173.35           C  
ATOM    285  CD1 LEU A  39     141.381 154.900 148.499  1.00173.35           C  
ATOM    286  CD2 LEU A  39     143.517 153.606 148.678  1.00173.35           C  
ATOM    287  N   PHE A  40     139.905 150.029 147.176  1.00190.30           N  
ATOM    288  CA  PHE A  40     139.786 148.618 146.832  1.00190.30           C  
ATOM    289  C   PHE A  40     138.332 148.290 146.510  1.00190.30           C  
ATOM    290  O   PHE A  40     137.440 148.517 147.335  1.00190.30           O  
ATOM    291  CB  PHE A  40     140.297 147.740 147.973  1.00190.30           C  
ATOM    292  CG  PHE A  40     141.786 147.801 148.166  1.00190.30           C  
ATOM    293  CD1 PHE A  40     142.611 148.266 147.155  1.00190.30           C  
ATOM    294  CD2 PHE A  40     142.360 147.394 149.359  1.00190.30           C  
ATOM    295  CE1 PHE A  40     143.981 148.325 147.331  1.00190.30           C  
ATOM    296  CE2 PHE A  40     143.730 147.450 149.540  1.00190.30           C  
ATOM    297  CZ  PHE A  40     144.541 147.916 148.525  1.00190.30           C  
ATOM    298  N   ASP A  41     138.101 147.758 145.314  1.00202.23           N  
ATOM    299  CA  ASP A  41     136.821 147.150 144.990  1.00202.23           C  
ATOM    300  C   ASP A  41     136.671 145.813 145.704  1.00202.23           C  
ATOM    301  O   ASP A  41     137.652 145.116 145.978  1.00202.23           O  
ATOM    302  CB  ASP A  41     136.695 146.939 143.482  1.00202.23           C  
ATOM    303  CG  ASP A  41     136.808 148.229 142.701  1.00202.23           C  
ATOM    304  OD1 ASP A  41     136.428 149.290 143.241  1.00202.23           O  
ATOM    305  OD2 ASP A  41     137.284 148.179 141.548  1.00202.23           O  
ATOM    306  N   LEU A  42     135.424 145.451 146.006  1.00211.36           N  
ATOM    307  CA  LEU A  42     135.147 144.207 146.708  1.00211.36           C  
ATOM    308  C   LEU A  42     134.942 143.038 145.751  1.00211.36           C  
ATOM    309  O   LEU A  42     134.371 142.014 146.145  1.00211.36           O  
ATOM    310  CB  LEU A  42     133.925 144.372 147.614  1.00211.36           C  
ATOM    311  CG  LEU A  42     134.127 145.256 148.847  1.00211.36           C  
ATOM    312  CD1 LEU A  42     132.817 145.446 149.595  1.00211.36           C  
ATOM    313  CD2 LEU A  42     135.192 144.669 149.760  1.00211.36           C  
ATOM    314  N   GLU A  43     135.397 143.175 144.503  1.00208.42           N  
ATOM    315  CA  GLU A  43     135.590 142.018 143.638  1.00208.42           C  
ATOM    316  C   GLU A  43     136.695 141.116 144.171  1.00208.42           C  
ATOM    317  O   GLU A  43     136.687 139.905 143.919  1.00208.42           O  
ATOM    318  CB  GLU A  43     135.907 142.480 142.215  1.00208.42           C  
ATOM    319  CG  GLU A  43     135.965 141.367 141.181  1.00208.42           C  
ATOM    320  CD  GLU A  43     136.327 141.879 139.800  1.00208.42           C  
ATOM    321  OE1 GLU A  43     136.572 143.096 139.660  1.00208.42           O  
ATOM    322  OE2 GLU A  43     136.365 141.066 138.853  1.00208.42           O  
ATOM    323  N   LYS A  44     137.649 141.699 144.899  1.00220.12           N  
ATOM    324  CA  LYS A  44     138.737 140.975 145.557  1.00220.12           C  
ATOM    325  C   LYS A  44     139.638 140.281 144.537  1.00220.12           C  
ATOM    326  O   LYS A  44     140.007 139.114 144.684  1.00220.12           O  
ATOM    327  CB  LYS A  44     138.195 139.977 146.586  1.00220.12           C  
ATOM    328  CG  LYS A  44     137.467 140.613 147.766  1.00220.12           C  
ATOM    329  CD  LYS A  44     138.433 141.257 148.755  1.00220.12           C  
ATOM    330  CE  LYS A  44     138.471 142.772 148.607  1.00220.12           C  
ATOM    331  NZ  LYS A  44     139.335 143.409 149.640  1.00220.12           N  
ATOM    332  N   ASP A  45     139.994 141.022 143.490  1.00228.23           N  
ATOM    333  CA  ASP A  45     141.258 140.832 142.802  1.00228.23           C  
ATOM    334  C   ASP A  45     142.370 141.514 143.599  1.00228.23           C  
ATOM    335  O   ASP A  45     142.117 142.270 144.541  1.00228.23           O  
ATOM    336  CB  ASP A  45     141.178 141.384 141.378  1.00228.23           C  
ATOM    337  CG  ASP A  45     142.315 140.901 140.496  1.00228.23           C  
ATOM    338  OD1 ASP A  45     143.177 140.146 140.992  1.00228.23           O  
ATOM    339  OD2 ASP A  45     142.343 141.275 139.305  1.00228.23           O  
ATOM    340  N   ARG A  46     143.620 141.243 143.222  1.00233.03           N  
ATOM    341  CA  ARG A  46     144.720 141.700 144.063  1.00233.03           C  
ATOM    342  C   ARG A  46     144.979 143.192 143.892  1.00233.03           C  
ATOM    343  O   ARG A  46     145.451 143.845 144.830  1.00233.03           O  
ATOM    344  CB  ARG A  46     145.987 140.901 143.747  1.00233.03           C  
ATOM    345  CG  ARG A  46     147.176 141.171 144.666  1.00233.03           C  
ATOM    346  CD  ARG A  46     147.024 140.510 146.032  1.00233.03           C  
ATOM    347  NE  ARG A  46     146.162 141.269 146.934  1.00233.03           N  
ATOM    348  CZ  ARG A  46     146.552 142.348 147.607  1.00233.03           C  
ATOM    349  NH1 ARG A  46     147.796 142.792 147.489  1.00233.03           N  
ATOM    350  NH2 ARG A  46     145.702 142.978 148.406  1.00233.03           N  
ATOM    351  N   ALA A  47     144.672 143.750 142.720  1.00206.27           N  
ATOM    352  CA  ALA A  47     144.755 145.188 142.471  1.00206.27           C  
ATOM    353  C   ALA A  47     143.376 145.724 142.096  1.00206.27           C  
ATOM    354  O   ALA A  47     143.154 146.134 140.948  1.00206.27           O  
ATOM    355  CB  ALA A  47     145.774 145.502 141.378  1.00206.27           C  
ATOM    356  N   PRO A  48     142.421 145.737 143.034  1.00195.51           N  
ATOM    357  CA  PRO A  48     141.061 146.149 142.664  1.00195.51           C  
ATOM    358  C   PRO A  48     140.877 147.660 142.662  1.00195.51           C  
ATOM    359  O   PRO A  48     140.714 148.275 143.721  1.00195.51           O  
ATOM    360  CB  PRO A  48     140.204 145.468 143.736  1.00195.51           C  
ATOM    361  CG  PRO A  48     141.089 145.470 144.960  1.00195.51           C  
ATOM    362  CD  PRO A  48     142.535 145.469 144.479  1.00195.51           C  
ATOM    363  N   LYS A  49     140.900 148.272 141.480  1.00178.61           N  
ATOM    364  CA  LYS A  49     140.895 149.727 141.352  1.00178.61           C  
ATOM    365  C   LYS A  49     139.895 150.123 140.273  1.00178.61           C  
ATOM    366  O   LYS A  49     140.149 149.905 139.084  1.00178.61           O  
ATOM    367  CB  LYS A  49     142.290 150.258 141.016  1.00178.61           C  
ATOM    368  CG  LYS A  49     143.203 150.451 142.220  1.00178.61           C  
ATOM    369  CD  LYS A  49     143.897 149.158 142.617  1.00178.61           C  
ATOM    370  CE  LYS A  49     144.781 149.356 143.836  1.00178.61           C  
ATOM    371  NZ  LYS A  49     145.335 148.066 144.331  1.00178.61           N  
ATOM    372  N   ALA A  50     138.760 150.700 140.673  1.00161.83           N  
ATOM    373  CA  ALA A  50     137.685 150.918 139.704  1.00161.83           C  
ATOM    374  C   ALA A  50     137.926 152.200 138.912  1.00161.83           C  
ATOM    375  O   ALA A  50     138.184 152.161 137.705  1.00161.83           O  
ATOM    376  CB  ALA A  50     136.330 150.962 140.418  1.00161.83           C  
ATOM    377  N   ASN A  51     137.844 153.342 139.581  1.00151.95           N  
ATOM    378  CA  ASN A  51     137.959 154.636 138.916  1.00151.95           C  
ATOM    379  C   ASN A  51     138.885 155.597 139.646  1.00151.95           C  
ATOM    380  O   ASN A  51     139.622 156.345 138.998  1.00151.95           O  
ATOM    381  CB  ASN A  51     136.567 155.269 138.756  1.00151.95           C  
ATOM    382  CG  ASN A  51     136.532 156.333 137.677  1.00151.95           C  
ATOM    383  OD1 ASN A  51     137.498 156.513 136.936  1.00151.95           O  
ATOM    384  ND2 ASN A  51     135.414 157.044 137.581  1.00151.95           N  
ATOM    385  N   GLY A  52     138.864 155.594 140.977  1.00159.46           N  
ATOM    386  CA  GLY A  52     139.390 156.691 141.767  1.00159.46           C  
ATOM    387  C   GLY A  52     140.508 156.291 142.707  1.00159.46           C  
ATOM    388  O   GLY A  52     140.533 156.721 143.864  1.00159.46           O  
ATOM    389  N   ALA A  53     141.436 155.473 142.229  1.00158.68           N  
ATOM    390  CA  ALA A  53     142.386 154.796 143.103  1.00158.68           C  
ATOM    391  C   ALA A  53     143.706 154.651 142.353  1.00158.68           C  
ATOM    392  O   ALA A  53     143.987 155.403 141.414  1.00158.68           O  
ATOM    393  CB  ALA A  53     141.809 153.452 143.579  1.00158.68           C  
ATOM    394  N   LEU A  54     144.521 153.681 142.769  1.00167.99           N  
ATOM    395  CA  LEU A  54     145.812 153.415 142.134  1.00167.99           C  
ATOM    396  C   LEU A  54     145.555 152.781 140.770  1.00167.99           C  
ATOM    397  O   LEU A  54     145.670 151.570 140.568  1.00167.99           O  
ATOM    398  CB  LEU A  54     146.673 152.520 143.016  1.00167.99           C  
ATOM    399  CG  LEU A  54     146.862 152.974 144.465  1.00167.99           C  
ATOM    400  CD1 LEU A  54     147.684 151.960 145.246  1.00167.99           C  
ATOM    401  CD2 LEU A  54     147.510 154.349 144.518  1.00167.99           C  
ATOM    402  N   ASP A  55     145.212 153.634 139.814  1.00155.95           N  
ATOM    403  CA  ASP A  55     144.593 153.202 138.568  1.00155.95           C  
ATOM    404  C   ASP A  55     145.652 152.623 137.635  1.00155.95           C  
ATOM    405  O   ASP A  55     146.721 153.220 137.475  1.00155.95           O  
ATOM    406  CB  ASP A  55     143.874 154.369 137.900  1.00155.95           C  
ATOM    407  CG  ASP A  55     143.106 153.951 136.667  1.00155.95           C  
ATOM    408  OD1 ASP A  55     142.018 153.356 136.813  1.00155.95           O  
ATOM    409  OD2 ASP A  55     143.589 154.222 135.551  1.00155.95           O  
ATOM    410  N   PRO A  56     145.395 151.471 137.007  1.00153.86           N  
ATOM    411  CA  PRO A  56     146.440 150.820 136.201  1.00153.86           C  
ATOM    412  C   PRO A  56     146.752 151.521 134.889  1.00153.86           C  
ATOM    413  O   PRO A  56     147.688 151.096 134.199  1.00153.86           O  
ATOM    414  CB  PRO A  56     145.865 149.420 135.950  1.00153.86           C  
ATOM    415  CG  PRO A  56     144.387 149.599 136.063  1.00153.86           C  
ATOM    416  CD  PRO A  56     144.184 150.641 137.122  1.00153.86           C  
ATOM    417  N   LYS A  57     146.018 152.570 134.515  1.00149.91           N  
ATOM    418  CA  LYS A  57     146.438 153.433 133.417  1.00149.91           C  
ATOM    419  C   LYS A  57     146.660 154.874 133.863  1.00149.91           C  
ATOM    420  O   LYS A  57     146.904 155.742 133.017  1.00149.91           O  
ATOM    421  CB  LYS A  57     145.434 153.369 132.259  1.00149.91           C  
ATOM    422  CG  LYS A  57     144.086 154.018 132.511  1.00149.91           C  
ATOM    423  CD  LYS A  57     143.151 153.772 131.334  1.00149.91           C  
ATOM    424  CE  LYS A  57     141.768 154.356 131.572  1.00149.91           C  
ATOM    425  NZ  LYS A  57     141.767 155.842 131.529  1.00149.91           N  
ATOM    426  N   MET A  58     146.582 155.152 135.167  1.00153.70           N  
ATOM    427  CA  MET A  58     147.311 156.285 135.726  1.00153.70           C  
ATOM    428  C   MET A  58     148.778 155.936 135.944  1.00153.70           C  
ATOM    429  O   MET A  58     149.666 156.744 135.650  1.00153.70           O  
ATOM    430  CB  MET A  58     146.686 156.721 137.053  1.00153.70           C  
ATOM    431  CG  MET A  58     147.437 157.857 137.739  1.00153.70           C  
ATOM    432  SD  MET A  58     146.822 158.270 139.387  1.00153.70           S  
ATOM    433  CE  MET A  58     145.358 159.222 139.004  1.00153.70           C  
ATOM    434  N   GLY A  59     149.039 154.740 136.451  1.00151.99           N  
ATOM    435  CA  GLY A  59     150.398 154.317 136.711  1.00151.99           C  
ATOM    436  C   GLY A  59     150.403 152.896 137.219  1.00151.99           C  
ATOM    437  O   GLY A  59     149.479 152.124 136.954  1.00151.99           O  
ATOM    438  N   VAL A  60     151.455 152.554 137.956  1.00156.43           N  
ATOM    439  CA  VAL A  60     151.615 151.208 138.497  1.00156.43           C  
ATOM    440  C   VAL A  60     152.488 151.295 139.741  1.00156.43           C  
ATOM    441  O   VAL A  60     153.544 151.934 139.727  1.00156.43           O  
ATOM    442  CB  VAL A  60     152.211 150.243 137.452  1.00156.43           C  
ATOM    443  CG1 VAL A  60     153.442 150.853 136.794  1.00156.43           C  
ATOM    444  CG2 VAL A  60     152.539 148.904 138.087  1.00156.43           C  
ATOM    445  N   SER A  61     152.039 150.661 140.826  1.00165.54           N  
ATOM    446  CA  SER A  61     152.761 150.669 142.093  1.00165.54           C  
ATOM    447  C   SER A  61     153.182 149.265 142.515  1.00165.54           C  
ATOM    448  O   SER A  61     153.358 148.995 143.704  1.00165.54           O  
ATOM    449  CB  SER A  61     151.918 151.326 143.186  1.00165.54           C  
ATOM    450  OG  SER A  61     152.613 151.350 144.420  1.00165.54           O  
ATOM    451  N   SER A  62     153.346 148.360 141.552  1.00170.05           N  
ATOM    452  CA  SER A  62     153.784 147.003 141.838  1.00170.05           C  
ATOM    453  C   SER A  62     154.681 146.513 140.713  1.00170.05           C  
ATOM    454  O   SER A  62     154.593 146.987 139.578  1.00170.05           O  
ATOM    455  CB  SER A  62     152.592 146.050 142.013  1.00170.05           C  
ATOM    456  OG  SER A  62     151.802 146.419 143.129  1.00170.05           O  
ATOM    457  N   SER A  63     155.549 145.559 141.037  1.00176.64           N  
ATOM    458  CA  SER A  63     156.414 144.944 140.040  1.00176.64           C  
ATOM    459  C   SER A  63     155.740 143.793 139.304  1.00176.64           C  
ATOM    460  O   SER A  63     156.385 143.149 138.469  1.00176.64           O  
ATOM    461  CB  SER A  63     157.707 144.448 140.696  1.00176.64           C  
ATOM    462  OG  SER A  63     158.559 143.837 139.743  1.00176.64           O  
ATOM    463  N   SER A  64     154.467 143.521 139.588  1.00178.25           N  
ATOM    464  CA  SER A  64     153.742 142.425 138.962  1.00178.25           C  
ATOM    465  C   SER A  64     152.640 142.894 138.023  1.00178.25           C  
ATOM    466  O   SER A  64     151.967 142.056 137.414  1.00178.25           O  
ATOM    467  CB  SER A  64     153.147 141.505 140.035  1.00178.25           C  
ATOM    468  OG  SER A  64     152.158 142.177 140.794  1.00178.25           O  
ATOM    469  N   LEU A  65     152.433 144.200 137.889  1.00167.18           N  
ATOM    470  CA  LEU A  65     151.357 144.744 137.077  1.00167.18           C  
ATOM    471  C   LEU A  65     151.924 145.314 135.777  1.00167.18           C  
ATOM    472  O   LEU A  65     153.119 145.192 135.486  1.00167.18           O  
ATOM    473  CB  LEU A  65     150.582 145.800 137.870  1.00167.18           C  
ATOM    474  CG  LEU A  65     149.363 145.338 138.676  1.00167.18           C  
ATOM    475  CD1 LEU A  65     148.296 144.756 137.760  1.00167.18           C  
ATOM    476  CD2 LEU A  65     149.753 144.340 139.759  1.00167.18           C  
ATOM    477  N   GLU A  66     151.052 145.938 134.989  1.00160.52           N  
ATOM    478  CA  GLU A  66     151.416 146.512 133.700  1.00160.52           C  
ATOM    479  C   GLU A  66     150.818 147.905 133.587  1.00160.52           C  
ATOM    480  O   GLU A  66     149.605 148.075 133.747  1.00160.52           O  
ATOM    481  CB  GLU A  66     150.930 145.630 132.544  1.00160.52           C  
ATOM    482  CG  GLU A  66     151.171 146.220 131.162  1.00160.52           C  
ATOM    483  CD  GLU A  66     152.643 146.350 130.824  1.00160.52           C  
ATOM    484  OE1 GLU A  66     153.449 145.548 131.342  1.00160.52           O  
ATOM    485  OE2 GLU A  66     152.995 147.254 130.038  1.00160.52           O  
ATOM    486  N   CYS A  67     151.663 148.897 133.312  1.00151.47           N  
ATOM    487  CA  CYS A  67     151.174 150.251 133.079  1.00151.47           C  
ATOM    488  C   CYS A  67     150.452 150.292 131.738  1.00151.47           C  
ATOM    489  O   CYS A  67     151.085 150.240 130.679  1.00151.47           O  
ATOM    490  CB  CYS A  67     152.329 151.247 133.111  1.00151.47           C  
ATOM    491  SG  CYS A  67     151.817 152.975 132.978  1.00151.47           S  
ATOM    492  N   ALA A  68     149.122 150.386 131.784  1.00145.28           N  
ATOM    493  CA  ALA A  68     148.317 150.290 130.573  1.00145.28           C  
ATOM    494  C   ALA A  68     148.474 151.493 129.653  1.00145.28           C  
ATOM    495  O   ALA A  68     148.180 151.380 128.458  1.00145.28           O  
ATOM    496  CB  ALA A  68     146.843 150.111 130.937  1.00145.28           C  
ATOM    497  N   THR A  69     148.926 152.637 130.170  1.00148.65           N  
ATOM    498  CA  THR A  69     149.034 153.823 129.325  1.00148.65           C  
ATOM    499  C   THR A  69     150.257 153.769 128.414  1.00148.65           C  
ATOM    500  O   THR A  69     150.126 153.740 127.186  1.00148.65           O  
ATOM    501  CB  THR A  69     149.073 155.081 130.198  1.00148.65           C  
ATOM    502  OG1 THR A  69     147.831 155.215 130.901  1.00148.65           O  
ATOM    503  CG2 THR A  69     149.301 156.317 129.343  1.00148.65           C  
ATOM    504  N   CYS A  70     151.457 153.752 128.995  1.00154.02           N  
ATOM    505  CA  CYS A  70     152.678 153.972 128.208  1.00154.02           C  
ATOM    506  C   CYS A  70     153.276 152.656 127.718  1.00154.02           C  
ATOM    507  O   CYS A  70     153.287 152.383 126.515  1.00154.02           O  
ATOM    508  CB  CYS A  70     153.694 154.769 129.030  1.00154.02           C  
ATOM    509  SG  CYS A  70     154.255 153.946 130.538  1.00154.02           S  
ATOM    510  N   HIS A  71     153.842 151.879 128.646  1.00159.13           N  
ATOM    511  CA  HIS A  71     153.796 150.423 128.780  1.00159.13           C  
ATOM    512  C   HIS A  71     154.801 150.034 129.856  1.00159.13           C  
ATOM    513  O   HIS A  71     155.491 150.902 130.399  1.00159.13           O  
ATOM    514  CB  HIS A  71     154.100 149.665 127.480  1.00159.13           C  
ATOM    515  CG  HIS A  71     152.914 149.485 126.581  1.00159.13           C  
ATOM    516  ND1 HIS A  71     151.823 148.723 126.939  1.00159.13           N  
ATOM    517  CD2 HIS A  71     152.673 149.915 125.319  1.00159.13           C  
ATOM    518  CE1 HIS A  71     150.943 148.725 125.954  1.00159.13           C  
ATOM    519  NE2 HIS A  71     151.434 149.441 124.959  1.00159.13           N  
ATOM    520  N   GLY A  72     154.893 148.753 130.182  1.00161.32           N  
ATOM    521  CA  GLY A  72     155.934 148.275 131.067  1.00161.32           C  
ATOM    522  C   GLY A  72     155.400 147.950 132.452  1.00161.32           C  
ATOM    523  O   GLY A  72     154.289 148.320 132.834  1.00161.32           O  
ATOM    524  N   ASN A  73     156.230 147.232 133.209  1.00154.17           N  
ATOM    525  CA  ASN A  73     155.814 146.729 134.514  1.00154.17           C  
ATOM    526  C   ASN A  73     156.142 147.730 135.620  1.00154.17           C  
ATOM    527  O   ASN A  73     155.238 148.228 136.298  1.00154.17           O  
ATOM    528  CB  ASN A  73     156.463 145.365 134.788  1.00154.17           C  
ATOM    529  CG  ASN A  73     157.960 145.366 134.542  1.00154.17           C  
ATOM    530  OD1 ASN A  73     158.552 146.404 134.246  1.00154.17           O  
ATOM    531  ND2 ASN A  73     158.580 144.198 134.664  1.00154.17           N  
ATOM    532  N   LEU A  74     157.418 148.029 135.818  1.00146.44           N  
ATOM    533  CA  LEU A  74     157.757 149.051 136.802  1.00146.44           C  
ATOM    534  C   LEU A  74     158.786 150.047 136.288  1.00146.44           C  
ATOM    535  O   LEU A  74     158.681 151.240 136.587  1.00146.44           O  
ATOM    536  CB  LEU A  74     158.262 148.377 138.096  1.00146.44           C  
ATOM    537  CG  LEU A  74     158.186 149.147 139.421  1.00146.44           C  
ATOM    538  CD1 LEU A  74     159.330 150.148 139.581  1.00146.44           C  
ATOM    539  CD2 LEU A  74     156.843 149.846 139.549  1.00146.44           C  
ATOM    540  N   ALA A  75     159.778 149.593 135.519  1.00142.49           N  
ATOM    541  CA  ALA A  75     160.862 150.480 135.115  1.00142.49           C  
ATOM    542  C   ALA A  75     160.472 151.379 133.949  1.00142.49           C  
ATOM    543  O   ALA A  75     161.007 152.487 133.820  1.00142.49           O  
ATOM    544  CB  ALA A  75     162.102 149.664 134.749  1.00142.49           C  
ATOM    545  N   SER A  76     159.550 150.927 133.096  1.00145.43           N  
ATOM    546  CA  SER A  76     159.175 151.688 131.910  1.00145.43           C  
ATOM    547  C   SER A  76     158.161 152.786 132.200  1.00145.43           C  
ATOM    548  O   SER A  76     158.054 153.734 131.413  1.00145.43           O  
ATOM    549  CB  SER A  76     158.622 150.749 130.837  1.00145.43           C  
ATOM    550  OG  SER A  76     159.601 149.814 130.419  1.00145.43           O  
ATOM    551  N   CYS A  77     157.418 152.684 133.298  1.00143.10           N  
ATOM    552  CA  CYS A  77     156.432 153.702 133.641  1.00143.10           C  
ATOM    553  C   CYS A  77     157.129 154.956 134.153  1.00143.10           C  
ATOM    554  O   CYS A  77     157.876 154.904 135.135  1.00143.10           O  
ATOM    555  CB  CYS A  77     155.460 153.163 134.687  1.00143.10           C  
ATOM    556  SG  CYS A  77     154.214 154.353 135.235  1.00143.10           S  
ATOM    557  N   HIS A  78     156.886 156.083 133.488  1.00136.14           N  
ATOM    558  CA  HIS A  78     157.377 157.372 133.953  1.00136.14           C  
ATOM    559  C   HIS A  78     156.367 158.110 134.821  1.00136.14           C  
ATOM    560  O   HIS A  78     156.676 159.199 135.317  1.00136.14           O  
ATOM    561  CB  HIS A  78     157.770 158.248 132.758  1.00136.14           C  
ATOM    562  CG  HIS A  78     158.965 157.745 132.009  1.00136.14           C  
ATOM    563  ND1 HIS A  78     159.409 158.324 130.839  1.00136.14           N  
ATOM    564  CD2 HIS A  78     159.809 156.717 132.264  1.00136.14           C  
ATOM    565  CE1 HIS A  78     160.475 157.674 130.406  1.00136.14           C  
ATOM    566  NE2 HIS A  78     160.738 156.695 131.253  1.00136.14           N  
ATOM    567  N   GLY A  79     155.174 157.551 135.016  1.00138.48           N  
ATOM    568  CA  GLY A  79     154.134 158.224 135.767  1.00138.48           C  
ATOM    569  C   GLY A  79     153.246 159.129 134.939  1.00138.48           C  
ATOM    570  O   GLY A  79     153.711 159.771 133.993  1.00138.48           O  
ATOM    571  N   HIS A  80     151.961 159.189 135.286  1.00138.69           N  
ATOM    572  CA  HIS A  80     150.993 159.993 134.554  1.00138.69           C  
ATOM    573  C   HIS A  80     150.051 160.653 135.548  1.00138.69           C  
ATOM    574  O   HIS A  80     149.705 160.060 136.574  1.00138.69           O  
ATOM    575  CB  HIS A  80     150.189 159.146 133.560  1.00138.69           C  
ATOM    576  CG  HIS A  80     151.026 158.215 132.741  1.00138.69           C  
ATOM    577  ND1 HIS A  80     151.801 158.643 131.684  1.00138.69           N  
ATOM    578  CD2 HIS A  80     151.211 156.876 132.824  1.00138.69           C  
ATOM    579  CE1 HIS A  80     152.426 157.608 131.152  1.00138.69           C  
ATOM    580  NE2 HIS A  80     152.085 156.524 131.826  1.00138.69           N  
ATOM    581  N   PHE A  81     149.640 161.878 135.241  1.00135.07           N  
ATOM    582  CA  PHE A  81     148.854 162.676 136.168  1.00135.07           C  
ATOM    583  C   PHE A  81     147.365 162.381 136.032  1.00135.07           C  
ATOM    584  O   PHE A  81     146.871 162.044 134.952  1.00135.07           O  
ATOM    585  CB  PHE A  81     149.108 164.169 135.945  1.00135.07           C  
ATOM    586  CG  PHE A  81     150.439 164.641 136.456  1.00135.07           C  
ATOM    587  CD1 PHE A  81     150.596 165.006 137.783  1.00135.07           C  
ATOM    588  CD2 PHE A  81     151.534 164.720 135.611  1.00135.07           C  
ATOM    589  CE1 PHE A  81     151.819 165.441 138.259  1.00135.07           C  
ATOM    590  CE2 PHE A  81     152.760 165.155 136.080  1.00135.07           C  
ATOM    591  CZ  PHE A  81     152.902 165.515 137.406  1.00135.07           C  
ATOM    592  N   GLY A  82     146.653 162.514 137.151  1.00139.77           N  
ATOM    593  CA  GLY A  82     145.211 162.576 137.167  1.00139.77           C  
ATOM    594  C   GLY A  82     144.743 163.962 137.584  1.00139.77           C  
ATOM    595  O   GLY A  82     145.534 164.874 137.811  1.00139.77           O  
ATOM    596  N   HIS A  83     143.423 164.110 137.677  1.00136.29           N  
ATOM    597  CA  HIS A  83     142.866 165.393 138.080  1.00136.29           C  
ATOM    598  C   HIS A  83     141.580 165.185 138.866  1.00136.29           C  
ATOM    599  O   HIS A  83     140.904 164.161 138.738  1.00136.29           O  
ATOM    600  CB  HIS A  83     142.601 166.292 136.867  1.00136.29           C  
ATOM    601  CG  HIS A  83     141.452 165.839 136.021  1.00136.29           C  
ATOM    602  ND1 HIS A  83     141.554 164.800 135.121  1.00136.29           N  
ATOM    603  CD2 HIS A  83     140.175 166.282 135.940  1.00136.29           C  
ATOM    604  CE1 HIS A  83     140.390 164.624 134.521  1.00136.29           C  
ATOM    605  NE2 HIS A  83     139.536 165.510 135.000  1.00136.29           N  
ATOM    606  N   LEU A  84     141.256 166.180 139.685  1.00131.80           N  
ATOM    607  CA  LEU A  84     139.996 166.281 140.406  1.00131.80           C  
ATOM    608  C   LEU A  84     139.158 167.428 139.856  1.00131.80           C  
ATOM    609  O   LEU A  84     139.626 168.260 139.073  1.00131.80           O  
ATOM    610  CB  LEU A  84     140.236 166.470 141.909  1.00131.80           C  
ATOM    611  CG  LEU A  84     140.359 165.195 142.742  1.00131.80           C  
ATOM    612  CD1 LEU A  84     140.830 165.502 144.149  1.00131.80           C  
ATOM    613  CD2 LEU A  84     139.008 164.512 142.788  1.00131.80           C  
ATOM    614  N   LYS A  85     137.897 167.460 140.281  1.00132.09           N  
ATOM    615  CA  LYS A  85     137.013 168.591 140.038  1.00132.09           C  
ATOM    616  C   LYS A  85     136.323 168.941 141.346  1.00132.09           C  
ATOM    617  O   LYS A  85     135.721 168.072 141.985  1.00132.09           O  
ATOM    618  CB  LYS A  85     135.976 168.269 138.956  1.00132.09           C  
ATOM    619  CG  LYS A  85     134.951 169.369 138.727  1.00132.09           C  
ATOM    620  CD  LYS A  85     134.096 169.087 137.501  1.00132.09           C  
ATOM    621  CE  LYS A  85     133.026 170.152 137.317  1.00132.09           C  
ATOM    622  NZ  LYS A  85     133.613 171.488 137.020  1.00132.09           N  
ATOM    623  N   LEU A  86     136.409 170.207 141.740  1.00128.22           N  
ATOM    624  CA  LEU A  86     135.759 170.688 142.949  1.00128.22           C  
ATOM    625  C   LEU A  86     134.413 171.324 142.628  1.00128.22           C  
ATOM    626  O   LEU A  86     134.186 171.826 141.524  1.00128.22           O  
ATOM    627  CB  LEU A  86     136.649 171.698 143.677  1.00128.22           C  
ATOM    628  CG  LEU A  86     138.005 171.172 144.152  1.00128.22           C  
ATOM    629  CD1 LEU A  86     138.829 172.288 144.777  1.00128.22           C  
ATOM    630  CD2 LEU A  86     137.823 170.022 145.131  1.00128.22           C  
ATOM    631  N   ALA A  87     133.515 171.294 143.615  1.00126.71           N  
ATOM    632  CA  ALA A  87     132.198 171.894 143.435  1.00126.71           C  
ATOM    633  C   ALA A  87     132.277 173.414 143.479  1.00126.71           C  
ATOM    634  O   ALA A  87     131.581 174.103 142.724  1.00126.71           O  
ATOM    635  CB  ALA A  87     131.232 171.372 144.497  1.00126.71           C  
ATOM    636  N   LEU A  88     133.118 173.952 144.359  1.00136.53           N  
ATOM    637  CA  LEU A  88     133.288 175.385 144.547  1.00136.53           C  
ATOM    638  C   LEU A  88     134.699 175.635 145.057  1.00136.53           C  
ATOM    639  O   LEU A  88     135.236 174.815 145.811  1.00136.53           O  
ATOM    640  CB  LEU A  88     132.237 175.960 145.512  1.00136.53           C  
ATOM    641  CG  LEU A  88     132.331 175.723 147.019  1.00136.53           C  
ATOM    642  CD1 LEU A  88     131.432 176.712 147.742  1.00136.53           C  
ATOM    643  CD2 LEU A  88     131.953 174.295 147.381  1.00136.53           C  
ATOM    644  N   PRO A  89     135.324 176.743 144.663  1.00134.70           N  
ATOM    645  CA  PRO A  89     136.767 176.900 144.878  1.00134.70           C  
ATOM    646  C   PRO A  89     137.137 177.086 146.343  1.00134.70           C  
ATOM    647  O   PRO A  89     136.316 177.437 147.194  1.00134.70           O  
ATOM    648  CB  PRO A  89     137.110 178.155 144.067  1.00134.70           C  
ATOM    649  CG  PRO A  89     136.023 178.255 143.046  1.00134.70           C  
ATOM    650  CD  PRO A  89     134.792 177.771 143.753  1.00134.70           C  
ATOM    651  N   VAL A  90     138.419 176.838 146.619  1.00137.18           N  
ATOM    652  CA  VAL A  90     139.045 177.084 147.912  1.00137.18           C  
ATOM    653  C   VAL A  90     140.360 177.822 147.678  1.00137.18           C  
ATOM    654  O   VAL A  90     140.812 177.988 146.545  1.00137.18           O  
ATOM    655  CB  VAL A  90     139.287 175.785 148.708  1.00137.18           C  
ATOM    656  CG1 VAL A  90     137.965 175.138 149.090  1.00137.18           C  
ATOM    657  CG2 VAL A  90     140.146 174.822 147.902  1.00137.18           C  
ATOM    658  N   PHE A  91     140.974 178.265 148.774  1.00138.53           N  
ATOM    659  CA  PHE A  91     142.252 178.955 148.677  1.00138.53           C  
ATOM    660  C   PHE A  91     143.382 177.986 148.337  1.00138.53           C  
ATOM    661  O   PHE A  91     143.290 176.772 148.540  1.00138.53           O  
ATOM    662  CB  PHE A  91     142.602 179.673 149.984  1.00138.53           C  
ATOM    663  CG  PHE A  91     141.780 180.899 150.256  1.00138.53           C  
ATOM    664  CD1 PHE A  91     141.902 182.021 149.454  1.00138.53           C  
ATOM    665  CD2 PHE A  91     140.934 180.954 151.352  1.00138.53           C  
ATOM    666  CE1 PHE A  91     141.161 183.159 149.710  1.00138.53           C  
ATOM    667  CE2 PHE A  91     140.195 182.093 151.618  1.00138.53           C  
ATOM    668  CZ  PHE A  91     140.307 183.195 150.794  1.00138.53           C  
ATOM    669  N   HIS A  92     144.463 178.556 147.812  1.00133.45           N  
ATOM    670  CA  HIS A  92     145.761 177.895 147.756  1.00133.45           C  
ATOM    671  C   HIS A  92     146.558 178.291 148.993  1.00133.45           C  
ATOM    672  O   HIS A  92     146.784 179.481 149.237  1.00133.45           O  
ATOM    673  CB  HIS A  92     146.504 178.290 146.480  1.00133.45           C  
ATOM    674  CG  HIS A  92     147.701 177.441 146.183  1.00133.45           C  
ATOM    675  ND1 HIS A  92     148.863 177.508 146.920  1.00133.45           N  
ATOM    676  CD2 HIS A  92     147.925 176.526 145.211  1.00133.45           C  
ATOM    677  CE1 HIS A  92     149.745 176.657 146.427  1.00133.45           C  
ATOM    678  NE2 HIS A  92     149.201 176.049 145.389  1.00133.45           N  
ATOM    679  N   ILE A  93     146.982 177.292 149.773  1.00130.59           N  
ATOM    680  CA  ILE A  93     147.642 177.579 151.043  1.00130.59           C  
ATOM    681  C   ILE A  93     149.037 178.154 150.822  1.00130.59           C  
ATOM    682  O   ILE A  93     149.540 178.914 151.659  1.00130.59           O  
ATOM    683  CB  ILE A  93     147.679 176.311 151.920  1.00130.59           C  
ATOM    684  CG1 ILE A  93     148.137 176.650 153.340  1.00130.59           C  
ATOM    685  CG2 ILE A  93     148.575 175.246 151.301  1.00130.59           C  
ATOM    686  CD1 ILE A  93     147.195 177.571 154.083  1.00130.59           C  
ATOM    687  N   GLY A  94     149.680 177.823 149.705  1.00131.70           N  
ATOM    688  CA  GLY A  94     150.976 178.400 149.411  1.00131.70           C  
ATOM    689  C   GLY A  94     150.856 179.820 148.898  1.00131.70           C  
ATOM    690  O   GLY A  94     151.677 180.680 149.229  1.00131.70           O  
ATOM    691  N   TYR A  95     149.832 180.076 148.086  1.00130.95           N  
ATOM    692  CA  TYR A  95     149.534 181.413 147.597  1.00130.95           C  
ATOM    693  C   TYR A  95     148.623 182.195 148.536  1.00130.95           C  
ATOM    694  O   TYR A  95     148.135 183.264 148.155  1.00130.95           O  
ATOM    695  CB  TYR A  95     148.903 181.342 146.202  1.00130.95           C  
ATOM    696  CG  TYR A  95     149.848 180.866 145.120  1.00130.95           C  
ATOM    697  CD1 TYR A  95     150.812 181.714 144.591  1.00130.95           C  
ATOM    698  CD2 TYR A  95     149.770 179.573 144.622  1.00130.95           C  
ATOM    699  CE1 TYR A  95     151.677 181.285 143.602  1.00130.95           C  
ATOM    700  CE2 TYR A  95     150.629 179.134 143.632  1.00130.95           C  
ATOM    701  CZ  TYR A  95     151.580 179.994 143.126  1.00130.95           C  
ATOM    702  OH  TYR A  95     152.437 179.563 142.139  1.00130.95           O  
ATOM    703  N   PHE A  96     148.381 181.688 149.749  1.00138.31           N  
ATOM    704  CA  PHE A  96     147.486 182.381 150.670  1.00138.31           C  
ATOM    705  C   PHE A  96     148.076 183.708 151.128  1.00138.31           C  
ATOM    706  O   PHE A  96     147.332 184.658 151.394  1.00138.31           O  
ATOM    707  CB  PHE A  96     147.177 181.488 151.872  1.00138.31           C  
ATOM    708  CG  PHE A  96     146.209 182.095 152.848  1.00138.31           C  
ATOM    709  CD1 PHE A  96     144.854 182.136 152.565  1.00138.31           C  
ATOM    710  CD2 PHE A  96     146.653 182.617 154.051  1.00138.31           C  
ATOM    711  CE1 PHE A  96     143.960 182.692 153.461  1.00138.31           C  
ATOM    712  CE2 PHE A  96     145.765 183.174 154.952  1.00138.31           C  
ATOM    713  CZ  PHE A  96     144.416 183.211 154.656  1.00138.31           C  
ATOM    714  N   LYS A  97     149.403 183.789 151.231  1.00134.40           N  
ATOM    715  CA  LYS A  97     150.050 185.051 151.568  1.00134.40           C  
ATOM    716  C   LYS A  97     150.053 185.999 150.375  1.00134.40           C  
ATOM    717  O   LYS A  97     149.880 187.212 150.538  1.00134.40           O  
ATOM    718  CB  LYS A  97     151.476 184.799 152.059  1.00134.40           C  
ATOM    719  CG  LYS A  97     152.194 186.047 152.544  1.00134.40           C  
ATOM    720  CD  LYS A  97     151.488 186.652 153.747  1.00134.40           C  
ATOM    721  CE  LYS A  97     151.608 185.753 154.967  1.00134.40           C  
ATOM    722  NZ  LYS A  97     150.985 186.365 156.173  1.00134.40           N  
ATOM    723  N   ALA A  98     150.246 185.459 149.174  1.00133.99           N  
ATOM    724  CA  ALA A  98     150.386 186.246 147.958  1.00133.99           C  
ATOM    725  C   ALA A  98     149.053 186.587 147.303  1.00133.99           C  
ATOM    726  O   ALA A  98     149.049 187.222 146.243  1.00133.99           O  
ATOM    727  CB  ALA A  98     151.275 185.507 146.952  1.00133.99           C  
ATOM    728  N   THR A  99     147.927 186.189 147.896  1.00138.49           N  
ATOM    729  CA  THR A  99     146.624 186.531 147.342  1.00138.49           C  
ATOM    730  C   THR A  99     145.972 187.713 148.046  1.00138.49           C  
ATOM    731  O   THR A  99     144.967 188.231 147.549  1.00138.49           O  
ATOM    732  CB  THR A  99     145.680 185.323 147.404  1.00138.49           C  
ATOM    733  OG1 THR A  99     144.468 185.624 146.702  1.00138.49           O  
ATOM    734  CG2 THR A  99     145.347 184.980 148.848  1.00138.49           C  
ATOM    735  N   ILE A 100     146.514 188.149 149.183  1.00140.86           N  
ATOM    736  CA  ILE A 100     146.034 189.356 149.844  1.00140.86           C  
ATOM    737  C   ILE A 100     146.872 190.572 149.462  1.00140.86           C  
ATOM    738  O   ILE A 100     146.405 191.709 149.628  1.00140.86           O  
ATOM    739  CB  ILE A 100     146.009 189.184 151.377  1.00140.86           C  
ATOM    740  CG1 ILE A 100     147.422 188.944 151.913  1.00140.86           C  
ATOM    741  CG2 ILE A 100     145.080 188.046 151.771  1.00140.86           C  
ATOM    742  CD1 ILE A 100     147.522 189.011 153.421  1.00140.86           C  
ATOM    743  N   GLN A 101     148.089 190.365 148.954  1.00140.62           N  
ATOM    744  CA  GLN A 101     148.929 191.474 148.516  1.00140.62           C  
ATOM    745  C   GLN A 101     148.392 192.110 147.240  1.00140.62           C  
ATOM    746  O   GLN A 101     148.442 193.335 147.082  1.00140.62           O  
ATOM    747  CB  GLN A 101     150.364 190.993 148.309  1.00140.62           C  
ATOM    748  CG  GLN A 101     151.069 190.568 149.586  1.00140.62           C  
ATOM    749  CD  GLN A 101     152.477 190.066 149.334  1.00140.62           C  
ATOM    750  OE1 GLN A 101     152.921 189.980 148.189  1.00140.62           O  
ATOM    751  NE2 GLN A 101     153.186 189.728 150.405  1.00140.62           N  
ATOM    752  N   ILE A 102     147.874 191.297 146.320  1.00144.32           N  
ATOM    753  CA  ILE A 102     147.193 191.817 145.139  1.00144.32           C  
ATOM    754  C   ILE A 102     145.717 192.046 145.435  1.00144.32           C  
ATOM    755  O   ILE A 102     144.935 192.364 144.531  1.00144.32           O  
ATOM    756  CB  ILE A 102     147.375 190.865 143.942  1.00144.32           C  
ATOM    757  CG1 ILE A 102     147.015 189.428 144.333  1.00144.32           C  
ATOM    758  CG2 ILE A 102     148.806 190.918 143.437  1.00144.32           C  
ATOM    759  CD1 ILE A 102     145.590 189.027 144.005  1.00144.32           C  
ATOM    760  N   LEU A 103     145.325 191.889 146.698  1.00148.74           N  
ATOM    761  CA  LEU A 103     143.963 192.191 147.119  1.00148.74           C  
ATOM    762  C   LEU A 103     143.860 193.506 147.876  1.00148.74           C  
ATOM    763  O   LEU A 103     142.810 194.155 147.834  1.00148.74           O  
ATOM    764  CB  LEU A 103     143.411 191.058 147.992  1.00148.74           C  
ATOM    765  CG  LEU A 103     141.916 191.102 148.317  1.00148.74           C  
ATOM    766  CD1 LEU A 103     141.089 191.006 147.044  1.00148.74           C  
ATOM    767  CD2 LEU A 103     141.541 189.994 149.290  1.00148.74           C  
ATOM    768  N   GLN A 104     144.931 193.914 148.562  1.00156.36           N  
ATOM    769  CA  GLN A 104     144.964 195.237 149.175  1.00156.36           C  
ATOM    770  C   GLN A 104     144.988 196.340 148.127  1.00156.36           C  
ATOM    771  O   GLN A 104     144.425 197.418 148.350  1.00156.36           O  
ATOM    772  CB  GLN A 104     146.175 195.354 150.100  1.00156.36           C  
ATOM    773  CG  GLN A 104     146.090 194.481 151.341  1.00156.36           C  
ATOM    774  CD  GLN A 104     147.320 194.589 152.218  1.00156.36           C  
ATOM    775  OE1 GLN A 104     148.295 195.249 151.861  1.00156.36           O  
ATOM    776  NE2 GLN A 104     147.281 193.938 153.375  1.00156.36           N  
ATOM    777  N   GLY A 105     145.629 196.093 146.981  1.00163.03           N  
ATOM    778  CA  GLY A 105     145.742 197.116 145.958  1.00163.03           C  
ATOM    779  C   GLY A 105     144.514 197.275 145.091  1.00163.03           C  
ATOM    780  O   GLY A 105     144.378 198.297 144.412  1.00163.03           O  
ATOM    781  N   ILE A 106     143.618 196.293 145.099  1.00165.33           N  
ATOM    782  CA  ILE A 106     142.444 196.322 144.242  1.00165.33           C  
ATOM    783  C   ILE A 106     141.297 196.972 145.006  1.00165.33           C  
ATOM    784  O   ILE A 106     141.268 196.990 146.240  1.00165.33           O  
ATOM    785  CB  ILE A 106     142.067 194.904 143.758  1.00165.33           C  
ATOM    786  CG1 ILE A 106     141.212 194.967 142.490  1.00165.33           C  
ATOM    787  CG2 ILE A 106     141.345 194.133 144.854  1.00165.33           C  
ATOM    788  CD1 ILE A 106     141.966 195.447 141.271  1.00165.33           C  
ATOM    789  N   CYS A 107     140.342 197.528 144.266  1.00165.43           N  
ATOM    790  CA  CYS A 107     139.104 197.981 144.880  1.00165.43           C  
ATOM    791  C   CYS A 107     138.234 196.795 145.280  1.00165.43           C  
ATOM    792  O   CYS A 107     138.224 195.750 144.624  1.00165.43           O  
ATOM    793  CB  CYS A 107     138.328 198.892 143.932  1.00165.43           C  
ATOM    794  SG  CYS A 107     136.730 199.422 144.590  1.00165.43           S  
ATOM    795  N   LYS A 108     137.498 196.968 146.373  1.00166.82           N  
ATOM    796  CA  LYS A 108     136.594 195.940 146.867  1.00166.82           C  
ATOM    797  C   LYS A 108     135.180 196.079 146.319  1.00166.82           C  
ATOM    798  O   LYS A 108     134.329 195.238 146.626  1.00166.82           O  
ATOM    799  CB  LYS A 108     136.565 195.952 148.399  1.00166.82           C  
ATOM    800  CG  LYS A 108     137.675 195.132 149.044  1.00166.82           C  
ATOM    801  CD  LYS A 108     139.017 195.847 148.987  1.00166.82           C  
ATOM    802  CE  LYS A 108     140.095 195.054 149.709  1.00166.82           C  
ATOM    803  NZ  LYS A 108     141.438 195.681 149.569  1.00166.82           N  
ATOM    804  N   ASN A 109     134.905 197.110 145.524  1.00167.79           N  
ATOM    805  CA  ASN A 109     133.579 197.289 144.946  1.00167.79           C  
ATOM    806  C   ASN A 109     133.583 197.307 143.426  1.00167.79           C  
ATOM    807  O   ASN A 109     132.723 196.675 142.808  1.00167.79           O  
ATOM    808  CB  ASN A 109     132.951 198.591 145.468  1.00167.79           C  
ATOM    809  CG  ASN A 109     131.443 198.609 145.327  1.00167.79           C  
ATOM    810  OD1 ASN A 109     130.833 197.610 144.952  1.00167.79           O  
ATOM    811  ND2 ASN A 109     130.834 199.750 145.626  1.00167.79           N  
ATOM    812  N   CYS A 110     134.526 198.013 142.802  1.00166.25           N  
ATOM    813  CA  CYS A 110     134.585 198.113 141.350  1.00166.25           C  
ATOM    814  C   CYS A 110     135.743 197.330 140.751  1.00166.25           C  
ATOM    815  O   CYS A 110     135.888 197.305 139.524  1.00166.25           O  
ATOM    816  CB  CYS A 110     134.679 199.582 140.917  1.00166.25           C  
ATOM    817  SG  CYS A 110     136.268 200.370 141.264  1.00166.25           S  
ATOM    818  N   SER A 111     136.569 196.696 141.585  1.00160.78           N  
ATOM    819  CA  SER A 111     137.692 195.865 141.148  1.00160.78           C  
ATOM    820  C   SER A 111     138.673 196.670 140.292  1.00160.78           C  
ATOM    821  O   SER A 111     138.917 196.369 139.121  1.00160.78           O  
ATOM    822  CB  SER A 111     137.196 194.621 140.402  1.00160.78           C  
ATOM    823  OG  SER A 111     136.719 194.954 139.109  1.00160.78           O  
ATOM    824  N   ALA A 112     139.237 197.711 140.903  1.00161.25           N  
ATOM    825  CA  ALA A 112     140.216 198.556 140.236  1.00161.25           C  
ATOM    826  C   ALA A 112     141.368 198.844 141.188  1.00161.25           C  
ATOM    827  O   ALA A 112     141.215 198.799 142.411  1.00161.25           O  
ATOM    828  CB  ALA A 112     139.591 199.870 139.747  1.00161.25           C  
ATOM    829  N   ILE A 113     142.530 199.145 140.610  1.00167.54           N  
ATOM    830  CA  ILE A 113     143.711 199.434 141.415  1.00167.54           C  
ATOM    831  C   ILE A 113     143.576 200.820 142.029  1.00167.54           C  
ATOM    832  O   ILE A 113     143.242 201.794 141.341  1.00167.54           O  
ATOM    833  CB  ILE A 113     144.987 199.314 140.569  1.00167.54           C  
ATOM    834  CG1 ILE A 113     145.246 197.851 140.204  1.00167.54           C  
ATOM    835  CG2 ILE A 113     146.182 199.897 141.310  1.00167.54           C  
ATOM    836  CD1 ILE A 113     146.452 197.648 139.316  1.00167.54           C  
ATOM    837  N   LEU A 114     143.835 200.917 143.334  1.00168.98           N  
ATOM    838  CA  LEU A 114     143.616 202.152 144.086  1.00168.98           C  
ATOM    839  C   LEU A 114     144.724 203.168 143.794  1.00168.98           C  
ATOM    840  O   LEU A 114     145.509 203.553 144.659  1.00168.98           O  
ATOM    841  CB  LEU A 114     143.517 201.849 145.576  1.00168.98           C  
ATOM    842  CG  LEU A 114     142.421 200.863 145.985  1.00168.98           C  
ATOM    843  CD1 LEU A 114     142.509 200.543 147.468  1.00168.98           C  
ATOM    844  CD2 LEU A 114     141.047 201.413 145.632  1.00168.98           C  
ATOM    845  N   LEU A 115     144.768 203.608 142.537  1.00176.62           N  
ATOM    846  CA  LEU A 115     145.714 204.624 142.100  1.00176.62           C  
ATOM    847  C   LEU A 115     145.053 205.512 141.056  1.00176.62           C  
ATOM    848  O   LEU A 115     144.032 205.156 140.462  1.00176.62           O  
ATOM    849  CB  LEU A 115     146.994 204.003 141.518  1.00176.62           C  
ATOM    850  CG  LEU A 115     147.936 203.256 142.463  1.00176.62           C  
ATOM    851  CD1 LEU A 115     149.087 202.637 141.687  1.00176.62           C  
ATOM    852  CD2 LEU A 115     148.463 204.190 143.541  1.00176.62           C  
ATOM    853  N   SER A 116     145.651 206.681 140.842  1.00170.27           N  
ATOM    854  CA  SER A 116     145.210 207.595 139.802  1.00170.27           C  
ATOM    855  C   SER A 116     145.806 207.195 138.453  1.00170.27           C  
ATOM    856  O   SER A 116     146.529 206.202 138.326  1.00170.27           O  
ATOM    857  CB  SER A 116     145.576 209.032 140.166  1.00170.27           C  
ATOM    858  OG  SER A 116     146.974 209.240 140.095  1.00170.27           O  
ATOM    859  N   GLU A 117     145.494 207.988 137.427  1.00176.70           N  
ATOM    860  CA  GLU A 117     145.852 207.630 136.057  1.00176.70           C  
ATOM    861  C   GLU A 117     147.346 207.808 135.812  1.00176.70           C  
ATOM    862  O   GLU A 117     148.056 206.848 135.492  1.00176.70           O  
ATOM    863  CB  GLU A 117     145.032 208.465 135.070  1.00176.70           C  
ATOM    864  CG  GLU A 117     144.993 207.904 133.655  1.00176.70           C  
ATOM    865  CD  GLU A 117     146.183 208.336 132.820  1.00176.70           C  
ATOM    866  OE1 GLU A 117     146.781 209.387 133.132  1.00176.70           O  
ATOM    867  OE2 GLU A 117     146.518 207.624 131.850  1.00176.70           O  
ATOM    868  N   THR A 118     147.841 209.038 135.953  1.00180.42           N  
ATOM    869  CA  THR A 118     149.233 209.349 135.652  1.00180.42           C  
ATOM    870  C   THR A 118     150.206 208.854 136.715  1.00180.42           C  
ATOM    871  O   THR A 118     151.412 208.808 136.449  1.00180.42           O  
ATOM    872  CB  THR A 118     149.409 210.860 135.468  1.00180.42           C  
ATOM    873  OG1 THR A 118     150.751 211.138 135.048  1.00180.42           O  
ATOM    874  CG2 THR A 118     149.127 211.594 136.770  1.00180.42           C  
ATOM    875  N   ASP A 119     149.723 208.486 137.902  1.00179.12           N  
ATOM    876  CA  ASP A 119     150.622 208.014 138.952  1.00179.12           C  
ATOM    877  C   ASP A 119     151.146 206.618 138.635  1.00179.12           C  
ATOM    878  O   ASP A 119     152.350 206.359 138.736  1.00179.12           O  
ATOM    879  CB  ASP A 119     149.906 208.030 140.303  1.00179.12           C  
ATOM    880  CG  ASP A 119     150.866 207.948 141.474  1.00179.12           C  
ATOM    881  OD1 ASP A 119     152.092 207.894 141.241  1.00179.12           O  
ATOM    882  OD2 ASP A 119     150.394 207.939 142.630  1.00179.12           O  
ATOM    883  N   LYS A 120     150.254 205.705 138.244  1.00173.54           N  
ATOM    884  CA  LYS A 120     150.680 204.375 137.821  1.00173.54           C  
ATOM    885  C   LYS A 120     151.450 204.406 136.506  1.00173.54           C  
ATOM    886  O   LYS A 120     152.206 203.471 136.225  1.00173.54           O  
ATOM    887  CB  LYS A 120     149.472 203.445 137.695  1.00173.54           C  
ATOM    888  CG  LYS A 120     148.478 203.852 136.620  1.00173.54           C  
ATOM    889  CD  LYS A 120     147.349 202.842 136.499  1.00173.54           C  
ATOM    890  CE  LYS A 120     146.400 202.927 137.683  1.00173.54           C  
ATOM    891  NZ  LYS A 120     145.222 202.031 137.516  1.00173.54           N  
ATOM    892  N   ARG A 121     151.273 205.455 135.699  1.00172.68           N  
ATOM    893  CA  ARG A 121     152.127 205.650 134.532  1.00172.68           C  
ATOM    894  C   ARG A 121     153.570 205.946 134.924  1.00172.68           C  
ATOM    895  O   ARG A 121     154.488 205.687 134.139  1.00172.68           O  
ATOM    896  CB  ARG A 121     151.583 206.780 133.659  1.00172.68           C  
ATOM    897  CG  ARG A 121     150.299 206.448 132.922  1.00172.68           C  
ATOM    898  CD  ARG A 121     149.865 207.617 132.055  1.00172.68           C  
ATOM    899  NE  ARG A 121     150.845 207.904 131.011  1.00172.68           N  
ATOM    900  CZ  ARG A 121     150.807 208.973 130.223  1.00172.68           C  
ATOM    901  NH1 ARG A 121     151.744 209.153 129.301  1.00172.68           N  
ATOM    902  NH2 ARG A 121     149.833 209.863 130.354  1.00172.68           N  
ATOM    903  N   GLN A 122     153.791 206.497 136.118  1.00175.56           N  
ATOM    904  CA  GLN A 122     155.153 206.724 136.586  1.00175.56           C  
ATOM    905  C   GLN A 122     155.821 205.442 137.071  1.00175.56           C  
ATOM    906  O   GLN A 122     157.032 205.277 136.885  1.00175.56           O  
ATOM    907  CB  GLN A 122     155.155 207.773 137.700  1.00175.56           C  
ATOM    908  CG  GLN A 122     156.538 208.281 138.087  1.00175.56           C  
ATOM    909  CD  GLN A 122     157.164 207.481 139.212  1.00175.56           C  
ATOM    910  OE1 GLN A 122     156.465 206.940 140.069  1.00175.56           O  
ATOM    911  NE2 GLN A 122     158.490 207.402 139.215  1.00175.56           N  
ATOM    912  N   PHE A 123     155.062 204.528 137.680  1.00174.34           N  
ATOM    913  CA  PHE A 123     155.677 203.402 138.379  1.00174.34           C  
ATOM    914  C   PHE A 123     156.294 202.399 137.410  1.00174.34           C  
ATOM    915  O   PHE A 123     157.395 201.891 137.656  1.00174.34           O  
ATOM    916  CB  PHE A 123     154.649 202.714 139.277  1.00174.34           C  
ATOM    917  CG  PHE A 123     154.379 203.446 140.562  1.00174.34           C  
ATOM    918  CD1 PHE A 123     155.300 203.416 141.596  1.00174.34           C  
ATOM    919  CD2 PHE A 123     153.204 204.155 140.739  1.00174.34           C  
ATOM    920  CE1 PHE A 123     155.056 204.085 142.781  1.00174.34           C  
ATOM    921  CE2 PHE A 123     152.953 204.827 141.921  1.00174.34           C  
ATOM    922  CZ  PHE A 123     153.881 204.791 142.943  1.00174.34           C  
ATOM    923  N   LEU A 124     155.604 202.088 136.311  1.00175.04           N  
ATOM    924  CA  LEU A 124     156.107 201.074 135.391  1.00175.04           C  
ATOM    925  C   LEU A 124     157.306 201.550 134.580  1.00175.04           C  
ATOM    926  O   LEU A 124     157.974 200.719 133.956  1.00175.04           O  
ATOM    927  CB  LEU A 124     154.999 200.604 134.442  1.00175.04           C  
ATOM    928  CG  LEU A 124     154.708 201.429 133.187  1.00175.04           C  
ATOM    929  CD1 LEU A 124     154.008 200.572 132.145  1.00175.04           C  
ATOM    930  CD2 LEU A 124     153.863 202.637 133.523  1.00175.04           C  
ATOM    931  N   HIS A 125     157.590 202.855 134.567  1.00176.83           N  
ATOM    932  CA  HIS A 125     158.855 203.332 134.016  1.00176.83           C  
ATOM    933  C   HIS A 125     160.052 202.756 134.761  1.00176.83           C  
ATOM    934  O   HIS A 125     161.105 202.522 134.156  1.00176.83           O  
ATOM    935  CB  HIS A 125     158.896 204.861 134.045  1.00176.83           C  
ATOM    936  CG  HIS A 125     160.031 205.450 133.267  1.00176.83           C  
ATOM    937  ND1 HIS A 125     160.496 206.729 133.483  1.00176.83           N  
ATOM    938  CD2 HIS A 125     160.792 204.936 132.271  1.00176.83           C  
ATOM    939  CE1 HIS A 125     161.496 206.977 132.655  1.00176.83           C  
ATOM    940  NE2 HIS A 125     161.695 205.905 131.910  1.00176.83           N  
ATOM    941  N   GLU A 126     159.916 202.516 136.066  1.00183.32           N  
ATOM    942  CA  GLU A 126     160.932 201.780 136.812  1.00183.32           C  
ATOM    943  C   GLU A 126     160.941 200.289 136.501  1.00183.32           C  
ATOM    944  O   GLU A 126     161.814 199.579 137.013  1.00183.32           O  
ATOM    945  CB  GLU A 126     160.749 201.992 138.318  1.00183.32           C  
ATOM    946  CG  GLU A 126     161.224 203.350 138.821  1.00183.32           C  
ATOM    947  CD  GLU A 126     160.152 204.416 138.743  1.00183.32           C  
ATOM    948  OE1 GLU A 126     158.995 204.074 138.426  1.00183.32           O  
ATOM    949  OE2 GLU A 126     160.467 205.597 139.001  1.00183.32           O  
ATOM    950  N   LEU A 127     160.005 199.796 135.691  1.00178.11           N  
ATOM    951  CA  LEU A 127     160.080 198.438 135.165  1.00178.11           C  
ATOM    952  C   LEU A 127     160.624 198.361 133.746  1.00178.11           C  
ATOM    953  O   LEU A 127     161.224 197.344 133.384  1.00178.11           O  
ATOM    954  CB  LEU A 127     158.696 197.776 135.196  1.00178.11           C  
ATOM    955  CG  LEU A 127     158.168 197.218 136.522  1.00178.11           C  
ATOM    956  CD1 LEU A 127     159.191 196.295 137.172  1.00178.11           C  
ATOM    957  CD2 LEU A 127     157.742 198.327 137.476  1.00178.11           C  
ATOM    958  N   ARG A 128     160.436 199.399 132.933  1.00180.88           N  
ATOM    959  CA  ARG A 128     160.716 199.312 131.506  1.00180.88           C  
ATOM    960  C   ARG A 128     162.173 199.582 131.150  1.00180.88           C  
ATOM    961  O   ARG A 128     162.540 199.442 129.978  1.00180.88           O  
ATOM    962  CB  ARG A 128     159.815 200.282 130.733  1.00180.88           C  
ATOM    963  CG  ARG A 128     158.335 199.952 130.818  1.00180.88           C  
ATOM    964  CD  ARG A 128     158.018 198.657 130.089  1.00180.88           C  
ATOM    965  NE  ARG A 128     156.620 198.268 130.245  1.00180.88           N  
ATOM    966  CZ  ARG A 128     155.638 198.672 129.447  1.00180.88           C  
ATOM    967  NH1 ARG A 128     155.897 199.486 128.433  1.00180.88           N  
ATOM    968  NH2 ARG A 128     154.394 198.266 129.664  1.00180.88           N  
ATOM    969  N   ARG A 129     163.011 199.963 132.113  1.00178.55           N  
ATOM    970  CA  ARG A 129     164.432 200.029 131.811  1.00178.55           C  
ATOM    971  C   ARG A 129     165.043 198.628 131.810  1.00178.55           C  
ATOM    972  O   ARG A 129     164.600 197.747 132.552  1.00178.55           O  
ATOM    973  CB  ARG A 129     165.165 200.931 132.803  1.00178.55           C  
ATOM    974  CG  ARG A 129     165.506 200.306 134.142  1.00178.55           C  
ATOM    975  CD  ARG A 129     164.322 200.374 135.084  1.00178.55           C  
ATOM    976  NE  ARG A 129     163.781 201.728 135.156  1.00178.55           N  
ATOM    977  CZ  ARG A 129     164.263 202.685 135.942  1.00178.55           C  
ATOM    978  NH1 ARG A 129     165.304 202.442 136.725  1.00178.55           N  
ATOM    979  NH2 ARG A 129     163.706 203.889 135.942  1.00178.55           N  
ATOM    980  N   PRO A 130     166.052 198.393 130.965  1.00178.56           N  
ATOM    981  CA  PRO A 130     166.597 197.032 130.847  1.00178.56           C  
ATOM    982  C   PRO A 130     167.315 196.548 132.095  1.00178.56           C  
ATOM    983  O   PRO A 130     167.383 195.332 132.317  1.00178.56           O  
ATOM    984  CB  PRO A 130     167.560 197.143 129.657  1.00178.56           C  
ATOM    985  CG  PRO A 130     167.065 198.315 128.876  1.00178.56           C  
ATOM    986  CD  PRO A 130     166.551 199.281 129.902  1.00178.56           C  
ATOM    987  N   GLY A 131     167.850 197.447 132.918  1.00176.50           N  
ATOM    988  CA  GLY A 131     168.511 197.019 134.135  1.00176.50           C  
ATOM    989  C   GLY A 131     167.575 196.919 135.323  1.00176.50           C  
ATOM    990  O   GLY A 131     167.346 197.905 136.030  1.00176.50           O  
ATOM    991  N   VAL A 132     167.037 195.722 135.552  1.00176.36           N  
ATOM    992  CA  VAL A 132     166.201 195.420 136.711  1.00176.36           C  
ATOM    993  C   VAL A 132     166.556 194.020 137.190  1.00176.36           C  
ATOM    994  O   VAL A 132     166.363 193.045 136.455  1.00176.36           O  
ATOM    995  CB  VAL A 132     164.696 195.503 136.396  1.00176.36           C  
ATOM    996  CG1 VAL A 132     163.885 194.971 137.567  1.00176.36           C  
ATOM    997  CG2 VAL A 132     164.286 196.930 136.080  1.00176.36           C  
ATOM    998  N   ASP A 133     167.072 193.915 138.410  1.00169.46           N  
ATOM    999  CA  ASP A 133     167.311 192.620 139.024  1.00169.46           C  
ATOM   1000  C   ASP A 133     166.158 192.263 139.960  1.00169.46           C  
ATOM   1001  O   ASP A 133     165.208 193.027 140.146  1.00169.46           O  
ATOM   1002  CB  ASP A 133     168.654 192.612 139.761  1.00169.46           C  
ATOM   1003  CG  ASP A 133     168.744 193.684 140.831  1.00169.46           C  
ATOM   1004  OD1 ASP A 133     167.846 194.549 140.892  1.00169.46           O  
ATOM   1005  OD2 ASP A 133     169.716 193.660 141.614  1.00169.46           O  
ATOM   1006  N   ASN A 134     166.249 191.073 140.557  1.00167.95           N  
ATOM   1007  CA  ASN A 134     165.229 190.615 141.493  1.00167.95           C  
ATOM   1008  C   ASN A 134     165.262 191.374 142.813  1.00167.95           C  
ATOM   1009  O   ASN A 134     164.278 191.336 143.560  1.00167.95           O  
ATOM   1010  CB  ASN A 134     165.388 189.115 141.749  1.00167.95           C  
ATOM   1011  CG  ASN A 134     164.101 188.464 142.222  1.00167.95           C  
ATOM   1012  OD1 ASN A 134     163.064 189.118 142.331  1.00167.95           O  
ATOM   1013  ND2 ASN A 134     164.162 187.168 142.502  1.00167.95           N  
ATOM   1014  N   LEU A 135     166.364 192.061 143.118  1.00165.93           N  
ATOM   1015  CA  LEU A 135     166.416 192.894 144.316  1.00165.93           C  
ATOM   1016  C   LEU A 135     165.505 194.110 144.195  1.00165.93           C  
ATOM   1017  O   LEU A 135     164.628 194.329 145.039  1.00165.93           O  
ATOM   1018  CB  LEU A 135     167.859 193.327 144.585  1.00165.93           C  
ATOM   1019  CG  LEU A 135     168.073 194.250 145.786  1.00165.93           C  
ATOM   1020  CD1 LEU A 135     167.637 193.570 147.072  1.00165.93           C  
ATOM   1021  CD2 LEU A 135     169.526 194.692 145.873  1.00165.93           C  
ATOM   1022  N   ARG A 136     165.695 194.919 143.151  1.00165.72           N  
ATOM   1023  CA  ARG A 136     164.927 196.153 143.036  1.00165.72           C  
ATOM   1024  C   ARG A 136     163.500 195.924 142.556  1.00165.72           C  
ATOM   1025  O   ARG A 136     162.631 196.760 142.826  1.00165.72           O  
ATOM   1026  CB  ARG A 136     165.631 197.138 142.099  1.00165.72           C  
ATOM   1027  CG  ARG A 136     165.591 196.764 140.627  1.00165.72           C  
ATOM   1028  CD  ARG A 136     166.319 197.808 139.800  1.00165.72           C  
ATOM   1029  NE  ARG A 136     165.617 199.088 139.819  1.00165.72           N  
ATOM   1030  CZ  ARG A 136     166.157 200.243 139.447  1.00165.72           C  
ATOM   1031  NH1 ARG A 136     167.413 200.286 139.025  1.00165.72           N  
ATOM   1032  NH2 ARG A 136     165.441 201.358 139.502  1.00165.72           N  
ATOM   1033  N   ARG A 137     163.235 194.818 141.856  1.00164.36           N  
ATOM   1034  CA  ARG A 137     161.879 194.564 141.379  1.00164.36           C  
ATOM   1035  C   ARG A 137     160.949 194.213 142.534  1.00164.36           C  
ATOM   1036  O   ARG A 137     159.819 194.710 142.601  1.00164.36           O  
ATOM   1037  CB  ARG A 137     161.890 193.451 140.330  1.00164.36           C  
ATOM   1038  CG  ARG A 137     160.552 193.233 139.635  1.00164.36           C  
ATOM   1039  CD  ARG A 137     159.818 192.014 140.174  1.00164.36           C  
ATOM   1040  NE  ARG A 137     158.603 191.737 139.414  1.00164.36           N  
ATOM   1041  CZ  ARG A 137     158.563 190.999 138.309  1.00164.36           C  
ATOM   1042  NH1 ARG A 137     159.676 190.464 137.826  1.00164.36           N  
ATOM   1043  NH2 ARG A 137     157.411 190.801 137.682  1.00164.36           N  
ATOM   1044  N   MET A 138     161.408 193.362 143.453  1.00164.66           N  
ATOM   1045  CA  MET A 138     160.666 193.116 144.684  1.00164.66           C  
ATOM   1046  C   MET A 138     160.756 194.285 145.656  1.00164.66           C  
ATOM   1047  O   MET A 138     159.957 194.356 146.596  1.00164.66           O  
ATOM   1048  CB  MET A 138     161.171 191.838 145.356  1.00164.66           C  
ATOM   1049  CG  MET A 138     160.870 190.568 144.575  1.00164.66           C  
ATOM   1050  SD  MET A 138     161.615 189.098 145.305  1.00164.66           S  
ATOM   1051  CE  MET A 138     160.666 188.949 146.816  1.00164.66           C  
ATOM   1052  N   GLY A 139     161.703 195.197 145.452  1.00162.63           N  
ATOM   1053  CA  GLY A 139     161.790 196.401 146.253  1.00162.63           C  
ATOM   1054  C   GLY A 139     160.739 197.430 145.892  1.00162.63           C  
ATOM   1055  O   GLY A 139     160.124 198.034 146.776  1.00162.63           O  
ATOM   1056  N   ILE A 140     160.524 197.640 144.592  1.00160.34           N  
ATOM   1057  CA  ILE A 140     159.567 198.651 144.154  1.00160.34           C  
ATOM   1058  C   ILE A 140     158.136 198.129 144.167  1.00160.34           C  
ATOM   1059  O   ILE A 140     157.194 198.932 144.188  1.00160.34           O  
ATOM   1060  CB  ILE A 140     159.928 199.174 142.754  1.00160.34           C  
ATOM   1061  CG1 ILE A 140     159.856 198.045 141.724  1.00160.34           C  
ATOM   1062  CG2 ILE A 140     161.310 199.809 142.762  1.00160.34           C  
ATOM   1063  CD1 ILE A 140     160.059 198.508 140.300  1.00160.34           C  
ATOM   1064  N   LEU A 141     157.943 196.808 144.155  1.00166.28           N  
ATOM   1065  CA  LEU A 141     156.614 196.260 144.402  1.00166.28           C  
ATOM   1066  C   LEU A 141     156.197 196.451 145.854  1.00166.28           C  
ATOM   1067  O   LEU A 141     155.001 196.570 146.145  1.00166.28           O  
ATOM   1068  CB  LEU A 141     156.572 194.779 144.025  1.00166.28           C  
ATOM   1069  CG  LEU A 141     156.550 194.456 142.529  1.00166.28           C  
ATOM   1070  CD1 LEU A 141     156.667 192.957 142.301  1.00166.28           C  
ATOM   1071  CD2 LEU A 141     155.289 195.005 141.878  1.00166.28           C  
ATOM   1072  N   LYS A 142     157.165 196.480 146.774  1.00165.84           N  
ATOM   1073  CA  LYS A 142     156.869 196.859 148.151  1.00165.84           C  
ATOM   1074  C   LYS A 142     156.437 198.317 148.236  1.00165.84           C  
ATOM   1075  O   LYS A 142     155.558 198.667 149.032  1.00165.84           O  
ATOM   1076  CB  LYS A 142     158.086 196.602 149.040  1.00165.84           C  
ATOM   1077  CG  LYS A 142     157.857 196.899 150.513  1.00165.84           C  
ATOM   1078  CD  LYS A 142     156.845 195.940 151.119  1.00165.84           C  
ATOM   1079  CE  LYS A 142     156.662 196.198 152.606  1.00165.84           C  
ATOM   1080  NZ  LYS A 142     157.887 195.860 153.382  1.00165.84           N  
ATOM   1081  N   LYS A 143     157.044 199.182 147.420  1.00159.98           N  
ATOM   1082  CA  LYS A 143     156.802 200.615 147.533  1.00159.98           C  
ATOM   1083  C   LYS A 143     155.475 201.013 146.901  1.00159.98           C  
ATOM   1084  O   LYS A 143     154.803 201.921 147.402  1.00159.98           O  
ATOM   1085  CB  LYS A 143     157.952 201.393 146.890  1.00159.98           C  
ATOM   1086  CG  LYS A 143     157.915 202.891 147.146  1.00159.98           C  
ATOM   1087  CD  LYS A 143     159.108 203.587 146.512  1.00159.98           C  
ATOM   1088  CE  LYS A 143     160.392 203.272 147.261  1.00159.98           C  
ATOM   1089  NZ  LYS A 143     161.553 204.037 146.728  1.00159.98           N  
ATOM   1090  N   ILE A 144     155.082 200.351 145.812  1.00164.64           N  
ATOM   1091  CA  ILE A 144     153.823 200.692 145.161  1.00164.64           C  
ATOM   1092  C   ILE A 144     152.645 200.133 145.953  1.00164.64           C  
ATOM   1093  O   ILE A 144     151.534 200.671 145.885  1.00164.64           O  
ATOM   1094  CB  ILE A 144     153.817 200.195 143.704  1.00164.64           C  
ATOM   1095  CG1 ILE A 144     152.632 200.786 142.936  1.00164.64           C  
ATOM   1096  CG2 ILE A 144     153.794 198.673 143.648  1.00164.64           C  
ATOM   1097  CD1 ILE A 144     152.649 200.480 141.456  1.00164.64           C  
ATOM   1098  N   LEU A 145     152.864 199.061 146.719  1.00168.69           N  
ATOM   1099  CA  LEU A 145     151.791 198.504 147.536  1.00168.69           C  
ATOM   1100  C   LEU A 145     151.487 199.409 148.723  1.00168.69           C  
ATOM   1101  O   LEU A 145     150.328 199.540 149.133  1.00168.69           O  
ATOM   1102  CB  LEU A 145     152.162 197.098 148.005  1.00168.69           C  
ATOM   1103  CG  LEU A 145     151.130 196.368 148.867  1.00168.69           C  
ATOM   1104  CD1 LEU A 145     149.821 196.202 148.110  1.00168.69           C  
ATOM   1105  CD2 LEU A 145     151.665 195.019 149.320  1.00168.69           C  
ATOM   1106  N   ASP A 146     152.519 200.044 149.287  1.00169.84           N  
ATOM   1107  CA  ASP A 146     152.304 200.977 150.387  1.00169.84           C  
ATOM   1108  C   ASP A 146     151.608 202.243 149.907  1.00169.84           C  
ATOM   1109  O   ASP A 146     150.917 202.905 150.690  1.00169.84           O  
ATOM   1110  CB  ASP A 146     153.636 201.319 151.055  1.00169.84           C  
ATOM   1111  CG  ASP A 146     154.324 200.101 151.639  1.00169.84           C  
ATOM   1112  OD1 ASP A 146     153.620 199.132 151.994  1.00169.84           O  
ATOM   1113  OD2 ASP A 146     155.568 200.113 151.743  1.00169.84           O  
ATOM   1114  N   GLN A 147     151.779 202.593 148.630  1.00169.57           N  
ATOM   1115  CA  GLN A 147     151.050 203.723 148.065  1.00169.57           C  
ATOM   1116  C   GLN A 147     149.561 203.417 147.973  1.00169.57           C  
ATOM   1117  O   GLN A 147     148.724 204.289 148.233  1.00169.57           O  
ATOM   1118  CB  GLN A 147     151.615 204.080 146.690  1.00169.57           C  
ATOM   1119  CG  GLN A 147     150.978 205.305 146.055  1.00169.57           C  
ATOM   1120  CD  GLN A 147     151.231 206.572 146.848  1.00169.57           C  
ATOM   1121  OE1 GLN A 147     150.351 207.060 147.558  1.00169.57           O  
ATOM   1122  NE2 GLN A 147     152.438 207.113 146.731  1.00169.57           N  
ATOM   1123  N   CYS A 148     149.212 202.182 147.605  1.00172.26           N  
ATOM   1124  CA  CYS A 148     147.812 201.821 147.426  1.00172.26           C  
ATOM   1125  C   CYS A 148     147.081 201.698 148.756  1.00172.26           C  
ATOM   1126  O   CYS A 148     145.856 201.855 148.792  1.00172.26           O  
ATOM   1127  CB  CYS A 148     147.699 200.510 146.648  1.00172.26           C  
ATOM   1128  SG  CYS A 148     148.303 200.593 144.947  1.00172.26           S  
ATOM   1129  N   LYS A 149     147.800 201.422 149.845  1.00167.15           N  
ATOM   1130  CA  LYS A 149     147.176 201.302 151.155  1.00167.15           C  
ATOM   1131  C   LYS A 149     146.853 202.655 151.772  1.00167.15           C  
ATOM   1132  O   LYS A 149     146.124 202.705 152.769  1.00167.15           O  
ATOM   1133  CB  LYS A 149     148.081 200.509 152.101  1.00167.15           C  
ATOM   1134  CG  LYS A 149     148.247 199.047 151.724  1.00167.15           C  
ATOM   1135  CD  LYS A 149     148.929 198.268 152.836  1.00167.15           C  
ATOM   1136  CE  LYS A 149     150.414 198.586 152.903  1.00167.15           C  
ATOM   1137  NZ  LYS A 149     151.120 197.733 153.899  1.00167.15           N  
ATOM   1138  N   LYS A 150     147.374 203.743 151.208  1.00166.68           N  
ATOM   1139  CA  LYS A 150     147.145 205.088 151.716  1.00166.68           C  
ATOM   1140  C   LYS A 150     146.036 205.803 150.957  1.00166.68           C  
ATOM   1141  O   LYS A 150     145.894 207.023 151.083  1.00166.68           O  
ATOM   1142  CB  LYS A 150     148.437 205.904 151.653  1.00166.68           C  
ATOM   1143  CG  LYS A 150     149.525 205.415 152.596  1.00166.68           C  
ATOM   1144  CD  LYS A 150     150.703 206.373 152.621  1.00166.68           C  
ATOM   1145  CE  LYS A 150     151.518 206.279 151.342  1.00166.68           C  
ATOM   1146  NZ  LYS A 150     152.739 207.130 151.398  1.00166.68           N  
ATOM   1147  N   GLN A 151     145.252 205.067 150.173  1.00168.07           N  
ATOM   1148  CA  GLN A 151     144.248 205.625 149.274  1.00168.07           C  
ATOM   1149  C   GLN A 151     142.912 205.002 149.654  1.00168.07           C  
ATOM   1150  O   GLN A 151     142.684 203.812 149.406  1.00168.07           O  
ATOM   1151  CB  GLN A 151     144.600 205.348 147.813  1.00168.07           C  
ATOM   1152  CG  GLN A 151     143.976 206.319 146.826  1.00168.07           C  
ATOM   1153  CD  GLN A 151     142.569 205.927 146.428  1.00168.07           C  
ATOM   1154  OE1 GLN A 151     142.216 204.747 146.426  1.00168.07           O  
ATOM   1155  NE2 GLN A 151     141.754 206.918 146.087  1.00168.07           N  
ATOM   1156  N   ARG A 152     142.032 205.802 150.256  1.00162.86           N  
ATOM   1157  CA  ARG A 152     140.844 205.252 150.899  1.00162.86           C  
ATOM   1158  C   ARG A 152     139.773 204.866 149.885  1.00162.86           C  
ATOM   1159  O   ARG A 152     139.182 203.785 149.983  1.00162.86           O  
ATOM   1160  CB  ARG A 152     140.286 206.256 151.910  1.00162.86           C  
ATOM   1161  CG  ARG A 152     141.162 206.458 153.136  1.00162.86           C  
ATOM   1162  CD  ARG A 152     141.197 205.207 154.001  1.00162.86           C  
ATOM   1163  NE  ARG A 152     141.891 205.432 155.266  1.00162.86           N  
ATOM   1164  CZ  ARG A 152     143.200 205.286 155.438  1.00162.86           C  
ATOM   1165  NH1 ARG A 152     143.969 204.929 154.418  1.00162.86           N  
ATOM   1166  NH2 ARG A 152     143.744 205.511 156.626  1.00162.86           N  
ATOM   1167  N   ARG A 153     139.507 205.727 148.907  1.00171.33           N  
ATOM   1168  CA  ARG A 153     138.320 205.598 148.075  1.00171.33           C  
ATOM   1169  C   ARG A 153     138.707 205.463 146.610  1.00171.33           C  
ATOM   1170  O   ARG A 153     139.559 206.203 146.109  1.00171.33           O  
ATOM   1171  CB  ARG A 153     137.394 206.803 148.261  1.00171.33           C  
ATOM   1172  CG  ARG A 153     137.025 207.059 149.711  1.00171.33           C  
ATOM   1173  CD  ARG A 153     135.956 208.123 149.837  1.00171.33           C  
ATOM   1174  NE  ARG A 153     134.666 207.642 149.353  1.00171.33           N  
ATOM   1175  CZ  ARG A 153     133.596 208.413 149.196  1.00171.33           C  
ATOM   1176  NH1 ARG A 153     133.666 209.705 149.481  1.00171.33           N  
ATOM   1177  NH2 ARG A 153     132.460 207.895 148.751  1.00171.33           N  
ATOM   1178  N   CYS A 154     138.064 204.517 145.928  1.00169.34           N  
ATOM   1179  CA  CYS A 154     138.426 204.175 144.563  1.00169.34           C  
ATOM   1180  C   CYS A 154     137.997 205.281 143.599  1.00169.34           C  
ATOM   1181  O   CYS A 154     137.256 206.203 143.949  1.00169.34           O  
ATOM   1182  CB  CYS A 154     137.793 202.846 144.158  1.00169.34           C  
ATOM   1183  SG  CYS A 154     135.989 202.884 144.080  1.00169.34           S  
ATOM   1184  N   LEU A 155     138.479 205.175 142.360  1.00170.00           N  
ATOM   1185  CA  LEU A 155     138.281 206.221 141.368  1.00170.00           C  
ATOM   1186  C   LEU A 155     137.080 205.981 140.464  1.00170.00           C  
ATOM   1187  O   LEU A 155     136.559 206.943 139.889  1.00170.00           O  
ATOM   1188  CB  LEU A 155     139.536 206.376 140.497  1.00170.00           C  
ATOM   1189  CG  LEU A 155     140.665 207.279 141.007  1.00170.00           C  
ATOM   1190  CD1 LEU A 155     140.166 208.704 141.209  1.00170.00           C  
ATOM   1191  CD2 LEU A 155     141.299 206.739 142.284  1.00170.00           C  
ATOM   1192  N   HIS A 156     136.629 204.734 140.321  1.00177.84           N  
ATOM   1193  CA  HIS A 156     135.575 204.419 139.363  1.00177.84           C  
ATOM   1194  C   HIS A 156     134.177 204.589 139.952  1.00177.84           C  
ATOM   1195  O   HIS A 156     133.328 205.253 139.351  1.00177.84           O  
ATOM   1196  CB  HIS A 156     135.756 202.993 138.833  1.00177.84           C  
ATOM   1197  CG  HIS A 156     137.009 202.800 138.037  1.00177.84           C  
ATOM   1198  ND1 HIS A 156     137.451 201.559 137.632  1.00177.84           N  
ATOM   1199  CD2 HIS A 156     137.914 203.692 137.568  1.00177.84           C  
ATOM   1200  CE1 HIS A 156     138.573 201.694 136.949  1.00177.84           C  
ATOM   1201  NE2 HIS A 156     138.877 202.978 136.896  1.00177.84           N  
ATOM   1202  N   CYS A 157     133.912 203.987 141.112  1.00173.61           N  
ATOM   1203  CA  CYS A 157     132.625 204.139 141.776  1.00173.61           C  
ATOM   1204  C   CYS A 157     132.720 204.865 143.111  1.00173.61           C  
ATOM   1205  O   CYS A 157     131.687 205.102 143.745  1.00173.61           O  
ATOM   1206  CB  CYS A 157     131.967 202.769 141.979  1.00173.61           C  
ATOM   1207  SG  CYS A 157     132.783 201.711 143.194  1.00173.61           S  
ATOM   1208  N   GLY A 158     133.923 205.223 143.554  1.00171.84           N  
ATOM   1209  CA  GLY A 158     134.077 206.069 144.720  1.00171.84           C  
ATOM   1210  C   GLY A 158     133.828 205.400 146.053  1.00171.84           C  
ATOM   1211  O   GLY A 158     133.781 206.094 147.073  1.00171.84           O  
ATOM   1212  N   ALA A 159     133.666 204.080 146.083  1.00173.50           N  
ATOM   1213  CA  ALA A 159     133.446 203.385 147.345  1.00173.50           C  
ATOM   1214  C   ALA A 159     134.736 203.322 148.152  1.00173.50           C  
ATOM   1215  O   ALA A 159     135.798 202.982 147.620  1.00173.50           O  
ATOM   1216  CB  ALA A 159     132.911 201.978 147.089  1.00173.50           C  
ATOM   1217  N   LEU A 160     134.644 203.649 149.438  1.00181.84           N  
ATOM   1218  CA  LEU A 160     135.822 203.647 150.293  1.00181.84           C  
ATOM   1219  C   LEU A 160     136.249 202.221 150.625  1.00181.84           C  
ATOM   1220  O   LEU A 160     135.430 201.300 150.695  1.00181.84           O  
ATOM   1221  CB  LEU A 160     135.558 204.426 151.583  1.00181.84           C  
ATOM   1222  CG  LEU A 160     134.677 203.799 152.666  1.00181.84           C  
ATOM   1223  CD1 LEU A 160     134.984 204.424 154.017  1.00181.84           C  
ATOM   1224  CD2 LEU A 160     133.204 203.963 152.333  1.00181.84           C  
ATOM   1225  N   ASN A 161     137.553 202.047 150.826  1.00179.64           N  
ATOM   1226  CA  ASN A 161     138.121 200.779 151.258  1.00179.64           C  
ATOM   1227  C   ASN A 161     139.075 201.033 152.415  1.00179.64           C  
ATOM   1228  O   ASN A 161     139.809 202.025 152.418  1.00179.64           O  
ATOM   1229  CB  ASN A 161     138.854 200.073 150.111  1.00179.64           C  
ATOM   1230  CG  ASN A 161     137.910 199.583 149.031  1.00179.64           C  
ATOM   1231  OD1 ASN A 161     136.814 199.102 149.320  1.00179.64           O  
ATOM   1232  ND2 ASN A 161     138.330 199.705 147.777  1.00179.64           N  
ATOM   1233  N   GLY A 162     139.062 200.134 153.395  1.00185.71           N  
ATOM   1234  CA  GLY A 162     139.964 200.254 154.523  1.00185.71           C  
ATOM   1235  C   GLY A 162     141.197 199.383 154.405  1.00185.71           C  
ATOM   1236  O   GLY A 162     142.100 199.672 153.615  1.00185.71           O  
ATOM   1237  N   VAL A 163     141.240 198.307 155.190  1.00184.51           N  
ATOM   1238  CA  VAL A 163     142.317 197.330 155.136  1.00184.51           C  
ATOM   1239  C   VAL A 163     141.696 195.939 155.147  1.00184.51           C  
ATOM   1240  O   VAL A 163     140.542 195.750 155.537  1.00184.51           O  
ATOM   1241  CB  VAL A 163     143.317 197.499 156.305  1.00184.51           C  
ATOM   1242  CG1 VAL A 163     142.742 196.929 157.594  1.00184.51           C  
ATOM   1243  CG2 VAL A 163     144.666 196.870 155.969  1.00184.51           C  
ATOM   1244  N   VAL A 164     142.477 194.958 154.701  1.00176.60           N  
ATOM   1245  CA  VAL A 164     142.065 193.561 154.705  1.00176.60           C  
ATOM   1246  C   VAL A 164     143.204 192.718 155.262  1.00176.60           C  
ATOM   1247  O   VAL A 164     144.372 192.919 154.910  1.00176.60           O  
ATOM   1248  CB  VAL A 164     141.652 193.083 153.294  1.00176.60           C  
ATOM   1249  CG1 VAL A 164     142.765 193.333 152.286  1.00176.60           C  
ATOM   1250  CG2 VAL A 164     141.264 191.611 153.316  1.00176.60           C  
ATOM   1251  N   LYS A 165     142.862 191.789 156.151  1.00169.33           N  
ATOM   1252  CA  LYS A 165     143.847 190.966 156.838  1.00169.33           C  
ATOM   1253  C   LYS A 165     143.188 189.650 157.228  1.00169.33           C  
ATOM   1254  O   LYS A 165     141.994 189.437 156.999  1.00169.33           O  
ATOM   1255  CB  LYS A 165     144.418 191.694 158.058  1.00169.33           C  
ATOM   1256  CG  LYS A 165     143.402 191.940 159.161  1.00169.33           C  
ATOM   1257  CD  LYS A 165     144.028 192.660 160.343  1.00169.33           C  
ATOM   1258  CE  LYS A 165     142.988 192.974 161.406  1.00169.33           C  
ATOM   1259  NZ  LYS A 165     142.424 191.738 162.014  1.00169.33           N  
ATOM   1260  N   LYS A 166     143.978 188.762 157.828  1.00166.08           N  
ATOM   1261  CA  LYS A 166     143.473 187.460 158.230  1.00166.08           C  
ATOM   1262  C   LYS A 166     142.520 187.594 159.417  1.00166.08           C  
ATOM   1263  O   LYS A 166     142.439 188.634 160.078  1.00166.08           O  
ATOM   1264  CB  LYS A 166     144.627 186.522 158.583  1.00166.08           C  
ATOM   1265  CG  LYS A 166     145.459 186.078 157.393  1.00166.08           C  
ATOM   1266  CD  LYS A 166     146.714 185.350 157.845  1.00166.08           C  
ATOM   1267  CE  LYS A 166     146.373 184.010 158.477  1.00166.08           C  
ATOM   1268  NZ  LYS A 166     147.593 183.238 158.843  1.00166.08           N  
ATOM   1269  N   ALA A 167     141.790 186.513 159.684  1.00165.58           N  
ATOM   1270  CA  ALA A 167     140.896 186.408 160.836  1.00165.58           C  
ATOM   1271  C   ALA A 167     141.365 185.231 161.687  1.00165.58           C  
ATOM   1272  O   ALA A 167     140.866 184.112 161.556  1.00165.58           O  
ATOM   1273  CB  ALA A 167     139.439 186.243 160.390  1.00165.58           C  
ATOM   1274  N   ALA A 168     142.333 185.492 162.560  1.00160.30           N  
ATOM   1275  CA  ALA A 168     142.879 184.457 163.429  1.00160.30           C  
ATOM   1276  C   ALA A 168     142.376 184.620 164.859  1.00160.30           C  
ATOM   1277  O   ALA A 168     141.582 185.514 165.150  1.00160.30           O  
ATOM   1278  CB  ALA A 168     144.399 184.484 163.394  1.00160.30           C  
ATOM   1279  N   ALA A 175     138.733 179.581 160.630  1.00166.41           N  
ATOM   1280  CA  ALA A 175     140.179 179.768 160.654  1.00166.41           C  
ATOM   1281  C   ALA A 175     140.749 179.789 159.240  1.00166.41           C  
ATOM   1282  O   ALA A 175     140.130 179.277 158.306  1.00166.41           O  
ATOM   1283  CB  ALA A 175     140.842 178.674 161.478  1.00166.41           C  
ATOM   1284  N   LEU A 176     141.930 180.395 159.097  1.00168.69           N  
ATOM   1285  CA  LEU A 176     142.628 180.493 157.813  1.00168.69           C  
ATOM   1286  C   LEU A 176     141.777 181.216 156.771  1.00168.69           C  
ATOM   1287  O   LEU A 176     141.792 180.877 155.585  1.00168.69           O  
ATOM   1288  CB  LEU A 176     143.055 179.113 157.303  1.00168.69           C  
ATOM   1289  CG  LEU A 176     144.401 178.559 157.780  1.00168.69           C  
ATOM   1290  CD1 LEU A 176     145.534 179.503 157.402  1.00168.69           C  
ATOM   1291  CD2 LEU A 176     144.399 178.284 159.278  1.00168.69           C  
ATOM   1292  N   LYS A 177     141.031 182.224 157.215  1.00167.61           N  
ATOM   1293  CA  LYS A 177     140.254 183.072 156.326  1.00167.61           C  
ATOM   1294  C   LYS A 177     140.515 184.535 156.659  1.00167.61           C  
ATOM   1295  O   LYS A 177     140.959 184.875 157.758  1.00167.61           O  
ATOM   1296  CB  LYS A 177     138.752 182.769 156.426  1.00167.61           C  
ATOM   1297  CG  LYS A 177     138.159 183.021 157.804  1.00167.61           C  
ATOM   1298  CD  LYS A 177     136.685 182.653 157.848  1.00167.61           C  
ATOM   1299  CE  LYS A 177     136.490 181.145 157.814  1.00167.61           C  
ATOM   1300  NZ  LYS A 177     135.059 180.764 157.964  1.00167.61           N  
ATOM   1301  N   ILE A 178     140.235 185.400 155.689  1.00162.39           N  
ATOM   1302  CA  ILE A 178     140.633 186.800 155.748  1.00162.39           C  
ATOM   1303  C   ILE A 178     139.384 187.664 155.837  1.00162.39           C  
ATOM   1304  O   ILE A 178     138.306 187.290 155.359  1.00162.39           O  
ATOM   1305  CB  ILE A 178     141.503 187.200 154.536  1.00162.39           C  
ATOM   1306  CG1 ILE A 178     140.807 186.844 153.220  1.00162.39           C  
ATOM   1307  CG2 ILE A 178     142.865 186.528 154.615  1.00162.39           C  
ATOM   1308  CD1 ILE A 178     140.098 188.009 152.559  1.00162.39           C  
ATOM   1309  N   ILE A 179     139.533 188.833 156.458  1.00170.67           N  
ATOM   1310  CA  ILE A 179     138.424 189.751 156.688  1.00170.67           C  
ATOM   1311  C   ILE A 179     138.832 191.142 156.222  1.00170.67           C  
ATOM   1312  O   ILE A 179     139.989 191.547 156.377  1.00170.67           O  
ATOM   1313  CB  ILE A 179     137.991 189.767 158.171  1.00170.67           C  
ATOM   1314  CG1 ILE A 179     139.205 189.880 159.099  1.00170.67           C  
ATOM   1315  CG2 ILE A 179     137.176 188.526 158.501  1.00170.67           C  
ATOM   1316  CD1 ILE A 179     139.534 191.296 159.533  1.00170.67           C  
ATOM   1317  N   HIS A 180     137.879 191.867 155.639  1.00183.78           N  
ATOM   1318  CA  HIS A 180     138.118 193.191 155.065  1.00183.78           C  
ATOM   1319  C   HIS A 180     137.623 194.253 156.041  1.00183.78           C  
ATOM   1320  O   HIS A 180     136.424 194.537 156.110  1.00183.78           O  
ATOM   1321  CB  HIS A 180     137.439 193.321 153.706  1.00183.78           C  
ATOM   1322  CG  HIS A 180     137.490 194.704 153.136  1.00183.78           C  
ATOM   1323  ND1 HIS A 180     138.672 195.323 152.790  1.00183.78           N  
ATOM   1324  CD2 HIS A 180     136.504 195.584 152.841  1.00183.78           C  
ATOM   1325  CE1 HIS A 180     138.413 196.529 152.316  1.00183.78           C  
ATOM   1326  NE2 HIS A 180     137.105 196.711 152.335  1.00183.78           N  
ATOM   1327  N   ASP A 181     138.547 194.837 156.800  1.00195.11           N  
ATOM   1328  CA  ASP A 181     138.196 195.841 157.803  1.00195.11           C  
ATOM   1329  C   ASP A 181     137.851 197.137 157.080  1.00195.11           C  
ATOM   1330  O   ASP A 181     138.734 197.913 156.710  1.00195.11           O  
ATOM   1331  CB  ASP A 181     139.345 196.032 158.787  1.00195.11           C  
ATOM   1332  CG  ASP A 181     138.916 196.747 160.053  1.00195.11           C  
ATOM   1333  OD1 ASP A 181     138.189 196.139 160.866  1.00195.11           O  
ATOM   1334  OD2 ASP A 181     139.316 197.914 160.241  1.00195.11           O  
ATOM   1335  N   THR A 182     136.554 197.373 156.876  1.00193.08           N  
ATOM   1336  CA  THR A 182     136.118 198.298 155.833  1.00193.08           C  
ATOM   1337  C   THR A 182     136.148 199.748 156.306  1.00193.08           C  
ATOM   1338  O   THR A 182     136.899 200.572 155.773  1.00193.08           O  
ATOM   1339  CB  THR A 182     134.708 197.928 155.363  1.00193.08           C  
ATOM   1340  OG1 THR A 182     134.665 196.544 154.995  1.00193.08           O  
ATOM   1341  CG2 THR A 182     134.308 198.781 154.166  1.00193.08           C  
ATOM   1342  N   PHE A 183     135.337 200.077 157.309  1.00197.70           N  
ATOM   1343  CA  PHE A 183     134.903 201.450 157.530  1.00197.70           C  
ATOM   1344  C   PHE A 183     135.898 202.187 158.419  1.00197.70           C  
ATOM   1345  O   PHE A 183     136.099 201.812 159.580  1.00197.70           O  
ATOM   1346  CB  PHE A 183     133.506 201.475 158.150  1.00197.70           C  
ATOM   1347  CG  PHE A 183     132.439 200.894 157.265  1.00197.70           C  
ATOM   1348  CD1 PHE A 183     131.903 201.637 156.226  1.00197.70           C  
ATOM   1349  CD2 PHE A 183     131.967 199.608 157.475  1.00197.70           C  
ATOM   1350  CE1 PHE A 183     130.920 201.108 155.409  1.00197.70           C  
ATOM   1351  CE2 PHE A 183     130.983 199.074 156.661  1.00197.70           C  
ATOM   1352  CZ  PHE A 183     130.459 199.825 155.627  1.00197.70           C  
ATOM   1353  N   ARG A 184     136.512 203.233 157.873  1.00192.11           N  
ATOM   1354  CA  ARG A 184     137.491 204.059 158.576  1.00192.11           C  
ATOM   1355  C   ARG A 184     136.847 205.423 158.816  1.00192.11           C  
ATOM   1356  O   ARG A 184     136.992 206.344 158.009  1.00192.11           O  
ATOM   1357  CB  ARG A 184     138.791 204.181 157.777  1.00192.11           C  
ATOM   1358  CG  ARG A 184     139.519 202.865 157.525  1.00192.11           C  
ATOM   1359  CD  ARG A 184     140.381 202.454 158.718  1.00192.11           C  
ATOM   1360  NE  ARG A 184     139.595 202.034 159.875  1.00192.11           N  
ATOM   1361  CZ  ARG A 184     138.957 200.871 159.968  1.00192.11           C  
ATOM   1362  NH1 ARG A 184     138.262 200.580 161.058  1.00192.11           N  
ATOM   1363  NH2 ARG A 184     139.015 199.997 158.972  1.00192.11           N  
ATOM   1364  N   TRP A 185     136.136 205.553 159.932  1.00215.89           N  
ATOM   1365  CA  TRP A 185     135.575 206.830 160.350  1.00215.89           C  
ATOM   1366  C   TRP A 185     136.473 207.476 161.396  1.00215.89           C  
ATOM   1367  O   TRP A 185     136.935 206.805 162.325  1.00215.89           O  
ATOM   1368  CB  TRP A 185     134.160 206.648 160.908  1.00215.89           C  
ATOM   1369  CG  TRP A 185     134.086 205.789 162.143  1.00215.89           C  
ATOM   1370  CD1 TRP A 185     134.241 206.198 163.438  1.00215.89           C  
ATOM   1371  CD2 TRP A 185     133.850 204.376 162.195  1.00215.89           C  
ATOM   1372  NE1 TRP A 185     134.111 205.129 164.291  1.00215.89           N  
ATOM   1373  CE2 TRP A 185     133.871 203.999 163.554  1.00215.89           C  
ATOM   1374  CE3 TRP A 185     133.622 203.395 161.227  1.00215.89           C  
ATOM   1375  CZ2 TRP A 185     133.671 202.682 163.966  1.00215.89           C  
ATOM   1376  CZ3 TRP A 185     133.424 202.088 161.639  1.00215.89           C  
ATOM   1377  CH2 TRP A 185     133.450 201.744 162.996  1.00215.89           C  
ATOM   1378  N   VAL A 186     136.729 208.772 161.234  1.00234.55           N  
ATOM   1379  CA  VAL A 186     137.430 209.573 162.236  1.00234.55           C  
ATOM   1380  C   VAL A 186     136.478 210.554 162.921  1.00234.55           C  
ATOM   1381  O   VAL A 186     136.274 210.490 164.135  1.00234.55           O  
ATOM   1382  CB  VAL A 186     138.648 210.297 161.618  1.00234.55           C  
ATOM   1383  CG1 VAL A 186     138.304 210.901 160.261  1.00234.55           C  
ATOM   1384  CG2 VAL A 186     139.180 211.358 162.571  1.00234.55           C  
ATOM   1385  N   GLY A 187     135.889 211.471 162.157  1.00242.67           N  
ATOM   1386  CA  GLY A 187     134.822 212.320 162.646  1.00242.67           C  
ATOM   1387  C   GLY A 187     133.773 212.569 161.583  1.00242.67           C  
ATOM   1388  O   GLY A 187     132.774 213.254 161.825  1.00242.67           O  
ATOM   1389  N   LYS A 188     133.997 212.011 160.395  1.00241.35           N  
ATOM   1390  CA  LYS A 188     133.047 212.116 159.288  1.00241.35           C  
ATOM   1391  C   LYS A 188     132.289 210.798 159.127  1.00241.35           C  
ATOM   1392  O   LYS A 188     132.506 210.021 158.196  1.00241.35           O  
ATOM   1393  CB  LYS A 188     133.771 212.511 158.005  1.00241.35           C  
ATOM   1394  CG  LYS A 188     134.448 213.872 158.072  1.00241.35           C  
ATOM   1395  CD  LYS A 188     133.445 214.973 158.379  1.00241.35           C  
ATOM   1396  CE  LYS A 188     132.478 215.183 157.222  1.00241.35           C  
ATOM   1397  NZ  LYS A 188     133.165 215.687 156.001  1.00241.35           N  
ATOM   1398  N   LYS A 189     131.377 210.557 160.069  1.00233.44           N  
ATOM   1399  CA  LYS A 189     130.536 209.368 160.006  1.00233.44           C  
ATOM   1400  C   LYS A 189     129.445 209.469 158.947  1.00233.44           C  
ATOM   1401  O   LYS A 189     128.775 208.466 158.679  1.00233.44           O  
ATOM   1402  CB  LYS A 189     129.902 209.098 161.373  1.00233.44           C  
ATOM   1403  CG  LYS A 189     130.753 208.244 162.304  1.00233.44           C  
ATOM   1404  CD  LYS A 189     131.880 209.051 162.933  1.00233.44           C  
ATOM   1405  CE  LYS A 189     131.348 210.022 163.977  1.00233.44           C  
ATOM   1406  NZ  LYS A 189     132.444 210.758 164.666  1.00233.44           N  
ATOM   1407  N   SER A 190     129.250 210.642 158.343  1.00237.08           N  
ATOM   1408  CA  SER A 190     128.254 210.825 157.287  1.00237.08           C  
ATOM   1409  C   SER A 190     128.786 210.206 155.997  1.00237.08           C  
ATOM   1410  O   SER A 190     129.246 210.888 155.077  1.00237.08           O  
ATOM   1411  CB  SER A 190     127.923 212.301 157.109  1.00237.08           C  
ATOM   1412  OG  SER A 190     127.003 212.494 156.050  1.00237.08           O  
ATOM   1413  N   ALA A 191     128.721 208.877 155.936  1.00229.57           N  
ATOM   1414  CA  ALA A 191     129.099 208.099 154.765  1.00229.57           C  
ATOM   1415  C   ALA A 191     127.863 207.656 153.993  1.00229.57           C  
ATOM   1416  O   ALA A 191     126.837 207.329 154.601  1.00229.57           O  
ATOM   1417  CB  ALA A 191     129.912 206.869 155.167  1.00229.57           C  
ATOM   1418  N   PRO A 192     127.919 207.629 152.658  1.00228.81           N  
ATOM   1419  CA  PRO A 192     126.776 207.122 151.883  1.00228.81           C  
ATOM   1420  C   PRO A 192     126.586 205.616 151.970  1.00228.81           C  
ATOM   1421  O   PRO A 192     125.642 205.095 151.363  1.00228.81           O  
ATOM   1422  CB  PRO A 192     127.118 207.544 150.444  1.00228.81           C  
ATOM   1423  CG  PRO A 192     128.102 208.662 150.591  1.00228.81           C  
ATOM   1424  CD  PRO A 192     128.907 208.307 151.803  1.00228.81           C  
ATOM   1425  N   GLU A 193     127.444 204.901 152.696  1.00227.82           N  
ATOM   1426  CA  GLU A 193     127.301 203.467 152.906  1.00227.82           C  
ATOM   1427  C   GLU A 193     126.815 203.115 154.301  1.00227.82           C  
ATOM   1428  O   GLU A 193     126.118 202.112 154.467  1.00227.82           O  
ATOM   1429  CB  GLU A 193     128.629 202.745 152.641  1.00227.82           C  
ATOM   1430  CG  GLU A 193     129.170 202.941 151.233  1.00227.82           C  
ATOM   1431  CD  GLU A 193     130.480 202.214 151.006  1.00227.82           C  
ATOM   1432  OE1 GLU A 193     130.979 201.575 151.956  1.00227.82           O  
ATOM   1433  OE2 GLU A 193     131.011 202.282 149.878  1.00227.82           O  
ATOM   1434  N   LYS A 194     127.174 203.922 155.302  1.00221.33           N  
ATOM   1435  CA  LYS A 194     126.829 203.617 156.687  1.00221.33           C  
ATOM   1436  C   LYS A 194     125.325 203.696 156.915  1.00221.33           C  
ATOM   1437  O   LYS A 194     124.765 202.891 157.668  1.00221.33           O  
ATOM   1438  CB  LYS A 194     127.569 204.564 157.631  1.00221.33           C  
ATOM   1439  CG  LYS A 194     127.383 204.244 159.105  1.00221.33           C  
ATOM   1440  CD  LYS A 194     128.050 205.289 159.984  1.00221.33           C  
ATOM   1441  CE  LYS A 194     129.564 205.143 159.963  1.00221.33           C  
ATOM   1442  NZ  LYS A 194     130.013 203.895 160.639  1.00221.33           N  
ATOM   1443  N   ASP A 195     124.653 204.653 156.271  1.00228.62           N  
ATOM   1444  CA  ASP A 195     123.204 204.763 156.407  1.00228.62           C  
ATOM   1445  C   ASP A 195     122.500 203.517 155.881  1.00228.62           C  
ATOM   1446  O   ASP A 195     121.527 203.047 156.483  1.00228.62           O  
ATOM   1447  CB  ASP A 195     122.701 206.013 155.686  1.00228.62           C  
ATOM   1448  CG  ASP A 195     123.243 206.131 154.275  1.00228.62           C  
ATOM   1449  OD1 ASP A 195     124.088 205.295 153.890  1.00228.62           O  
ATOM   1450  OD2 ASP A 195     122.824 207.057 153.550  1.00228.62           O  
ATOM   1451  N   ILE A 196     122.970 202.968 154.759  1.00227.90           N  
ATOM   1452  CA  ILE A 196     122.452 201.677 154.316  1.00227.90           C  
ATOM   1453  C   ILE A 196     122.914 200.574 155.262  1.00227.90           C  
ATOM   1454  O   ILE A 196     122.161 199.639 155.564  1.00227.90           O  
ATOM   1455  CB  ILE A 196     122.872 201.401 152.859  1.00227.90           C  
ATOM   1456  CG1 ILE A 196     122.062 202.269 151.893  1.00227.90           C  
ATOM   1457  CG2 ILE A 196     122.701 199.929 152.511  1.00227.90           C  
ATOM   1458  CD1 ILE A 196     122.746 203.557 151.496  1.00227.90           C  
ATOM   1459  N   TRP A 197     124.149 200.676 155.760  1.00225.88           N  
ATOM   1460  CA  TRP A 197     124.632 199.725 156.758  1.00225.88           C  
ATOM   1461  C   TRP A 197     123.822 199.826 158.046  1.00225.88           C  
ATOM   1462  O   TRP A 197     123.582 198.818 158.720  1.00225.88           O  
ATOM   1463  CB  TRP A 197     126.117 199.960 157.032  1.00225.88           C  
ATOM   1464  CG  TRP A 197     126.681 199.066 158.094  1.00225.88           C  
ATOM   1465  CD1 TRP A 197     126.997 199.411 159.375  1.00225.88           C  
ATOM   1466  CD2 TRP A 197     126.999 197.674 157.963  1.00225.88           C  
ATOM   1467  NE1 TRP A 197     127.491 198.322 160.051  1.00225.88           N  
ATOM   1468  CE2 TRP A 197     127.502 197.243 159.207  1.00225.88           C  
ATOM   1469  CE3 TRP A 197     126.907 196.752 156.916  1.00225.88           C  
ATOM   1470  CZ2 TRP A 197     127.912 195.930 159.432  1.00225.88           C  
ATOM   1471  CZ3 TRP A 197     127.314 195.449 157.142  1.00225.88           C  
ATOM   1472  CH2 TRP A 197     127.810 195.051 158.389  1.00225.88           C  
ATOM   1473  N   VAL A 198     123.392 201.040 158.400  1.00224.35           N  
ATOM   1474  CA  VAL A 198     122.432 201.211 159.487  1.00224.35           C  
ATOM   1475  C   VAL A 198     121.056 200.712 159.065  1.00224.35           C  
ATOM   1476  O   VAL A 198     120.307 200.164 159.885  1.00224.35           O  
ATOM   1477  CB  VAL A 198     122.395 202.684 159.941  1.00224.35           C  
ATOM   1478  CG1 VAL A 198     121.224 202.936 160.879  1.00224.35           C  
ATOM   1479  CG2 VAL A 198     123.702 203.058 160.625  1.00224.35           C  
ATOM   1480  N   GLY A 199     120.704 200.866 157.788  1.00223.61           N  
ATOM   1481  CA  GLY A 199     119.441 200.324 157.314  1.00223.61           C  
ATOM   1482  C   GLY A 199     119.421 198.809 157.356  1.00223.61           C  
ATOM   1483  O   GLY A 199     118.387 198.201 157.649  1.00223.61           O  
ATOM   1484  N   GLU A 200     120.560 198.176 157.065  1.00225.16           N  
ATOM   1485  CA  GLU A 200     120.666 196.734 157.257  1.00225.16           C  
ATOM   1486  C   GLU A 200     120.688 196.395 158.742  1.00225.16           C  
ATOM   1487  O   GLU A 200     120.139 195.370 159.164  1.00225.16           O  
ATOM   1488  CB  GLU A 200     121.924 196.202 156.569  1.00225.16           C  
ATOM   1489  CG  GLU A 200     121.981 196.439 155.066  1.00225.16           C  
ATOM   1490  CD  GLU A 200     120.906 195.691 154.305  1.00225.16           C  
ATOM   1491  OE1 GLU A 200     120.524 194.585 154.739  1.00225.16           O  
ATOM   1492  OE2 GLU A 200     120.448 196.208 153.265  1.00225.16           O  
ATOM   1493  N   TRP A 201     121.330 197.249 159.544  1.00226.09           N  
ATOM   1494  CA  TRP A 201     121.341 197.083 160.995  1.00226.09           C  
ATOM   1495  C   TRP A 201     119.927 197.134 161.563  1.00226.09           C  
ATOM   1496  O   TRP A 201     119.529 196.271 162.354  1.00226.09           O  
ATOM   1497  CB  TRP A 201     122.220 198.165 161.627  1.00226.09           C  
ATOM   1498  CG  TRP A 201     122.312 198.111 163.125  1.00226.09           C  
ATOM   1499  CD1 TRP A 201     121.436 198.650 164.020  1.00226.09           C  
ATOM   1500  CD2 TRP A 201     123.364 197.521 163.900  1.00226.09           C  
ATOM   1501  NE1 TRP A 201     121.862 198.412 165.304  1.00226.09           N  
ATOM   1502  CE2 TRP A 201     123.045 197.722 165.258  1.00226.09           C  
ATOM   1503  CE3 TRP A 201     124.538 196.833 163.578  1.00226.09           C  
ATOM   1504  CZ2 TRP A 201     123.858 197.261 166.292  1.00226.09           C  
ATOM   1505  CZ3 TRP A 201     125.344 196.378 164.607  1.00226.09           C  
ATOM   1506  CH2 TRP A 201     125.000 196.593 165.946  1.00226.09           C  
ATOM   1507  N   LYS A 202     119.151 198.146 161.163  1.00224.49           N  
ATOM   1508  CA  LYS A 202     117.920 198.488 161.872  1.00224.49           C  
ATOM   1509  C   LYS A 202     116.842 197.428 161.673  1.00224.49           C  
ATOM   1510  O   LYS A 202     116.077 197.135 162.600  1.00224.49           O  
ATOM   1511  CB  LYS A 202     117.419 199.856 161.410  1.00224.49           C  
ATOM   1512  CG  LYS A 202     116.116 200.301 162.053  1.00224.49           C  
ATOM   1513  CD  LYS A 202     116.298 200.613 163.528  1.00224.49           C  
ATOM   1514  CE  LYS A 202     114.986 201.048 164.159  1.00224.49           C  
ATOM   1515  NZ  LYS A 202     114.495 202.330 163.581  1.00224.49           N  
ATOM   1516  N   GLU A 203     116.766 196.841 160.478  1.00218.68           N  
ATOM   1517  CA  GLU A 203     115.670 195.933 160.160  1.00218.68           C  
ATOM   1518  C   GLU A 203     115.776 194.613 160.912  1.00218.68           C  
ATOM   1519  O   GLU A 203     114.762 193.929 161.084  1.00218.68           O  
ATOM   1520  CB  GLU A 203     115.619 195.676 158.653  1.00218.68           C  
ATOM   1521  CG  GLU A 203     115.298 196.912 157.833  1.00218.68           C  
ATOM   1522  CD  GLU A 203     113.893 197.428 158.081  1.00218.68           C  
ATOM   1523  OE1 GLU A 203     112.998 196.606 158.372  1.00218.68           O  
ATOM   1524  OE2 GLU A 203     113.684 198.655 157.987  1.00218.68           O  
ATOM   1525  N   VAL A 204     116.971 194.245 161.362  1.00224.13           N  
ATOM   1526  CA  VAL A 204     117.207 192.975 162.033  1.00224.13           C  
ATOM   1527  C   VAL A 204     117.379 193.189 163.540  1.00224.13           C  
ATOM   1528  O   VAL A 204     117.859 192.309 164.251  1.00224.13           O  
ATOM   1529  CB  VAL A 204     118.409 192.240 161.416  1.00224.13           C  
ATOM   1530  CG1 VAL A 204     118.372 190.748 161.739  1.00224.13           C  
ATOM   1531  CG2 VAL A 204     118.447 192.460 159.912  1.00224.13           C  
ATOM   1532  N   LEU A 205     116.977 194.361 164.033  1.00226.36           N  
ATOM   1533  CA  LEU A 205     116.887 194.620 165.465  1.00226.36           C  
ATOM   1534  C   LEU A 205     115.550 194.193 166.053  1.00226.36           C  
ATOM   1535  O   LEU A 205     115.486 193.841 167.237  1.00226.36           O  
ATOM   1536  CB  LEU A 205     117.106 196.108 165.752  1.00226.36           C  
ATOM   1537  CG  LEU A 205     118.466 196.700 165.382  1.00226.36           C  
ATOM   1538  CD1 LEU A 205     118.533 198.163 165.795  1.00226.36           C  
ATOM   1539  CD2 LEU A 205     119.599 195.899 166.004  1.00226.36           C  
ATOM   1540  N   ALA A 206     114.484 194.216 165.253  1.00227.76           N  
ATOM   1541  CA  ALA A 206     113.168 193.810 165.735  1.00227.76           C  
ATOM   1542  C   ALA A 206     113.067 192.291 165.815  1.00227.76           C  
ATOM   1543  O   ALA A 206     112.756 191.733 166.872  1.00227.76           O  
ATOM   1544  CB  ALA A 206     112.075 194.380 164.827  1.00227.76           C  
ATOM   1545  N   HIS A 207     113.329 191.608 164.705  1.00227.33           N  
ATOM   1546  CA  HIS A 207     113.409 190.156 164.715  1.00227.33           C  
ATOM   1547  C   HIS A 207     114.789 189.715 165.185  1.00227.33           C  
ATOM   1548  O   HIS A 207     115.810 190.280 164.779  1.00227.33           O  
ATOM   1549  CB  HIS A 207     113.119 189.592 163.325  1.00227.33           C  
ATOM   1550  CG  HIS A 207     112.853 188.119 163.315  1.00227.33           C  
ATOM   1551  ND1 HIS A 207     112.887 187.364 162.162  1.00227.33           N  
ATOM   1552  CD2 HIS A 207     112.544 187.262 164.316  1.00227.33           C  
ATOM   1553  CE1 HIS A 207     112.613 186.105 162.454  1.00227.33           C  
ATOM   1554  NE2 HIS A 207     112.401 186.016 163.754  1.00227.33           N  
ATOM   1555  N   ASN A 208     114.810 188.692 166.043  1.00231.37           N  
ATOM   1556  CA  ASN A 208     115.995 188.238 166.763  1.00231.37           C  
ATOM   1557  C   ASN A 208     116.662 189.401 167.490  1.00231.37           C  
ATOM   1558  O   ASN A 208     117.682 189.927 167.027  1.00231.37           O  
ATOM   1559  CB  ASN A 208     116.987 187.570 165.807  1.00231.37           C  
ATOM   1560  CG  ASN A 208     116.400 186.356 165.114  1.00231.37           C  
ATOM   1561  OD1 ASN A 208     116.249 186.338 163.892  1.00231.37           O  
ATOM   1562  ND2 ASN A 208     116.067 185.333 165.892  1.00231.37           N  
ATOM   1563  N   PRO A 209     116.110 189.832 168.630  1.00237.23           N  
ATOM   1564  CA  PRO A 209     116.675 190.990 169.343  1.00237.23           C  
ATOM   1565  C   PRO A 209     118.058 190.748 169.930  1.00237.23           C  
ATOM   1566  O   PRO A 209     118.722 191.721 170.313  1.00237.23           O  
ATOM   1567  CB  PRO A 209     115.647 191.254 170.454  1.00237.23           C  
ATOM   1568  CG  PRO A 209     114.389 190.587 169.982  1.00237.23           C  
ATOM   1569  CD  PRO A 209     114.856 189.370 169.247  1.00237.23           C  
ATOM   1570  N   GLU A 210     118.512 189.498 170.013  1.00234.16           N  
ATOM   1571  CA  GLU A 210     119.807 189.183 170.607  1.00234.16           C  
ATOM   1572  C   GLU A 210     120.968 189.484 169.662  1.00234.16           C  
ATOM   1573  O   GLU A 210     121.810 188.620 169.398  1.00234.16           O  
ATOM   1574  CB  GLU A 210     119.832 187.714 171.051  1.00234.16           C  
ATOM   1575  CG  GLU A 210     119.540 186.697 169.950  1.00234.16           C  
ATOM   1576  CD  GLU A 210     118.058 186.422 169.781  1.00234.16           C  
ATOM   1577  OE1 GLU A 210     117.240 187.184 170.339  1.00234.16           O  
ATOM   1578  OE2 GLU A 210     117.711 185.442 169.087  1.00234.16           O  
ATOM   1579  N   LEU A 211     121.033 190.722 169.170  1.00227.23           N  
ATOM   1580  CA  LEU A 211     121.962 191.075 168.108  1.00227.23           C  
ATOM   1581  C   LEU A 211     122.683 192.393 168.361  1.00227.23           C  
ATOM   1582  O   LEU A 211     123.522 192.784 167.544  1.00227.23           O  
ATOM   1583  CB  LEU A 211     121.231 191.138 166.757  1.00227.23           C  
ATOM   1584  CG  LEU A 211     120.865 189.781 166.149  1.00227.23           C  
ATOM   1585  CD1 LEU A 211     120.151 189.968 164.822  1.00227.23           C  
ATOM   1586  CD2 LEU A 211     122.092 188.900 165.977  1.00227.23           C  
ATOM   1587  N   GLU A 212     122.379 193.089 169.460  1.00223.17           N  
ATOM   1588  CA  GLU A 212     123.067 194.325 169.819  1.00223.17           C  
ATOM   1589  C   GLU A 212     124.539 194.105 170.144  1.00223.17           C  
ATOM   1590  O   GLU A 212     125.317 195.065 170.119  1.00223.17           O  
ATOM   1591  CB  GLU A 212     122.376 194.983 171.015  1.00223.17           C  
ATOM   1592  CG  GLU A 212     120.988 195.529 170.727  1.00223.17           C  
ATOM   1593  CD  GLU A 212     121.009 196.708 169.775  1.00223.17           C  
ATOM   1594  OE1 GLU A 212     121.993 197.476 169.799  1.00223.17           O  
ATOM   1595  OE2 GLU A 212     120.037 196.872 169.010  1.00223.17           O  
ATOM   1596  N   ARG A 213     124.937 192.870 170.447  1.00208.70           N  
ATOM   1597  CA  ARG A 213     126.299 192.541 170.851  1.00208.70           C  
ATOM   1598  C   ARG A 213     127.133 191.940 169.725  1.00208.70           C  
ATOM   1599  O   ARG A 213     128.272 192.365 169.509  1.00208.70           O  
ATOM   1600  CB  ARG A 213     126.276 191.582 172.048  1.00208.70           C  
ATOM   1601  CG  ARG A 213     127.654 191.278 172.616  1.00208.70           C  
ATOM   1602  CD  ARG A 213     128.258 192.514 173.266  1.00208.70           C  
ATOM   1603  NE  ARG A 213     129.558 192.241 173.873  1.00208.70           N  
ATOM   1604  CZ  ARG A 213     130.362 193.177 174.367  1.00208.70           C  
ATOM   1605  NH1 ARG A 213     130.002 194.452 174.327  1.00208.70           N  
ATOM   1606  NH2 ARG A 213     131.527 192.838 174.901  1.00208.70           N  
ATOM   1607  N   TYR A 214     126.596 190.962 168.998  1.00207.76           N  
ATOM   1608  CA  TYR A 214     127.400 190.212 168.042  1.00207.76           C  
ATOM   1609  C   TYR A 214     127.438 190.846 166.657  1.00207.76           C  
ATOM   1610  O   TYR A 214     128.373 190.571 165.897  1.00207.76           O  
ATOM   1611  CB  TYR A 214     126.877 188.777 167.931  1.00207.76           C  
ATOM   1612  CG  TYR A 214     127.200 187.919 169.134  1.00207.76           C  
ATOM   1613  CD1 TYR A 214     128.245 188.250 169.986  1.00207.76           C  
ATOM   1614  CD2 TYR A 214     126.454 186.784 169.423  1.00207.76           C  
ATOM   1615  CE1 TYR A 214     128.545 187.471 171.087  1.00207.76           C  
ATOM   1616  CE2 TYR A 214     126.745 185.999 170.523  1.00207.76           C  
ATOM   1617  CZ  TYR A 214     127.792 186.347 171.351  1.00207.76           C  
ATOM   1618  OH  TYR A 214     128.085 185.571 172.450  1.00207.76           O  
ATOM   1619  N   VAL A 215     126.456 191.681 166.307  1.00219.10           N  
ATOM   1620  CA  VAL A 215     126.499 192.377 165.021  1.00219.10           C  
ATOM   1621  C   VAL A 215     127.359 193.629 165.102  1.00219.10           C  
ATOM   1622  O   VAL A 215     127.754 194.177 164.065  1.00219.10           O  
ATOM   1623  CB  VAL A 215     125.066 192.706 164.554  1.00219.10           C  
ATOM   1624  CG1 VAL A 215     125.054 193.236 163.124  1.00219.10           C  
ATOM   1625  CG2 VAL A 215     124.189 191.478 164.660  1.00219.10           C  
ATOM   1626  N   LYS A 216     127.695 194.068 166.316  1.00213.92           N  
ATOM   1627  CA  LYS A 216     128.644 195.148 166.559  1.00213.92           C  
ATOM   1628  C   LYS A 216     130.066 194.806 166.132  1.00213.92           C  
ATOM   1629  O   LYS A 216     130.919 195.699 166.118  1.00213.92           O  
ATOM   1630  CB  LYS A 216     128.632 195.532 168.040  1.00213.92           C  
ATOM   1631  N   ARG A 217     130.342 193.550 165.783  1.00209.79           N  
ATOM   1632  CA  ARG A 217     131.680 193.146 165.370  1.00209.79           C  
ATOM   1633  C   ARG A 217     131.657 192.458 164.010  1.00209.79           C  
ATOM   1634  O   ARG A 217     132.633 192.538 163.257  1.00209.79           O  
ATOM   1635  CB  ARG A 217     132.301 192.224 166.423  1.00209.79           C  
ATOM   1636  CG  ARG A 217     133.730 191.783 166.130  1.00209.79           C  
ATOM   1637  CD  ARG A 217     134.738 192.881 166.446  1.00209.79           C  
ATOM   1638  NE  ARG A 217     134.842 193.876 165.382  1.00209.79           N  
ATOM   1639  CZ  ARG A 217     135.542 193.707 164.264  1.00209.79           C  
ATOM   1640  NH1 ARG A 217     136.214 192.582 164.064  1.00209.79           N  
ATOM   1641  NH2 ARG A 217     135.579 194.667 163.351  1.00209.79           N  
ATOM   1642  N   CYS A 218     130.557 191.783 163.684  1.00203.67           N  
ATOM   1643  CA  CYS A 218     130.527 190.932 162.502  1.00203.67           C  
ATOM   1644  C   CYS A 218     130.621 191.782 161.241  1.00203.67           C  
ATOM   1645  O   CYS A 218     130.030 192.862 161.151  1.00203.67           O  
ATOM   1646  CB  CYS A 218     129.255 190.088 162.474  1.00203.67           C  
ATOM   1647  SG  CYS A 218     127.747 190.980 162.033  1.00203.67           S  
ATOM   1648  N   MET A 219     131.388 191.295 160.269  1.00197.19           N  
ATOM   1649  CA  MET A 219     131.845 192.114 159.159  1.00197.19           C  
ATOM   1650  C   MET A 219     131.871 191.261 157.896  1.00197.19           C  
ATOM   1651  O   MET A 219     131.788 190.031 157.951  1.00197.19           O  
ATOM   1652  CB  MET A 219     133.225 192.706 159.481  1.00197.19           C  
ATOM   1653  CG  MET A 219     133.711 193.813 158.572  1.00197.19           C  
ATOM   1654  SD  MET A 219     135.194 194.564 159.262  1.00197.19           S  
ATOM   1655  CE  MET A 219     136.310 193.163 159.224  1.00197.19           C  
ATOM   1656  N   ASP A 220     131.982 191.927 156.747  1.00195.28           N  
ATOM   1657  CA  ASP A 220     131.990 191.233 155.464  1.00195.28           C  
ATOM   1658  C   ASP A 220     133.251 190.387 155.319  1.00195.28           C  
ATOM   1659  O   ASP A 220     134.372 190.894 155.435  1.00195.28           O  
ATOM   1660  CB  ASP A 220     131.864 192.230 154.312  1.00195.28           C  
ATOM   1661  CG  ASP A 220     132.847 193.381 154.414  1.00195.28           C  
ATOM   1662  OD1 ASP A 220     133.522 193.508 155.455  1.00195.28           O  
ATOM   1663  OD2 ASP A 220     132.942 194.164 153.445  1.00195.28           O  
ATOM   1664  N   ASP A 221     133.059 189.096 155.070  1.00177.77           N  
ATOM   1665  CA  ASP A 221     134.131 188.175 154.730  1.00177.77           C  
ATOM   1666  C   ASP A 221     134.314 188.100 153.215  1.00177.77           C  
ATOM   1667  O   ASP A 221     133.510 188.616 152.436  1.00177.77           O  
ATOM   1668  CB  ASP A 221     133.852 186.788 155.309  1.00177.77           C  
ATOM   1669  CG  ASP A 221     132.514 186.226 154.864  1.00177.77           C  
ATOM   1670  OD1 ASP A 221     131.718 186.977 154.261  1.00177.77           O  
ATOM   1671  OD2 ASP A 221     132.258 185.031 155.119  1.00177.77           O  
ATOM   1672  N   LEU A 222     135.400 187.440 152.801  1.00154.77           N  
ATOM   1673  CA  LEU A 222     135.667 187.144 151.390  1.00154.77           C  
ATOM   1674  C   LEU A 222     135.939 185.646 151.276  1.00154.77           C  
ATOM   1675  O   LEU A 222     137.089 185.199 151.285  1.00154.77           O  
ATOM   1676  CB  LEU A 222     136.843 187.978 150.860  1.00154.77           C  
ATOM   1677  CG  LEU A 222     136.607 189.416 150.383  1.00154.77           C  
ATOM   1678  CD1 LEU A 222     135.562 189.458 149.279  1.00154.77           C  
ATOM   1679  CD2 LEU A 222     136.233 190.350 151.527  1.00154.77           C  
ATOM   1680  N   ASN A 223     134.860 184.875 151.168  1.00145.35           N  
ATOM   1681  CA  ASN A 223     134.964 183.439 150.978  1.00145.35           C  
ATOM   1682  C   ASN A 223     135.516 183.122 149.587  1.00145.35           C  
ATOM   1683  O   ASN A 223     135.351 183.907 148.649  1.00145.35           O  
ATOM   1684  CB  ASN A 223     133.601 182.777 151.168  1.00145.35           C  
ATOM   1685  CG  ASN A 223     132.510 183.440 150.352  1.00145.35           C  
ATOM   1686  OD1 ASN A 223     132.728 184.476 149.726  1.00145.35           O  
ATOM   1687  ND2 ASN A 223     131.326 182.839 150.350  1.00145.35           N  
ATOM   1688  N   PRO A 224     136.184 181.970 149.428  1.00142.10           N  
ATOM   1689  CA  PRO A 224     136.884 181.679 148.167  1.00142.10           C  
ATOM   1690  C   PRO A 224     135.970 181.478 146.966  1.00142.10           C  
ATOM   1691  O   PRO A 224     136.449 181.124 145.884  1.00142.10           O  
ATOM   1692  CB  PRO A 224     137.642 180.383 148.481  1.00142.10           C  
ATOM   1693  CG  PRO A 224     137.793 180.377 149.951  1.00142.10           C  
ATOM   1694  CD  PRO A 224     136.556 181.022 150.492  1.00142.10           C  
ATOM   1695  N   LEU A 225     134.665 181.689 147.130  1.00141.78           N  
ATOM   1696  CA  LEU A 225     133.775 181.784 145.979  1.00141.78           C  
ATOM   1697  C   LEU A 225     133.580 183.219 145.507  1.00141.78           C  
ATOM   1698  O   LEU A 225     133.394 183.450 144.307  1.00141.78           O  
ATOM   1699  CB  LEU A 225     132.417 181.159 146.309  1.00141.78           C  
ATOM   1700  CG  LEU A 225     131.405 181.083 145.163  1.00141.78           C  
ATOM   1701  CD1 LEU A 225     131.978 180.290 144.000  1.00141.78           C  
ATOM   1702  CD2 LEU A 225     130.104 180.466 145.641  1.00141.78           C  
ATOM   1703  N   LYS A 226     133.604 184.186 146.423  1.00141.23           N  
ATOM   1704  CA  LYS A 226     133.487 185.587 146.034  1.00141.23           C  
ATOM   1705  C   LYS A 226     134.788 186.124 145.447  1.00141.23           C  
ATOM   1706  O   LYS A 226     134.757 187.034 144.611  1.00141.23           O  
ATOM   1707  CB  LYS A 226     133.049 186.430 147.233  1.00141.23           C  
ATOM   1708  CG  LYS A 226     132.703 187.872 146.898  1.00141.23           C  
ATOM   1709  CD  LYS A 226     132.234 188.625 148.132  1.00141.23           C  
ATOM   1710  CE  LYS A 226     131.924 190.078 147.812  1.00141.23           C  
ATOM   1711  NZ  LYS A 226     131.506 190.834 149.024  1.00141.23           N  
ATOM   1712  N   THR A 227     135.931 185.571 145.862  1.00146.59           N  
ATOM   1713  CA  THR A 227     137.219 186.182 145.545  1.00146.59           C  
ATOM   1714  C   THR A 227     137.584 186.010 144.074  1.00146.59           C  
ATOM   1715  O   THR A 227     138.087 186.947 143.445  1.00146.59           O  
ATOM   1716  CB  THR A 227     138.312 185.594 146.437  1.00146.59           C  
ATOM   1717  OG1 THR A 227     138.373 184.175 146.249  1.00146.59           O  
ATOM   1718  CG2 THR A 227     138.023 185.896 147.900  1.00146.59           C  
ATOM   1719  N   LEU A 228     137.345 184.825 143.505  1.00142.16           N  
ATOM   1720  CA  LEU A 228     137.648 184.636 142.089  1.00142.16           C  
ATOM   1721  C   LEU A 228     136.677 185.411 141.208  1.00142.16           C  
ATOM   1722  O   LEU A 228     137.069 185.911 140.148  1.00142.16           O  
ATOM   1723  CB  LEU A 228     137.651 183.150 141.718  1.00142.16           C  
ATOM   1724  CG  LEU A 228     136.348 182.375 141.517  1.00142.16           C  
ATOM   1725  CD1 LEU A 228     136.609 181.130 140.686  1.00142.16           C  
ATOM   1726  CD2 LEU A 228     135.749 181.990 142.850  1.00142.16           C  
ATOM   1727  N   ASN A 229     135.417 185.524 141.625  1.00148.13           N  
ATOM   1728  CA  ASN A 229     134.458 186.379 140.937  1.00148.13           C  
ATOM   1729  C   ASN A 229     134.638 187.852 141.280  1.00148.13           C  
ATOM   1730  O   ASN A 229     133.919 188.693 140.731  1.00148.13           O  
ATOM   1731  CB  ASN A 229     133.030 185.936 141.264  1.00148.13           C  
ATOM   1732  CG  ASN A 229     132.734 184.527 140.786  1.00148.13           C  
ATOM   1733  OD1 ASN A 229     132.489 183.626 141.587  1.00148.13           O  
ATOM   1734  ND2 ASN A 229     132.756 184.331 139.472  1.00148.13           N  
ATOM   1735  N   LEU A 230     135.571 188.178 142.176  1.00150.66           N  
ATOM   1736  CA  LEU A 230     136.116 189.524 142.290  1.00150.66           C  
ATOM   1737  C   LEU A 230     137.362 189.713 141.435  1.00150.66           C  
ATOM   1738  O   LEU A 230     137.669 190.845 141.044  1.00150.66           O  
ATOM   1739  CB  LEU A 230     136.441 189.841 143.754  1.00150.66           C  
ATOM   1740  CG  LEU A 230     136.880 191.268 144.091  1.00150.66           C  
ATOM   1741  CD1 LEU A 230     135.799 192.269 143.711  1.00150.66           C  
ATOM   1742  CD2 LEU A 230     137.235 191.388 145.565  1.00150.66           C  
ATOM   1743  N   PHE A 231     138.069 188.626 141.131  1.00148.16           N  
ATOM   1744  CA  PHE A 231     139.267 188.659 140.301  1.00148.16           C  
ATOM   1745  C   PHE A 231     138.946 188.531 138.820  1.00148.16           C  
ATOM   1746  O   PHE A 231     139.729 188.990 137.981  1.00148.16           O  
ATOM   1747  CB  PHE A 231     140.230 187.541 140.711  1.00148.16           C  
ATOM   1748  CG  PHE A 231     140.879 187.757 142.049  1.00148.16           C  
ATOM   1749  CD1 PHE A 231     140.940 189.022 142.610  1.00148.16           C  
ATOM   1750  CD2 PHE A 231     141.431 186.693 142.743  1.00148.16           C  
ATOM   1751  CE1 PHE A 231     141.538 189.221 143.839  1.00148.16           C  
ATOM   1752  CE2 PHE A 231     142.030 186.886 143.973  1.00148.16           C  
ATOM   1753  CZ  PHE A 231     142.084 188.152 144.522  1.00148.16           C  
ATOM   1754  N   LYS A 232     137.814 187.910 138.483  1.00142.04           N  
ATOM   1755  CA  LYS A 232     137.533 187.536 137.103  1.00142.04           C  
ATOM   1756  C   LYS A 232     137.188 188.737 136.232  1.00142.04           C  
ATOM   1757  O   LYS A 232     137.314 188.651 135.006  1.00142.04           O  
ATOM   1758  CB  LYS A 232     136.382 186.526 137.070  1.00142.04           C  
ATOM   1759  CG  LYS A 232     136.242 185.748 135.774  1.00142.04           C  
ATOM   1760  CD  LYS A 232     135.193 184.657 135.908  1.00142.04           C  
ATOM   1761  CE  LYS A 232     135.699 183.511 136.768  1.00142.04           C  
ATOM   1762  NZ  LYS A 232     134.723 182.388 136.831  1.00142.04           N  
ATOM   1763  N   GLN A 233     136.765 189.851 136.826  1.00152.48           N  
ATOM   1764  CA  GLN A 233     136.340 191.013 136.060  1.00152.48           C  
ATOM   1765  C   GLN A 233     137.367 192.139 136.044  1.00152.48           C  
ATOM   1766  O   GLN A 233     137.115 193.175 135.421  1.00152.48           O  
ATOM   1767  CB  GLN A 233     135.006 191.540 136.603  1.00152.48           C  
ATOM   1768  CG  GLN A 233     135.123 192.347 137.887  1.00152.48           C  
ATOM   1769  CD  GLN A 233     135.205 191.473 139.124  1.00152.48           C  
ATOM   1770  OE1 GLN A 233     135.497 190.280 139.039  1.00152.48           O  
ATOM   1771  NE2 GLN A 233     134.943 192.064 140.284  1.00152.48           N  
ATOM   1772  N   ILE A 234     138.514 191.969 136.707  1.00149.20           N  
ATOM   1773  CA  ILE A 234     139.579 192.957 136.575  1.00149.20           C  
ATOM   1774  C   ILE A 234     140.206 192.862 135.187  1.00149.20           C  
ATOM   1775  O   ILE A 234     140.098 191.849 134.485  1.00149.20           O  
ATOM   1776  CB  ILE A 234     140.639 192.788 137.676  1.00149.20           C  
ATOM   1777  CG1 ILE A 234     141.513 191.564 137.399  1.00149.20           C  
ATOM   1778  CG2 ILE A 234     139.977 192.671 139.040  1.00149.20           C  
ATOM   1779  CD1 ILE A 234     142.733 191.478 138.287  1.00149.20           C  
ATOM   1780  N   LYS A 235     140.872 193.939 134.786  1.00159.04           N  
ATOM   1781  CA  LYS A 235     141.367 194.053 133.423  1.00159.04           C  
ATOM   1782  C   LYS A 235     142.805 193.553 133.328  1.00159.04           C  
ATOM   1783  O   LYS A 235     143.536 193.485 134.319  1.00159.04           O  
ATOM   1784  CB  LYS A 235     141.281 195.500 132.938  1.00159.04           C  
ATOM   1785  CG  LYS A 235     139.885 196.099 133.011  1.00159.04           C  
ATOM   1786  CD  LYS A 235     138.875 195.239 132.270  1.00159.04           C  
ATOM   1787  CE  LYS A 235     139.085 195.314 130.767  1.00159.04           C  
ATOM   1788  NZ  LYS A 235     138.102 194.476 130.027  1.00159.04           N  
ATOM   1789  N   SER A 236     143.205 193.198 132.106  1.00158.04           N  
ATOM   1790  CA  SER A 236     144.573 192.776 131.834  1.00158.04           C  
ATOM   1791  C   SER A 236     145.527 193.945 131.629  1.00158.04           C  
ATOM   1792  O   SER A 236     146.743 193.729 131.584  1.00158.04           O  
ATOM   1793  CB  SER A 236     144.608 191.866 130.602  1.00158.04           C  
ATOM   1794  OG  SER A 236     143.841 190.693 130.812  1.00158.04           O  
ATOM   1795  N   ALA A 237     145.011 195.170 131.514  1.00162.93           N  
ATOM   1796  CA  ALA A 237     145.849 196.343 131.293  1.00162.93           C  
ATOM   1797  C   ALA A 237     146.678 196.736 132.508  1.00162.93           C  
ATOM   1798  O   ALA A 237     147.562 197.589 132.375  1.00162.93           O  
ATOM   1799  CB  ALA A 237     144.983 197.527 130.860  1.00162.93           C  
ATOM   1800  N   ASP A 238     146.425 196.148 133.681  1.00163.82           N  
ATOM   1801  CA  ASP A 238     147.174 196.537 134.870  1.00163.82           C  
ATOM   1802  C   ASP A 238     147.589 195.344 135.726  1.00163.82           C  
ATOM   1803  O   ASP A 238     147.802 195.506 136.934  1.00163.82           O  
ATOM   1804  CB  ASP A 238     146.359 197.524 135.714  1.00163.82           C  
ATOM   1805  CG  ASP A 238     144.972 197.004 136.043  1.00163.82           C  
ATOM   1806  OD1 ASP A 238     144.585 195.948 135.501  1.00163.82           O  
ATOM   1807  OD2 ASP A 238     144.267 197.655 136.842  1.00163.82           O  
ATOM   1808  N   CYS A 239     147.710 194.151 135.138  1.00164.60           N  
ATOM   1809  CA  CYS A 239     148.306 193.030 135.856  1.00164.60           C  
ATOM   1810  C   CYS A 239     149.813 193.184 136.019  1.00164.60           C  
ATOM   1811  O   CYS A 239     150.394 192.562 136.914  1.00164.60           O  
ATOM   1812  CB  CYS A 239     147.994 191.715 135.138  1.00164.60           C  
ATOM   1813  SG  CYS A 239     146.243 191.268 135.125  1.00164.60           S  
ATOM   1814  N   GLU A 240     150.455 194.000 135.180  1.00163.99           N  
ATOM   1815  CA  GLU A 240     151.884 194.258 135.323  1.00163.99           C  
ATOM   1816  C   GLU A 240     152.195 195.158 136.511  1.00163.99           C  
ATOM   1817  O   GLU A 240     153.352 195.224 136.938  1.00163.99           O  
ATOM   1818  CB  GLU A 240     152.437 194.873 134.037  1.00163.99           C  
ATOM   1819  CG  GLU A 240     152.462 193.911 132.857  1.00163.99           C  
ATOM   1820  CD  GLU A 240     151.142 193.861 132.113  1.00163.99           C  
ATOM   1821  OE1 GLU A 240     150.232 194.645 132.458  1.00163.99           O  
ATOM   1822  OE2 GLU A 240     151.011 193.032 131.188  1.00163.99           O  
ATOM   1823  N   LEU A 241     151.193 195.849 137.050  1.00162.90           N  
ATOM   1824  CA  LEU A 241     151.353 196.660 138.250  1.00162.90           C  
ATOM   1825  C   LEU A 241     151.300 195.837 139.531  1.00162.90           C  
ATOM   1826  O   LEU A 241     151.391 196.413 140.620  1.00162.90           O  
ATOM   1827  CB  LEU A 241     150.281 197.755 138.296  1.00162.90           C  
ATOM   1828  CG  LEU A 241     150.532 199.037 137.494  1.00162.90           C  
ATOM   1829  CD1 LEU A 241     151.863 199.664 137.883  1.00162.90           C  
ATOM   1830  CD2 LEU A 241     150.464 198.798 135.987  1.00162.90           C  
ATOM   1831  N   LEU A 242     151.154 194.512 139.430  1.00163.07           N  
ATOM   1832  CA  LEU A 242     151.030 193.655 140.602  1.00163.07           C  
ATOM   1833  C   LEU A 242     151.804 192.351 140.430  1.00163.07           C  
ATOM   1834  O   LEU A 242     151.446 191.329 141.026  1.00163.07           O  
ATOM   1835  CB  LEU A 242     149.558 193.361 140.910  1.00163.07           C  
ATOM   1836  CG  LEU A 242     148.653 192.955 139.741  1.00163.07           C  
ATOM   1837  CD1 LEU A 242     148.574 191.438 139.589  1.00163.07           C  
ATOM   1838  CD2 LEU A 242     147.264 193.552 139.915  1.00163.07           C  
ATOM   1839  N   GLY A 243     152.872 192.370 139.636  1.00156.05           N  
ATOM   1840  CA  GLY A 243     153.827 191.278 139.635  1.00156.05           C  
ATOM   1841  C   GLY A 243     153.710 190.362 138.434  1.00156.05           C  
ATOM   1842  O   GLY A 243     154.724 189.920 137.885  1.00156.05           O  
ATOM   1843  N   ILE A 244     152.482 190.065 138.016  1.00156.52           N  
ATOM   1844  CA  ILE A 244     152.274 189.129 136.919  1.00156.52           C  
ATOM   1845  C   ILE A 244     152.489 189.850 135.592  1.00156.52           C  
ATOM   1846  O   ILE A 244     152.390 191.076 135.496  1.00156.52           O  
ATOM   1847  CB  ILE A 244     150.868 188.505 136.998  1.00156.52           C  
ATOM   1848  CG1 ILE A 244     150.537 188.117 138.438  1.00156.52           C  
ATOM   1849  CG2 ILE A 244     150.764 187.271 136.112  1.00156.52           C  
ATOM   1850  CD1 ILE A 244     149.067 187.836 138.668  1.00156.52           C  
ATOM   1851  N   ASP A 245     152.791 189.080 134.552  1.00159.75           N  
ATOM   1852  CA  ASP A 245     152.727 189.583 133.190  1.00159.75           C  
ATOM   1853  C   ASP A 245     151.594 188.908 132.428  1.00159.75           C  
ATOM   1854  O   ASP A 245     151.107 187.838 132.804  1.00159.75           O  
ATOM   1855  CB  ASP A 245     154.061 189.366 132.466  1.00159.75           C  
ATOM   1856  CG  ASP A 245     154.479 187.906 132.428  1.00159.75           C  
ATOM   1857  OD1 ASP A 245     153.844 187.079 133.116  1.00159.75           O  
ATOM   1858  OD2 ASP A 245     155.448 187.583 131.710  1.00159.75           O  
ATOM   1859  N   ALA A 246     151.177 189.556 131.347  1.00154.64           N  
ATOM   1860  CA  ALA A 246     150.230 188.981 130.404  1.00154.64           C  
ATOM   1861  C   ALA A 246     150.978 188.204 129.318  1.00154.64           C  
ATOM   1862  O   ALA A 246     152.145 187.837 129.485  1.00154.64           O  
ATOM   1863  CB  ALA A 246     149.341 190.087 129.827  1.00154.64           C  
ATOM   1864  N   THR A 247     150.283 187.921 128.213  1.00152.28           N  
ATOM   1865  CA  THR A 247     150.780 187.303 126.984  1.00152.28           C  
ATOM   1866  C   THR A 247     151.051 185.811 127.141  1.00152.28           C  
ATOM   1867  O   THR A 247     151.345 185.130 126.153  1.00152.28           O  
ATOM   1868  CB  THR A 247     152.044 188.007 126.468  1.00152.28           C  
ATOM   1869  OG1 THR A 247     153.124 187.814 127.391  1.00152.28           O  
ATOM   1870  CG2 THR A 247     151.792 189.498 126.284  1.00152.28           C  
ATOM   1871  N   VAL A 248     150.962 185.289 128.360  1.00148.18           N  
ATOM   1872  CA  VAL A 248     150.823 183.847 128.550  1.00148.18           C  
ATOM   1873  C   VAL A 248     149.348 183.549 128.788  1.00148.18           C  
ATOM   1874  O   VAL A 248     148.632 184.402 129.332  1.00148.18           O  
ATOM   1875  CB  VAL A 248     151.702 183.344 129.706  1.00148.18           C  
ATOM   1876  CG1 VAL A 248     153.174 183.481 129.350  1.00148.18           C  
ATOM   1877  CG2 VAL A 248     151.392 184.107 130.982  1.00148.18           C  
ATOM   1878  N   PRO A 249     148.841 182.378 128.395  1.00148.63           N  
ATOM   1879  CA  PRO A 249     147.445 182.056 128.730  1.00148.63           C  
ATOM   1880  C   PRO A 249     147.207 181.934 130.225  1.00148.63           C  
ATOM   1881  O   PRO A 249     146.097 182.211 130.697  1.00148.63           O  
ATOM   1882  CB  PRO A 249     147.214 180.720 128.009  1.00148.63           C  
ATOM   1883  CG  PRO A 249     148.226 180.704 126.907  1.00148.63           C  
ATOM   1884  CD  PRO A 249     149.432 181.394 127.473  1.00148.63           C  
ATOM   1885  N   SER A 250     148.226 181.527 130.983  1.00146.28           N  
ATOM   1886  CA  SER A 250     148.155 181.382 132.430  1.00146.28           C  
ATOM   1887  C   SER A 250     148.432 182.682 133.180  1.00146.28           C  
ATOM   1888  O   SER A 250     148.687 182.642 134.389  1.00146.28           O  
ATOM   1889  CB  SER A 250     149.127 180.295 132.895  1.00146.28           C  
ATOM   1890  OG  SER A 250     150.470 180.670 132.645  1.00146.28           O  
ATOM   1891  N   GLY A 251     148.389 183.827 132.503  1.00144.54           N  
ATOM   1892  CA  GLY A 251     148.673 185.063 133.200  1.00144.54           C  
ATOM   1893  C   GLY A 251     147.559 185.632 134.041  1.00144.54           C  
ATOM   1894  O   GLY A 251     147.755 186.669 134.681  1.00144.54           O  
ATOM   1895  N   ARG A 252     146.394 184.996 134.065  1.00144.99           N  
ATOM   1896  CA  ARG A 252     145.298 185.555 134.836  1.00144.99           C  
ATOM   1897  C   ARG A 252     145.515 185.309 136.329  1.00144.99           C  
ATOM   1898  O   ARG A 252     146.062 184.275 136.722  1.00144.99           O  
ATOM   1899  CB  ARG A 252     143.971 184.944 134.400  1.00144.99           C  
ATOM   1900  CG  ARG A 252     143.562 185.301 132.981  1.00144.99           C  
ATOM   1901  CD  ARG A 252     143.336 186.797 132.837  1.00144.99           C  
ATOM   1902  NE  ARG A 252     142.296 187.284 133.740  1.00144.99           N  
ATOM   1903  CZ  ARG A 252     142.147 188.557 134.089  1.00144.99           C  
ATOM   1904  NH1 ARG A 252     142.969 189.480 133.608  1.00144.99           N  
ATOM   1905  NH2 ARG A 252     141.172 188.910 134.916  1.00144.99           N  
ATOM   1906  N   PRO A 253     145.095 186.247 137.183  1.00141.71           N  
ATOM   1907  CA  PRO A 253     145.111 185.989 138.631  1.00141.71           C  
ATOM   1908  C   PRO A 253     144.001 185.061 139.094  1.00141.71           C  
ATOM   1909  O   PRO A 253     143.916 184.773 140.294  1.00141.71           O  
ATOM   1910  CB  PRO A 253     144.944 187.391 139.229  1.00141.71           C  
ATOM   1911  CG  PRO A 253     144.155 188.126 138.201  1.00141.71           C  
ATOM   1912  CD  PRO A 253     144.632 187.610 136.868  1.00141.71           C  
ATOM   1913  N   GLU A 254     143.152 184.592 138.178  1.00143.27           N  
ATOM   1914  CA  GLU A 254     142.100 183.644 138.526  1.00143.27           C  
ATOM   1915  C   GLU A 254     142.663 182.295 138.956  1.00143.27           C  
ATOM   1916  O   GLU A 254     142.021 181.577 139.732  1.00143.27           O  
ATOM   1917  CB  GLU A 254     141.163 183.464 137.334  1.00143.27           C  
ATOM   1918  CG  GLU A 254     140.585 184.765 136.807  1.00143.27           C  
ATOM   1919  CD  GLU A 254     139.817 184.581 135.515  1.00143.27           C  
ATOM   1920  OE1 GLU A 254     139.768 183.441 135.007  1.00143.27           O  
ATOM   1921  OE2 GLU A 254     139.278 185.580 134.995  1.00143.27           O  
ATOM   1922  N   THR A 255     143.849 181.932 138.468  1.00130.27           N  
ATOM   1923  CA  THR A 255     144.385 180.588 138.632  1.00130.27           C  
ATOM   1924  C   THR A 255     145.234 180.427 139.889  1.00130.27           C  
ATOM   1925  O   THR A 255     145.995 179.457 139.988  1.00130.27           O  
ATOM   1926  CB  THR A 255     145.203 180.195 137.400  1.00130.27           C  
ATOM   1927  OG1 THR A 255     146.325 181.077 137.266  1.00130.27           O  
ATOM   1928  CG2 THR A 255     144.346 180.280 136.147  1.00130.27           C  
ATOM   1929  N   TYR A 256     145.126 181.345 140.848  1.00134.28           N  
ATOM   1930  CA  TYR A 256     145.946 181.300 142.050  1.00134.28           C  
ATOM   1931  C   TYR A 256     145.176 180.788 143.260  1.00134.28           C  
ATOM   1932  O   TYR A 256     145.663 180.901 144.389  1.00134.28           O  
ATOM   1933  CB  TYR A 256     146.527 182.684 142.344  1.00134.28           C  
ATOM   1934  CG  TYR A 256     147.617 183.100 141.383  1.00134.28           C  
ATOM   1935  CD1 TYR A 256     148.251 182.164 140.576  1.00134.28           C  
ATOM   1936  CD2 TYR A 256     148.010 184.426 141.282  1.00134.28           C  
ATOM   1937  CE1 TYR A 256     149.247 182.538 139.695  1.00134.28           C  
ATOM   1938  CE2 TYR A 256     149.006 184.809 140.404  1.00134.28           C  
ATOM   1939  CZ  TYR A 256     149.620 183.862 139.613  1.00134.28           C  
ATOM   1940  OH  TYR A 256     150.612 184.241 138.739  1.00134.28           O  
ATOM   1941  N   ILE A 257     143.986 180.226 143.046  1.00130.64           N  
ATOM   1942  CA  ILE A 257     143.245 179.495 144.062  1.00130.64           C  
ATOM   1943  C   ILE A 257     142.741 178.204 143.434  1.00130.64           C  
ATOM   1944  O   ILE A 257     142.580 178.101 142.216  1.00130.64           O  
ATOM   1945  CB  ILE A 257     142.071 180.312 144.642  1.00130.64           C  
ATOM   1946  CG1 ILE A 257     141.167 180.819 143.518  1.00130.64           C  
ATOM   1947  CG2 ILE A 257     142.586 181.471 145.483  1.00130.64           C  
ATOM   1948  CD1 ILE A 257     139.873 181.427 144.008  1.00130.64           C  
ATOM   1949  N   TRP A 258     142.491 177.209 144.281  1.00127.69           N  
ATOM   1950  CA  TRP A 258     142.186 175.873 143.786  1.00127.69           C  
ATOM   1951  C   TRP A 258     140.736 175.802 143.326  1.00127.69           C  
ATOM   1952  O   TRP A 258     139.814 176.037 144.113  1.00127.69           O  
ATOM   1953  CB  TRP A 258     142.433 174.816 144.862  1.00127.69           C  
ATOM   1954  CG  TRP A 258     143.865 174.591 145.225  1.00127.69           C  
ATOM   1955  CD1 TRP A 258     144.502 175.016 146.353  1.00127.69           C  
ATOM   1956  CD2 TRP A 258     144.836 173.858 144.468  1.00127.69           C  
ATOM   1957  NE1 TRP A 258     145.812 174.603 146.341  1.00127.69           N  
ATOM   1958  CE2 TRP A 258     146.042 173.890 145.194  1.00127.69           C  
ATOM   1959  CE3 TRP A 258     144.803 173.183 143.244  1.00127.69           C  
ATOM   1960  CZ2 TRP A 258     147.206 173.275 144.736  1.00127.69           C  
ATOM   1961  CZ3 TRP A 258     145.958 172.572 142.791  1.00127.69           C  
ATOM   1962  CH2 TRP A 258     147.143 172.623 143.535  1.00127.69           C  
ATOM   1963  N   ARG A 259     140.541 175.476 142.054  1.00126.86           N  
ATOM   1964  CA  ARG A 259     139.236 175.106 141.525  1.00126.86           C  
ATOM   1965  C   ARG A 259     139.247 173.701 140.953  1.00126.86           C  
ATOM   1966  O   ARG A 259     138.314 172.930 141.194  1.00126.86           O  
ATOM   1967  CB  ARG A 259     138.786 176.108 140.451  1.00126.86           C  
ATOM   1968  CG  ARG A 259     137.384 175.863 139.920  1.00126.86           C  
ATOM   1969  CD  ARG A 259     136.978 176.936 138.922  1.00126.86           C  
ATOM   1970  NE  ARG A 259     137.840 176.954 137.745  1.00126.86           N  
ATOM   1971  CZ  ARG A 259     137.796 177.892 136.804  1.00126.86           C  
ATOM   1972  NH1 ARG A 259     136.922 178.884 136.896  1.00126.86           N  
ATOM   1973  NH2 ARG A 259     138.618 177.833 135.766  1.00126.86           N  
ATOM   1974  N   TYR A 260     140.286 173.352 140.201  1.00128.79           N  
ATOM   1975  CA  TYR A 260     140.624 171.972 139.894  1.00128.79           C  
ATOM   1976  C   TYR A 260     141.939 171.656 140.595  1.00128.79           C  
ATOM   1977  O   TYR A 260     142.815 172.520 140.695  1.00128.79           O  
ATOM   1978  CB  TYR A 260     140.761 171.749 138.384  1.00128.79           C  
ATOM   1979  CG  TYR A 260     139.461 171.828 137.613  1.00128.79           C  
ATOM   1980  CD1 TYR A 260     138.237 171.817 138.268  1.00128.79           C  
ATOM   1981  CD2 TYR A 260     139.459 171.911 136.226  1.00128.79           C  
ATOM   1982  CE1 TYR A 260     137.049 171.893 137.566  1.00128.79           C  
ATOM   1983  CE2 TYR A 260     138.276 171.983 135.515  1.00128.79           C  
ATOM   1984  CZ  TYR A 260     137.074 171.974 136.190  1.00128.79           C  
ATOM   1985  OH  TYR A 260     135.893 172.044 135.487  1.00128.79           O  
ATOM   1986  N   LEU A 261     142.083 170.426 141.082  1.00130.73           N  
ATOM   1987  CA  LEU A 261     143.407 170.024 141.523  1.00130.73           C  
ATOM   1988  C   LEU A 261     143.837 168.747 140.812  1.00130.73           C  
ATOM   1989  O   LEU A 261     143.024 167.833 140.638  1.00130.73           O  
ATOM   1990  CB  LEU A 261     143.458 169.827 143.050  1.00130.73           C  
ATOM   1991  CG  LEU A 261     142.785 168.632 143.728  1.00130.73           C  
ATOM   1992  CD1 LEU A 261     143.786 167.505 143.941  1.00130.73           C  
ATOM   1993  CD2 LEU A 261     142.155 169.052 145.047  1.00130.73           C  
ATOM   1994  N   PRO A 262     145.091 168.654 140.381  1.00130.76           N  
ATOM   1995  CA  PRO A 262     145.552 167.431 139.723  1.00130.76           C  
ATOM   1996  C   PRO A 262     145.894 166.344 140.731  1.00130.76           C  
ATOM   1997  O   PRO A 262     146.198 166.604 141.897  1.00130.76           O  
ATOM   1998  CB  PRO A 262     146.802 167.891 138.967  1.00130.76           C  
ATOM   1999  CG  PRO A 262     147.330 169.009 139.803  1.00130.76           C  
ATOM   2000  CD  PRO A 262     146.123 169.706 140.383  1.00130.76           C  
ATOM   2001  N   ALA A 263     145.840 165.103 140.252  1.00140.60           N  
ATOM   2002  CA  ALA A 263     146.381 163.967 140.986  1.00140.60           C  
ATOM   2003  C   ALA A 263     147.765 163.622 140.465  1.00140.60           C  
ATOM   2004  O   ALA A 263     147.931 163.444 139.249  1.00140.60           O  
ATOM   2005  CB  ALA A 263     145.462 162.755 140.857  1.00140.60           C  
ATOM   2006  N   PRO A 264     148.774 163.518 141.323  1.00141.65           N  
ATOM   2007  CA  PRO A 264     150.107 163.131 140.853  1.00141.65           C  
ATOM   2008  C   PRO A 264     150.130 161.663 140.472  1.00141.65           C  
ATOM   2009  O   PRO A 264     149.174 160.927 140.759  1.00141.65           O  
ATOM   2010  CB  PRO A 264     151.003 163.411 142.068  1.00141.65           C  
ATOM   2011  CG  PRO A 264     150.091 163.277 143.238  1.00141.65           C  
ATOM   2012  CD  PRO A 264     148.738 163.747 142.778  1.00141.65           C  
ATOM   2013  N   PRO A 265     151.194 161.193 139.824  1.00140.52           N  
ATOM   2014  CA  PRO A 265     151.306 159.758 139.542  1.00140.52           C  
ATOM   2015  C   PRO A 265     151.471 158.955 140.824  1.00140.52           C  
ATOM   2016  O   PRO A 265     151.745 159.485 141.902  1.00140.52           O  
ATOM   2017  CB  PRO A 265     152.555 159.666 138.662  1.00140.52           C  
ATOM   2018  CG  PRO A 265     152.668 161.013 138.032  1.00140.52           C  
ATOM   2019  CD  PRO A 265     152.193 161.979 139.079  1.00140.52           C  
ATOM   2020  N   VAL A 266     151.293 157.637 140.691  1.00148.87           N  
ATOM   2021  CA  VAL A 266     151.480 156.739 141.829  1.00148.87           C  
ATOM   2022  C   VAL A 266     152.937 156.377 142.060  1.00148.87           C  
ATOM   2023  O   VAL A 266     153.256 155.767 143.089  1.00148.87           O  
ATOM   2024  CB  VAL A 266     150.662 155.447 141.654  1.00148.87           C  
ATOM   2025  CG1 VAL A 266     149.182 155.773 141.513  1.00148.87           C  
ATOM   2026  CG2 VAL A 266     151.159 154.666 140.451  1.00148.87           C  
ATOM   2027  N   CYS A 267     153.830 156.730 141.132  1.00148.48           N  
ATOM   2028  CA  CYS A 267     155.246 156.428 141.313  1.00148.48           C  
ATOM   2029  C   CYS A 267     155.859 157.234 142.449  1.00148.48           C  
ATOM   2030  O   CYS A 267     156.770 156.749 143.129  1.00148.48           O  
ATOM   2031  CB  CYS A 267     156.005 156.685 140.011  1.00148.48           C  
ATOM   2032  SG  CYS A 267     155.503 155.626 138.636  1.00148.48           S  
ATOM   2033  N   ILE A 268     155.380 158.460 142.672  1.00147.95           N  
ATOM   2034  CA  ILE A 268     155.904 159.269 143.766  1.00147.95           C  
ATOM   2035  C   ILE A 268     155.261 158.913 145.099  1.00147.95           C  
ATOM   2036  O   ILE A 268     155.790 159.290 146.153  1.00147.95           O  
ATOM   2037  CB  ILE A 268     155.733 160.768 143.466  1.00147.95           C  
ATOM   2038  CG1 ILE A 268     154.278 161.097 143.115  1.00147.95           C  
ATOM   2039  CG2 ILE A 268     156.667 161.196 142.342  1.00147.95           C  
ATOM   2040  CD1 ILE A 268     153.449 161.595 144.285  1.00147.95           C  
ATOM   2041  N   ARG A 269     154.139 158.197 145.088  1.00153.67           N  
ATOM   2042  CA  ARG A 269     153.460 157.769 146.311  1.00153.67           C  
ATOM   2043  C   ARG A 269     153.205 156.263 146.285  1.00153.67           C  
ATOM   2044  O   ARG A 269     152.061 155.804 146.349  1.00153.67           O  
ATOM   2045  CB  ARG A 269     152.166 158.561 146.506  1.00153.67           C  
ATOM   2046  CG  ARG A 269     151.151 158.464 145.370  1.00153.67           C  
ATOM   2047  CD  ARG A 269     149.940 159.343 145.647  1.00153.67           C  
ATOM   2048  NE  ARG A 269     148.760 158.906 144.906  1.00153.67           N  
ATOM   2049  CZ  ARG A 269     148.525 159.197 143.631  1.00153.67           C  
ATOM   2050  NH1 ARG A 269     149.394 159.923 142.943  1.00153.67           N  
ATOM   2051  NH2 ARG A 269     147.422 158.755 143.040  1.00153.67           N  
ATOM   2052  N   PRO A 270     154.265 155.459 146.218  1.00171.29           N  
ATOM   2053  CA  PRO A 270     154.086 154.036 145.918  1.00171.29           C  
ATOM   2054  C   PRO A 270     153.496 153.285 147.102  1.00171.29           C  
ATOM   2055  O   PRO A 270     153.716 153.632 148.265  1.00171.29           O  
ATOM   2056  CB  PRO A 270     155.510 153.565 145.612  1.00171.29           C  
ATOM   2057  CG  PRO A 270     156.355 154.427 146.491  1.00171.29           C  
ATOM   2058  CD  PRO A 270     155.664 155.775 146.558  1.00171.29           C  
ATOM   2059  N   SER A 271     152.741 152.235 146.790  1.00192.12           N  
ATOM   2060  CA  SER A 271     152.094 151.418 147.816  1.00192.12           C  
ATOM   2061  C   SER A 271     153.143 150.544 148.490  1.00192.12           C  
ATOM   2062  O   SER A 271     153.485 149.467 147.996  1.00192.12           O  
ATOM   2063  CB  SER A 271     150.983 150.573 147.202  1.00192.12           C  
ATOM   2064  OG  SER A 271     151.509 149.606 146.311  1.00192.12           O  
ATOM   2065  N   VAL A 272     153.663 151.008 149.626  1.00217.64           N  
ATOM   2066  CA  VAL A 272     154.689 150.266 150.350  1.00217.64           C  
ATOM   2067  C   VAL A 272     154.072 149.005 150.945  1.00217.64           C  
ATOM   2068  O   VAL A 272     153.150 149.072 151.767  1.00217.64           O  
ATOM   2069  CB  VAL A 272     155.341 151.140 151.430  1.00217.64           C  
ATOM   2070  CG1 VAL A 272     154.288 151.901 152.228  1.00217.64           C  
ATOM   2071  CG2 VAL A 272     156.212 150.291 152.347  1.00217.64           C  
ATOM   2072  N   MET A 273     154.563 147.847 150.511  1.00253.15           N  
ATOM   2073  CA  MET A 273     154.100 146.553 151.008  1.00253.15           C  
ATOM   2074  C   MET A 273     155.054 146.086 152.102  1.00253.15           C  
ATOM   2075  O   MET A 273     156.108 145.513 151.817  1.00253.15           O  
ATOM   2076  CB  MET A 273     154.011 145.540 149.872  1.00253.15           C  
ATOM   2077  CG  MET A 273     153.424 144.198 150.279  1.00253.15           C  
ATOM   2078  SD  MET A 273     151.692 144.315 150.770  1.00253.15           S  
ATOM   2079  CE  MET A 273     151.544 142.882 151.835  1.00253.15           C  
ATOM   2080  N   MET A 274     154.679 146.329 153.359  1.00269.04           N  
ATOM   2081  CA  MET A 274     155.565 146.068 154.487  1.00269.04           C  
ATOM   2082  C   MET A 274     155.684 144.585 154.814  1.00269.04           C  
ATOM   2083  O   MET A 274     156.593 144.205 155.561  1.00269.04           O  
ATOM   2084  CB  MET A 274     155.078 146.824 155.725  1.00269.04           C  
ATOM   2085  CG  MET A 274     153.806 146.255 156.332  1.00269.04           C  
ATOM   2086  SD  MET A 274     152.338 146.621 155.351  1.00269.04           S  
ATOM   2087  CE  MET A 274     151.041 146.321 156.549  1.00269.04           C  
ATOM   2088  N   GLN A 275     154.788 143.754 154.278  1.00280.16           N  
ATOM   2089  CA  GLN A 275     154.739 142.319 154.564  1.00280.16           C  
ATOM   2090  C   GLN A 275     154.618 142.056 156.068  1.00280.16           C  
ATOM   2091  O   GLN A 275     155.332 141.233 156.643  1.00280.16           O  
ATOM   2092  CB  GLN A 275     155.956 141.603 153.967  1.00280.16           C  
ATOM   2093  CG  GLN A 275     155.794 140.096 153.810  1.00280.16           C  
ATOM   2094  CD  GLN A 275     154.603 139.728 152.947  1.00280.16           C  
ATOM   2095  OE1 GLN A 275     153.573 139.275 153.448  1.00280.16           O  
ATOM   2096  NE2 GLN A 275     154.738 139.921 151.640  1.00280.16           N  
ATOM   2097  N   ASP A 276     153.702 142.781 156.709  1.00286.52           N  
ATOM   2098  CA  ASP A 276     153.227 142.443 158.044  1.00286.52           C  
ATOM   2099  C   ASP A 276     151.836 141.824 158.029  1.00286.52           C  
ATOM   2100  O   ASP A 276     151.299 141.508 159.095  1.00286.52           O  
ATOM   2101  CB  ASP A 276     153.231 143.687 158.939  1.00286.52           C  
ATOM   2102  CG  ASP A 276     154.629 144.217 159.195  1.00286.52           C  
ATOM   2103  OD1 ASP A 276     155.586 143.415 159.162  1.00286.52           O  
ATOM   2104  OD2 ASP A 276     154.770 145.436 159.428  1.00286.52           O  
ATOM   2105  N   SER A 277     151.247 141.652 156.850  1.00280.64           N  
ATOM   2106  CA  SER A 277     149.856 141.260 156.673  1.00280.64           C  
ATOM   2107  C   SER A 277     149.663 140.829 155.225  1.00280.64           C  
ATOM   2108  O   SER A 277     150.588 140.970 154.415  1.00280.64           O  
ATOM   2109  CB  SER A 277     148.916 142.413 157.033  1.00280.64           C  
ATOM   2110  OG  SER A 277     149.074 143.497 156.135  1.00280.64           O  
ATOM   2111  N   PRO A 278     148.493 140.308 154.848  1.00271.99           N  
ATOM   2112  CA  PRO A 278     148.151 140.244 153.423  1.00271.99           C  
ATOM   2113  C   PRO A 278     147.647 141.560 152.852  1.00271.99           C  
ATOM   2114  O   PRO A 278     147.280 141.602 151.673  1.00271.99           O  
ATOM   2115  CB  PRO A 278     147.045 139.176 153.383  1.00271.99           C  
ATOM   2116  CG  PRO A 278     146.462 139.189 154.753  1.00271.99           C  
ATOM   2117  CD  PRO A 278     147.610 139.461 155.669  1.00271.99           C  
ATOM   2118  N   ALA A 279     147.621 142.624 153.648  1.00272.41           N  
ATOM   2119  CA  ALA A 279     147.228 143.948 153.195  1.00272.41           C  
ATOM   2120  C   ALA A 279     148.421 144.892 153.269  1.00272.41           C  
ATOM   2121  O   ALA A 279     149.392 144.644 153.990  1.00272.41           O  
ATOM   2122  CB  ALA A 279     146.067 144.497 154.032  1.00272.41           C  
ATOM   2123  N   SER A 280     148.341 145.983 152.515  1.00245.90           N  
ATOM   2124  CA  SER A 280     149.433 146.942 152.427  1.00245.90           C  
ATOM   2125  C   SER A 280     149.164 148.120 153.354  1.00245.90           C  
ATOM   2126  O   SER A 280     148.023 148.573 153.483  1.00245.90           O  
ATOM   2127  CB  SER A 280     149.611 147.436 150.990  1.00245.90           C  
ATOM   2128  OG  SER A 280     148.483 148.180 150.563  1.00245.90           O  
ATOM   2129  N   ASN A 281     150.218 148.613 154.000  1.00226.52           N  
ATOM   2130  CA  ASN A 281     150.151 149.892 154.705  1.00226.52           C  
ATOM   2131  C   ASN A 281     150.131 151.007 153.669  1.00226.52           C  
ATOM   2132  O   ASN A 281     151.166 151.359 153.099  1.00226.52           O  
ATOM   2133  CB  ASN A 281     151.331 150.042 155.658  1.00226.52           C  
ATOM   2134  CG  ASN A 281     151.174 151.220 156.601  1.00226.52           C  
ATOM   2135  OD1 ASN A 281     150.153 151.907 156.593  1.00226.52           O  
ATOM   2136  ND2 ASN A 281     152.191 151.460 157.422  1.00226.52           N  
ATOM   2137  N   GLU A 282     148.954 151.571 153.415  1.00202.03           N  
ATOM   2138  CA  GLU A 282     148.822 152.559 152.356  1.00202.03           C  
ATOM   2139  C   GLU A 282     149.271 153.930 152.850  1.00202.03           C  
ATOM   2140  O   GLU A 282     148.958 154.336 153.972  1.00202.03           O  
ATOM   2141  CB  GLU A 282     147.374 152.612 151.869  1.00202.03           C  
ATOM   2142  CG  GLU A 282     147.150 153.495 150.662  1.00202.03           C  
ATOM   2143  CD  GLU A 282     147.889 153.002 149.432  1.00202.03           C  
ATOM   2144  OE1 GLU A 282     148.068 151.774 149.294  1.00202.03           O  
ATOM   2145  OE2 GLU A 282     148.291 153.845 148.603  1.00202.03           O  
ATOM   2146  N   ASP A 283     150.012 154.641 152.002  1.00183.52           N  
ATOM   2147  CA  ASP A 283     150.788 155.786 152.457  1.00183.52           C  
ATOM   2148  C   ASP A 283     149.881 156.988 152.730  1.00183.52           C  
ATOM   2149  O   ASP A 283     148.655 156.931 152.591  1.00183.52           O  
ATOM   2150  CB  ASP A 283     151.867 156.129 151.433  1.00183.52           C  
ATOM   2151  CG  ASP A 283     151.302 156.377 150.048  1.00183.52           C  
ATOM   2152  OD1 ASP A 283     150.083 156.188 149.852  1.00183.52           O  
ATOM   2153  OD2 ASP A 283     152.082 156.759 149.152  1.00183.52           O  
ATOM   2154  N   ASP A 284     150.508 158.100 153.124  1.00170.54           N  
ATOM   2155  CA  ASP A 284     149.773 159.219 153.706  1.00170.54           C  
ATOM   2156  C   ASP A 284     149.071 160.064 152.649  1.00170.54           C  
ATOM   2157  O   ASP A 284     148.056 160.704 152.945  1.00170.54           O  
ATOM   2158  CB  ASP A 284     150.718 160.095 154.530  1.00170.54           C  
ATOM   2159  CG  ASP A 284     151.145 159.434 155.825  1.00170.54           C  
ATOM   2160  OD1 ASP A 284     150.375 158.604 156.353  1.00170.54           O  
ATOM   2161  OD2 ASP A 284     152.251 159.744 156.316  1.00170.54           O  
ATOM   2162  N   LEU A 285     149.595 160.079 151.421  1.00166.43           N  
ATOM   2163  CA  LEU A 285     149.053 160.947 150.378  1.00166.43           C  
ATOM   2164  C   LEU A 285     147.704 160.444 149.878  1.00166.43           C  
ATOM   2165  O   LEU A 285     146.749 161.218 149.748  1.00166.43           O  
ATOM   2166  CB  LEU A 285     150.051 161.066 149.225  1.00166.43           C  
ATOM   2167  CG  LEU A 285     151.394 161.712 149.574  1.00166.43           C  
ATOM   2168  CD1 LEU A 285     152.334 161.696 148.378  1.00166.43           C  
ATOM   2169  CD2 LEU A 285     151.190 163.133 150.080  1.00166.43           C  
ATOM   2170  N   THR A 286     147.612 159.145 149.589  1.00168.77           N  
ATOM   2171  CA  THR A 286     146.359 158.568 149.112  1.00168.77           C  
ATOM   2172  C   THR A 286     145.278 158.598 150.186  1.00168.77           C  
ATOM   2173  O   THR A 286     144.105 158.840 149.882  1.00168.77           O  
ATOM   2174  CB  THR A 286     146.594 157.138 148.630  1.00168.77           C  
ATOM   2175  OG1 THR A 286     147.210 156.384 149.678  1.00168.77           O  
ATOM   2176  CG2 THR A 286     147.496 157.128 147.408  1.00168.77           C  
ATOM   2177  N   VAL A 287     145.647 158.356 151.449  1.00171.34           N  
ATOM   2178  CA  VAL A 287     144.658 158.380 152.526  1.00171.34           C  
ATOM   2179  C   VAL A 287     144.307 159.790 152.966  1.00171.34           C  
ATOM   2180  O   VAL A 287     143.441 159.959 153.835  1.00171.34           O  
ATOM   2181  CB  VAL A 287     145.141 157.583 153.755  1.00171.34           C  
ATOM   2182  CG1 VAL A 287     145.532 156.169 153.353  1.00171.34           C  
ATOM   2183  CG2 VAL A 287     146.298 158.299 154.434  1.00171.34           C  
ATOM   2184  N   LYS A 288     144.955 160.808 152.402  1.00157.01           N  
ATOM   2185  CA  LYS A 288     144.472 162.180 152.487  1.00157.01           C  
ATOM   2186  C   LYS A 288     143.664 162.590 151.264  1.00157.01           C  
ATOM   2187  O   LYS A 288     142.706 163.359 151.391  1.00157.01           O  
ATOM   2188  CB  LYS A 288     145.650 163.145 152.668  1.00157.01           C  
ATOM   2189  CG  LYS A 288     145.258 164.605 152.817  1.00157.01           C  
ATOM   2190  CD  LYS A 288     144.400 164.826 154.050  1.00157.01           C  
ATOM   2191  CE  LYS A 288     145.194 164.598 155.325  1.00157.01           C  
ATOM   2192  NZ  LYS A 288     146.252 165.629 155.514  1.00157.01           N  
ATOM   2193  N   LEU A 289     144.030 162.081 150.085  1.00152.56           N  
ATOM   2194  CA  LEU A 289     143.340 162.416 148.846  1.00152.56           C  
ATOM   2195  C   LEU A 289     141.989 161.719 148.737  1.00152.56           C  
ATOM   2196  O   LEU A 289     141.137 162.157 147.957  1.00152.56           O  
ATOM   2197  CB  LEU A 289     144.229 162.062 147.648  1.00152.56           C  
ATOM   2198  CG  LEU A 289     143.852 162.545 146.243  1.00152.56           C  
ATOM   2199  CD1 LEU A 289     145.108 162.869 145.453  1.00152.56           C  
ATOM   2200  CD2 LEU A 289     143.030 161.501 145.502  1.00152.56           C  
ATOM   2201  N   THR A 290     141.770 160.661 149.520  1.00153.65           N  
ATOM   2202  CA  THR A 290     140.542 159.880 149.409  1.00153.65           C  
ATOM   2203  C   THR A 290     139.335 160.660 149.918  1.00153.65           C  
ATOM   2204  O   THR A 290     138.297 160.718 149.250  1.00153.65           O  
ATOM   2205  CB  THR A 290     140.689 158.563 150.172  1.00153.65           C  
ATOM   2206  OG1 THR A 290     141.853 157.869 149.707  1.00153.65           O  
ATOM   2207  CG2 THR A 290     139.464 157.686 149.964  1.00153.65           C  
ATOM   2208  N   GLU A 291     139.446 161.264 151.101  1.00158.00           N  
ATOM   2209  CA  GLU A 291     138.332 162.035 151.637  1.00158.00           C  
ATOM   2210  C   GLU A 291     138.188 163.403 150.985  1.00158.00           C  
ATOM   2211  O   GLU A 291     137.166 164.064 151.198  1.00158.00           O  
ATOM   2212  CB  GLU A 291     138.477 162.202 153.153  1.00158.00           C  
ATOM   2213  CG  GLU A 291     139.626 163.096 153.586  1.00158.00           C  
ATOM   2214  CD  GLU A 291     140.934 162.343 153.721  1.00158.00           C  
ATOM   2215  OE1 GLU A 291     141.044 161.231 153.162  1.00158.00           O  
ATOM   2216  OE2 GLU A 291     141.851 162.861 154.390  1.00158.00           O  
ATOM   2217  N   ILE A 292     139.179 163.846 150.207  1.00151.00           N  
ATOM   2218  CA  ILE A 292     139.026 165.082 149.443  1.00151.00           C  
ATOM   2219  C   ILE A 292     137.909 164.935 148.417  1.00151.00           C  
ATOM   2220  O   ILE A 292     137.011 165.780 148.322  1.00151.00           O  
ATOM   2221  CB  ILE A 292     140.358 165.468 148.773  1.00151.00           C  
ATOM   2222  CG1 ILE A 292     141.338 166.020 149.808  1.00151.00           C  
ATOM   2223  CG2 ILE A 292     140.125 166.490 147.670  1.00151.00           C  
ATOM   2224  CD1 ILE A 292     140.864 167.296 150.460  1.00151.00           C  
ATOM   2225  N   VAL A 293     137.945 163.852 147.636  1.00150.04           N  
ATOM   2226  CA  VAL A 293     136.885 163.598 146.670  1.00150.04           C  
ATOM   2227  C   VAL A 293     135.612 163.115 147.352  1.00150.04           C  
ATOM   2228  O   VAL A 293     134.521 163.243 146.785  1.00150.04           O  
ATOM   2229  CB  VAL A 293     137.358 162.589 145.604  1.00150.04           C  
ATOM   2230  CG1 VAL A 293     137.468 161.191 146.192  1.00150.04           C  
ATOM   2231  CG2 VAL A 293     136.425 162.598 144.401  1.00150.04           C  
ATOM   2232  N   TRP A 294     135.716 162.578 148.570  1.00156.15           N  
ATOM   2233  CA  TRP A 294     134.518 162.169 149.297  1.00156.15           C  
ATOM   2234  C   TRP A 294     133.752 163.373 149.830  1.00156.15           C  
ATOM   2235  O   TRP A 294     132.521 163.424 149.728  1.00156.15           O  
ATOM   2236  CB  TRP A 294     134.892 161.219 150.434  1.00156.15           C  
ATOM   2237  CG  TRP A 294     133.716 160.779 151.251  1.00156.15           C  
ATOM   2238  CD1 TRP A 294     133.381 161.209 152.501  1.00156.15           C  
ATOM   2239  CD2 TRP A 294     132.705 159.841 150.864  1.00156.15           C  
ATOM   2240  NE1 TRP A 294     132.232 160.585 152.924  1.00156.15           N  
ATOM   2241  CE2 TRP A 294     131.796 159.742 151.936  1.00156.15           C  
ATOM   2242  CE3 TRP A 294     132.484 159.071 149.718  1.00156.15           C  
ATOM   2243  CZ2 TRP A 294     130.683 158.904 151.896  1.00156.15           C  
ATOM   2244  CZ3 TRP A 294     131.378 158.240 149.681  1.00156.15           C  
ATOM   2245  CH2 TRP A 294     130.493 158.163 150.762  1.00156.15           C  
ATOM   2246  N   THR A 295     134.457 164.349 150.405  1.00151.67           N  
ATOM   2247  CA  THR A 295     133.781 165.547 150.889  1.00151.67           C  
ATOM   2248  C   THR A 295     133.254 166.385 149.730  1.00151.67           C  
ATOM   2249  O   THR A 295     132.158 166.951 149.812  1.00151.67           O  
ATOM   2250  CB  THR A 295     134.729 166.369 151.764  1.00151.67           C  
ATOM   2251  OG1 THR A 295     135.206 165.557 152.844  1.00151.67           O  
ATOM   2252  CG2 THR A 295     134.015 167.586 152.334  1.00151.67           C  
ATOM   2253  N   SER A 296     134.018 166.471 148.638  1.00150.42           N  
ATOM   2254  CA  SER A 296     133.567 167.215 147.468  1.00150.42           C  
ATOM   2255  C   SER A 296     132.441 166.507 146.726  1.00150.42           C  
ATOM   2256  O   SER A 296     131.737 167.147 145.938  1.00150.42           O  
ATOM   2257  CB  SER A 296     134.740 167.462 146.518  1.00150.42           C  
ATOM   2258  OG  SER A 296     134.316 168.142 145.349  1.00150.42           O  
ATOM   2259  N   SER A 297     132.254 165.206 146.959  1.00150.38           N  
ATOM   2260  CA  SER A 297     131.123 164.495 146.371  1.00150.38           C  
ATOM   2261  C   SER A 297     129.824 164.784 147.112  1.00150.38           C  
ATOM   2262  O   SER A 297     128.780 164.984 146.480  1.00150.38           O  
ATOM   2263  CB  SER A 297     131.398 162.991 146.351  1.00150.38           C  
ATOM   2264  OG  SER A 297     130.303 162.280 145.802  1.00150.38           O  
ATOM   2265  N   LEU A 298     129.863 164.810 148.446  1.00152.45           N  
ATOM   2266  CA  LEU A 298     128.651 165.076 149.210  1.00152.45           C  
ATOM   2267  C   LEU A 298     128.240 166.542 149.159  1.00152.45           C  
ATOM   2268  O   LEU A 298     127.071 166.850 149.409  1.00152.45           O  
ATOM   2269  CB  LEU A 298     128.833 164.626 150.664  1.00152.45           C  
ATOM   2270  CG  LEU A 298     129.968 165.232 151.495  1.00152.45           C  
ATOM   2271  CD1 LEU A 298     129.513 166.475 152.253  1.00152.45           C  
ATOM   2272  CD2 LEU A 298     130.537 164.197 152.455  1.00152.45           C  
ATOM   2273  N   ILE A 299     129.167 167.449 148.849  1.00147.76           N  
ATOM   2274  CA  ILE A 299     128.777 168.831 148.593  1.00147.76           C  
ATOM   2275  C   ILE A 299     128.180 168.972 147.198  1.00147.76           C  
ATOM   2276  O   ILE A 299     127.222 169.726 146.993  1.00147.76           O  
ATOM   2277  CB  ILE A 299     129.984 169.766 148.795  1.00147.76           C  
ATOM   2278  CG1 ILE A 299     130.466 169.709 150.245  1.00147.76           C  
ATOM   2279  CG2 ILE A 299     129.630 171.196 148.412  1.00147.76           C  
ATOM   2280  CD1 ILE A 299     131.782 170.418 150.479  1.00147.76           C  
ATOM   2281  N   LYS A 300     128.723 168.241 146.221  1.00149.12           N  
ATOM   2282  CA  LYS A 300     128.121 168.218 144.892  1.00149.12           C  
ATOM   2283  C   LYS A 300     126.742 167.570 144.920  1.00149.12           C  
ATOM   2284  O   LYS A 300     125.815 168.037 144.247  1.00149.12           O  
ATOM   2285  CB  LYS A 300     129.045 167.488 143.915  1.00149.12           C  
ATOM   2286  CG  LYS A 300     128.524 167.404 142.489  1.00149.12           C  
ATOM   2287  CD  LYS A 300     128.023 166.005 142.162  1.00149.12           C  
ATOM   2288  CE  LYS A 300     127.573 165.903 140.715  1.00149.12           C  
ATOM   2289  NZ  LYS A 300     128.707 166.091 139.768  1.00149.12           N  
ATOM   2290  N   ALA A 301     126.586 166.494 145.695  1.00160.01           N  
ATOM   2291  CA  ALA A 301     125.309 165.794 145.758  1.00160.01           C  
ATOM   2292  C   ALA A 301     124.356 166.449 146.750  1.00160.01           C  
ATOM   2293  O   ALA A 301     123.142 166.479 146.521  1.00160.01           O  
ATOM   2294  CB  ALA A 301     125.531 164.326 146.124  1.00160.01           C  
ATOM   2295  N   GLY A 302     124.888 166.974 147.855  1.00165.88           N  
ATOM   2296  CA  GLY A 302     124.030 167.552 148.877  1.00165.88           C  
ATOM   2297  C   GLY A 302     123.360 168.836 148.430  1.00165.88           C  
ATOM   2298  O   GLY A 302     122.179 169.060 148.713  1.00165.88           O  
ATOM   2299  N   LEU A 303     124.097 169.698 147.725  1.00162.13           N  
ATOM   2300  CA  LEU A 303     123.488 170.902 147.175  1.00162.13           C  
ATOM   2301  C   LEU A 303     122.561 170.598 146.007  1.00162.13           C  
ATOM   2302  O   LEU A 303     121.655 171.392 145.731  1.00162.13           O  
ATOM   2303  CB  LEU A 303     124.570 171.893 146.740  1.00162.13           C  
ATOM   2304  CG  LEU A 303     125.114 172.847 147.808  1.00162.13           C  
ATOM   2305  CD1 LEU A 303     125.969 172.115 148.833  1.00162.13           C  
ATOM   2306  CD2 LEU A 303     125.899 173.979 147.162  1.00162.13           C  
ATOM   2307  N   ASP A 304     122.763 169.474 145.315  1.00166.78           N  
ATOM   2308  CA  ASP A 304     121.789 169.051 144.314  1.00166.78           C  
ATOM   2309  C   ASP A 304     120.495 168.598 144.977  1.00166.78           C  
ATOM   2310  O   ASP A 304     119.399 168.951 144.525  1.00166.78           O  
ATOM   2311  CB  ASP A 304     122.377 167.934 143.451  1.00166.78           C  
ATOM   2312  CG  ASP A 304     121.579 167.691 142.184  1.00166.78           C  
ATOM   2313  OD1 ASP A 304     120.588 168.414 141.951  1.00166.78           O  
ATOM   2314  OD2 ASP A 304     121.945 166.775 141.418  1.00166.78           O  
ATOM   2315  N   LYS A 305     120.605 167.813 146.050  1.00161.18           N  
ATOM   2316  CA  LYS A 305     119.425 167.399 146.802  1.00161.18           C  
ATOM   2317  C   LYS A 305     118.807 168.582 147.538  1.00161.18           C  
ATOM   2318  O   LYS A 305     117.593 168.805 147.473  1.00161.18           O  
ATOM   2319  CB  LYS A 305     119.792 166.284 147.782  1.00161.18           C  
ATOM   2320  CG  LYS A 305     118.612 165.736 148.569  1.00161.18           C  
ATOM   2321  CD  LYS A 305     117.649 164.982 147.668  1.00161.18           C  
ATOM   2322  CE  LYS A 305     118.273 163.696 147.150  1.00161.18           C  
ATOM   2323  NZ  LYS A 305     117.324 162.919 146.307  1.00161.18           N  
ATOM   2324  N   GLY A 306     119.634 169.349 148.243  1.00160.34           N  
ATOM   2325  CA  GLY A 306     119.164 170.402 149.120  1.00160.34           C  
ATOM   2326  C   GLY A 306     119.436 170.099 150.578  1.00160.34           C  
ATOM   2327  O   GLY A 306     118.678 169.372 151.226  1.00160.34           O  
ATOM   2328  N   ILE A 307     120.524 170.659 151.102  1.00158.25           N  
ATOM   2329  CA  ILE A 307     120.924 170.474 152.488  1.00158.25           C  
ATOM   2330  C   ILE A 307     121.043 171.844 153.145  1.00158.25           C  
ATOM   2331  O   ILE A 307     120.925 172.884 152.496  1.00158.25           O  
ATOM   2332  CB  ILE A 307     122.242 169.686 152.618  1.00158.25           C  
ATOM   2333  CG1 ILE A 307     123.368 170.400 151.867  1.00158.25           C  
ATOM   2334  CG2 ILE A 307     122.068 168.266 152.101  1.00158.25           C  
ATOM   2335  CD1 ILE A 307     124.742 169.827 152.140  1.00158.25           C  
ATOM   2336  N   SER A 308     121.277 171.830 154.455  1.00160.51           N  
ATOM   2337  CA  SER A 308     121.377 173.071 155.209  1.00160.51           C  
ATOM   2338  C   SER A 308     122.632 173.837 154.809  1.00160.51           C  
ATOM   2339  O   SER A 308     123.727 173.269 154.746  1.00160.51           O  
ATOM   2340  CB  SER A 308     121.389 172.780 156.709  1.00160.51           C  
ATOM   2341  OG  SER A 308     121.596 173.964 157.458  1.00160.51           O  
ATOM   2342  N   ILE A 309     122.468 175.134 154.539  1.00162.31           N  
ATOM   2343  CA  ILE A 309     123.612 175.999 154.276  1.00162.31           C  
ATOM   2344  C   ILE A 309     124.404 176.273 155.548  1.00162.31           C  
ATOM   2345  O   ILE A 309     125.585 176.629 155.478  1.00162.31           O  
ATOM   2346  CB  ILE A 309     123.142 177.308 153.610  1.00162.31           C  
ATOM   2347  CG1 ILE A 309     124.332 178.107 153.071  1.00162.31           C  
ATOM   2348  CG2 ILE A 309     122.329 178.144 154.584  1.00162.31           C  
ATOM   2349  CD1 ILE A 309     123.937 179.243 152.153  1.00162.31           C  
ATOM   2350  N   ASN A 310     123.784 176.094 156.717  1.00160.35           N  
ATOM   2351  CA  ASN A 310     124.528 176.057 157.970  1.00160.35           C  
ATOM   2352  C   ASN A 310     125.337 174.776 158.130  1.00160.35           C  
ATOM   2353  O   ASN A 310     126.245 174.734 158.967  1.00160.35           O  
ATOM   2354  CB  ASN A 310     123.571 176.219 159.151  1.00160.35           C  
ATOM   2355  CG  ASN A 310     124.242 176.822 160.372  1.00160.35           C  
ATOM   2356  OD1 ASN A 310     123.578 177.177 161.346  1.00160.35           O  
ATOM   2357  ND2 ASN A 310     125.563 176.948 160.322  1.00160.35           N  
ATOM   2358  N   ASN A 311     125.034 173.736 157.354  1.00164.33           N  
ATOM   2359  CA  ASN A 311     125.796 172.494 157.415  1.00164.33           C  
ATOM   2360  C   ASN A 311     126.922 172.464 156.385  1.00164.33           C  
ATOM   2361  O   ASN A 311     128.069 172.165 156.729  1.00164.33           O  
ATOM   2362  CB  ASN A 311     124.861 171.296 157.214  1.00164.33           C  
ATOM   2363  CG  ASN A 311     125.384 170.029 157.868  1.00164.33           C  
ATOM   2364  OD1 ASN A 311     124.651 169.052 158.024  1.00164.33           O  
ATOM   2365  ND2 ASN A 311     126.654 170.041 158.256  1.00164.33           N  
ATOM   2366  N   MET A 312     126.615 172.767 155.123  1.00165.98           N  
ATOM   2367  CA  MET A 312     127.630 172.715 154.076  1.00165.98           C  
ATOM   2368  C   MET A 312     128.662 173.828 154.198  1.00165.98           C  
ATOM   2369  O   MET A 312     129.707 173.754 153.542  1.00165.98           O  
ATOM   2370  CB  MET A 312     126.964 172.763 152.696  1.00165.98           C  
ATOM   2371  CG  MET A 312     126.034 173.952 152.469  1.00165.98           C  
ATOM   2372  SD  MET A 312     126.866 175.495 152.038  1.00165.98           S  
ATOM   2373  CE  MET A 312     127.471 175.110 150.397  1.00165.98           C  
ATOM   2374  N   MET A 313     128.393 174.853 155.010  1.00162.78           N  
ATOM   2375  CA  MET A 313     129.373 175.913 155.230  1.00162.78           C  
ATOM   2376  C   MET A 313     130.625 175.383 155.919  1.00162.78           C  
ATOM   2377  O   MET A 313     131.750 175.685 155.503  1.00162.78           O  
ATOM   2378  CB  MET A 313     128.747 177.043 156.046  1.00162.78           C  
ATOM   2379  CG  MET A 313     129.658 178.245 156.232  1.00162.78           C  
ATOM   2380  SD  MET A 313     130.056 179.052 154.669  1.00162.78           S  
ATOM   2381  CE  MET A 313     131.615 179.835 155.078  1.00162.78           C  
ATOM   2382  N   GLU A 314     130.454 174.588 156.978  1.00164.37           N  
ATOM   2383  CA  GLU A 314     131.613 173.988 157.630  1.00164.37           C  
ATOM   2384  C   GLU A 314     132.201 172.835 156.827  1.00164.37           C  
ATOM   2385  O   GLU A 314     133.404 172.571 156.933  1.00164.37           O  
ATOM   2386  CB  GLU A 314     131.249 173.528 159.046  1.00164.37           C  
ATOM   2387  CG  GLU A 314     130.071 172.573 159.138  1.00164.37           C  
ATOM   2388  CD  GLU A 314     130.478 171.121 158.987  1.00164.37           C  
ATOM   2389  OE1 GLU A 314     131.672 170.812 159.185  1.00164.37           O  
ATOM   2390  OE2 GLU A 314     129.602 170.286 158.678  1.00164.37           O  
ATOM   2391  N   HIS A 315     131.387 172.133 156.033  1.00159.55           N  
ATOM   2392  CA  HIS A 315     131.941 171.111 155.149  1.00159.55           C  
ATOM   2393  C   HIS A 315     132.878 171.735 154.124  1.00159.55           C  
ATOM   2394  O   HIS A 315     133.972 171.217 153.869  1.00159.55           O  
ATOM   2395  CB  HIS A 315     130.818 170.346 154.447  1.00159.55           C  
ATOM   2396  CG  HIS A 315     130.124 169.347 155.319  1.00159.55           C  
ATOM   2397  ND1 HIS A 315     130.703 168.151 155.688  1.00159.55           N  
ATOM   2398  CD2 HIS A 315     128.893 169.358 155.882  1.00159.55           C  
ATOM   2399  CE1 HIS A 315     129.862 167.474 156.449  1.00159.55           C  
ATOM   2400  NE2 HIS A 315     128.756 168.184 156.582  1.00159.55           N  
ATOM   2401  N   TRP A 316     132.460 172.852 153.526  1.00149.76           N  
ATOM   2402  CA  TRP A 316     133.317 173.587 152.603  1.00149.76           C  
ATOM   2403  C   TRP A 316     134.490 174.235 153.327  1.00149.76           C  
ATOM   2404  O   TRP A 316     135.536 174.484 152.715  1.00149.76           O  
ATOM   2405  CB  TRP A 316     132.490 174.626 151.846  1.00149.76           C  
ATOM   2406  CG  TRP A 316     133.282 175.484 150.915  1.00149.76           C  
ATOM   2407  CD1 TRP A 316     134.223 175.070 150.018  1.00149.76           C  
ATOM   2408  CD2 TRP A 316     133.172 176.902 150.757  1.00149.76           C  
ATOM   2409  NE1 TRP A 316     134.724 176.147 149.327  1.00149.76           N  
ATOM   2410  CE2 TRP A 316     134.093 177.283 149.761  1.00149.76           C  
ATOM   2411  CE3 TRP A 316     132.391 177.889 151.367  1.00149.76           C  
ATOM   2412  CZ2 TRP A 316     134.252 178.606 149.360  1.00149.76           C  
ATOM   2413  CZ3 TRP A 316     132.552 179.201 150.968  1.00149.76           C  
ATOM   2414  CH2 TRP A 316     133.474 179.547 149.973  1.00149.76           C  
ATOM   2415  N   ASP A 317     134.339 174.507 154.624  1.00153.66           N  
ATOM   2416  CA  ASP A 317     135.477 174.911 155.444  1.00153.66           C  
ATOM   2417  C   ASP A 317     136.328 173.711 155.844  1.00153.66           C  
ATOM   2418  O   ASP A 317     137.555 173.826 155.944  1.00153.66           O  
ATOM   2419  CB  ASP A 317     134.990 175.659 156.685  1.00153.66           C  
ATOM   2420  CG  ASP A 317     136.127 176.265 157.484  1.00153.66           C  
ATOM   2421  OD1 ASP A 317     136.682 177.293 157.043  1.00153.66           O  
ATOM   2422  OD2 ASP A 317     136.463 175.715 158.553  1.00153.66           O  
ATOM   2423  N   TYR A 318     135.698 172.558 156.082  1.00147.99           N  
ATOM   2424  CA  TYR A 318     136.464 171.330 156.270  1.00147.99           C  
ATOM   2425  C   TYR A 318     137.240 170.974 155.009  1.00147.99           C  
ATOM   2426  O   TYR A 318     138.379 170.498 155.083  1.00147.99           O  
ATOM   2427  CB  TYR A 318     135.537 170.182 156.670  1.00147.99           C  
ATOM   2428  CG  TYR A 318     136.258 168.876 156.914  1.00147.99           C  
ATOM   2429  CD1 TYR A 318     136.999 168.674 158.071  1.00147.99           C  
ATOM   2430  CD2 TYR A 318     136.200 167.846 155.985  1.00147.99           C  
ATOM   2431  CE1 TYR A 318     137.661 167.482 158.297  1.00147.99           C  
ATOM   2432  CE2 TYR A 318     136.859 166.651 156.201  1.00147.99           C  
ATOM   2433  CZ  TYR A 318     137.587 166.474 157.358  1.00147.99           C  
ATOM   2434  OH  TYR A 318     138.244 165.285 157.578  1.00147.99           O  
ATOM   2435  N   LEU A 319     136.638 171.197 153.839  1.00143.91           N  
ATOM   2436  CA  LEU A 319     137.344 170.969 152.583  1.00143.91           C  
ATOM   2437  C   LEU A 319     138.419 172.024 152.355  1.00143.91           C  
ATOM   2438  O   LEU A 319     139.445 171.738 151.728  1.00143.91           O  
ATOM   2439  CB  LEU A 319     136.346 170.946 151.421  1.00143.91           C  
ATOM   2440  CG  LEU A 319     136.760 170.353 150.068  1.00143.91           C  
ATOM   2441  CD1 LEU A 319     137.511 171.356 149.198  1.00143.91           C  
ATOM   2442  CD2 LEU A 319     137.586 169.089 150.267  1.00143.91           C  
ATOM   2443  N   GLN A 320     138.207 173.242 152.861  1.00147.26           N  
ATOM   2444  CA  GLN A 320     139.247 174.263 152.798  1.00147.26           C  
ATOM   2445  C   GLN A 320     140.450 173.883 153.654  1.00147.26           C  
ATOM   2446  O   GLN A 320     141.598 174.031 153.220  1.00147.26           O  
ATOM   2447  CB  GLN A 320     138.682 175.613 153.237  1.00147.26           C  
ATOM   2448  CG  GLN A 320     139.697 176.745 153.234  1.00147.26           C  
ATOM   2449  CD  GLN A 320     139.134 178.032 153.803  1.00147.26           C  
ATOM   2450  OE1 GLN A 320     137.968 178.094 154.193  1.00147.26           O  
ATOM   2451  NE2 GLN A 320     139.963 179.068 153.856  1.00147.26           N  
ATOM   2452  N   LEU A 321     140.210 173.391 154.872  1.00142.63           N  
ATOM   2453  CA  LEU A 321     141.321 173.098 155.771  1.00142.63           C  
ATOM   2454  C   LEU A 321     142.050 171.827 155.352  1.00142.63           C  
ATOM   2455  O   LEU A 321     143.253 171.691 155.606  1.00142.63           O  
ATOM   2456  CB  LEU A 321     140.807 172.987 157.210  1.00142.63           C  
ATOM   2457  CG  LEU A 321     141.798 172.935 158.380  1.00142.63           C  
ATOM   2458  CD1 LEU A 321     142.267 171.514 158.677  1.00142.63           C  
ATOM   2459  CD2 LEU A 321     142.985 173.854 158.123  1.00142.63           C  
ATOM   2460  N   THR A 322     141.347 170.895 154.705  1.00142.74           N  
ATOM   2461  CA  THR A 322     141.930 169.595 154.392  1.00142.74           C  
ATOM   2462  C   THR A 322     142.898 169.690 153.218  1.00142.74           C  
ATOM   2463  O   THR A 322     143.951 169.042 153.223  1.00142.74           O  
ATOM   2464  CB  THR A 322     140.827 168.577 154.098  1.00142.74           C  
ATOM   2465  OG1 THR A 322     139.865 168.597 155.160  1.00142.74           O  
ATOM   2466  CG2 THR A 322     141.414 167.177 153.997  1.00142.74           C  
ATOM   2467  N   VAL A 323     142.560 170.495 152.206  1.00135.11           N  
ATOM   2468  CA  VAL A 323     143.481 170.742 151.103  1.00135.11           C  
ATOM   2469  C   VAL A 323     144.649 171.615 151.546  1.00135.11           C  
ATOM   2470  O   VAL A 323     145.726 171.562 150.940  1.00135.11           O  
ATOM   2471  CB  VAL A 323     142.731 171.371 149.911  1.00135.11           C  
ATOM   2472  CG1 VAL A 323     142.273 172.785 150.244  1.00135.11           C  
ATOM   2473  CG2 VAL A 323     143.593 171.354 148.654  1.00135.11           C  
ATOM   2474  N   ALA A 324     144.470 172.406 152.601  1.00146.72           N  
ATOM   2475  CA  ALA A 324     145.543 173.202 153.181  1.00146.72           C  
ATOM   2476  C   ALA A 324     146.426 172.389 154.118  1.00146.72           C  
ATOM   2477  O   ALA A 324     147.294 172.959 154.786  1.00146.72           O  
ATOM   2478  CB  ALA A 324     144.963 174.408 153.925  1.00146.72           C  
ATOM   2479  N   MET A 325     146.206 171.077 154.183  1.00153.23           N  
ATOM   2480  CA  MET A 325     147.050 170.133 154.902  1.00153.23           C  
ATOM   2481  C   MET A 325     147.642 169.055 154.007  1.00153.23           C  
ATOM   2482  O   MET A 325     148.769 168.619 154.251  1.00153.23           O  
ATOM   2483  CB  MET A 325     146.256 169.461 156.034  1.00153.23           C  
ATOM   2484  CG  MET A 325     147.095 168.609 156.972  1.00153.23           C  
ATOM   2485  SD  MET A 325     146.098 167.751 158.205  1.00153.23           S  
ATOM   2486  CE  MET A 325     145.502 169.129 159.180  1.00153.23           C  
ATOM   2487  N   TYR A 326     146.905 168.612 152.984  1.00147.50           N  
ATOM   2488  CA  TYR A 326     147.464 167.735 151.959  1.00147.50           C  
ATOM   2489  C   TYR A 326     148.715 168.332 151.325  1.00147.50           C  
ATOM   2490  O   TYR A 326     149.688 167.617 151.061  1.00147.50           O  
ATOM   2491  CB  TYR A 326     146.407 167.447 150.892  1.00147.50           C  
ATOM   2492  CG  TYR A 326     146.939 166.750 149.660  1.00147.50           C  
ATOM   2493  CD1 TYR A 326     147.281 165.404 149.692  1.00147.50           C  
ATOM   2494  CD2 TYR A 326     147.090 167.436 148.462  1.00147.50           C  
ATOM   2495  CE1 TYR A 326     147.764 164.763 148.567  1.00147.50           C  
ATOM   2496  CE2 TYR A 326     147.573 166.803 147.332  1.00147.50           C  
ATOM   2497  CZ  TYR A 326     147.907 165.467 147.389  1.00147.50           C  
ATOM   2498  OH  TYR A 326     148.389 164.834 146.267  1.00147.50           O  
ATOM   2499  N   ILE A 327     148.712 169.640 151.074  1.00141.31           N  
ATOM   2500  CA  ILE A 327     149.892 170.295 150.516  1.00141.31           C  
ATOM   2501  C   ILE A 327     150.931 170.545 151.602  1.00141.31           C  
ATOM   2502  O   ILE A 327     152.077 170.092 151.505  1.00141.31           O  
ATOM   2503  CB  ILE A 327     149.498 171.601 149.803  1.00141.31           C  
ATOM   2504  CG1 ILE A 327     148.504 171.315 148.676  1.00141.31           C  
ATOM   2505  CG2 ILE A 327     150.732 172.308 149.264  1.00141.31           C  
ATOM   2506  CD1 ILE A 327     149.045 170.392 147.606  1.00141.31           C  
ATOM   2507  N   ASN A 328     150.548 171.268 152.653  1.00154.84           N  
ATOM   2508  CA  ASN A 328     151.470 171.658 153.716  1.00154.84           C  
ATOM   2509  C   ASN A 328     150.776 171.401 155.046  1.00154.84           C  
ATOM   2510  O   ASN A 328     149.786 172.062 155.372  1.00154.84           O  
ATOM   2511  CB  ASN A 328     151.882 173.124 153.581  1.00154.84           C  
ATOM   2512  CG  ASN A 328     153.028 173.496 154.502  1.00154.84           C  
ATOM   2513  OD1 ASN A 328     153.529 172.665 155.260  1.00154.84           O  
ATOM   2514  ND2 ASN A 328     153.453 174.753 154.439  1.00154.84           N  
ATOM   2515  N   SER A 329     151.303 170.452 155.819  1.00164.28           N  
ATOM   2516  CA  SER A 329     150.698 170.039 157.078  1.00164.28           C  
ATOM   2517  C   SER A 329     151.152 170.883 158.264  1.00164.28           C  
ATOM   2518  O   SER A 329     151.047 170.429 159.410  1.00164.28           O  
ATOM   2519  CB  SER A 329     150.996 168.561 157.344  1.00164.28           C  
ATOM   2520  OG  SER A 329     150.462 168.149 158.590  1.00164.28           O  
ATOM   2521  N   ASP A 330     151.650 172.097 158.022  1.00169.84           N  
ATOM   2522  CA  ASP A 330     151.978 172.991 159.124  1.00169.84           C  
ATOM   2523  C   ASP A 330     150.748 173.658 159.725  1.00169.84           C  
ATOM   2524  O   ASP A 330     150.810 174.128 160.866  1.00169.84           O  
ATOM   2525  CB  ASP A 330     152.973 174.058 158.659  1.00169.84           C  
ATOM   2526  CG  ASP A 330     152.451 174.876 157.491  1.00169.84           C  
ATOM   2527  OD1 ASP A 330     151.372 174.543 156.957  1.00169.84           O  
ATOM   2528  OD2 ASP A 330     153.123 175.856 157.104  1.00169.84           O  
ATOM   2529  N   SER A 331     149.637 173.710 158.986  1.00172.42           N  
ATOM   2530  CA  SER A 331     148.434 174.411 159.419  1.00172.42           C  
ATOM   2531  C   SER A 331     147.469 173.510 160.181  1.00172.42           C  
ATOM   2532  O   SER A 331     146.253 173.743 160.147  1.00172.42           O  
ATOM   2533  CB  SER A 331     147.733 175.042 158.215  1.00172.42           C  
ATOM   2534  OG  SER A 331     148.566 175.997 157.583  1.00172.42           O  
ATOM   2535  N   VAL A 332     147.974 172.483 160.868  1.00180.19           N  
ATOM   2536  CA  VAL A 332     147.087 171.568 161.579  1.00180.19           C  
ATOM   2537  C   VAL A 332     146.532 172.225 162.838  1.00180.19           C  
ATOM   2538  O   VAL A 332     145.329 172.141 163.117  1.00180.19           O  
ATOM   2539  CB  VAL A 332     147.815 170.245 161.888  1.00180.19           C  
ATOM   2540  CG1 VAL A 332     149.155 170.503 162.566  1.00180.19           C  
ATOM   2541  CG2 VAL A 332     146.940 169.342 162.746  1.00180.19           C  
ATOM   2542  N   ASN A 333     147.389 172.909 163.603  1.00180.37           N  
ATOM   2543  CA  ASN A 333     147.066 173.457 164.916  1.00180.37           C  
ATOM   2544  C   ASN A 333     146.362 172.421 165.786  1.00180.37           C  
ATOM   2545  O   ASN A 333     145.151 172.526 166.019  1.00180.37           O  
ATOM   2546  CB  ASN A 333     146.199 174.710 164.774  1.00180.37           C  
ATOM   2547  CG  ASN A 333     146.914 175.833 164.048  1.00180.37           C  
ATOM   2548  OD1 ASN A 333     146.505 176.248 162.964  1.00180.37           O  
ATOM   2549  ND2 ASN A 333     147.991 176.331 164.645  1.00180.37           N  
ATOM   2550  N   PRO A 334     147.083 171.405 166.286  1.00185.08           N  
ATOM   2551  CA  PRO A 334     146.467 170.291 167.013  1.00185.08           C  
ATOM   2552  C   PRO A 334     145.934 170.704 168.382  1.00185.08           C  
ATOM   2553  O   PRO A 334     144.717 170.775 168.554  1.00185.08           O  
ATOM   2554  CB  PRO A 334     147.616 169.292 167.153  1.00185.08           C  
ATOM   2555  CG  PRO A 334     148.836 170.143 167.175  1.00185.08           C  
ATOM   2556  CD  PRO A 334     148.552 171.292 166.244  1.00185.08           C  
ATOM   2557  N   LYS A 348     152.520 161.419 164.500  1.00179.90           N  
ATOM   2558  CA  LYS A 348     151.065 161.538 164.535  1.00179.90           C  
ATOM   2559  C   LYS A 348     150.533 162.665 163.633  1.00179.90           C  
ATOM   2560  O   LYS A 348     149.490 162.497 163.001  1.00179.90           O  
ATOM   2561  CB  LYS A 348     150.581 161.736 165.978  1.00179.90           C  
ATOM   2562  CG  LYS A 348     149.071 161.805 166.126  1.00179.90           C  
ATOM   2563  CD  LYS A 348     148.421 160.478 165.773  1.00179.90           C  
ATOM   2564  CE  LYS A 348     146.923 160.514 166.029  1.00179.90           C  
ATOM   2565  NZ  LYS A 348     146.227 161.455 165.109  1.00179.90           N  
ATOM   2566  N   PRO A 349     151.230 163.803 163.558  1.00174.06           N  
ATOM   2567  CA  PRO A 349     150.963 164.737 162.455  1.00174.06           C  
ATOM   2568  C   PRO A 349     151.369 164.129 161.121  1.00174.06           C  
ATOM   2569  O   PRO A 349     152.447 163.546 160.990  1.00174.06           O  
ATOM   2570  CB  PRO A 349     151.823 165.958 162.805  1.00174.06           C  
ATOM   2571  CG  PRO A 349     151.953 165.903 164.278  1.00174.06           C  
ATOM   2572  CD  PRO A 349     152.070 164.438 164.591  1.00174.06           C  
ATOM   2573  N   ILE A 350     150.493 164.267 160.129  1.00176.79           N  
ATOM   2574  CA  ILE A 350     150.657 163.558 158.866  1.00176.79           C  
ATOM   2575  C   ILE A 350     151.738 164.242 158.039  1.00176.79           C  
ATOM   2576  O   ILE A 350     151.915 165.465 158.090  1.00176.79           O  
ATOM   2577  CB  ILE A 350     149.314 163.485 158.110  1.00176.79           C  
ATOM   2578  CG1 ILE A 350     149.413 162.531 156.917  1.00176.79           C  
ATOM   2579  CG2 ILE A 350     148.862 164.870 157.664  1.00176.79           C  
ATOM   2580  CD1 ILE A 350     148.072 162.123 156.348  1.00176.79           C  
ATOM   2581  N   ARG A 351     152.485 163.443 157.282  1.00173.16           N  
ATOM   2582  CA  ARG A 351     153.463 163.991 156.356  1.00173.16           C  
ATOM   2583  C   ARG A 351     152.775 164.658 155.167  1.00173.16           C  
ATOM   2584  O   ARG A 351     151.586 164.457 154.903  1.00173.16           O  
ATOM   2585  CB  ARG A 351     154.407 162.894 155.862  1.00173.16           C  
ATOM   2586  CG  ARG A 351     155.314 162.320 156.938  1.00173.16           C  
ATOM   2587  CD  ARG A 351     156.245 161.263 156.366  1.00173.16           C  
ATOM   2588  NE  ARG A 351     157.184 161.824 155.399  1.00173.16           N  
ATOM   2589  CZ  ARG A 351     157.960 161.096 154.602  1.00173.16           C  
ATOM   2590  NH1 ARG A 351     157.907 159.772 154.650  1.00173.16           N  
ATOM   2591  NH2 ARG A 351     158.785 161.692 153.752  1.00173.16           N  
ATOM   2592  N   GLY A 352     153.548 165.467 154.446  1.00165.47           N  
ATOM   2593  CA  GLY A 352     153.053 166.141 153.263  1.00165.47           C  
ATOM   2594  C   GLY A 352     154.144 166.449 152.259  1.00165.47           C  
ATOM   2595  O   GLY A 352     155.264 165.942 152.370  1.00165.47           O  
ATOM   2596  N   PHE A 353     153.826 167.283 151.267  1.00163.33           N  
ATOM   2597  CA  PHE A 353     154.822 167.691 150.282  1.00163.33           C  
ATOM   2598  C   PHE A 353     155.844 168.637 150.902  1.00163.33           C  
ATOM   2599  O   PHE A 353     157.052 168.375 150.879  1.00163.33           O  
ATOM   2600  CB  PHE A 353     154.137 168.343 149.079  1.00163.33           C  
ATOM   2601  CG  PHE A 353     153.258 167.406 148.301  1.00163.33           C  
ATOM   2602  CD1 PHE A 353     153.805 166.520 147.388  1.00163.33           C  
ATOM   2603  CD2 PHE A 353     151.885 167.413 148.480  1.00163.33           C  
ATOM   2604  CE1 PHE A 353     153.000 165.656 146.669  1.00163.33           C  
ATOM   2605  CE2 PHE A 353     151.074 166.553 147.764  1.00163.33           C  
ATOM   2606  CZ  PHE A 353     151.633 165.673 146.858  1.00163.33           C  
ATOM   2607  N   CYS A 354     155.368 169.746 151.472  1.00167.45           N  
ATOM   2608  CA  CYS A 354     156.240 170.698 152.150  1.00167.45           C  
ATOM   2609  C   CYS A 354     156.876 170.114 153.406  1.00167.45           C  
ATOM   2610  O   CYS A 354     157.935 170.589 153.828  1.00167.45           O  
ATOM   2611  CB  CYS A 354     155.452 171.963 152.497  1.00167.45           C  
ATOM   2612  SG  CYS A 354     156.405 173.264 153.312  1.00167.45           S  
ATOM   2613  N   GLN A 355     156.265 169.090 154.002  1.00169.22           N  
ATOM   2614  CA  GLN A 355     156.797 168.466 155.208  1.00169.22           C  
ATOM   2615  C   GLN A 355     158.007 167.580 154.942  1.00169.22           C  
ATOM   2616  O   GLN A 355     158.559 167.023 155.898  1.00169.22           O  
ATOM   2617  CB  GLN A 355     155.703 167.650 155.899  1.00169.22           C  
ATOM   2618  CG  GLN A 355     154.524 168.477 156.377  1.00169.22           C  
ATOM   2619  CD  GLN A 355     154.905 169.454 157.471  1.00169.22           C  
ATOM   2620  OE1 GLN A 355     155.696 169.133 158.358  1.00169.22           O  
ATOM   2621  NE2 GLN A 355     154.344 170.657 157.413  1.00169.22           N  
ATOM   2622  N   ARG A 356     158.434 167.430 153.688  1.00160.91           N  
ATOM   2623  CA  ARG A 356     159.626 166.653 153.369  1.00160.91           C  
ATOM   2624  C   ARG A 356     160.638 167.385 152.497  1.00160.91           C  
ATOM   2625  O   ARG A 356     161.811 166.993 152.500  1.00160.91           O  
ATOM   2626  CB  ARG A 356     159.241 165.327 152.693  1.00160.91           C  
ATOM   2627  CG  ARG A 356     158.517 165.460 151.363  1.00160.91           C  
ATOM   2628  CD  ARG A 356     158.032 164.096 150.889  1.00160.91           C  
ATOM   2629  NE  ARG A 356     157.364 164.152 149.593  1.00160.91           N  
ATOM   2630  CZ  ARG A 356     156.819 163.100 148.989  1.00160.91           C  
ATOM   2631  NH1 ARG A 356     156.233 163.239 147.808  1.00160.91           N  
ATOM   2632  NH2 ARG A 356     156.863 161.907 149.566  1.00160.91           N  
ATOM   2633  N   LEU A 357     160.240 168.427 151.761  1.00161.43           N  
ATOM   2634  CA  LEU A 357     161.205 169.200 150.986  1.00161.43           C  
ATOM   2635  C   LEU A 357     162.144 170.007 151.873  1.00161.43           C  
ATOM   2636  O   LEU A 357     163.259 170.327 151.446  1.00161.43           O  
ATOM   2637  CB  LEU A 357     160.484 170.135 150.012  1.00161.43           C  
ATOM   2638  CG  LEU A 357     160.262 169.618 148.588  1.00161.43           C  
ATOM   2639  CD1 LEU A 357     159.244 168.492 148.559  1.00161.43           C  
ATOM   2640  CD2 LEU A 357     159.834 170.754 147.669  1.00161.43           C  
ATOM   2641  N   LYS A 358     161.724 170.340 153.089  1.00162.11           N  
ATOM   2642  CA  LYS A 358     162.557 171.016 154.071  1.00162.11           C  
ATOM   2643  C   LYS A 358     162.831 170.085 155.245  1.00162.11           C  
ATOM   2644  O   LYS A 358     162.113 169.107 155.474  1.00162.11           O  
ATOM   2645  CB  LYS A 358     161.903 172.313 154.562  1.00162.11           C  
ATOM   2646  CG  LYS A 358     160.534 172.134 155.191  1.00162.11           C  
ATOM   2647  CD  LYS A 358     159.950 173.476 155.604  1.00162.11           C  
ATOM   2648  CE  LYS A 358     159.606 174.325 154.391  1.00162.11           C  
ATOM   2649  NZ  LYS A 358     158.946 175.604 154.774  1.00162.11           N  
ATOM   2650  N   GLY A 359     163.881 170.398 155.988  1.00165.63           N  
ATOM   2651  CA  GLY A 359     164.329 169.565 157.085  1.00165.63           C  
ATOM   2652  C   GLY A 359     165.686 168.941 156.805  1.00165.63           C  
ATOM   2653  O   GLY A 359     166.219 168.990 155.696  1.00165.63           O  
ATOM   2654  N   LYS A 360     166.243 168.343 157.855  1.00170.53           N  
ATOM   2655  CA  LYS A 360     167.551 167.701 157.764  1.00170.53           C  
ATOM   2656  C   LYS A 360     167.439 166.412 156.960  1.00170.53           C  
ATOM   2657  O   LYS A 360     166.870 165.421 157.430  1.00170.53           O  
ATOM   2658  CB  LYS A 360     168.099 167.428 159.161  1.00170.53           C  
ATOM   2659  CG  LYS A 360     168.262 168.672 160.018  1.00170.53           C  
ATOM   2660  CD  LYS A 360     169.315 169.604 159.443  1.00170.53           C  
ATOM   2661  CE  LYS A 360     170.713 169.035 159.624  1.00170.53           C  
ATOM   2662  NZ  LYS A 360     171.764 169.991 159.179  1.00170.53           N  
ATOM   2663  N   GLN A 361     167.980 166.437 155.740  1.00173.64           N  
ATOM   2664  CA  GLN A 361     168.126 165.257 154.888  1.00173.64           C  
ATOM   2665  C   GLN A 361     166.778 164.643 154.521  1.00173.64           C  
ATOM   2666  O   GLN A 361     166.659 163.424 154.375  1.00173.64           O  
ATOM   2667  CB  GLN A 361     169.031 164.206 155.539  1.00173.64           C  
ATOM   2668  CG  GLN A 361     170.514 164.545 155.504  1.00173.64           C  
ATOM   2669  CD  GLN A 361     170.886 165.660 156.462  1.00173.64           C  
ATOM   2670  OE1 GLN A 361     171.375 166.712 156.049  1.00173.64           O  
ATOM   2671  NE2 GLN A 361     170.658 165.435 157.750  1.00173.64           N  
ATOM   2672  N   GLY A 362     165.753 165.477 154.368  1.00170.57           N  
ATOM   2673  CA  GLY A 362     164.488 165.013 153.835  1.00170.57           C  
ATOM   2674  C   GLY A 362     164.458 165.087 152.323  1.00170.57           C  
ATOM   2675  O   GLY A 362     164.246 164.080 151.641  1.00170.57           O  
ATOM   2676  N   ARG A 363     164.677 166.289 151.793  1.00169.75           N  
ATOM   2677  CA  ARG A 363     165.021 166.499 150.394  1.00169.75           C  
ATOM   2678  C   ARG A 363     166.130 167.539 150.317  1.00169.75           C  
ATOM   2679  O   ARG A 363     166.474 168.185 151.311  1.00169.75           O  
ATOM   2680  CB  ARG A 363     163.807 166.958 149.573  1.00169.75           C  
ATOM   2681  CG  ARG A 363     162.639 165.983 149.544  1.00169.75           C  
ATOM   2682  CD  ARG A 363     162.952 164.744 148.721  1.00169.75           C  
ATOM   2683  NE  ARG A 363     163.079 165.060 147.301  1.00169.75           N  
ATOM   2684  CZ  ARG A 363     163.571 164.227 146.390  1.00169.75           C  
ATOM   2685  NH1 ARG A 363     163.983 163.018 146.746  1.00169.75           N  
ATOM   2686  NH2 ARG A 363     163.649 164.603 145.121  1.00169.75           N  
ATOM   2687  N   PHE A 364     166.708 167.676 149.120  1.00165.42           N  
ATOM   2688  CA  PHE A 364     167.645 168.751 148.800  1.00165.42           C  
ATOM   2689  C   PHE A 364     168.959 168.672 149.573  1.00165.42           C  
ATOM   2690  O   PHE A 364     169.877 169.456 149.313  1.00165.42           O  
ATOM   2691  CB  PHE A 364     166.987 170.115 149.036  1.00165.42           C  
ATOM   2692  CG  PHE A 364     165.999 170.504 147.973  1.00165.42           C  
ATOM   2693  CD1 PHE A 364     166.002 169.874 146.739  1.00165.42           C  
ATOM   2694  CD2 PHE A 364     165.065 171.499 148.208  1.00165.42           C  
ATOM   2695  CE1 PHE A 364     165.094 170.229 145.760  1.00165.42           C  
ATOM   2696  CE2 PHE A 364     164.154 171.859 147.233  1.00165.42           C  
ATOM   2697  CZ  PHE A 364     164.168 171.224 146.008  1.00165.42           C  
ATOM   2698  N   ARG A 365     169.068 167.747 150.516  1.00163.65           N  
ATOM   2699  CA  ARG A 365     170.319 167.566 151.248  1.00163.65           C  
ATOM   2700  C   ARG A 365     170.783 166.119 151.288  1.00163.65           C  
ATOM   2701  O   ARG A 365     171.989 165.866 151.229  1.00163.65           O  
ATOM   2702  CB  ARG A 365     170.170 168.100 152.683  1.00163.65           C  
ATOM   2703  CG  ARG A 365     170.021 169.610 152.774  1.00163.65           C  
ATOM   2704  CD  ARG A 365     169.956 170.071 154.220  1.00163.65           C  
ATOM   2705  NE  ARG A 365     169.796 171.518 154.327  1.00163.65           N  
ATOM   2706  CZ  ARG A 365     169.719 172.177 155.478  1.00163.65           C  
ATOM   2707  NH1 ARG A 365     169.798 171.520 156.627  1.00163.65           N  
ATOM   2708  NH2 ARG A 365     169.571 173.495 155.481  1.00163.65           N  
ATOM   2709  N   GLY A 366     169.860 165.164 151.387  1.00165.01           N  
ATOM   2710  CA  GLY A 366     170.187 163.756 151.297  1.00165.01           C  
ATOM   2711  C   GLY A 366     169.699 163.077 150.039  1.00165.01           C  
ATOM   2712  O   GLY A 366     169.837 161.852 149.922  1.00165.01           O  
ATOM   2713  N   ASN A 367     169.133 163.820 149.091  1.00169.09           N  
ATOM   2714  CA  ASN A 367     168.578 163.246 147.873  1.00169.09           C  
ATOM   2715  C   ASN A 367     169.079 163.988 146.640  1.00169.09           C  
ATOM   2716  O   ASN A 367     169.208 163.397 145.564  1.00169.09           O  
ATOM   2717  CB  ASN A 367     167.049 163.264 147.922  1.00169.09           C  
ATOM   2718  CG  ASN A 367     166.489 162.295 148.945  1.00169.09           C  
ATOM   2719  OD1 ASN A 367     166.969 161.170 149.080  1.00169.09           O  
ATOM   2720  ND2 ASN A 367     165.467 162.729 149.673  1.00169.09           N  
ATOM   2721  N   LEU A 368     169.362 165.283 146.784  1.00157.76           N  
ATOM   2722  CA  LEU A 368     169.856 166.095 145.678  1.00157.76           C  
ATOM   2723  C   LEU A 368     171.265 166.618 145.906  1.00157.76           C  
ATOM   2724  O   LEU A 368     172.100 166.541 144.997  1.00157.76           O  
ATOM   2725  CB  LEU A 368     168.902 167.275 145.421  1.00157.76           C  
ATOM   2726  CG  LEU A 368     167.713 167.045 144.483  1.00157.76           C  
ATOM   2727  CD1 LEU A 368     168.189 166.571 143.116  1.00157.76           C  
ATOM   2728  CD2 LEU A 368     166.706 166.072 145.077  1.00157.76           C  
ATOM   2729  N   SER A 369     171.564 167.151 147.093  1.00154.25           N  
ATOM   2730  CA  SER A 369     172.923 167.611 147.359  1.00154.25           C  
ATOM   2731  C   SER A 369     173.859 166.433 147.608  1.00154.25           C  
ATOM   2732  O   SER A 369     174.873 166.275 146.919  1.00154.25           O  
ATOM   2733  CB  SER A 369     172.931 168.572 148.550  1.00154.25           C  
ATOM   2734  OG  SER A 369     172.164 169.731 148.274  1.00154.25           O  
ATOM   2735  N   GLY A 370     173.536 165.598 148.591  1.00140.40           N  
ATOM   2736  CA  GLY A 370     174.350 164.431 148.866  1.00140.40           C  
ATOM   2737  C   GLY A 370     173.582 163.154 148.603  1.00140.40           C  
ATOM   2738  O   GLY A 370     172.687 162.796 149.375  1.00140.40           O  
ATOM   2739  N   LYS A 371     173.919 162.453 147.526  1.00125.55           N  
ATOM   2740  CA  LYS A 371     173.209 161.237 147.167  1.00125.55           C  
ATOM   2741  C   LYS A 371     173.934 160.022 147.744  1.00125.55           C  
ATOM   2742  O   LYS A 371     174.816 160.141 148.599  1.00125.55           O  
ATOM   2743  CB  LYS A 371     173.059 161.152 145.650  1.00125.55           C  
ATOM   2744  CG  LYS A 371     172.211 162.266 145.061  1.00125.55           C  
ATOM   2745  CD  LYS A 371     172.138 162.170 143.549  1.00125.55           C  
ATOM   2746  CE  LYS A 371     171.366 163.340 142.962  1.00125.55           C  
ATOM   2747  NZ  LYS A 371     171.353 163.301 141.475  1.00125.55           N  
ATOM   2748  N   ARG A 372     173.563 158.833 147.277  1.00109.60           N  
ATOM   2749  CA  ARG A 372     174.268 157.600 147.593  1.00109.60           C  
ATOM   2750  C   ARG A 372     174.835 156.996 146.317  1.00109.60           C  
ATOM   2751  O   ARG A 372     174.214 157.079 145.253  1.00109.60           O  
ATOM   2752  CB  ARG A 372     173.343 156.601 148.292  1.00109.60           C  
ATOM   2753  CG  ARG A 372     172.810 157.106 149.621  1.00109.60           C  
ATOM   2754  CD  ARG A 372     171.973 156.058 150.328  1.00109.60           C  
ATOM   2755  NE  ARG A 372     171.296 156.610 151.497  1.00109.60           N  
ATOM   2756  CZ  ARG A 372     171.845 156.697 152.704  1.00109.60           C  
ATOM   2757  NH1 ARG A 372     173.081 156.263 152.904  1.00109.60           N  
ATOM   2758  NH2 ARG A 372     171.157 157.215 153.712  1.00109.60           N  
ATOM   2759  N   VAL A 373     176.011 156.387 146.425  1.00 98.08           N  
ATOM   2760  CA  VAL A 373     176.787 155.996 145.258  1.00 98.08           C  
ATOM   2761  C   VAL A 373     176.831 154.476 145.184  1.00 98.08           C  
ATOM   2762  O   VAL A 373     176.576 153.768 146.163  1.00 98.08           O  
ATOM   2763  CB  VAL A 373     178.213 156.585 145.289  1.00 98.08           C  
ATOM   2764  CG1 VAL A 373     178.159 158.103 145.341  1.00 98.08           C  
ATOM   2765  CG2 VAL A 373     178.989 156.032 146.474  1.00 98.08           C  
ATOM   2766  N   ASP A 374     177.157 153.972 143.999  1.00 95.47           N  
ATOM   2767  CA  ASP A 374     177.486 152.567 143.815  1.00 95.47           C  
ATOM   2768  C   ASP A 374     178.998 152.368 143.822  1.00 95.47           C  
ATOM   2769  O   ASP A 374     179.779 153.321 143.757  1.00 95.47           O  
ATOM   2770  CB  ASP A 374     176.885 152.040 142.508  1.00 95.47           C  
ATOM   2771  CG  ASP A 374     175.383 151.855 142.590  1.00 95.47           C  
ATOM   2772  OD1 ASP A 374     174.873 151.615 143.703  1.00 95.47           O  
ATOM   2773  OD2 ASP A 374     174.712 151.945 141.539  1.00 95.47           O  
ATOM   2774  N   PHE A 375     179.402 151.099 143.909  1.00 74.85           N  
ATOM   2775  CA  PHE A 375     180.802 150.686 143.817  1.00 74.85           C  
ATOM   2776  C   PHE A 375     181.638 151.336 144.925  1.00 74.85           C  
ATOM   2777  O   PHE A 375     182.531 152.150 144.682  1.00 74.85           O  
ATOM   2778  CB  PHE A 375     181.372 151.008 142.430  1.00 74.85           C  
ATOM   2779  CG  PHE A 375     180.685 150.281 141.309  1.00 74.85           C  
ATOM   2780  CD1 PHE A 375     180.972 148.952 141.046  1.00 74.85           C  
ATOM   2781  CD2 PHE A 375     179.744 150.926 140.524  1.00 74.85           C  
ATOM   2782  CE1 PHE A 375     180.339 148.281 140.016  1.00 74.85           C  
ATOM   2783  CE2 PHE A 375     179.106 150.261 139.492  1.00 74.85           C  
ATOM   2784  CZ  PHE A 375     179.404 148.937 139.238  1.00 74.85           C  
ATOM   2785  N   SER A 376     181.321 150.951 146.161  1.00 73.18           N  
ATOM   2786  CA  SER A 376     182.009 151.495 147.323  1.00 73.18           C  
ATOM   2787  C   SER A 376     182.346 150.369 148.293  1.00 73.18           C  
ATOM   2788  O   SER A 376     182.068 149.192 148.042  1.00 73.18           O  
ATOM   2789  CB  SER A 376     181.163 152.575 148.008  1.00 73.18           C  
ATOM   2790  OG  SER A 376     181.774 153.019 149.207  1.00 73.18           O  
ATOM   2791  N   GLY A 377     182.954 150.750 149.412  1.00 74.23           N  
ATOM   2792  CA  GLY A 377     183.271 149.830 150.488  1.00 74.23           C  
ATOM   2793  C   GLY A 377     183.487 150.614 151.760  1.00 74.23           C  
ATOM   2794  O   GLY A 377     183.678 151.834 151.729  1.00 74.23           O  
ATOM   2795  N   ARG A 378     183.450 149.907 152.890  1.00 78.72           N  
ATOM   2796  CA  ARG A 378     183.687 150.561 154.177  1.00 78.72           C  
ATOM   2797  C   ARG A 378     184.262 149.534 155.150  1.00 78.72           C  
ATOM   2798  O   ARG A 378     183.516 148.737 155.728  1.00 78.72           O  
ATOM   2799  CB  ARG A 378     182.402 151.180 154.709  1.00 78.72           C  
ATOM   2800  CG  ARG A 378     182.568 151.990 155.984  1.00 78.72           C  
ATOM   2801  CD  ARG A 378     181.255 152.648 156.380  1.00 78.72           C  
ATOM   2802  NE  ARG A 378     181.386 153.463 157.585  1.00 78.72           N  
ATOM   2803  CZ  ARG A 378     181.779 154.733 157.589  1.00 78.72           C  
ATOM   2804  NH1 ARG A 378     182.084 155.337 156.449  1.00 78.72           N  
ATOM   2805  NH2 ARG A 378     181.870 155.398 158.732  1.00 78.72           N  
ATOM   2806  N   THR A 379     185.583 149.561 155.324  1.00 68.72           N  
ATOM   2807  CA  THR A 379     186.294 148.608 156.164  1.00 68.72           C  
ATOM   2808  C   THR A 379     187.200 149.371 157.124  1.00 68.72           C  
ATOM   2809  O   THR A 379     187.398 150.582 156.996  1.00 68.72           O  
ATOM   2810  CB  THR A 379     187.123 147.616 155.333  1.00 68.72           C  
ATOM   2811  OG1 THR A 379     188.189 148.311 154.676  1.00 68.72           O  
ATOM   2812  CG2 THR A 379     186.254 146.926 154.289  1.00 68.72           C  
ATOM   2813  N   VAL A 380     187.758 148.646 158.093  1.00 69.06           N  
ATOM   2814  CA  VAL A 380     188.738 149.214 159.014  1.00 69.06           C  
ATOM   2815  C   VAL A 380     190.071 149.358 158.290  1.00 69.06           C  
ATOM   2816  O   VAL A 380     190.253 148.819 157.192  1.00 69.06           O  
ATOM   2817  CB  VAL A 380     188.879 148.347 160.280  1.00 69.06           C  
ATOM   2818  CG1 VAL A 380     189.802 147.163 160.019  1.00 69.06           C  
ATOM   2819  CG2 VAL A 380     189.362 149.180 161.464  1.00 69.06           C  
ATOM   2820  N   ILE A 381     191.013 150.082 158.895  1.00 68.20           N  
ATOM   2821  CA  ILE A 381     192.327 150.295 158.307  1.00 68.20           C  
ATOM   2822  C   ILE A 381     193.396 149.798 159.274  1.00 68.20           C  
ATOM   2823  O   ILE A 381     193.167 149.654 160.477  1.00 68.20           O  
ATOM   2824  CB  ILE A 381     192.567 151.775 157.944  1.00 68.20           C  
ATOM   2825  CG1 ILE A 381     192.365 152.666 159.172  1.00 68.20           C  
ATOM   2826  CG2 ILE A 381     191.646 152.202 156.813  1.00 68.20           C  
ATOM   2827  CD1 ILE A 381     192.724 154.118 158.939  1.00 68.20           C  
ATOM   2828  N   SER A 382     194.583 149.536 158.722  1.00 74.60           N  
ATOM   2829  CA  SER A 382     195.760 149.142 159.482  1.00 74.60           C  
ATOM   2830  C   SER A 382     196.983 149.669 158.747  1.00 74.60           C  
ATOM   2831  O   SER A 382     196.988 149.683 157.508  1.00 74.60           O  
ATOM   2832  CB  SER A 382     195.861 147.623 159.656  1.00 74.60           C  
ATOM   2833  OG  SER A 382     196.061 146.978 158.412  1.00 74.60           O  
ATOM   2834  N   PRO A 383     198.016 150.109 159.460  1.00 76.83           N  
ATOM   2835  CA  PRO A 383     199.125 150.804 158.800  1.00 76.83           C  
ATOM   2836  C   PRO A 383     200.035 149.843 158.047  1.00 76.83           C  
ATOM   2837  O   PRO A 383     200.042 148.632 158.272  1.00 76.83           O  
ATOM   2838  CB  PRO A 383     199.880 151.457 159.967  1.00 76.83           C  
ATOM   2839  CG  PRO A 383     198.930 151.404 161.136  1.00 76.83           C  
ATOM   2840  CD  PRO A 383     198.145 150.150 160.924  1.00 76.83           C  
ATOM   2841  N   ASP A 384     200.814 150.421 157.133  1.00 77.64           N  
ATOM   2842  CA  ASP A 384     201.840 149.694 156.396  1.00 77.64           C  
ATOM   2843  C   ASP A 384     202.914 150.677 155.943  1.00 77.64           C  
ATOM   2844  O   ASP A 384     202.644 151.550 155.108  1.00 77.64           O  
ATOM   2845  CB  ASP A 384     201.228 148.961 155.200  1.00 77.64           C  
ATOM   2846  CG  ASP A 384     202.223 148.060 154.490  1.00 77.64           C  
ATOM   2847  OD1 ASP A 384     203.369 147.926 154.969  1.00 77.64           O  
ATOM   2848  OD2 ASP A 384     201.857 147.484 153.444  1.00 77.64           O  
ATOM   2849  N   PRO A 385     204.134 150.580 156.470  1.00 71.08           N  
ATOM   2850  CA  PRO A 385     205.218 151.445 155.981  1.00 71.08           C  
ATOM   2851  C   PRO A 385     205.799 151.005 154.645  1.00 71.08           C  
ATOM   2852  O   PRO A 385     206.223 151.842 153.842  1.00 71.08           O  
ATOM   2853  CB  PRO A 385     206.271 151.342 157.091  1.00 71.08           C  
ATOM   2854  CG  PRO A 385     205.513 150.913 158.303  1.00 71.08           C  
ATOM   2855  CD  PRO A 385     204.450 149.994 157.782  1.00 71.08           C  
ATOM   2856  N   ASN A 386     205.826 149.697 154.398  1.00 73.50           N  
ATOM   2857  CA  ASN A 386     206.668 149.119 153.357  1.00 73.50           C  
ATOM   2858  C   ASN A 386     206.131 149.319 151.942  1.00 73.50           C  
ATOM   2859  O   ASN A 386     206.723 148.783 151.000  1.00 73.50           O  
ATOM   2860  CB  ASN A 386     206.876 147.625 153.619  1.00 73.50           C  
ATOM   2861  CG  ASN A 386     207.672 147.362 154.882  1.00 73.50           C  
ATOM   2862  OD1 ASN A 386     207.178 146.743 155.823  1.00 73.50           O  
ATOM   2863  ND2 ASN A 386     208.910 147.840 154.910  1.00 73.50           N  
ATOM   2864  N   LEU A 387     205.043 150.062 151.758  1.00 70.35           N  
ATOM   2865  CA  LEU A 387     204.626 150.492 150.433  1.00 70.35           C  
ATOM   2866  C   LEU A 387     204.710 152.010 150.333  1.00 70.35           C  
ATOM   2867  O   LEU A 387     204.756 152.719 151.342  1.00 70.35           O  
ATOM   2868  CB  LEU A 387     203.205 150.010 150.104  1.00 70.35           C  
ATOM   2869  CG  LEU A 387     202.004 150.817 150.599  1.00 70.35           C  
ATOM   2870  CD1 LEU A 387     200.741 150.336 149.902  1.00 70.35           C  
ATOM   2871  CD2 LEU A 387     201.851 150.719 152.104  1.00 70.35           C  
ATOM   2872  N   SER A 388     204.731 152.504 149.099  1.00 74.51           N  
ATOM   2873  CA  SER A 388     205.072 153.897 148.863  1.00 74.51           C  
ATOM   2874  C   SER A 388     203.855 154.796 149.063  1.00 74.51           C  
ATOM   2875  O   SER A 388     202.705 154.349 149.049  1.00 74.51           O  
ATOM   2876  CB  SER A 388     205.634 154.079 147.452  1.00 74.51           C  
ATOM   2877  OG  SER A 388     205.953 155.437 147.203  1.00 74.51           O  
ATOM   2878  N   ILE A 389     204.128 156.088 149.252  1.00 73.80           N  
ATOM   2879  CA  ILE A 389     203.090 157.104 149.138  1.00 73.80           C  
ATOM   2880  C   ILE A 389     202.594 157.170 147.700  1.00 73.80           C  
ATOM   2881  O   ILE A 389     203.387 157.100 146.753  1.00 73.80           O  
ATOM   2882  CB  ILE A 389     203.628 158.466 149.613  1.00 73.80           C  
ATOM   2883  CG1 ILE A 389     204.057 158.385 151.078  1.00 73.80           C  
ATOM   2884  CG2 ILE A 389     202.585 159.560 149.437  1.00 73.80           C  
ATOM   2885  CD1 ILE A 389     204.790 159.610 151.565  1.00 73.80           C  
ATOM   2886  N   ASP A 390     201.281 157.375 147.550  1.00 79.82           N  
ATOM   2887  CA  ASP A 390     200.389 157.343 146.373  1.00 79.82           C  
ATOM   2888  C   ASP A 390     199.868 155.937 146.099  1.00 79.82           C  
ATOM   2889  O   ASP A 390     199.055 155.772 145.184  1.00 79.82           O  
ATOM   2890  CB  ASP A 390     201.005 157.902 145.069  1.00 79.82           C  
ATOM   2891  CG  ASP A 390     201.938 156.915 144.340  1.00 79.82           C  
ATOM   2892  OD1 ASP A 390     202.276 155.827 144.855  1.00 79.82           O  
ATOM   2893  OD2 ASP A 390     202.340 157.245 143.207  1.00 79.82           O  
ATOM   2894  N   GLU A 391     200.298 154.926 146.849  1.00 80.56           N  
ATOM   2895  CA  GLU A 391     199.787 153.570 146.700  1.00 80.56           C  
ATOM   2896  C   GLU A 391     199.079 153.159 147.981  1.00 80.56           C  
ATOM   2897  O   GLU A 391     199.675 153.197 149.063  1.00 80.56           O  
ATOM   2898  CB  GLU A 391     200.919 152.593 146.375  1.00 80.56           C  
ATOM   2899  CG  GLU A 391     201.424 152.676 144.943  1.00 80.56           C  
ATOM   2900  CD  GLU A 391     202.544 151.694 144.664  1.00 80.56           C  
ATOM   2901  OE1 GLU A 391     203.071 151.104 145.631  1.00 80.56           O  
ATOM   2902  OE2 GLU A 391     202.897 151.511 143.480  1.00 80.56           O  
ATOM   2903  N   VAL A 392     197.811 152.781 147.857  1.00 68.90           N  
ATOM   2904  CA  VAL A 392     197.053 152.177 148.945  1.00 68.90           C  
ATOM   2905  C   VAL A 392     196.893 150.695 148.636  1.00 68.90           C  
ATOM   2906  O   VAL A 392     196.822 150.290 147.469  1.00 68.90           O  
ATOM   2907  CB  VAL A 392     195.685 152.869 149.144  1.00 68.90           C  
ATOM   2908  CG1 VAL A 392     194.767 152.616 147.955  1.00 68.90           C  
ATOM   2909  CG2 VAL A 392     195.033 152.421 150.445  1.00 68.90           C  
ATOM   2910  N   ALA A 393     196.857 149.877 149.684  1.00 65.64           N  
ATOM   2911  CA  ALA A 393     196.656 148.447 149.511  1.00 65.64           C  
ATOM   2912  C   ALA A 393     195.179 148.113 149.658  1.00 65.64           C  
ATOM   2913  O   ALA A 393     194.500 148.624 150.553  1.00 65.64           O  
ATOM   2914  CB  ALA A 393     197.482 147.651 150.522  1.00 65.64           C  
ATOM   2915  N   VAL A 394     194.686 147.252 148.774  1.00 66.77           N  
ATOM   2916  CA  VAL A 394     193.287 146.850 148.746  1.00 66.77           C  
ATOM   2917  C   VAL A 394     193.226 145.341 148.936  1.00 66.77           C  
ATOM   2918  O   VAL A 394     193.941 144.614 148.243  1.00 66.77           O  
ATOM   2919  CB  VAL A 394     192.590 147.253 147.433  1.00 66.77           C  
ATOM   2920  CG1 VAL A 394     191.184 146.681 147.374  1.00 66.77           C  
ATOM   2921  CG2 VAL A 394     192.563 148.768 147.292  1.00 66.77           C  
ATOM   2922  N   PRO A 395     192.408 144.830 149.852  1.00 64.93           N  
ATOM   2923  CA  PRO A 395     192.272 143.377 149.987  1.00 64.93           C  
ATOM   2924  C   PRO A 395     191.594 142.778 148.765  1.00 64.93           C  
ATOM   2925  O   PRO A 395     190.866 143.449 148.030  1.00 64.93           O  
ATOM   2926  CB  PRO A 395     191.404 143.213 151.239  1.00 64.93           C  
ATOM   2927  CG  PRO A 395     190.695 144.515 151.388  1.00 64.93           C  
ATOM   2928  CD  PRO A 395     191.635 145.557 150.871  1.00 64.93           C  
ATOM   2929  N   ASP A 396     191.846 141.487 148.549  1.00 69.90           N  
ATOM   2930  CA  ASP A 396     191.397 140.867 147.310  1.00 69.90           C  
ATOM   2931  C   ASP A 396     189.923 140.485 147.338  1.00 69.90           C  
ATOM   2932  O   ASP A 396     189.303 140.396 146.273  1.00 69.90           O  
ATOM   2933  CB  ASP A 396     192.246 139.630 147.005  1.00 69.90           C  
ATOM   2934  CG  ASP A 396     192.292 138.653 148.163  1.00 69.90           C  
ATOM   2935  OD1 ASP A 396     191.749 138.975 149.241  1.00 69.90           O  
ATOM   2936  OD2 ASP A 396     192.873 137.560 147.996  1.00 69.90           O  
ATOM   2937  N   ARG A 397     189.347 140.257 148.522  1.00 65.02           N  
ATOM   2938  CA  ARG A 397     187.953 139.836 148.590  1.00 65.02           C  
ATOM   2939  C   ARG A 397     186.985 140.976 148.300  1.00 65.02           C  
ATOM   2940  O   ARG A 397     185.822 140.717 147.969  1.00 65.02           O  
ATOM   2941  CB  ARG A 397     187.657 139.228 149.960  1.00 65.02           C  
ATOM   2942  CG  ARG A 397     188.434 137.952 150.243  1.00 65.02           C  
ATOM   2943  CD  ARG A 397     188.138 137.420 151.633  1.00 65.02           C  
ATOM   2944  NE  ARG A 397     188.941 136.244 151.953  1.00 65.02           N  
ATOM   2945  CZ  ARG A 397     190.151 136.291 152.500  1.00 65.02           C  
ATOM   2946  NH1 ARG A 397     190.711 137.460 152.779  1.00 65.02           N  
ATOM   2947  NH2 ARG A 397     190.808 135.168 152.757  1.00 65.02           N  
ATOM   2948  N   VAL A 398     187.435 142.225 148.417  1.00 64.90           N  
ATOM   2949  CA  VAL A 398     186.704 143.359 147.864  1.00 64.90           C  
ATOM   2950  C   VAL A 398     187.174 143.709 146.455  1.00 64.90           C  
ATOM   2951  O   VAL A 398     186.413 144.320 145.690  1.00 64.90           O  
ATOM   2952  CB  VAL A 398     186.812 144.582 148.796  1.00 64.90           C  
ATOM   2953  CG1 VAL A 398     188.229 145.123 148.818  1.00 64.90           C  
ATOM   2954  CG2 VAL A 398     185.811 145.664 148.404  1.00 64.90           C  
ATOM   2955  N   ALA A 399     188.393 143.316 146.080  1.00 69.41           N  
ATOM   2956  CA  ALA A 399     188.926 143.650 144.767  1.00 69.41           C  
ATOM   2957  C   ALA A 399     188.316 142.819 143.648  1.00 69.41           C  
ATOM   2958  O   ALA A 399     188.316 143.269 142.497  1.00 69.41           O  
ATOM   2959  CB  ALA A 399     190.446 143.483 144.757  1.00 69.41           C  
ATOM   2960  N   LYS A 400     187.800 141.626 143.944  1.00 71.19           N  
ATOM   2961  CA  LYS A 400     187.087 140.847 142.942  1.00 71.19           C  
ATOM   2962  C   LYS A 400     185.580 141.063 143.018  1.00 71.19           C  
ATOM   2963  O   LYS A 400     184.810 140.202 142.579  1.00 71.19           O  
ATOM   2964  CB  LYS A 400     187.418 139.359 143.076  1.00 71.19           C  
ATOM   2965  CG  LYS A 400     187.025 138.728 144.403  1.00 71.19           C  
ATOM   2966  CD  LYS A 400     187.381 137.248 144.418  1.00 71.19           C  
ATOM   2967  CE  LYS A 400     186.982 136.579 145.723  1.00 71.19           C  
ATOM   2968  NZ  LYS A 400     187.811 137.038 146.869  1.00 71.19           N  
ATOM   2969  N   VAL A 401     185.150 142.201 143.564  1.00 63.04           N  
ATOM   2970  CA  VAL A 401     183.758 142.632 143.536  1.00 63.04           C  
ATOM   2971  C   VAL A 401     183.615 143.996 142.870  1.00 63.04           C  
ATOM   2972  O   VAL A 401     182.807 144.173 141.954  1.00 63.04           O  
ATOM   2973  CB  VAL A 401     183.145 142.651 144.955  1.00 63.04           C  
ATOM   2974  CG1 VAL A 401     181.727 143.198 144.913  1.00 63.04           C  
ATOM   2975  CG2 VAL A 401     183.169 141.258 145.563  1.00 63.04           C  
ATOM   2976  N   LEU A 402     184.400 144.974 143.320  1.00 69.80           N  
ATOM   2977  CA  LEU A 402     184.410 146.304 142.719  1.00 69.80           C  
ATOM   2978  C   LEU A 402     185.076 146.238 141.350  1.00 69.80           C  
ATOM   2979  O   LEU A 402     186.287 146.015 141.250  1.00 69.80           O  
ATOM   2980  CB  LEU A 402     185.141 147.283 143.632  1.00 69.80           C  
ATOM   2981  CG  LEU A 402     184.513 147.530 145.005  1.00 69.80           C  
ATOM   2982  CD1 LEU A 402     185.399 148.434 145.850  1.00 69.80           C  
ATOM   2983  CD2 LEU A 402     183.117 148.110 144.870  1.00 69.80           C  
ATOM   2984  N   THR A 403     184.292 146.432 140.295  1.00 80.00           N  
ATOM   2985  CA  THR A 403     184.779 146.307 138.931  1.00 80.00           C  
ATOM   2986  C   THR A 403     184.990 147.681 138.302  1.00 80.00           C  
ATOM   2987  O   THR A 403     184.641 148.719 138.868  1.00 80.00           O  
ATOM   2988  CB  THR A 403     183.804 145.483 138.085  1.00 80.00           C  
ATOM   2989  OG1 THR A 403     184.401 145.196 136.815  1.00 80.00           O  
ATOM   2990  CG2 THR A 403     182.508 146.249 137.868  1.00 80.00           C  
ATOM   2991  N   TYR A 404     185.575 147.670 137.102  1.00 80.17           N  
ATOM   2992  CA  TYR A 404     185.840 148.877 136.340  1.00 80.17           C  
ATOM   2993  C   TYR A 404     185.676 148.581 134.855  1.00 80.17           C  
ATOM   2994  O   TYR A 404     186.312 147.640 134.352  1.00 80.17           O  
ATOM   2995  CB  TYR A 404     187.248 149.405 136.617  1.00 80.17           C  
ATOM   2996  CG  TYR A 404     187.619 150.636 135.825  1.00 80.17           C  
ATOM   2997  CD1 TYR A 404     187.060 151.872 136.118  1.00 80.17           C  
ATOM   2998  CD2 TYR A 404     188.537 150.562 134.785  1.00 80.17           C  
ATOM   2999  CE1 TYR A 404     187.402 152.999 135.394  1.00 80.17           C  
ATOM   3000  CE2 TYR A 404     188.885 151.682 134.057  1.00 80.17           C  
ATOM   3001  CZ  TYR A 404     188.315 152.898 134.366  1.00 80.17           C  
ATOM   3002  OH  TYR A 404     188.660 154.016 133.642  1.00 80.17           O  
ATOM   3003  N   PRO A 405     184.850 149.340 134.139  1.00 80.83           N  
ATOM   3004  CA  PRO A 405     184.593 149.022 132.731  1.00 80.83           C  
ATOM   3005  C   PRO A 405     185.811 149.297 131.862  1.00 80.83           C  
ATOM   3006  O   PRO A 405     186.692 150.089 132.204  1.00 80.83           O  
ATOM   3007  CB  PRO A 405     183.433 149.954 132.363  1.00 80.83           C  
ATOM   3008  CG  PRO A 405     182.780 150.278 133.671  1.00 80.83           C  
ATOM   3009  CD  PRO A 405     183.913 150.352 134.653  1.00 80.83           C  
ATOM   3010  N   GLU A 406     185.848 148.621 130.715  1.00 98.30           N  
ATOM   3011  CA  GLU A 406     187.049 148.605 129.882  1.00 98.30           C  
ATOM   3012  C   GLU A 406     186.635 148.291 128.450  1.00 98.30           C  
ATOM   3013  O   GLU A 406     186.256 147.154 128.154  1.00 98.30           O  
ATOM   3014  CB  GLU A 406     188.056 147.585 130.401  1.00 98.30           C  
ATOM   3015  CG  GLU A 406     189.358 147.549 129.619  1.00 98.30           C  
ATOM   3016  CD  GLU A 406     190.216 148.777 129.855  1.00 98.30           C  
ATOM   3017  OE1 GLU A 406     190.124 149.367 130.952  1.00 98.30           O  
ATOM   3018  OE2 GLU A 406     190.982 149.152 128.943  1.00 98.30           O  
ATOM   3019  N   LYS A 407     186.707 149.288 127.571  1.00101.55           N  
ATOM   3020  CA  LYS A 407     186.456 149.046 126.157  1.00101.55           C  
ATOM   3021  C   LYS A 407     187.626 148.296 125.531  1.00101.55           C  
ATOM   3022  O   LYS A 407     188.791 148.549 125.850  1.00101.55           O  
ATOM   3023  CB  LYS A 407     186.220 150.366 125.423  1.00101.55           C  
ATOM   3024  CG  LYS A 407     184.915 151.055 125.790  1.00101.55           C  
ATOM   3025  CD  LYS A 407     184.747 152.362 125.030  1.00101.55           C  
ATOM   3026  CE  LYS A 407     184.446 152.114 123.560  1.00101.55           C  
ATOM   3027  NZ  LYS A 407     183.118 151.471 123.362  1.00101.55           N  
ATOM   3028  N   VAL A 408     187.308 147.366 124.636  1.00104.19           N  
ATOM   3029  CA  VAL A 408     188.327 146.599 123.928  1.00104.19           C  
ATOM   3030  C   VAL A 408     188.913 147.443 122.804  1.00104.19           C  
ATOM   3031  O   VAL A 408     188.193 148.172 122.110  1.00104.19           O  
ATOM   3032  CB  VAL A 408     187.727 145.286 123.391  1.00104.19           C  
ATOM   3033  CG1 VAL A 408     188.759 144.504 122.590  1.00104.19           C  
ATOM   3034  CG2 VAL A 408     187.178 144.447 124.534  1.00104.19           C  
ATOM   3035  N   THR A 409     190.230 147.350 122.621  1.00101.95           N  
ATOM   3036  CA  THR A 409     190.915 148.005 121.515  1.00101.95           C  
ATOM   3037  C   THR A 409     191.894 146.999 120.917  1.00101.95           C  
ATOM   3038  O   THR A 409     192.114 145.918 121.470  1.00101.95           O  
ATOM   3039  CB  THR A 409     191.625 149.285 121.989  1.00101.95           C  
ATOM   3040  OG1 THR A 409     190.760 150.003 122.876  1.00101.95           O  
ATOM   3041  CG2 THR A 409     191.950 150.199 120.814  1.00101.95           C  
ATOM   3042  N   ARG A 410     192.490 147.353 119.774  1.00 99.72           N  
ATOM   3043  CA  ARG A 410     193.555 146.527 119.213  1.00 99.72           C  
ATOM   3044  C   ARG A 410     194.800 146.497 120.092  1.00 99.72           C  
ATOM   3045  O   ARG A 410     195.633 145.599 119.931  1.00 99.72           O  
ATOM   3046  CB  ARG A 410     193.933 147.000 117.806  1.00 99.72           C  
ATOM   3047  CG  ARG A 410     194.846 148.216 117.760  1.00 99.72           C  
ATOM   3048  CD  ARG A 410     194.070 149.514 117.876  1.00 99.72           C  
ATOM   3049  NE  ARG A 410     193.201 149.725 116.723  1.00 99.72           N  
ATOM   3050  CZ  ARG A 410     193.578 150.344 115.608  1.00 99.72           C  
ATOM   3051  NH1 ARG A 410     194.805 150.837 115.504  1.00 99.72           N  
ATOM   3052  NH2 ARG A 410     192.723 150.490 114.606  1.00 99.72           N  
ATOM   3053  N   TYR A 411     194.949 147.453 121.011  1.00100.68           N  
ATOM   3054  CA  TYR A 411     196.115 147.465 121.888  1.00100.68           C  
ATOM   3055  C   TYR A 411     195.962 146.481 123.041  1.00100.68           C  
ATOM   3056  O   TYR A 411     196.932 145.822 123.431  1.00100.68           O  
ATOM   3057  CB  TYR A 411     196.358 148.880 122.413  1.00100.68           C  
ATOM   3058  CG  TYR A 411     196.439 149.916 121.316  1.00100.68           C  
ATOM   3059  CD1 TYR A 411     197.530 149.965 120.459  1.00100.68           C  
ATOM   3060  CD2 TYR A 411     195.423 150.846 121.136  1.00100.68           C  
ATOM   3061  CE1 TYR A 411     197.605 150.907 119.451  1.00100.68           C  
ATOM   3062  CE2 TYR A 411     195.490 151.794 120.133  1.00100.68           C  
ATOM   3063  CZ  TYR A 411     196.583 151.819 119.293  1.00100.68           C  
ATOM   3064  OH  TYR A 411     196.654 152.761 118.293  1.00100.68           O  
ATOM   3065  N   ASN A 412     194.755 146.368 123.598  1.00 99.33           N  
ATOM   3066  CA  ASN A 412     194.516 145.594 124.809  1.00 99.33           C  
ATOM   3067  C   ASN A 412     193.712 144.329 124.530  1.00 99.33           C  
ATOM   3068  O   ASN A 412     193.185 143.712 125.461  1.00 99.33           O  
ATOM   3069  CB  ASN A 412     193.816 146.456 125.863  1.00 99.33           C  
ATOM   3070  CG  ASN A 412     192.508 147.046 125.367  1.00 99.33           C  
ATOM   3071  OD1 ASN A 412     192.041 146.730 124.273  1.00 99.33           O  
ATOM   3072  ND2 ASN A 412     191.908 147.911 126.177  1.00 99.33           N  
ATOM   3073  N   ARG A 413     193.608 143.933 123.259  1.00 98.83           N  
ATOM   3074  CA  ARG A 413     192.883 142.714 122.916  1.00 98.83           C  
ATOM   3075  C   ARG A 413     193.602 141.477 123.438  1.00 98.83           C  
ATOM   3076  O   ARG A 413     192.959 140.510 123.861  1.00 98.83           O  
ATOM   3077  CB  ARG A 413     192.701 142.632 121.400  1.00 98.83           C  
ATOM   3078  CG  ARG A 413     191.844 141.473 120.918  1.00 98.83           C  
ATOM   3079  CD  ARG A 413     191.684 141.517 119.405  1.00 98.83           C  
ATOM   3080  NE  ARG A 413     190.935 140.376 118.887  1.00 98.83           N  
ATOM   3081  CZ  ARG A 413     189.613 140.351 118.750  1.00 98.83           C  
ATOM   3082  NH1 ARG A 413     188.888 141.404 119.099  1.00 98.83           N  
ATOM   3083  NH2 ARG A 413     189.015 139.269 118.271  1.00 98.83           N  
ATOM   3084  N   HIS A 414     194.937 141.489 123.414  1.00101.56           N  
ATOM   3085  CA  HIS A 414     195.699 140.317 123.834  1.00101.56           C  
ATOM   3086  C   HIS A 414     195.533 140.048 125.326  1.00101.56           C  
ATOM   3087  O   HIS A 414     195.414 138.890 125.743  1.00101.56           O  
ATOM   3088  CB  HIS A 414     197.175 140.501 123.482  1.00101.56           C  
ATOM   3089  CG  HIS A 414     198.010 139.281 123.716  1.00101.56           C  
ATOM   3090  ND1 HIS A 414     199.378 139.335 123.876  1.00101.56           N  
ATOM   3091  CD2 HIS A 414     197.673 137.973 123.809  1.00101.56           C  
ATOM   3092  CE1 HIS A 414     199.847 138.114 124.062  1.00101.56           C  
ATOM   3093  NE2 HIS A 414     198.833 137.269 124.026  1.00101.56           N  
ATOM   3094  N   LYS A 415     195.520 141.103 126.144  1.00 98.70           N  
ATOM   3095  CA  LYS A 415     195.425 140.912 127.589  1.00 98.70           C  
ATOM   3096  C   LYS A 415     194.023 140.489 128.007  1.00 98.70           C  
ATOM   3097  O   LYS A 415     193.863 139.633 128.885  1.00 98.70           O  
ATOM   3098  CB  LYS A 415     195.839 142.193 128.314  1.00 98.70           C  
ATOM   3099  CG  LYS A 415     195.816 142.085 129.830  1.00 98.70           C  
ATOM   3100  CD  LYS A 415     196.875 141.118 130.335  1.00 98.70           C  
ATOM   3101  CE  LYS A 415     196.900 141.071 131.854  1.00 98.70           C  
ATOM   3102  NZ  LYS A 415     197.887 140.079 132.364  1.00 98.70           N  
ATOM   3103  N   LEU A 416     192.993 141.075 127.392  1.00 95.81           N  
ATOM   3104  CA  LEU A 416     191.623 140.782 127.799  1.00 95.81           C  
ATOM   3105  C   LEU A 416     191.182 139.379 127.404  1.00 95.81           C  
ATOM   3106  O   LEU A 416     190.268 138.834 128.032  1.00 95.81           O  
ATOM   3107  CB  LEU A 416     190.661 141.821 127.217  1.00 95.81           C  
ATOM   3108  CG  LEU A 416     190.393 143.062 128.076  1.00 95.81           C  
ATOM   3109  CD1 LEU A 416     191.653 143.888 128.297  1.00 95.81           C  
ATOM   3110  CD2 LEU A 416     189.294 143.915 127.462  1.00 95.81           C  
ATOM   3111  N   GLN A 417     191.799 138.784 126.380  1.00103.66           N  
ATOM   3112  CA  GLN A 417     191.515 137.388 126.064  1.00103.66           C  
ATOM   3113  C   GLN A 417     191.987 136.467 127.182  1.00103.66           C  
ATOM   3114  O   GLN A 417     191.263 135.557 127.601  1.00103.66           O  
ATOM   3115  CB  GLN A 417     192.177 137.003 124.740  1.00103.66           C  
ATOM   3116  CG  GLN A 417     191.543 137.629 123.510  1.00103.66           C  
ATOM   3117  CD  GLN A 417     192.280 137.277 122.233  1.00103.66           C  
ATOM   3118  OE1 GLN A 417     193.319 136.618 122.263  1.00103.66           O  
ATOM   3119  NE2 GLN A 417     191.742 137.715 121.100  1.00103.66           N  
ATOM   3120  N   GLU A 418     193.206 136.691 127.678  1.00102.71           N  
ATOM   3121  CA  GLU A 418     193.688 135.947 128.836  1.00102.71           C  
ATOM   3122  C   GLU A 418     192.914 136.301 130.101  1.00102.71           C  
ATOM   3123  O   GLU A 418     192.791 135.465 131.003  1.00102.71           O  
ATOM   3124  CB  GLU A 418     195.183 136.205 129.032  1.00102.71           C  
ATOM   3125  CG  GLU A 418     195.872 135.267 130.014  1.00102.71           C  
ATOM   3126  CD  GLU A 418     195.818 135.771 131.444  1.00102.71           C  
ATOM   3127  OE1 GLU A 418     195.747 137.003 131.638  1.00102.71           O  
ATOM   3128  OE2 GLU A 418     195.848 134.936 132.372  1.00102.71           O  
ATOM   3129  N   LEU A 419     192.380 137.521 130.184  1.00 94.72           N  
ATOM   3130  CA  LEU A 419     191.646 137.922 131.378  1.00 94.72           C  
ATOM   3131  C   LEU A 419     190.254 137.306 131.442  1.00 94.72           C  
ATOM   3132  O   LEU A 419     189.766 137.010 132.538  1.00 94.72           O  
ATOM   3133  CB  LEU A 419     191.552 139.450 131.442  1.00 94.72           C  
ATOM   3134  CG  LEU A 419     190.937 140.089 132.690  1.00 94.72           C  
ATOM   3135  CD1 LEU A 419     191.705 141.343 133.074  1.00 94.72           C  
ATOM   3136  CD2 LEU A 419     189.466 140.418 132.472  1.00 94.72           C  
ATOM   3137  N   ILE A 420     189.602 137.101 130.296  1.00 93.73           N  
ATOM   3138  CA  ILE A 420     188.220 136.632 130.321  1.00 93.73           C  
ATOM   3139  C   ILE A 420     188.127 135.128 130.555  1.00 93.73           C  
ATOM   3140  O   ILE A 420     187.073 134.637 130.980  1.00 93.73           O  
ATOM   3141  CB  ILE A 420     187.502 137.030 129.019  1.00 93.73           C  
ATOM   3142  CG1 ILE A 420     185.984 136.910 129.174  1.00 93.73           C  
ATOM   3143  CG2 ILE A 420     187.997 136.189 127.851  1.00 93.73           C  
ATOM   3144  CD1 ILE A 420     185.394 137.887 130.167  1.00 93.73           C  
ATOM   3145  N   VAL A 421     189.207 134.379 130.307  1.00 92.22           N  
ATOM   3146  CA  VAL A 421     189.208 132.943 130.578  1.00 92.22           C  
ATOM   3147  C   VAL A 421     189.422 132.633 132.050  1.00 92.22           C  
ATOM   3148  O   VAL A 421     189.210 131.489 132.474  1.00 92.22           O  
ATOM   3149  CB  VAL A 421     190.283 132.240 129.725  1.00 92.22           C  
ATOM   3150  CG1 VAL A 421     191.667 132.441 130.328  1.00 92.22           C  
ATOM   3151  CG2 VAL A 421     189.960 130.760 129.545  1.00 92.22           C  
ATOM   3152  N   ASN A 422     189.823 133.626 132.847  1.00 86.93           N  
ATOM   3153  CA  ASN A 422     189.965 133.420 134.285  1.00 86.93           C  
ATOM   3154  C   ASN A 422     188.614 133.207 134.955  1.00 86.93           C  
ATOM   3155  O   ASN A 422     188.484 132.363 135.850  1.00 86.93           O  
ATOM   3156  CB  ASN A 422     190.691 134.611 134.908  1.00 86.93           C  
ATOM   3157  CG  ASN A 422     192.155 134.670 134.522  1.00 86.93           C  
ATOM   3158  OD1 ASN A 422     192.603 135.620 133.880  1.00 86.93           O  
ATOM   3159  ND2 ASN A 422     192.911 133.650 134.912  1.00 86.93           N  
ATOM   3160  N   GLY A 423     187.601 133.959 134.538  1.00 81.56           N  
ATOM   3161  CA  GLY A 423     186.296 133.904 135.151  1.00 81.56           C  
ATOM   3162  C   GLY A 423     186.245 134.669 136.458  1.00 81.56           C  
ATOM   3163  O   GLY A 423     187.248 135.221 136.922  1.00 81.56           O  
ATOM   3164  N   PRO A 424     185.060 134.717 137.083  1.00 81.49           N  
ATOM   3165  CA  PRO A 424     184.896 135.397 138.374  1.00 81.49           C  
ATOM   3166  C   PRO A 424     185.185 134.508 139.584  1.00 81.49           C  
ATOM   3167  O   PRO A 424     184.396 134.438 140.533  1.00 81.49           O  
ATOM   3168  CB  PRO A 424     183.428 135.831 138.340  1.00 81.49           C  
ATOM   3169  CG  PRO A 424     182.766 134.788 137.514  1.00 81.49           C  
ATOM   3170  CD  PRO A 424     183.765 134.388 136.464  1.00 81.49           C  
ATOM   3171  N   ASN A 425     186.319 133.820 139.564  1.00 79.58           N  
ATOM   3172  CA  ASN A 425     186.710 133.090 140.766  1.00 79.58           C  
ATOM   3173  C   ASN A 425     188.135 133.382 141.211  1.00 79.58           C  
ATOM   3174  O   ASN A 425     188.375 133.543 142.410  1.00 79.58           O  
ATOM   3175  CB  ASN A 425     186.537 131.579 140.538  1.00 79.58           C  
ATOM   3176  CG  ASN A 425     185.086 131.180 140.355  1.00 79.58           C  
ATOM   3177  OD1 ASN A 425     184.691 130.697 139.294  1.00 79.58           O  
ATOM   3178  ND2 ASN A 425     184.283 131.380 141.394  1.00 79.58           N  
ATOM   3179  N   VAL A 426     189.084 133.455 140.280  1.00 81.43           N  
ATOM   3180  CA  VAL A 426     190.436 133.911 140.583  1.00 81.43           C  
ATOM   3181  C   VAL A 426     190.480 135.428 140.465  1.00 81.43           C  
ATOM   3182  O   VAL A 426     189.546 136.047 139.944  1.00 81.43           O  
ATOM   3183  CB  VAL A 426     191.480 133.246 139.668  1.00 81.43           C  
ATOM   3184  CG1 VAL A 426     191.463 131.735 139.856  1.00 81.43           C  
ATOM   3185  CG2 VAL A 426     191.222 133.609 138.224  1.00 81.43           C  
ATOM   3186  N   HIS A 427     191.566 136.039 140.957  1.00 82.47           N  
ATOM   3187  CA  HIS A 427     191.576 137.495 141.111  1.00 82.47           C  
ATOM   3188  C   HIS A 427     191.586 138.214 139.767  1.00 82.47           C  
ATOM   3189  O   HIS A 427     190.671 139.015 139.508  1.00 82.47           O  
ATOM   3190  CB  HIS A 427     192.743 137.920 142.007  1.00 82.47           C  
ATOM   3191  CG  HIS A 427     192.925 139.404 142.091  1.00 82.47           C  
ATOM   3192  ND1 HIS A 427     193.729 140.105 141.219  1.00 82.47           N  
ATOM   3193  CD2 HIS A 427     192.402 140.320 142.940  1.00 82.47           C  
ATOM   3194  CE1 HIS A 427     193.696 141.389 141.528  1.00 82.47           C  
ATOM   3195  NE2 HIS A 427     192.897 141.546 142.568  1.00 82.47           N  
ATOM   3196  N   PRO A 428     192.568 137.993 138.869  1.00 83.28           N  
ATOM   3197  CA  PRO A 428     192.628 138.886 137.690  1.00 83.28           C  
ATOM   3198  C   PRO A 428     191.702 138.443 136.562  1.00 83.28           C  
ATOM   3199  O   PRO A 428     192.118 137.953 135.506  1.00 83.28           O  
ATOM   3200  CB  PRO A 428     194.107 138.806 137.301  1.00 83.28           C  
ATOM   3201  CG  PRO A 428     194.492 137.409 137.657  1.00 83.28           C  
ATOM   3202  CD  PRO A 428     193.675 137.017 138.866  1.00 83.28           C  
ATOM   3203  N   GLY A 429     190.402 138.618 136.784  1.00 84.23           N  
ATOM   3204  CA  GLY A 429     189.399 138.170 135.838  1.00 84.23           C  
ATOM   3205  C   GLY A 429     188.291 139.189 135.671  1.00 84.23           C  
ATOM   3206  O   GLY A 429     188.482 140.370 135.976  1.00 84.23           O  
ATOM   3207  N   ALA A 430     187.131 138.753 135.187  1.00 84.77           N  
ATOM   3208  CA  ALA A 430     186.007 139.643 134.940  1.00 84.77           C  
ATOM   3209  C   ALA A 430     184.759 139.082 135.610  1.00 84.77           C  
ATOM   3210  O   ALA A 430     184.725 137.930 136.052  1.00 84.77           O  
ATOM   3211  CB  ALA A 430     185.766 139.839 133.437  1.00 84.77           C  
ATOM   3212  N   ASN A 431     183.721 139.915 135.682  1.00 84.60           N  
ATOM   3213  CA  ASN A 431     182.446 139.529 136.276  1.00 84.60           C  
ATOM   3214  C   ASN A 431     181.315 139.555 135.262  1.00 84.60           C  
ATOM   3215  O   ASN A 431     180.523 138.608 135.193  1.00 84.60           O  
ATOM   3216  CB  ASN A 431     182.099 140.450 137.458  1.00 84.60           C  
ATOM   3217  CG  ASN A 431     182.987 140.217 138.662  1.00 84.60           C  
ATOM   3218  OD1 ASN A 431     183.285 139.078 139.018  1.00 84.60           O  
ATOM   3219  ND2 ASN A 431     183.401 141.301 139.307  1.00 84.60           N  
ATOM   3220  N   TYR A 432     181.222 140.621 134.473  1.00 91.50           N  
ATOM   3221  CA  TYR A 432     180.147 140.824 133.516  1.00 91.50           C  
ATOM   3222  C   TYR A 432     180.756 141.096 132.147  1.00 91.50           C  
ATOM   3223  O   TYR A 432     181.958 141.337 132.014  1.00 91.50           O  
ATOM   3224  CB  TYR A 432     179.229 141.979 133.939  1.00 91.50           C  
ATOM   3225  CG  TYR A 432     178.395 141.677 135.163  1.00 91.50           C  
ATOM   3226  CD1 TYR A 432     177.181 141.012 135.054  1.00 91.50           C  
ATOM   3227  CD2 TYR A 432     178.825 142.054 136.429  1.00 91.50           C  
ATOM   3228  CE1 TYR A 432     176.415 140.736 136.171  1.00 91.50           C  
ATOM   3229  CE2 TYR A 432     178.067 141.780 137.551  1.00 91.50           C  
ATOM   3230  CZ  TYR A 432     176.864 141.122 137.416  1.00 91.50           C  
ATOM   3231  OH  TYR A 432     176.107 140.845 138.531  1.00 91.50           O  
ATOM   3232  N   LEU A 433     179.911 141.058 131.121  1.00 98.80           N  
ATOM   3233  CA  LEU A 433     180.354 141.364 129.770  1.00 98.80           C  
ATOM   3234  C   LEU A 433     179.176 141.913 128.983  1.00 98.80           C  
ATOM   3235  O   LEU A 433     178.029 141.508 129.188  1.00 98.80           O  
ATOM   3236  CB  LEU A 433     180.942 140.123 129.081  1.00 98.80           C  
ATOM   3237  CG  LEU A 433     181.759 140.301 127.797  1.00 98.80           C  
ATOM   3238  CD1 LEU A 433     182.827 139.223 127.703  1.00 98.80           C  
ATOM   3239  CD2 LEU A 433     180.870 140.264 126.562  1.00 98.80           C  
ATOM   3240  N   LEU A 434     179.474 142.840 128.075  1.00109.66           N  
ATOM   3241  CA  LEU A 434     178.456 143.480 127.249  1.00109.66           C  
ATOM   3242  C   LEU A 434     179.011 143.604 125.839  1.00109.66           C  
ATOM   3243  O   LEU A 434     179.904 144.421 125.591  1.00109.66           O  
ATOM   3244  CB  LEU A 434     178.066 144.848 127.816  1.00109.66           C  
ATOM   3245  CG  LEU A 434     176.871 145.602 127.222  1.00109.66           C  
ATOM   3246  CD1 LEU A 434     176.255 146.502 128.279  1.00109.66           C  
ATOM   3247  CD2 LEU A 434     177.270 146.429 126.007  1.00109.66           C  
ATOM   3248  N   LYS A 435     178.488 142.798 124.922  1.00120.54           N  
ATOM   3249  CA  LYS A 435     178.772 142.974 123.508  1.00120.54           C  
ATOM   3250  C   LYS A 435     177.941 144.119 122.945  1.00120.54           C  
ATOM   3251  O   LYS A 435     176.835 144.401 123.414  1.00120.54           O  
ATOM   3252  CB  LYS A 435     178.495 141.687 122.730  1.00120.54           C  
ATOM   3253  CG  LYS A 435     179.506 140.583 122.991  1.00120.54           C  
ATOM   3254  CD  LYS A 435     179.344 139.440 122.003  1.00120.54           C  
ATOM   3255  CE  LYS A 435     178.516 138.315 122.593  1.00120.54           C  
ATOM   3256  NZ  LYS A 435     177.073 138.676 122.645  1.00120.54           N  
ATOM   3257  N   ARG A 436     178.488 144.785 121.926  1.00124.40           N  
ATOM   3258  CA  ARG A 436     177.827 145.970 121.396  1.00124.40           C  
ATOM   3259  C   ARG A 436     176.551 145.620 120.645  1.00124.40           C  
ATOM   3260  O   ARG A 436     175.687 146.488 120.479  1.00124.40           O  
ATOM   3261  CB  ARG A 436     178.782 146.748 120.488  1.00124.40           C  
ATOM   3262  CG  ARG A 436     179.210 146.001 119.236  1.00124.40           C  
ATOM   3263  CD  ARG A 436     180.143 146.852 118.388  1.00124.40           C  
ATOM   3264  NE  ARG A 436     180.584 146.155 117.184  1.00124.40           N  
ATOM   3265  CZ  ARG A 436     181.383 146.687 116.265  1.00124.40           C  
ATOM   3266  NH1 ARG A 436     181.828 147.928 116.409  1.00124.40           N  
ATOM   3267  NH2 ARG A 436     181.735 145.981 115.199  1.00124.40           N  
ATOM   3268  N   ASN A 437     176.411 144.374 120.189  1.00138.92           N  
ATOM   3269  CA  ASN A 437     175.128 143.925 119.664  1.00138.92           C  
ATOM   3270  C   ASN A 437     174.181 143.513 120.784  1.00138.92           C  
ATOM   3271  O   ASN A 437     172.963 143.676 120.651  1.00138.92           O  
ATOM   3272  CB  ASN A 437     175.332 142.765 118.689  1.00138.92           C  
ATOM   3273  CG  ASN A 437     176.247 143.128 117.535  1.00138.92           C  
ATOM   3274  OD1 ASN A 437     177.325 142.556 117.378  1.00138.92           O  
ATOM   3275  ND2 ASN A 437     175.818 144.085 116.719  1.00138.92           N  
ATOM   3276  N   GLU A 438     174.716 142.980 121.881  1.00138.01           N  
ATOM   3277  CA  GLU A 438     173.889 142.605 123.019  1.00138.01           C  
ATOM   3278  C   GLU A 438     173.326 143.859 123.681  1.00138.01           C  
ATOM   3279  O   GLU A 438     173.902 144.946 123.587  1.00138.01           O  
ATOM   3280  CB  GLU A 438     174.707 141.784 124.018  1.00138.01           C  
ATOM   3281  CG  GLU A 438     173.889 141.017 125.045  1.00138.01           C  
ATOM   3282  CD  GLU A 438     173.616 141.831 126.292  1.00138.01           C  
ATOM   3283  OE1 GLU A 438     174.452 142.695 126.628  1.00138.01           O  
ATOM   3284  OE2 GLU A 438     172.567 141.609 126.932  1.00138.01           O  
ATOM   3285  N   ASP A 439     172.187 143.708 124.357  1.00148.83           N  
ATOM   3286  CA  ASP A 439     171.429 144.881 124.773  1.00148.83           C  
ATOM   3287  C   ASP A 439     171.605 145.252 126.241  1.00148.83           C  
ATOM   3288  O   ASP A 439     171.684 146.443 126.558  1.00148.83           O  
ATOM   3289  CB  ASP A 439     169.939 144.666 124.488  1.00148.83           C  
ATOM   3290  CG  ASP A 439     169.162 145.967 124.423  1.00148.83           C  
ATOM   3291  OD1 ASP A 439     169.785 147.043 124.539  1.00148.83           O  
ATOM   3292  OD2 ASP A 439     167.925 145.914 124.259  1.00148.83           O  
ATOM   3293  N   ALA A 440     171.677 144.284 127.157  1.00130.53           N  
ATOM   3294  CA  ALA A 440     171.648 144.594 128.584  1.00130.53           C  
ATOM   3295  C   ALA A 440     172.970 144.296 129.282  1.00130.53           C  
ATOM   3296  O   ALA A 440     173.634 145.223 129.748  1.00130.53           O  
ATOM   3297  CB  ALA A 440     170.498 143.836 129.252  1.00130.53           C  
ATOM   3298  N   ARG A 441     173.376 143.027 129.347  1.00108.25           N  
ATOM   3299  CA  ARG A 441     174.678 142.537 129.800  1.00108.25           C  
ATOM   3300  C   ARG A 441     174.654 141.018 129.670  1.00108.25           C  
ATOM   3301  O   ARG A 441     173.625 140.422 129.338  1.00108.25           O  
ATOM   3302  CB  ARG A 441     175.026 142.921 131.245  1.00108.25           C  
ATOM   3303  CG  ARG A 441     175.876 144.174 131.402  1.00108.25           C  
ATOM   3304  CD  ARG A 441     176.270 144.391 132.853  1.00108.25           C  
ATOM   3305  NE  ARG A 441     175.127 144.750 133.686  1.00108.25           N  
ATOM   3306  CZ  ARG A 441     175.162 144.813 135.013  1.00108.25           C  
ATOM   3307  NH1 ARG A 441     176.285 144.538 135.662  1.00108.25           N  
ATOM   3308  NH2 ARG A 441     174.074 145.148 135.692  1.00108.25           N  
ATOM   3309  N   ARG A 442     175.801 140.398 129.939  1.00 98.20           N  
ATOM   3310  CA  ARG A 442     175.873 138.950 130.070  1.00 98.20           C  
ATOM   3311  C   ARG A 442     176.736 138.591 131.269  1.00 98.20           C  
ATOM   3312  O   ARG A 442     177.793 139.189 131.487  1.00 98.20           O  
ATOM   3313  CB  ARG A 442     176.441 138.283 128.810  1.00 98.20           C  
ATOM   3314  CG  ARG A 442     175.486 138.253 127.633  1.00 98.20           C  
ATOM   3315  CD  ARG A 442     176.071 137.456 126.479  1.00 98.20           C  
ATOM   3316  NE  ARG A 442     175.123 137.305 125.380  1.00 98.20           N  
ATOM   3317  CZ  ARG A 442     175.378 136.636 124.260  1.00 98.20           C  
ATOM   3318  NH1 ARG A 442     176.558 136.056 124.085  1.00 98.20           N  
ATOM   3319  NH2 ARG A 442     174.455 136.550 123.312  1.00 98.20           N  
ATOM   3320  N   ASN A 443     176.277 137.610 132.042  1.00 89.92           N  
ATOM   3321  CA  ASN A 443     177.013 137.143 133.206  1.00 89.92           C  
ATOM   3322  C   ASN A 443     178.067 136.121 132.798  1.00 89.92           C  
ATOM   3323  O   ASN A 443     177.938 135.434 131.780  1.00 89.92           O  
ATOM   3324  CB  ASN A 443     176.055 136.532 134.232  1.00 89.92           C  
ATOM   3325  CG  ASN A 443     176.706 136.313 135.585  1.00 89.92           C  
ATOM   3326  OD1 ASN A 443     177.892 136.587 135.771  1.00 89.92           O  
ATOM   3327  ND2 ASN A 443     175.929 135.815 136.540  1.00 89.92           N  
ATOM   3328  N   LEU A 444     179.123 136.027 133.607  1.00 87.50           N  
ATOM   3329  CA  LEU A 444     180.249 135.156 133.298  1.00 87.50           C  
ATOM   3330  C   LEU A 444     180.187 133.808 134.004  1.00 87.50           C  
ATOM   3331  O   LEU A 444     180.876 132.875 133.578  1.00 87.50           O  
ATOM   3332  CB  LEU A 444     181.572 135.847 133.656  1.00 87.50           C  
ATOM   3333  CG  LEU A 444     182.309 136.541 132.507  1.00 87.50           C  
ATOM   3334  CD1 LEU A 444     182.666 135.539 131.419  1.00 87.50           C  
ATOM   3335  CD2 LEU A 444     181.480 137.681 131.938  1.00 87.50           C  
ATOM   3336  N   ARG A 445     179.386 133.681 135.065  1.00 97.71           N  
ATOM   3337  CA  ARG A 445     179.294 132.404 135.767  1.00 97.71           C  
ATOM   3338  C   ARG A 445     178.559 131.361 134.934  1.00 97.71           C  
ATOM   3339  O   ARG A 445     178.954 130.189 134.909  1.00 97.71           O  
ATOM   3340  CB  ARG A 445     178.605 132.598 137.117  1.00 97.71           C  
ATOM   3341  CG  ARG A 445     179.453 133.330 138.144  1.00 97.71           C  
ATOM   3342  CD  ARG A 445     178.773 133.366 139.502  1.00 97.71           C  
ATOM   3343  NE  ARG A 445     179.586 134.056 140.500  1.00 97.71           N  
ATOM   3344  CZ  ARG A 445     179.507 135.358 140.758  1.00 97.71           C  
ATOM   3345  NH1 ARG A 445     178.641 136.115 140.098  1.00 97.71           N  
ATOM   3346  NH2 ARG A 445     180.286 135.901 141.683  1.00 97.71           N  
ATOM   3347  N   TYR A 446     177.494 131.764 134.249  1.00102.21           N  
ATOM   3348  CA  TYR A 446     176.608 130.835 133.564  1.00102.21           C  
ATOM   3349  C   TYR A 446     176.962 130.789 132.084  1.00102.21           C  
ATOM   3350  O   TYR A 446     177.210 131.827 131.463  1.00102.21           O  
ATOM   3351  CB  TYR A 446     175.143 131.238 133.744  1.00102.21           C  
ATOM   3352  CG  TYR A 446     174.645 131.140 135.171  1.00102.21           C  
ATOM   3353  CD1 TYR A 446     175.322 130.379 136.115  1.00102.21           C  
ATOM   3354  CD2 TYR A 446     173.496 131.811 135.573  1.00102.21           C  
ATOM   3355  CE1 TYR A 446     174.870 130.289 137.419  1.00102.21           C  
ATOM   3356  CE2 TYR A 446     173.037 131.726 136.874  1.00102.21           C  
ATOM   3357  CZ  TYR A 446     173.727 130.964 137.793  1.00102.21           C  
ATOM   3358  OH  TYR A 446     173.274 130.876 139.089  1.00102.21           O  
ATOM   3359  N   GLY A 447     176.984 129.586 131.523  1.00106.34           N  
ATOM   3360  CA  GLY A 447     177.407 129.406 130.152  1.00106.34           C  
ATOM   3361  C   GLY A 447     178.906 129.190 130.029  1.00106.34           C  
ATOM   3362  O   GLY A 447     179.686 129.470 130.938  1.00106.34           O  
ATOM   3363  N   ASP A 448     179.306 128.675 128.869  1.00114.09           N  
ATOM   3364  CA  ASP A 448     180.712 128.377 128.634  1.00114.09           C  
ATOM   3365  C   ASP A 448     181.501 129.667 128.446  1.00114.09           C  
ATOM   3366  O   ASP A 448     181.067 130.587 127.748  1.00114.09           O  
ATOM   3367  CB  ASP A 448     180.867 127.478 127.408  1.00114.09           C  
ATOM   3368  CG  ASP A 448     182.238 126.833 127.325  1.00114.09           C  
ATOM   3369  OD1 ASP A 448     183.067 127.070 128.230  1.00114.09           O  
ATOM   3370  OD2 ASP A 448     182.488 126.089 126.354  1.00114.09           O  
ATOM   3371  N   ARG A 449     182.673 129.727 129.078  1.00102.22           N  
ATOM   3372  CA  ARG A 449     183.522 130.911 129.032  1.00102.22           C  
ATOM   3373  C   ARG A 449     184.540 130.851 127.898  1.00102.22           C  
ATOM   3374  O   ARG A 449     184.731 131.840 127.182  1.00102.22           O  
ATOM   3375  CB  ARG A 449     184.239 131.092 130.373  1.00102.22           C  
ATOM   3376  CG  ARG A 449     183.331 131.541 131.506  1.00102.22           C  
ATOM   3377  CD  ARG A 449     184.115 131.753 132.791  1.00102.22           C  
ATOM   3378  NE  ARG A 449     184.571 130.493 133.369  1.00102.22           N  
ATOM   3379  CZ  ARG A 449     185.848 130.155 133.514  1.00102.22           C  
ATOM   3380  NH1 ARG A 449     186.804 130.991 133.131  1.00102.22           N  
ATOM   3381  NH2 ARG A 449     186.171 128.986 134.050  1.00102.22           N  
ATOM   3382  N   MET A 450     185.204 129.705 127.724  1.00110.67           N  
ATOM   3383  CA  MET A 450     186.194 129.584 126.659  1.00110.67           C  
ATOM   3384  C   MET A 450     185.554 129.674 125.279  1.00110.67           C  
ATOM   3385  O   MET A 450     186.181 130.179 124.340  1.00110.67           O  
ATOM   3386  CB  MET A 450     186.963 128.270 126.808  1.00110.67           C  
ATOM   3387  CG  MET A 450     188.086 128.082 125.799  1.00110.67           C  
ATOM   3388  SD  MET A 450     189.383 129.324 125.969  1.00110.67           S  
ATOM   3389  CE  MET A 450     190.084 129.312 124.321  1.00110.67           C  
ATOM   3390  N   LYS A 451     184.314 129.200 125.134  1.00108.17           N  
ATOM   3391  CA  LYS A 451     183.612 129.365 123.866  1.00108.17           C  
ATOM   3392  C   LYS A 451     183.261 130.825 123.607  1.00108.17           C  
ATOM   3393  O   LYS A 451     183.230 131.258 122.449  1.00108.17           O  
ATOM   3394  CB  LYS A 451     182.351 128.500 123.846  1.00108.17           C  
ATOM   3395  CG  LYS A 451     181.676 128.417 122.487  1.00108.17           C  
ATOM   3396  CD  LYS A 451     180.544 127.402 122.492  1.00108.17           C  
ATOM   3397  CE  LYS A 451     179.849 127.345 121.142  1.00108.17           C  
ATOM   3398  NZ  LYS A 451     180.743 126.800 120.082  1.00108.17           N  
ATOM   3399  N   LEU A 452     183.000 131.595 124.665  1.00102.50           N  
ATOM   3400  CA  LEU A 452     182.784 133.029 124.530  1.00102.50           C  
ATOM   3401  C   LEU A 452     184.091 133.808 124.461  1.00102.50           C  
ATOM   3402  O   LEU A 452     184.100 134.942 123.971  1.00102.50           O  
ATOM   3403  CB  LEU A 452     181.933 133.538 125.699  1.00102.50           C  
ATOM   3404  CG  LEU A 452     181.443 134.988 125.661  1.00102.50           C  
ATOM   3405  CD1 LEU A 452     180.578 135.232 124.435  1.00102.50           C  
ATOM   3406  CD2 LEU A 452     180.686 135.334 126.935  1.00102.50           C  
ATOM   3407  N   ALA A 453     185.193 133.217 124.927  1.00103.05           N  
ATOM   3408  CA  ALA A 453     186.472 133.917 124.964  1.00103.05           C  
ATOM   3409  C   ALA A 453     187.077 134.104 123.580  1.00103.05           C  
ATOM   3410  O   ALA A 453     187.973 134.939 123.419  1.00103.05           O  
ATOM   3411  CB  ALA A 453     187.456 133.164 125.860  1.00103.05           C  
ATOM   3412  N   LYS A 454     186.623 133.344 122.583  1.00102.16           N  
ATOM   3413  CA  LYS A 454     187.288 133.365 121.285  1.00102.16           C  
ATOM   3414  C   LYS A 454     186.869 134.569 120.446  1.00102.16           C  
ATOM   3415  O   LYS A 454     187.691 135.128 119.713  1.00102.16           O  
ATOM   3416  CB  LYS A 454     187.002 132.065 120.533  1.00102.16           C  
ATOM   3417  CG  LYS A 454     187.646 130.837 121.160  1.00102.16           C  
ATOM   3418  CD  LYS A 454     187.348 129.579 120.360  1.00102.16           C  
ATOM   3419  CE  LYS A 454     187.950 128.349 121.023  1.00102.16           C  
ATOM   3420  NZ  LYS A 454     187.632 127.101 120.275  1.00102.16           N  
ATOM   3421  N   ASN A 455     185.604 134.983 120.534  1.00107.42           N  
ATOM   3422  CA  ASN A 455     185.104 136.005 119.621  1.00107.42           C  
ATOM   3423  C   ASN A 455     185.474 137.410 120.081  1.00107.42           C  
ATOM   3424  O   ASN A 455     186.396 138.020 119.530  1.00107.42           O  
ATOM   3425  CB  ASN A 455     183.585 135.887 119.473  1.00107.42           C  
ATOM   3426  CG  ASN A 455     183.152 134.524 118.971  1.00107.42           C  
ATOM   3427  OD1 ASN A 455     182.488 133.770 119.682  1.00107.42           O  
ATOM   3428  ND2 ASN A 455     183.523 134.203 117.737  1.00107.42           N  
ATOM   3429  N   LEU A 456     184.774 137.913 121.104  1.00110.94           N  
ATOM   3430  CA  LEU A 456     184.979 139.249 121.664  1.00110.94           C  
ATOM   3431  C   LEU A 456     185.170 140.304 120.576  1.00110.94           C  
ATOM   3432  O   LEU A 456     186.268 140.842 120.404  1.00110.94           O  
ATOM   3433  CB  LEU A 456     186.135 139.242 122.678  1.00110.94           C  
ATOM   3434  CG  LEU A 456     187.528 138.626 122.487  1.00110.94           C  
ATOM   3435  CD1 LEU A 456     188.553 139.599 121.928  1.00110.94           C  
ATOM   3436  CD2 LEU A 456     188.003 138.073 123.820  1.00110.94           C  
ATOM   3437  N   GLN A 457     184.104 140.585 119.825  1.00114.03           N  
ATOM   3438  CA  GLN A 457     184.116 141.658 118.835  1.00114.03           C  
ATOM   3439  C   GLN A 457     184.667 142.951 119.424  1.00114.03           C  
ATOM   3440  O   GLN A 457     184.238 143.397 120.490  1.00114.03           O  
ATOM   3441  CB  GLN A 457     182.700 141.886 118.300  1.00114.03           C  
ATOM   3442  CG  GLN A 457     182.589 142.999 117.269  1.00114.03           C  
ATOM   3443  CD  GLN A 457     183.291 142.665 115.968  1.00114.03           C  
ATOM   3444  OE1 GLN A 457     183.197 141.543 115.469  1.00114.03           O  
ATOM   3445  NE2 GLN A 457     183.997 143.640 115.408  1.00114.03           N  
ATOM   3446  N   ILE A 458     185.622 143.553 118.709  1.00108.35           N  
ATOM   3447  CA  ILE A 458     186.526 144.539 119.293  1.00108.35           C  
ATOM   3448  C   ILE A 458     185.824 145.812 119.743  1.00108.35           C  
ATOM   3449  O   ILE A 458     186.416 146.608 120.479  1.00108.35           O  
ATOM   3450  CB  ILE A 458     187.643 144.882 118.284  1.00108.35           C  
ATOM   3451  CG1 ILE A 458     188.881 145.429 119.000  1.00108.35           C  
ATOM   3452  CG2 ILE A 458     187.141 145.872 117.242  1.00108.35           C  
ATOM   3453  CD1 ILE A 458     190.112 145.495 118.123  1.00108.35           C  
ATOM   3454  N   GLY A 459     184.575 146.021 119.336  1.00115.11           N  
ATOM   3455  CA  GLY A 459     183.849 147.216 119.718  1.00115.11           C  
ATOM   3456  C   GLY A 459     183.025 147.139 120.988  1.00115.11           C  
ATOM   3457  O   GLY A 459     182.113 147.951 121.173  1.00115.11           O  
ATOM   3458  N   ASP A 460     183.316 146.187 121.872  1.00112.69           N  
ATOM   3459  CA  ASP A 460     182.482 145.991 123.047  1.00112.69           C  
ATOM   3460  C   ASP A 460     183.256 146.325 124.323  1.00112.69           C  
ATOM   3461  O   ASP A 460     184.387 146.824 124.283  1.00112.69           O  
ATOM   3462  CB  ASP A 460     181.941 144.558 123.070  1.00112.69           C  
ATOM   3463  CG  ASP A 460     183.034 143.512 123.237  1.00112.69           C  
ATOM   3464  OD1 ASP A 460     184.231 143.868 123.214  1.00112.69           O  
ATOM   3465  OD2 ASP A 460     182.689 142.322 123.392  1.00112.69           O  
ATOM   3466  N   VAL A 461     182.633 146.044 125.466  1.00 99.88           N  
ATOM   3467  CA  VAL A 461     183.152 146.425 126.774  1.00 99.88           C  
ATOM   3468  C   VAL A 461     183.040 145.232 127.714  1.00 99.88           C  
ATOM   3469  O   VAL A 461     182.093 144.443 127.622  1.00 99.88           O  
ATOM   3470  CB  VAL A 461     182.408 147.656 127.342  1.00 99.88           C  
ATOM   3471  CG1 VAL A 461     180.937 147.341 127.583  1.00 99.88           C  
ATOM   3472  CG2 VAL A 461     183.076 148.156 128.617  1.00 99.88           C  
ATOM   3473  N   VAL A 462     184.021 145.087 128.607  1.00 90.62           N  
ATOM   3474  CA  VAL A 462     183.992 144.060 129.638  1.00 90.62           C  
ATOM   3475  C   VAL A 462     184.295 144.731 130.972  1.00 90.62           C  
ATOM   3476  O   VAL A 462     184.788 145.859 131.028  1.00 90.62           O  
ATOM   3477  CB  VAL A 462     184.996 142.918 129.354  1.00 90.62           C  
ATOM   3478  CG1 VAL A 462     186.399 143.311 129.797  1.00 90.62           C  
ATOM   3479  CG2 VAL A 462     184.549 141.620 130.016  1.00 90.62           C  
ATOM   3480  N   GLU A 463     183.986 144.025 132.058  1.00 89.99           N  
ATOM   3481  CA  GLU A 463     184.158 144.559 133.408  1.00 89.99           C  
ATOM   3482  C   GLU A 463     185.150 143.686 134.174  1.00 89.99           C  
ATOM   3483  O   GLU A 463     184.764 142.712 134.824  1.00 89.99           O  
ATOM   3484  CB  GLU A 463     182.811 144.643 134.127  1.00 89.99           C  
ATOM   3485  CG  GLU A 463     181.853 145.662 133.531  1.00 89.99           C  
ATOM   3486  CD  GLU A 463     180.529 145.717 134.265  1.00 89.99           C  
ATOM   3487  OE1 GLU A 463     180.327 144.904 135.193  1.00 89.99           O  
ATOM   3488  OE2 GLU A 463     179.690 146.574 133.918  1.00 89.99           O  
ATOM   3489  N   ARG A 464     186.429 144.040 134.091  1.00 78.07           N  
ATOM   3490  CA  ARG A 464     187.465 143.334 134.828  1.00 78.07           C  
ATOM   3491  C   ARG A 464     187.341 143.610 136.325  1.00 78.07           C  
ATOM   3492  O   ARG A 464     186.670 144.552 136.757  1.00 78.07           O  
ATOM   3493  CB  ARG A 464     188.846 143.755 134.326  1.00 78.07           C  
ATOM   3494  CG  ARG A 464     189.177 145.208 134.623  1.00 78.07           C  
ATOM   3495  CD  ARG A 464     190.551 145.595 134.110  1.00 78.07           C  
ATOM   3496  NE  ARG A 464     190.913 146.949 134.517  1.00 78.07           N  
ATOM   3497  CZ  ARG A 464     192.061 147.542 134.206  1.00 78.07           C  
ATOM   3498  NH1 ARG A 464     192.963 146.903 133.475  1.00 78.07           N  
ATOM   3499  NH2 ARG A 464     192.304 148.778 134.622  1.00 78.07           N  
ATOM   3500  N   HIS A 465     188.001 142.775 137.125  1.00 76.86           N  
ATOM   3501  CA  HIS A 465     188.128 143.089 138.539  1.00 76.86           C  
ATOM   3502  C   HIS A 465     189.136 144.220 138.735  1.00 76.86           C  
ATOM   3503  O   HIS A 465     189.881 144.593 137.823  1.00 76.86           O  
ATOM   3504  CB  HIS A 465     188.555 141.861 139.345  1.00 76.86           C  
ATOM   3505  CG  HIS A 465     187.621 140.697 139.226  1.00 76.86           C  
ATOM   3506  ND1 HIS A 465     187.977 139.518 138.610  1.00 76.86           N  
ATOM   3507  CD2 HIS A 465     186.343 140.534 139.641  1.00 76.86           C  
ATOM   3508  CE1 HIS A 465     186.960 138.676 138.653  1.00 76.86           C  
ATOM   3509  NE2 HIS A 465     185.955 139.268 139.273  1.00 76.86           N  
ATOM   3510  N   LEU A 466     189.156 144.771 139.945  1.00 78.56           N  
ATOM   3511  CA  LEU A 466     190.150 145.781 140.277  1.00 78.56           C  
ATOM   3512  C   LEU A 466     191.537 145.148 140.312  1.00 78.56           C  
ATOM   3513  O   LEU A 466     191.699 143.995 140.720  1.00 78.56           O  
ATOM   3514  CB  LEU A 466     189.813 146.425 141.624  1.00 78.56           C  
ATOM   3515  CG  LEU A 466     190.421 147.778 142.013  1.00 78.56           C  
ATOM   3516  CD1 LEU A 466     191.828 147.635 142.582  1.00 78.56           C  
ATOM   3517  CD2 LEU A 466     190.412 148.732 140.827  1.00 78.56           C  
ATOM   3518  N   GLU A 467     192.542 145.907 139.880  1.00 89.63           N  
ATOM   3519  CA  GLU A 467     193.905 145.401 139.797  1.00 89.63           C  
ATOM   3520  C   GLU A 467     194.873 146.493 140.228  1.00 89.63           C  
ATOM   3521  O   GLU A 467     194.497 147.655 140.404  1.00 89.63           O  
ATOM   3522  CB  GLU A 467     194.246 144.908 138.385  1.00 89.63           C  
ATOM   3523  CG  GLU A 467     194.289 145.999 137.330  1.00 89.63           C  
ATOM   3524  CD  GLU A 467     194.558 145.450 135.942  1.00 89.63           C  
ATOM   3525  OE1 GLU A 467     194.676 144.215 135.802  1.00 89.63           O  
ATOM   3526  OE2 GLU A 467     194.664 146.254 134.993  1.00 89.63           O  
ATOM   3527  N   ASP A 468     196.135 146.105 140.403  1.00 87.86           N  
ATOM   3528  CA  ASP A 468     197.165 147.055 140.807  1.00 87.86           C  
ATOM   3529  C   ASP A 468     197.412 148.048 139.676  1.00 87.86           C  
ATOM   3530  O   ASP A 468     197.709 147.650 138.545  1.00 87.86           O  
ATOM   3531  CB  ASP A 468     198.450 146.319 141.180  1.00 87.86           C  
ATOM   3532  CG  ASP A 468     198.846 145.270 140.155  1.00 87.86           C  
ATOM   3533  OD1 ASP A 468     198.047 145.001 139.233  1.00 87.86           O  
ATOM   3534  OD2 ASP A 468     199.958 144.715 140.272  1.00 87.86           O  
ATOM   3535  N   GLY A 469     197.289 149.336 139.977  1.00 84.08           N  
ATOM   3536  CA  GLY A 469     197.572 150.386 139.014  1.00 84.08           C  
ATOM   3537  C   GLY A 469     196.405 151.305 138.725  1.00 84.08           C  
ATOM   3538  O   GLY A 469     196.598 152.342 138.073  1.00 84.08           O  
ATOM   3539  N   ASP A 470     195.200 150.971 139.181  1.00 80.64           N  
ATOM   3540  CA  ASP A 470     194.019 151.776 138.917  1.00 80.64           C  
ATOM   3541  C   ASP A 470     193.924 152.931 139.913  1.00 80.64           C  
ATOM   3542  O   ASP A 470     194.769 153.102 140.797  1.00 80.64           O  
ATOM   3543  CB  ASP A 470     192.767 150.904 138.957  1.00 80.64           C  
ATOM   3544  CG  ASP A 470     192.718 149.902 137.817  1.00 80.64           C  
ATOM   3545  OD1 ASP A 470     193.290 150.190 136.744  1.00 80.64           O  
ATOM   3546  OD2 ASP A 470     192.111 148.826 137.995  1.00 80.64           O  
ATOM   3547  N   VAL A 471     192.875 153.735 139.764  1.00 73.14           N  
ATOM   3548  CA  VAL A 471     192.764 155.039 140.408  1.00 73.14           C  
ATOM   3549  C   VAL A 471     191.570 155.013 141.352  1.00 73.14           C  
ATOM   3550  O   VAL A 471     190.444 154.713 140.933  1.00 73.14           O  
ATOM   3551  CB  VAL A 471     192.624 156.170 139.378  1.00 73.14           C  
ATOM   3552  CG1 VAL A 471     192.486 157.511 140.078  1.00 73.14           C  
ATOM   3553  CG2 VAL A 471     193.822 156.176 138.446  1.00 73.14           C  
ATOM   3554  N   VAL A 472     191.818 155.326 142.622  1.00 68.35           N  
ATOM   3555  CA  VAL A 472     190.886 155.077 143.715  1.00 68.35           C  
ATOM   3556  C   VAL A 472     190.743 156.363 144.516  1.00 68.35           C  
ATOM   3557  O   VAL A 472     191.743 156.938 144.959  1.00 68.35           O  
ATOM   3558  CB  VAL A 472     191.359 153.923 144.620  1.00 68.35           C  
ATOM   3559  CG1 VAL A 472     190.437 153.776 145.822  1.00 68.35           C  
ATOM   3560  CG2 VAL A 472     191.428 152.623 143.833  1.00 68.35           C  
ATOM   3561  N   LEU A 473     189.504 156.809 144.700  1.00 66.73           N  
ATOM   3562  CA  LEU A 473     189.204 157.845 145.677  1.00 66.73           C  
ATOM   3563  C   LEU A 473     189.012 157.249 147.067  1.00 66.73           C  
ATOM   3564  O   LEU A 473     188.629 156.087 147.225  1.00 66.73           O  
ATOM   3565  CB  LEU A 473     187.950 158.619 145.269  1.00 66.73           C  
ATOM   3566  CG  LEU A 473     188.146 159.817 144.337  1.00 66.73           C  
ATOM   3567  CD1 LEU A 473     188.356 159.366 142.898  1.00 66.73           C  
ATOM   3568  CD2 LEU A 473     186.965 160.769 144.439  1.00 66.73           C  
ATOM   3569  N   PHE A 474     189.281 158.072 148.080  1.00 69.31           N  
ATOM   3570  CA  PHE A 474     189.475 157.605 149.447  1.00 69.31           C  
ATOM   3571  C   PHE A 474     189.440 158.805 150.386  1.00 69.31           C  
ATOM   3572  O   PHE A 474     190.180 159.773 150.183  1.00 69.31           O  
ATOM   3573  CB  PHE A 474     190.800 156.845 149.554  1.00 69.31           C  
ATOM   3574  CG  PHE A 474     191.075 156.276 150.913  1.00 69.31           C  
ATOM   3575  CD1 PHE A 474     190.450 155.114 151.332  1.00 69.31           C  
ATOM   3576  CD2 PHE A 474     191.978 156.892 151.763  1.00 69.31           C  
ATOM   3577  CE1 PHE A 474     190.710 154.584 152.579  1.00 69.31           C  
ATOM   3578  CE2 PHE A 474     192.242 156.367 153.010  1.00 69.31           C  
ATOM   3579  CZ  PHE A 474     191.607 155.212 153.420  1.00 69.31           C  
ATOM   3580  N   ASN A 475     188.591 158.759 151.413  1.00 71.73           N  
ATOM   3581  CA  ASN A 475     188.460 159.895 152.316  1.00 71.73           C  
ATOM   3582  C   ASN A 475     187.911 159.442 153.660  1.00 71.73           C  
ATOM   3583  O   ASN A 475     187.378 158.339 153.801  1.00 71.73           O  
ATOM   3584  CB  ASN A 475     187.555 160.981 151.722  1.00 71.73           C  
ATOM   3585  CG  ASN A 475     186.221 160.435 151.241  1.00 71.73           C  
ATOM   3586  OD1 ASN A 475     185.982 159.228 151.272  1.00 71.73           O  
ATOM   3587  ND2 ASN A 475     185.346 161.327 150.791  1.00 71.73           N  
ATOM   3588  N   ARG A 476     188.053 160.326 154.644  1.00 80.73           N  
ATOM   3589  CA  ARG A 476     187.451 160.172 155.959  1.00 80.73           C  
ATOM   3590  C   ARG A 476     186.029 160.721 155.916  1.00 80.73           C  
ATOM   3591  O   ARG A 476     185.732 161.661 155.174  1.00 80.73           O  
ATOM   3592  CB  ARG A 476     188.287 160.905 157.014  1.00 80.73           C  
ATOM   3593  CG  ARG A 476     187.759 160.840 158.440  1.00 80.73           C  
ATOM   3594  CD  ARG A 476     187.783 159.420 158.982  1.00 80.73           C  
ATOM   3595  NE  ARG A 476     187.421 159.366 160.396  1.00 80.73           N  
ATOM   3596  CZ  ARG A 476     188.288 159.492 161.395  1.00 80.73           C  
ATOM   3597  NH1 ARG A 476     189.575 159.690 161.139  1.00 80.73           N  
ATOM   3598  NH2 ARG A 476     187.869 159.428 162.652  1.00 80.73           N  
ATOM   3599  N   GLN A 477     185.145 160.130 156.721  1.00 89.25           N  
ATOM   3600  CA  GLN A 477     183.734 160.476 156.591  1.00 89.25           C  
ATOM   3601  C   GLN A 477     183.421 161.840 157.203  1.00 89.25           C  
ATOM   3602  O   GLN A 477     182.698 162.624 156.575  1.00 89.25           O  
ATOM   3603  CB  GLN A 477     182.850 159.387 157.208  1.00 89.25           C  
ATOM   3604  CG  GLN A 477     181.363 159.579 156.953  1.00 89.25           C  
ATOM   3605  CD  GLN A 477     181.007 159.538 155.480  1.00 89.25           C  
ATOM   3606  OE1 GLN A 477     180.718 160.568 154.872  1.00 89.25           O  
ATOM   3607  NE2 GLN A 477     181.021 158.344 154.899  1.00 89.25           N  
ATOM   3608  N   PRO A 478     183.923 162.191 158.402  1.00 77.43           N  
ATOM   3609  CA  PRO A 478     183.842 163.599 158.817  1.00 77.43           C  
ATOM   3610  C   PRO A 478     184.945 164.409 158.154  1.00 77.43           C  
ATOM   3611  O   PRO A 478     186.124 164.291 158.504  1.00 77.43           O  
ATOM   3612  CB  PRO A 478     184.017 163.523 160.341  1.00 77.43           C  
ATOM   3613  CG  PRO A 478     184.803 162.292 160.570  1.00 77.43           C  
ATOM   3614  CD  PRO A 478     184.390 161.324 159.501  1.00 77.43           C  
ATOM   3615  N   SER A 479     184.562 165.241 157.189  1.00 82.98           N  
ATOM   3616  CA  SER A 479     185.525 165.922 156.335  1.00 82.98           C  
ATOM   3617  C   SER A 479     185.865 167.291 156.911  1.00 82.98           C  
ATOM   3618  O   SER A 479     184.968 168.096 157.182  1.00 82.98           O  
ATOM   3619  CB  SER A 479     184.977 166.062 154.914  1.00 82.98           C  
ATOM   3620  OG  SER A 479     183.890 166.969 154.876  1.00 82.98           O  
ATOM   3621  N   LEU A 480     187.159 167.555 157.096  1.00 86.76           N  
ATOM   3622  CA  LEU A 480     187.561 168.857 157.615  1.00 86.76           C  
ATOM   3623  C   LEU A 480     187.632 169.892 156.496  1.00 86.76           C  
ATOM   3624  O   LEU A 480     187.058 170.981 156.607  1.00 86.76           O  
ATOM   3625  CB  LEU A 480     188.907 168.749 158.331  1.00 86.76           C  
ATOM   3626  CG  LEU A 480     188.963 167.827 159.550  1.00 86.76           C  
ATOM   3627  CD1 LEU A 480     190.373 167.777 160.117  1.00 86.76           C  
ATOM   3628  CD2 LEU A 480     187.965 168.265 160.613  1.00 86.76           C  
ATOM   3629  N   HIS A 481     188.337 169.566 155.416  1.00 82.89           N  
ATOM   3630  CA  HIS A 481     188.635 170.523 154.358  1.00 82.89           C  
ATOM   3631  C   HIS A 481     188.856 169.756 153.056  1.00 82.89           C  
ATOM   3632  O   HIS A 481     188.646 168.542 152.985  1.00 82.89           O  
ATOM   3633  CB  HIS A 481     189.840 171.388 154.749  1.00 82.89           C  
ATOM   3634  CG  HIS A 481     190.989 170.605 155.302  1.00 82.89           C  
ATOM   3635  ND1 HIS A 481     191.814 169.833 154.513  1.00 82.89           N  
ATOM   3636  CD2 HIS A 481     191.450 170.473 156.568  1.00 82.89           C  
ATOM   3637  CE1 HIS A 481     192.734 169.260 155.269  1.00 82.89           C  
ATOM   3638  NE2 HIS A 481     192.535 169.633 156.520  1.00 82.89           N  
ATOM   3639  N   ARG A 482     189.280 170.479 152.016  1.00 90.89           N  
ATOM   3640  CA  ARG A 482     189.423 169.893 150.688  1.00 90.89           C  
ATOM   3641  C   ARG A 482     190.560 168.881 150.614  1.00 90.89           C  
ATOM   3642  O   ARG A 482     190.613 168.092 149.665  1.00 90.89           O  
ATOM   3643  CB  ARG A 482     189.654 170.984 149.644  1.00 90.89           C  
ATOM   3644  CG  ARG A 482     191.009 171.661 149.755  1.00 90.89           C  
ATOM   3645  CD  ARG A 482     191.099 172.856 148.833  1.00 90.89           C  
ATOM   3646  NE  ARG A 482     191.196 172.453 147.433  1.00 90.89           N  
ATOM   3647  CZ  ARG A 482     192.340 172.177 146.812  1.00 90.89           C  
ATOM   3648  NH1 ARG A 482     193.489 172.244 147.469  1.00 90.89           N  
ATOM   3649  NH2 ARG A 482     192.336 171.824 145.534  1.00 90.89           N  
ATOM   3650  N   LEU A 483     191.464 168.883 151.594  1.00 86.73           N  
ATOM   3651  CA  LEU A 483     192.608 167.981 151.631  1.00 86.73           C  
ATOM   3652  C   LEU A 483     192.343 166.781 152.537  1.00 86.73           C  
ATOM   3653  O   LEU A 483     193.271 166.179 153.084  1.00 86.73           O  
ATOM   3654  CB  LEU A 483     193.855 168.770 152.053  1.00 86.73           C  
ATOM   3655  CG  LEU A 483     195.312 168.283 151.988  1.00 86.73           C  
ATOM   3656  CD1 LEU A 483     195.814 167.773 153.330  1.00 86.73           C  
ATOM   3657  CD2 LEU A 483     195.486 167.216 150.911  1.00 86.73           C  
ATOM   3658  N   SER A 484     191.071 166.408 152.681  1.00 79.83           N  
ATOM   3659  CA  SER A 484     190.671 165.181 153.352  1.00 79.83           C  
ATOM   3660  C   SER A 484     190.247 164.094 152.374  1.00 79.83           C  
ATOM   3661  O   SER A 484     190.001 162.960 152.798  1.00 79.83           O  
ATOM   3662  CB  SER A 484     189.521 165.458 154.330  1.00 79.83           C  
ATOM   3663  OG  SER A 484     189.072 164.259 154.933  1.00 79.83           O  
ATOM   3664  N   ILE A 485     190.159 164.413 151.084  1.00 74.04           N  
ATOM   3665  CA  ILE A 485     189.798 163.465 150.037  1.00 74.04           C  
ATOM   3666  C   ILE A 485     190.855 163.570 148.947  1.00 74.04           C  
ATOM   3667  O   ILE A 485     191.097 164.660 148.415  1.00 74.04           O  
ATOM   3668  CB  ILE A 485     188.391 163.729 149.469  1.00 74.04           C  
ATOM   3669  CG1 ILE A 485     188.210 163.039 148.112  1.00 74.04           C  
ATOM   3670  CG2 ILE A 485     188.112 165.227 149.368  1.00 74.04           C  
ATOM   3671  CD1 ILE A 485     188.190 161.522 148.183  1.00 74.04           C  
ATOM   3672  N   LEU A 486     191.493 162.445 148.629  1.00 76.27           N  
ATOM   3673  CA  LEU A 486     192.588 162.400 147.671  1.00 76.27           C  
ATOM   3674  C   LEU A 486     192.451 161.145 146.821  1.00 76.27           C  
ATOM   3675  O   LEU A 486     191.563 160.314 147.037  1.00 76.27           O  
ATOM   3676  CB  LEU A 486     193.953 162.433 148.372  1.00 76.27           C  
ATOM   3677  CG  LEU A 486     194.405 163.746 149.019  1.00 76.27           C  
ATOM   3678  CD1 LEU A 486     193.874 163.891 150.443  1.00 76.27           C  
ATOM   3679  CD2 LEU A 486     195.922 163.853 149.003  1.00 76.27           C  
ATOM   3680  N   SER A 487     193.338 161.013 145.841  1.00 77.01           N  
ATOM   3681  CA  SER A 487     193.406 159.840 144.986  1.00 77.01           C  
ATOM   3682  C   SER A 487     194.660 159.040 145.312  1.00 77.01           C  
ATOM   3683  O   SER A 487     195.654 159.575 145.814  1.00 77.01           O  
ATOM   3684  CB  SER A 487     193.406 160.235 143.506  1.00 77.01           C  
ATOM   3685  OG  SER A 487     193.535 159.091 142.679  1.00 77.01           O  
ATOM   3686  N   HIS A 488     194.609 157.746 145.005  1.00 72.09           N  
ATOM   3687  CA  HIS A 488     195.733 156.854 145.249  1.00 72.09           C  
ATOM   3688  C   HIS A 488     195.755 155.770 144.181  1.00 72.09           C  
ATOM   3689  O   HIS A 488     194.758 155.517 143.502  1.00 72.09           O  
ATOM   3690  CB  HIS A 488     195.665 156.219 146.645  1.00 72.09           C  
ATOM   3691  CG  HIS A 488     195.859 157.193 147.765  1.00 72.09           C  
ATOM   3692  ND1 HIS A 488     194.833 157.967 148.263  1.00 72.09           N  
ATOM   3693  CD2 HIS A 488     196.958 157.515 148.488  1.00 72.09           C  
ATOM   3694  CE1 HIS A 488     195.293 158.728 149.240  1.00 72.09           C  
ATOM   3695  NE2 HIS A 488     196.579 158.472 149.397  1.00 72.09           N  
ATOM   3696  N   TYR A 489     196.912 155.130 144.047  1.00 73.59           N  
ATOM   3697  CA  TYR A 489     197.036 153.892 143.294  1.00 73.59           C  
ATOM   3698  C   TYR A 489     196.723 152.698 144.190  1.00 73.59           C  
ATOM   3699  O   TYR A 489     196.845 152.759 145.417  1.00 73.59           O  
ATOM   3700  CB  TYR A 489     198.439 153.757 142.697  1.00 73.59           C  
ATOM   3701  CG  TYR A 489     198.749 154.775 141.624  1.00 73.59           C  
ATOM   3702  CD1 TYR A 489     198.269 154.617 140.331  1.00 73.59           C  
ATOM   3703  CD2 TYR A 489     199.523 155.894 141.903  1.00 73.59           C  
ATOM   3704  CE1 TYR A 489     198.549 155.544 139.346  1.00 73.59           C  
ATOM   3705  CE2 TYR A 489     199.809 156.827 140.925  1.00 73.59           C  
ATOM   3706  CZ  TYR A 489     199.319 156.647 139.648  1.00 73.59           C  
ATOM   3707  OH  TYR A 489     199.601 157.573 138.670  1.00 73.59           O  
ATOM   3708  N   ALA A 490     196.309 151.606 143.560  1.00 72.30           N  
ATOM   3709  CA  ALA A 490     195.905 150.402 144.267  1.00 72.30           C  
ATOM   3710  C   ALA A 490     196.996 149.339 144.208  1.00 72.30           C  
ATOM   3711  O   ALA A 490     197.846 149.327 143.314  1.00 72.30           O  
ATOM   3712  CB  ALA A 490     194.604 149.844 143.685  1.00 72.30           C  
ATOM   3713  N   LYS A 491     196.957 148.436 145.186  1.00 65.99           N  
ATOM   3714  CA  LYS A 491     197.841 147.279 145.226  1.00 65.99           C  
ATOM   3715  C   LYS A 491     197.135 146.164 145.978  1.00 65.99           C  
ATOM   3716  O   LYS A 491     196.626 146.385 147.080  1.00 65.99           O  
ATOM   3717  CB  LYS A 491     199.175 147.621 145.900  1.00 65.99           C  
ATOM   3718  CG  LYS A 491     200.183 146.483 145.896  1.00 65.99           C  
ATOM   3719  CD  LYS A 491     201.466 146.885 146.608  1.00 65.99           C  
ATOM   3720  CE  LYS A 491     202.278 147.867 145.780  1.00 65.99           C  
ATOM   3721  NZ  LYS A 491     202.794 147.245 144.529  1.00 65.99           N  
ATOM   3722  N   ILE A 492     197.102 144.976 145.386  1.00 64.06           N  
ATOM   3723  CA  ILE A 492     196.264 143.889 145.877  1.00 64.06           C  
ATOM   3724  C   ILE A 492     197.061 143.041 146.856  1.00 64.06           C  
ATOM   3725  O   ILE A 492     198.157 142.565 146.535  1.00 64.06           O  
ATOM   3726  CB  ILE A 492     195.736 143.036 144.712  1.00 64.06           C  
ATOM   3727  CG1 ILE A 492     195.056 143.924 143.666  1.00 64.06           C  
ATOM   3728  CG2 ILE A 492     194.777 141.974 145.229  1.00 64.06           C  
ATOM   3729  CD1 ILE A 492     193.893 144.725 144.209  1.00 64.06           C  
ATOM   3730  N   ARG A 493     196.513 142.856 148.052  1.00 66.31           N  
ATOM   3731  CA  ARG A 493     197.175 142.162 149.143  1.00 66.31           C  
ATOM   3732  C   ARG A 493     196.181 141.210 149.790  1.00 66.31           C  
ATOM   3733  O   ARG A 493     194.982 141.510 149.850  1.00 66.31           O  
ATOM   3734  CB  ARG A 493     197.722 143.146 150.188  1.00 66.31           C  
ATOM   3735  CG  ARG A 493     198.827 144.055 149.670  1.00 66.31           C  
ATOM   3736  CD  ARG A 493     200.053 143.252 149.265  1.00 66.31           C  
ATOM   3737  NE  ARG A 493     201.172 144.110 148.885  1.00 66.31           N  
ATOM   3738  CZ  ARG A 493     202.326 143.659 148.405  1.00 66.31           C  
ATOM   3739  NH1 ARG A 493     202.515 142.357 148.241  1.00 66.31           N  
ATOM   3740  NH2 ARG A 493     203.292 144.510 148.085  1.00 66.31           N  
ATOM   3741  N   PRO A 494     196.645 140.060 150.282  1.00 60.40           N  
ATOM   3742  CA  PRO A 494     195.730 138.956 150.594  1.00 60.40           C  
ATOM   3743  C   PRO A 494     195.061 139.026 151.959  1.00 60.40           C  
ATOM   3744  O   PRO A 494     194.406 138.053 152.345  1.00 60.40           O  
ATOM   3745  CB  PRO A 494     196.656 137.732 150.513  1.00 60.40           C  
ATOM   3746  CG  PRO A 494     197.974 138.258 150.949  1.00 60.40           C  
ATOM   3747  CD  PRO A 494     198.058 139.652 150.390  1.00 60.40           C  
ATOM   3748  N   TRP A 495     195.185 140.117 152.711  1.00 63.07           N  
ATOM   3749  CA  TRP A 495     194.547 140.180 154.019  1.00 63.07           C  
ATOM   3750  C   TRP A 495     193.143 140.770 153.862  1.00 63.07           C  
ATOM   3751  O   TRP A 495     192.588 140.783 152.760  1.00 63.07           O  
ATOM   3752  CB  TRP A 495     195.427 140.970 154.992  1.00 63.07           C  
ATOM   3753  CG  TRP A 495     196.652 140.221 155.427  1.00 63.07           C  
ATOM   3754  CD1 TRP A 495     197.946 140.522 155.120  1.00 63.07           C  
ATOM   3755  CD2 TRP A 495     196.696 139.023 156.215  1.00 63.07           C  
ATOM   3756  NE1 TRP A 495     198.794 139.602 155.686  1.00 63.07           N  
ATOM   3757  CE2 TRP A 495     198.052 138.670 156.361  1.00 63.07           C  
ATOM   3758  CE3 TRP A 495     195.721 138.221 156.817  1.00 63.07           C  
ATOM   3759  CZ2 TRP A 495     198.458 137.550 157.084  1.00 63.07           C  
ATOM   3760  CZ3 TRP A 495     196.126 137.111 157.536  1.00 63.07           C  
ATOM   3761  CH2 TRP A 495     197.483 136.786 157.663  1.00 63.07           C  
ATOM   3762  N   ARG A 496     192.542 141.246 154.953  1.00 60.94           N  
ATOM   3763  CA  ARG A 496     191.127 141.606 154.948  1.00 60.94           C  
ATOM   3764  C   ARG A 496     190.904 143.033 155.442  1.00 60.94           C  
ATOM   3765  O   ARG A 496     189.930 143.312 156.148  1.00 60.94           O  
ATOM   3766  CB  ARG A 496     190.324 140.619 155.795  1.00 60.94           C  
ATOM   3767  CG  ARG A 496     188.844 140.518 155.450  1.00 60.94           C  
ATOM   3768  CD  ARG A 496     188.130 139.574 156.406  1.00 60.94           C  
ATOM   3769  NE  ARG A 496     188.539 138.185 156.223  1.00 60.94           N  
ATOM   3770  CZ  ARG A 496     187.959 137.343 155.375  1.00 60.94           C  
ATOM   3771  NH1 ARG A 496     186.931 137.745 154.641  1.00 60.94           N  
ATOM   3772  NH2 ARG A 496     188.397 136.096 155.270  1.00 60.94           N  
ATOM   3773  N   THR A 497     191.782 143.969 155.085  1.00 61.07           N  
ATOM   3774  CA  THR A 497     191.571 145.356 155.485  1.00 61.07           C  
ATOM   3775  C   THR A 497     192.385 146.283 154.592  1.00 61.07           C  
ATOM   3776  O   THR A 497     193.202 145.842 153.780  1.00 61.07           O  
ATOM   3777  CB  THR A 497     191.935 145.576 156.958  1.00 61.07           C  
ATOM   3778  OG1 THR A 497     191.829 146.969 157.277  1.00 61.07           O  
ATOM   3779  CG2 THR A 497     193.352 145.100 157.236  1.00 61.07           C  
ATOM   3780  N   PHE A 498     192.146 147.584 154.761  1.00 63.81           N  
ATOM   3781  CA  PHE A 498     192.729 148.609 153.904  1.00 63.81           C  
ATOM   3782  C   PHE A 498     194.070 149.029 154.496  1.00 63.81           C  
ATOM   3783  O   PHE A 498     194.131 149.440 155.660  1.00 63.81           O  
ATOM   3784  CB  PHE A 498     191.811 149.827 153.782  1.00 63.81           C  
ATOM   3785  CG  PHE A 498     190.556 149.579 152.994  1.00 63.81           C  
ATOM   3786  CD1 PHE A 498     190.390 148.418 152.263  1.00 63.81           C  
ATOM   3787  CD2 PHE A 498     189.545 150.527 152.973  1.00 63.81           C  
ATOM   3788  CE1 PHE A 498     189.236 148.197 151.536  1.00 63.81           C  
ATOM   3789  CE2 PHE A 498     188.388 150.313 152.247  1.00 63.81           C  
ATOM   3790  CZ  PHE A 498     188.234 149.146 151.528  1.00 63.81           C  
ATOM   3791  N   ARG A 499     195.139 148.931 153.711  1.00 65.23           N  
ATOM   3792  CA  ARG A 499     196.465 149.310 154.182  1.00 65.23           C  
ATOM   3793  C   ARG A 499     196.986 150.479 153.360  1.00 65.23           C  
ATOM   3794  O   ARG A 499     197.051 150.400 152.129  1.00 65.23           O  
ATOM   3795  CB  ARG A 499     197.434 148.126 154.123  1.00 65.23           C  
ATOM   3796  CG  ARG A 499     197.389 147.250 155.365  1.00 65.23           C  
ATOM   3797  CD  ARG A 499     196.222 146.279 155.339  1.00 65.23           C  
ATOM   3798  NE  ARG A 499     196.305 145.331 154.235  1.00 65.23           N  
ATOM   3799  CZ  ARG A 499     196.933 144.163 154.312  1.00 65.23           C  
ATOM   3800  NH1 ARG A 499     197.525 143.801 155.442  1.00 65.23           N  
ATOM   3801  NH2 ARG A 499     196.964 143.353 153.265  1.00 65.23           N  
ATOM   3802  N   LEU A 500     197.350 151.560 154.043  1.00 75.92           N  
ATOM   3803  CA  LEU A 500     197.883 152.760 153.419  1.00 75.92           C  
ATOM   3804  C   LEU A 500     199.255 153.063 154.007  1.00 75.92           C  
ATOM   3805  O   LEU A 500     199.601 152.597 155.096  1.00 75.92           O  
ATOM   3806  CB  LEU A 500     196.930 153.951 153.606  1.00 75.92           C  
ATOM   3807  CG  LEU A 500     196.360 154.206 155.007  1.00 75.92           C  
ATOM   3808  CD1 LEU A 500     197.290 155.052 155.865  1.00 75.92           C  
ATOM   3809  CD2 LEU A 500     194.983 154.849 154.914  1.00 75.92           C  
ATOM   3810  N   ASN A 501     200.044 153.850 153.280  1.00 80.17           N  
ATOM   3811  CA  ASN A 501     201.317 154.291 153.828  1.00 80.17           C  
ATOM   3812  C   ASN A 501     201.085 155.320 154.930  1.00 80.17           C  
ATOM   3813  O   ASN A 501     200.150 156.122 154.876  1.00 80.17           O  
ATOM   3814  CB  ASN A 501     202.207 154.876 152.732  1.00 80.17           C  
ATOM   3815  CG  ASN A 501     203.655 155.018 153.171  1.00 80.17           C  
ATOM   3816  OD1 ASN A 501     203.988 154.796 154.335  1.00 80.17           O  
ATOM   3817  ND2 ASN A 501     204.524 155.379 152.235  1.00 80.17           N  
ATOM   3818  N   GLU A 502     201.956 155.292 155.938  1.00 88.73           N  
ATOM   3819  CA  GLU A 502     201.623 155.916 157.213  1.00 88.73           C  
ATOM   3820  C   GLU A 502     201.711 157.437 157.153  1.00 88.73           C  
ATOM   3821  O   GLU A 502     200.975 158.125 157.868  1.00 88.73           O  
ATOM   3822  CB  GLU A 502     202.540 155.376 158.313  1.00 88.73           C  
ATOM   3823  CG  GLU A 502     202.041 155.617 159.731  1.00 88.73           C  
ATOM   3824  CD  GLU A 502     202.437 156.975 160.276  1.00 88.73           C  
ATOM   3825  OE1 GLU A 502     203.513 157.481 159.895  1.00 88.73           O  
ATOM   3826  OE2 GLU A 502     201.674 157.536 161.090  1.00 88.73           O  
ATOM   3827  N   CYS A 503     202.593 157.974 156.307  1.00 81.99           N  
ATOM   3828  CA  CYS A 503     202.877 159.405 156.297  1.00 81.99           C  
ATOM   3829  C   CYS A 503     201.721 160.263 155.796  1.00 81.99           C  
ATOM   3830  O   CYS A 503     201.784 161.488 155.944  1.00 81.99           O  
ATOM   3831  CB  CYS A 503     204.117 159.680 155.443  1.00 81.99           C  
ATOM   3832  SG  CYS A 503     205.670 159.098 156.164  1.00 81.99           S  
ATOM   3833  N   VAL A 504     200.675 159.672 155.215  1.00 78.71           N  
ATOM   3834  CA  VAL A 504     199.512 160.442 154.788  1.00 78.71           C  
ATOM   3835  C   VAL A 504     198.401 160.444 155.833  1.00 78.71           C  
ATOM   3836  O   VAL A 504     197.292 160.906 155.547  1.00 78.71           O  
ATOM   3837  CB  VAL A 504     198.984 159.940 153.434  1.00 78.71           C  
ATOM   3838  CG1 VAL A 504     200.068 160.046 152.370  1.00 78.71           C  
ATOM   3839  CG2 VAL A 504     198.480 158.513 153.554  1.00 78.71           C  
ATOM   3840  N   CYS A 505     198.662 159.926 157.035  1.00 86.76           N  
ATOM   3841  CA  CYS A 505     197.605 159.846 158.037  1.00 86.76           C  
ATOM   3842  C   CYS A 505     197.275 161.205 158.641  1.00 86.76           C  
ATOM   3843  O   CYS A 505     196.222 161.349 159.271  1.00 86.76           O  
ATOM   3844  CB  CYS A 505     198.002 158.874 159.149  1.00 86.76           C  
ATOM   3845  SG  CYS A 505     199.295 159.494 160.248  1.00 86.76           S  
ATOM   3846  N   THR A 506     198.145 162.197 158.465  1.00 82.04           N  
ATOM   3847  CA  THR A 506     197.962 163.523 159.045  1.00 82.04           C  
ATOM   3848  C   THR A 506     196.877 164.340 158.343  1.00 82.04           C  
ATOM   3849  O   THR A 506     196.144 165.077 159.017  1.00 82.04           O  
ATOM   3850  CB  THR A 506     199.291 164.289 159.041  1.00 82.04           C  
ATOM   3851  OG1 THR A 506     200.302 163.498 159.676  1.00 82.04           O  
ATOM   3852  CG2 THR A 506     199.155 165.612 159.783  1.00 82.04           C  
ATOM   3853  N   PRO A 507     196.719 164.248 157.014  1.00 79.62           N  
ATOM   3854  CA  PRO A 507     195.491 164.801 156.415  1.00 79.62           C  
ATOM   3855  C   PRO A 507     194.216 164.139 156.903  1.00 79.62           C  
ATOM   3856  O   PRO A 507     193.218 164.831 157.141  1.00 79.62           O  
ATOM   3857  CB  PRO A 507     195.708 164.557 154.918  1.00 79.62           C  
ATOM   3858  CG  PRO A 507     197.171 164.658 154.750  1.00 79.62           C  
ATOM   3859  CD  PRO A 507     197.755 164.021 155.987  1.00 79.62           C  
ATOM   3860  N   TYR A 508     194.213 162.816 157.061  1.00 83.61           N  
ATOM   3861  CA  TYR A 508     192.987 162.121 157.432  1.00 83.61           C  
ATOM   3862  C   TYR A 508     192.732 162.133 158.933  1.00 83.61           C  
ATOM   3863  O   TYR A 508     191.692 161.626 159.362  1.00 83.61           O  
ATOM   3864  CB  TYR A 508     193.027 160.679 156.923  1.00 83.61           C  
ATOM   3865  CG  TYR A 508     193.080 160.571 155.415  1.00 83.61           C  
ATOM   3866  CD1 TYR A 508     191.923 160.656 154.652  1.00 83.61           C  
ATOM   3867  CD2 TYR A 508     194.287 160.379 154.756  1.00 83.61           C  
ATOM   3868  CE1 TYR A 508     191.967 160.555 153.274  1.00 83.61           C  
ATOM   3869  CE2 TYR A 508     194.341 160.278 153.378  1.00 83.61           C  
ATOM   3870  CZ  TYR A 508     193.179 160.367 152.642  1.00 83.61           C  
ATOM   3871  OH  TYR A 508     193.227 160.268 151.270  1.00 83.61           O  
ATOM   3872  N   ASN A 509     193.692 162.637 159.717  1.00 91.48           N  
ATOM   3873  CA  ASN A 509     193.800 162.549 161.175  1.00 91.48           C  
ATOM   3874  C   ASN A 509     193.229 161.248 161.735  1.00 91.48           C  
ATOM   3875  O   ASN A 509     192.493 161.259 162.727  1.00 91.48           O  
ATOM   3876  CB  ASN A 509     193.186 163.790 161.859  1.00 91.48           C  
ATOM   3877  CG  ASN A 509     191.672 163.929 161.680  1.00 91.48           C  
ATOM   3878  OD1 ASN A 509     190.971 163.007 161.281  1.00 91.48           O  
ATOM   3879  ND2 ASN A 509     191.168 165.118 161.986  1.00 91.48           N  
ATOM   3880  N   ALA A 510     193.585 160.123 161.123  1.00 92.51           N  
ATOM   3881  CA  ALA A 510     193.104 158.832 161.583  1.00 92.51           C  
ATOM   3882  C   ALA A 510     193.890 158.379 162.809  1.00 92.51           C  
ATOM   3883  O   ALA A 510     195.002 158.845 163.072  1.00 92.51           O  
ATOM   3884  CB  ALA A 510     193.209 157.788 160.472  1.00 92.51           C  
ATOM   3885  N   ASP A 511     193.298 157.455 163.569  1.00 93.98           N  
ATOM   3886  CA  ASP A 511     193.895 157.047 164.830  1.00 93.98           C  
ATOM   3887  C   ASP A 511     194.008 155.537 164.989  1.00 93.98           C  
ATOM   3888  O   ASP A 511     194.504 155.081 166.025  1.00 93.98           O  
ATOM   3889  CB  ASP A 511     193.100 157.627 166.010  1.00 93.98           C  
ATOM   3890  CG  ASP A 511     191.602 157.557 165.795  1.00 93.98           C  
ATOM   3891  OD1 ASP A 511     191.176 157.102 164.713  1.00 93.98           O  
ATOM   3892  OD2 ASP A 511     190.849 157.963 166.705  1.00 93.98           O  
ATOM   3893  N   PHE A 512     193.564 154.753 164.003  1.00 87.32           N  
ATOM   3894  CA  PHE A 512     193.830 153.313 163.952  1.00 87.32           C  
ATOM   3895  C   PHE A 512     193.275 152.586 165.176  1.00 87.32           C  
ATOM   3896  O   PHE A 512     193.872 151.630 165.674  1.00 87.32           O  
ATOM   3897  CB  PHE A 512     195.323 153.031 163.767  1.00 87.32           C  
ATOM   3898  CG  PHE A 512     195.816 153.306 162.373  1.00 87.32           C  
ATOM   3899  CD1 PHE A 512     195.427 152.498 161.317  1.00 87.32           C  
ATOM   3900  CD2 PHE A 512     196.664 154.371 162.117  1.00 87.32           C  
ATOM   3901  CE1 PHE A 512     195.873 152.749 160.032  1.00 87.32           C  
ATOM   3902  CE2 PHE A 512     197.115 154.625 160.835  1.00 87.32           C  
ATOM   3903  CZ  PHE A 512     196.719 153.813 159.792  1.00 87.32           C  
ATOM   3904  N   ASP A 513     192.122 153.040 165.671  1.00102.87           N  
ATOM   3905  CA  ASP A 513     191.533 152.477 166.882  1.00102.87           C  
ATOM   3906  C   ASP A 513     190.157 151.872 166.631  1.00102.87           C  
ATOM   3907  O   ASP A 513     189.359 151.741 167.565  1.00102.87           O  
ATOM   3908  CB  ASP A 513     191.450 153.543 167.975  1.00102.87           C  
ATOM   3909  CG  ASP A 513     190.700 154.783 167.525  1.00102.87           C  
ATOM   3910  OD1 ASP A 513     190.313 154.853 166.340  1.00102.87           O  
ATOM   3911  OD2 ASP A 513     190.497 155.689 168.360  1.00102.87           O  
ATOM   3912  N   GLY A 514     189.863 151.500 165.388  1.00102.26           N  
ATOM   3913  CA  GLY A 514     188.540 151.058 164.996  1.00102.26           C  
ATOM   3914  C   GLY A 514     187.795 152.010 164.091  1.00102.26           C  
ATOM   3915  O   GLY A 514     186.647 151.722 163.733  1.00102.26           O  
ATOM   3916  N   ASP A 515     188.399 153.132 163.711  1.00 91.28           N  
ATOM   3917  CA  ASP A 515     187.817 153.976 162.680  1.00 91.28           C  
ATOM   3918  C   ASP A 515     187.834 153.254 161.338  1.00 91.28           C  
ATOM   3919  O   ASP A 515     188.756 152.495 161.026  1.00 91.28           O  
ATOM   3920  CB  ASP A 515     188.580 155.296 162.572  1.00 91.28           C  
ATOM   3921  CG  ASP A 515     190.081 155.097 162.495  1.00 91.28           C  
ATOM   3922  OD1 ASP A 515     190.554 153.989 162.825  1.00 91.28           O  
ATOM   3923  OD2 ASP A 515     190.789 156.047 162.100  1.00 91.28           O  
ATOM   3924  N   GLU A 516     186.800 153.495 160.540  1.00 82.60           N  
ATOM   3925  CA  GLU A 516     186.650 152.843 159.249  1.00 82.60           C  
ATOM   3926  C   GLU A 516     186.550 153.899 158.157  1.00 82.60           C  
ATOM   3927  O   GLU A 516     185.905 154.937 158.337  1.00 82.60           O  
ATOM   3928  CB  GLU A 516     185.424 151.918 159.239  1.00 82.60           C  
ATOM   3929  CG  GLU A 516     184.089 152.618 159.419  1.00 82.60           C  
ATOM   3930  CD  GLU A 516     182.937 151.641 159.547  1.00 82.60           C  
ATOM   3931  OE1 GLU A 516     183.196 150.422 159.622  1.00 82.60           O  
ATOM   3932  OE2 GLU A 516     181.773 152.093 159.577  1.00 82.60           O  
ATOM   3933  N   MET A 517     187.205 153.633 157.034  1.00 73.93           N  
ATOM   3934  CA  MET A 517     187.233 154.538 155.896  1.00 73.93           C  
ATOM   3935  C   MET A 517     186.357 153.985 154.780  1.00 73.93           C  
ATOM   3936  O   MET A 517     185.971 152.813 154.784  1.00 73.93           O  
ATOM   3937  CB  MET A 517     188.673 154.731 155.410  1.00 73.93           C  
ATOM   3938  CG  MET A 517     189.612 155.260 156.486  1.00 73.93           C  
ATOM   3939  SD  MET A 517     189.370 156.998 156.886  1.00 73.93           S  
ATOM   3940  CE  MET A 517     190.225 157.770 155.520  1.00 73.93           C  
ATOM   3941  N   ASN A 518     186.041 154.841 153.809  1.00 71.29           N  
ATOM   3942  CA  ASN A 518     185.366 154.395 152.599  1.00 71.29           C  
ATOM   3943  C   ASN A 518     186.153 154.809 151.364  1.00 71.29           C  
ATOM   3944  O   ASN A 518     186.687 155.920 151.296  1.00 71.29           O  
ATOM   3945  CB  ASN A 518     183.938 154.954 152.521  1.00 71.29           C  
ATOM   3946  CG  ASN A 518     183.877 156.449 152.778  1.00 71.29           C  
ATOM   3947  OD1 ASN A 518     184.897 157.096 153.013  1.00 71.29           O  
ATOM   3948  ND2 ASN A 518     182.673 157.006 152.729  1.00 71.29           N  
ATOM   3949  N   LEU A 519     186.227 153.902 150.394  1.00 66.67           N  
ATOM   3950  CA  LEU A 519     186.917 154.140 149.136  1.00 66.67           C  
ATOM   3951  C   LEU A 519     185.912 154.239 147.995  1.00 66.67           C  
ATOM   3952  O   LEU A 519     184.829 153.650 148.049  1.00 66.67           O  
ATOM   3953  CB  LEU A 519     187.935 153.029 148.847  1.00 66.67           C  
ATOM   3954  CG  LEU A 519     187.461 151.788 148.084  1.00 66.67           C  
ATOM   3955  CD1 LEU A 519     188.649 150.952 147.636  1.00 66.67           C  
ATOM   3956  CD2 LEU A 519     186.510 150.954 148.931  1.00 66.67           C  
ATOM   3957  N   HIS A 520     186.275 154.994 146.959  1.00 67.13           N  
ATOM   3958  CA  HIS A 520     185.440 155.125 145.775  1.00 67.13           C  
ATOM   3959  C   HIS A 520     186.265 154.770 144.546  1.00 67.13           C  
ATOM   3960  O   HIS A 520     187.497 154.830 144.564  1.00 67.13           O  
ATOM   3961  CB  HIS A 520     184.867 156.543 145.637  1.00 67.13           C  
ATOM   3962  CG  HIS A 520     183.847 156.891 146.677  1.00 67.13           C  
ATOM   3963  ND1 HIS A 520     183.448 158.187 146.923  1.00 67.13           N  
ATOM   3964  CD2 HIS A 520     183.140 156.111 147.530  1.00 67.13           C  
ATOM   3965  CE1 HIS A 520     182.542 158.191 147.885  1.00 67.13           C  
ATOM   3966  NE2 HIS A 520     182.338 156.945 148.271  1.00 67.13           N  
ATOM   3967  N   VAL A 521     185.576 154.399 143.471  1.00 65.15           N  
ATOM   3968  CA  VAL A 521     186.240 154.162 142.190  1.00 65.15           C  
ATOM   3969  C   VAL A 521     185.479 154.856 141.065  1.00 65.15           C  
ATOM   3970  O   VAL A 521     184.267 154.640 140.915  1.00 65.15           O  
ATOM   3971  CB  VAL A 521     186.397 152.655 141.920  1.00 65.15           C  
ATOM   3972  CG1 VAL A 521     185.074 151.922 142.122  1.00 65.15           C  
ATOM   3973  CG2 VAL A 521     186.938 152.417 140.518  1.00 65.15           C  
ATOM   3974  N   PRO A 522     186.123 155.703 140.265  1.00 69.58           N  
ATOM   3975  CA  PRO A 522     185.427 156.285 139.113  1.00 69.58           C  
ATOM   3976  C   PRO A 522     185.245 155.240 138.024  1.00 69.58           C  
ATOM   3977  O   PRO A 522     186.005 154.273 137.931  1.00 69.58           O  
ATOM   3978  CB  PRO A 522     186.369 157.406 138.655  1.00 69.58           C  
ATOM   3979  CG  PRO A 522     187.238 157.687 139.845  1.00 69.58           C  
ATOM   3980  CD  PRO A 522     187.418 156.358 140.511  1.00 69.58           C  
ATOM   3981  N   GLN A 523     184.223 155.434 137.194  1.00 72.20           N  
ATOM   3982  CA  GLN A 523     183.912 154.466 136.144  1.00 72.20           C  
ATOM   3983  C   GLN A 523     183.676 155.158 134.807  1.00 72.20           C  
ATOM   3984  O   GLN A 523     182.682 154.913 134.120  1.00 72.20           O  
ATOM   3985  CB  GLN A 523     182.711 153.609 136.530  1.00 72.20           C  
ATOM   3986  CG  GLN A 523     183.035 152.541 137.558  1.00 72.20           C  
ATOM   3987  CD  GLN A 523     181.919 151.534 137.727  1.00 72.20           C  
ATOM   3988  OE1 GLN A 523     180.826 151.702 137.185  1.00 72.20           O  
ATOM   3989  NE2 GLN A 523     182.193 150.469 138.471  1.00 72.20           N  
ATOM   3990  N   THR A 524     184.590 156.037 134.414  1.00 80.37           N  
ATOM   3991  CA  THR A 524     184.761 156.403 133.015  1.00 80.37           C  
ATOM   3992  C   THR A 524     186.179 156.039 132.578  1.00 80.37           C  
ATOM   3993  O   THR A 524     186.944 155.423 133.325  1.00 80.37           O  
ATOM   3994  CB  THR A 524     184.471 157.890 132.795  1.00 80.37           C  
ATOM   3995  OG1 THR A 524     185.482 158.678 133.435  1.00 80.37           O  
ATOM   3996  CG2 THR A 524     183.108 158.260 133.355  1.00 80.37           C  
ATOM   3997  N   GLU A 525     186.530 156.431 131.356  1.00 93.73           N  
ATOM   3998  CA  GLU A 525     187.922 156.521 130.942  1.00 93.73           C  
ATOM   3999  C   GLU A 525     188.443 157.950 130.975  1.00 93.73           C  
ATOM   4000  O   GLU A 525     189.626 158.174 130.698  1.00 93.73           O  
ATOM   4001  CB  GLU A 525     188.098 155.935 129.537  1.00 93.73           C  
ATOM   4002  CG  GLU A 525     187.757 154.456 129.436  1.00 93.73           C  
ATOM   4003  CD  GLU A 525     188.729 153.578 130.200  1.00 93.73           C  
ATOM   4004  OE1 GLU A 525     189.937 153.894 130.209  1.00 93.73           O  
ATOM   4005  OE2 GLU A 525     188.285 152.572 130.792  1.00 93.73           O  
ATOM   4006  N   GLU A 526     187.588 158.917 131.307  1.00 86.14           N  
ATOM   4007  CA  GLU A 526     187.954 160.325 131.402  1.00 86.14           C  
ATOM   4008  C   GLU A 526     188.148 160.792 132.841  1.00 86.14           C  
ATOM   4009  O   GLU A 526     189.166 161.414 133.159  1.00 86.14           O  
ATOM   4010  CB  GLU A 526     186.889 161.185 130.710  1.00 86.14           C  
ATOM   4011  CG  GLU A 526     187.240 162.660 130.607  1.00 86.14           C  
ATOM   4012  CD  GLU A 526     186.700 163.471 131.766  1.00 86.14           C  
ATOM   4013  OE1 GLU A 526     185.695 163.043 132.371  1.00 86.14           O  
ATOM   4014  OE2 GLU A 526     187.282 164.532 132.073  1.00 86.14           O  
ATOM   4015  N   ALA A 527     187.185 160.504 133.720  1.00 75.46           N  
ATOM   4016  CA  ALA A 527     187.312 160.883 135.123  1.00 75.46           C  
ATOM   4017  C   ALA A 527     188.360 160.063 135.862  1.00 75.46           C  
ATOM   4018  O   ALA A 527     188.804 160.479 136.938  1.00 75.46           O  
ATOM   4019  CB  ALA A 527     185.961 160.753 135.829  1.00 75.46           C  
ATOM   4020  N   ARG A 528     188.764 158.912 135.320  1.00 81.10           N  
ATOM   4021  CA  ARG A 528     189.913 158.209 135.880  1.00 81.10           C  
ATOM   4022  C   ARG A 528     191.188 159.027 135.721  1.00 81.10           C  
ATOM   4023  O   ARG A 528     192.063 158.993 136.594  1.00 81.10           O  
ATOM   4024  CB  ARG A 528     190.051 156.838 135.214  1.00 81.10           C  
ATOM   4025  CG  ARG A 528     191.027 155.886 135.888  1.00 81.10           C  
ATOM   4026  CD  ARG A 528     192.377 155.895 135.190  1.00 81.10           C  
ATOM   4027  NE  ARG A 528     192.256 155.593 133.767  1.00 81.10           N  
ATOM   4028  CZ  ARG A 528     192.169 154.364 133.268  1.00 81.10           C  
ATOM   4029  NH1 ARG A 528     192.071 154.183 131.958  1.00 81.10           N  
ATOM   4030  NH2 ARG A 528     192.190 153.314 134.078  1.00 81.10           N  
ATOM   4031  N   ALA A 529     191.308 159.767 134.617  1.00 82.32           N  
ATOM   4032  CA  ALA A 529     192.418 160.694 134.432  1.00 82.32           C  
ATOM   4033  C   ALA A 529     192.234 161.974 135.238  1.00 82.32           C  
ATOM   4034  O   ALA A 529     193.220 162.642 135.570  1.00 82.32           O  
ATOM   4035  CB  ALA A 529     192.582 161.030 132.950  1.00 82.32           C  
ATOM   4036  N   GLU A 530     190.986 162.326 135.552  1.00 84.11           N  
ATOM   4037  CA  GLU A 530     190.709 163.539 136.317  1.00 84.11           C  
ATOM   4038  C   GLU A 530     191.242 163.446 137.742  1.00 84.11           C  
ATOM   4039  O   GLU A 530     191.711 164.447 138.299  1.00 84.11           O  
ATOM   4040  CB  GLU A 530     189.205 163.814 136.323  1.00 84.11           C  
ATOM   4041  CG  GLU A 530     188.808 165.121 136.987  1.00 84.11           C  
ATOM   4042  CD  GLU A 530     189.133 166.330 136.131  1.00 84.11           C  
ATOM   4043  OE1 GLU A 530     189.145 166.196 134.890  1.00 84.11           O  
ATOM   4044  OE2 GLU A 530     189.373 167.415 136.700  1.00 84.11           O  
ATOM   4045  N   ALA A 531     191.186 162.261 138.351  1.00 78.41           N  
ATOM   4046  CA  ALA A 531     191.470 162.156 139.778  1.00 78.41           C  
ATOM   4047  C   ALA A 531     192.963 162.195 140.077  1.00 78.41           C  
ATOM   4048  O   ALA A 531     193.360 162.658 141.152  1.00 78.41           O  
ATOM   4049  CB  ALA A 531     190.857 160.873 140.344  1.00 78.41           C  
ATOM   4050  N   ILE A 532     193.801 161.715 139.158  1.00 71.99           N  
ATOM   4051  CA  ILE A 532     195.243 161.734 139.389  1.00 71.99           C  
ATOM   4052  C   ILE A 532     195.787 163.151 139.251  1.00 71.99           C  
ATOM   4053  O   ILE A 532     196.454 163.671 140.154  1.00 71.99           O  
ATOM   4054  CB  ILE A 532     195.954 160.761 138.430  1.00 71.99           C  
ATOM   4055  CG1 ILE A 532     195.607 159.315 138.786  1.00 71.99           C  
ATOM   4056  CG2 ILE A 532     197.460 160.975 138.472  1.00 71.99           C  
ATOM   4057  CD1 ILE A 532     196.026 158.912 140.183  1.00 71.99           C  
ATOM   4058  N   ASN A 533     195.506 163.797 138.118  1.00 75.52           N  
ATOM   4059  CA  ASN A 533     196.111 165.076 137.761  1.00 75.52           C  
ATOM   4060  C   ASN A 533     195.659 166.234 138.644  1.00 75.52           C  
ATOM   4061  O   ASN A 533     196.235 167.323 138.539  1.00 75.52           O  
ATOM   4062  CB  ASN A 533     195.810 165.403 136.297  1.00 75.52           C  
ATOM   4063  CG  ASN A 533     196.489 164.448 135.335  1.00 75.52           C  
ATOM   4064  OD1 ASN A 533     195.833 163.644 134.673  1.00 75.52           O  
ATOM   4065  ND2 ASN A 533     197.812 164.530 135.255  1.00 75.52           N  
ATOM   4066  N   LEU A 534     194.665 166.040 139.498  1.00 74.02           N  
ATOM   4067  CA  LEU A 534     194.318 167.076 140.467  1.00 74.02           C  
ATOM   4068  C   LEU A 534     194.292 166.578 141.904  1.00 74.02           C  
ATOM   4069  O   LEU A 534     194.726 167.303 142.803  1.00 74.02           O  
ATOM   4070  CB  LEU A 534     192.956 167.696 140.112  1.00 74.02           C  
ATOM   4071  CG  LEU A 534     192.922 168.572 138.858  1.00 74.02           C  
ATOM   4072  CD1 LEU A 534     191.501 169.011 138.548  1.00 74.02           C  
ATOM   4073  CD2 LEU A 534     193.836 169.777 139.017  1.00 74.02           C  
ATOM   4074  N   MET A 535     193.798 165.365 142.148  1.00 78.08           N  
ATOM   4075  CA  MET A 535     193.623 164.861 143.504  1.00 78.08           C  
ATOM   4076  C   MET A 535     194.630 163.774 143.852  1.00 78.08           C  
ATOM   4077  O   MET A 535     194.507 163.141 144.907  1.00 78.08           O  
ATOM   4078  CB  MET A 535     192.197 164.342 143.700  1.00 78.08           C  
ATOM   4079  CG  MET A 535     191.121 165.382 143.445  1.00 78.08           C  
ATOM   4080  SD  MET A 535     189.465 164.763 143.789  1.00 78.08           S  
ATOM   4081  CE  MET A 535     189.257 163.610 142.436  1.00 78.08           C  
ATOM   4082  N   GLY A 536     195.620 163.541 142.994  1.00 73.74           N  
ATOM   4083  CA  GLY A 536     196.736 162.700 143.375  1.00 73.74           C  
ATOM   4084  C   GLY A 536     197.573 163.346 144.462  1.00 73.74           C  
ATOM   4085  O   GLY A 536     197.703 164.568 144.541  1.00 73.74           O  
ATOM   4086  N   VAL A 537     198.150 162.502 145.321  1.00 70.56           N  
ATOM   4087  CA  VAL A 537     198.878 163.013 146.475  1.00 70.56           C  
ATOM   4088  C   VAL A 537     200.206 163.645 146.075  1.00 70.56           C  
ATOM   4089  O   VAL A 537     200.783 164.409 146.858  1.00 70.56           O  
ATOM   4090  CB  VAL A 537     199.092 161.887 147.505  1.00 70.56           C  
ATOM   4091  CG1 VAL A 537     200.173 160.929 147.032  1.00 70.56           C  
ATOM   4092  CG2 VAL A 537     199.422 162.458 148.880  1.00 70.56           C  
ATOM   4093  N   LYS A 538     200.707 163.362 144.869  1.00 70.12           N  
ATOM   4094  CA  LYS A 538     201.899 164.058 144.394  1.00 70.12           C  
ATOM   4095  C   LYS A 538     201.625 165.534 144.137  1.00 70.12           C  
ATOM   4096  O   LYS A 538     202.535 166.361 144.258  1.00 70.12           O  
ATOM   4097  CB  LYS A 538     202.431 163.401 143.121  1.00 70.12           C  
ATOM   4098  CG  LYS A 538     202.910 161.973 143.294  1.00 70.12           C  
ATOM   4099  CD  LYS A 538     203.638 161.501 142.045  1.00 70.12           C  
ATOM   4100  CE  LYS A 538     204.135 160.075 142.194  1.00 70.12           C  
ATOM   4101  NZ  LYS A 538     203.019 159.098 142.093  1.00 70.12           N  
ATOM   4102  N   ASN A 539     200.387 165.886 143.800  1.00 77.16           N  
ATOM   4103  CA  ASN A 539     200.033 167.272 143.532  1.00 77.16           C  
ATOM   4104  C   ASN A 539     199.643 168.044 144.784  1.00 77.16           C  
ATOM   4105  O   ASN A 539     199.450 169.262 144.705  1.00 77.16           O  
ATOM   4106  CB  ASN A 539     198.885 167.338 142.518  1.00 77.16           C  
ATOM   4107  CG  ASN A 539     199.288 166.828 141.149  1.00 77.16           C  
ATOM   4108  OD1 ASN A 539     200.378 167.125 140.659  1.00 77.16           O  
ATOM   4109  ND2 ASN A 539     198.408 166.056 140.522  1.00 77.16           N  
ATOM   4110  N   ASN A 540     199.522 167.376 145.928  1.00 74.74           N  
ATOM   4111  CA  ASN A 540     198.917 167.970 147.113  1.00 74.74           C  
ATOM   4112  C   ASN A 540     199.770 167.718 148.347  1.00 74.74           C  
ATOM   4113  O   ASN A 540     199.257 167.383 149.419  1.00 74.74           O  
ATOM   4114  CB  ASN A 540     197.500 167.441 147.323  1.00 74.74           C  
ATOM   4115  CG  ASN A 540     196.574 167.779 146.170  1.00 74.74           C  
ATOM   4116  OD1 ASN A 540     196.082 166.891 145.473  1.00 74.74           O  
ATOM   4117  ND2 ASN A 540     196.331 169.068 145.963  1.00 74.74           N  
ATOM   4118  N   LEU A 541     201.091 167.873 148.223  1.00 78.57           N  
ATOM   4119  CA  LEU A 541     201.928 167.887 149.417  1.00 78.57           C  
ATOM   4120  C   LEU A 541     201.736 169.161 150.227  1.00 78.57           C  
ATOM   4121  O   LEU A 541     202.017 169.165 151.431  1.00 78.57           O  
ATOM   4122  CB  LEU A 541     203.405 167.734 149.048  1.00 78.57           C  
ATOM   4123  CG  LEU A 541     203.944 166.340 148.715  1.00 78.57           C  
ATOM   4124  CD1 LEU A 541     203.590 165.934 147.296  1.00 78.57           C  
ATOM   4125  CD2 LEU A 541     205.450 166.289 148.930  1.00 78.57           C  
ATOM   4126  N   LEU A 542     201.268 170.232 149.596  1.00 90.99           N  
ATOM   4127  CA  LEU A 542     201.099 171.522 150.247  1.00 90.99           C  
ATOM   4128  C   LEU A 542     199.624 171.734 150.558  1.00 90.99           C  
ATOM   4129  O   LEU A 542     198.758 171.437 149.731  1.00 90.99           O  
ATOM   4130  CB  LEU A 542     201.620 172.656 149.363  1.00 90.99           C  
ATOM   4131  CG  LEU A 542     203.118 172.648 149.050  1.00 90.99           C  
ATOM   4132  CD1 LEU A 542     203.456 173.709 148.013  1.00 90.99           C  
ATOM   4133  CD2 LEU A 542     203.943 172.840 150.313  1.00 90.99           C  
ATOM   4134  N   THR A 543     199.341 172.245 151.748  1.00 98.79           N  
ATOM   4135  CA  THR A 543     197.958 172.589 152.023  1.00 98.79           C  
ATOM   4136  C   THR A 543     197.598 173.931 151.385  1.00 98.79           C  
ATOM   4137  O   THR A 543     198.437 174.832 151.299  1.00 98.79           O  
ATOM   4138  CB  THR A 543     197.708 172.647 153.529  1.00 98.79           C  
ATOM   4139  OG1 THR A 543     196.350 173.033 153.778  1.00 98.79           O  
ATOM   4140  CG2 THR A 543     198.649 173.640 154.200  1.00 98.79           C  
ATOM   4141  N   PRO A 544     196.357 174.081 150.912  1.00100.18           N  
ATOM   4142  CA  PRO A 544     195.918 175.387 150.400  1.00100.18           C  
ATOM   4143  C   PRO A 544     195.593 176.381 151.498  1.00100.18           C  
ATOM   4144  O   PRO A 544     195.330 177.553 151.195  1.00100.18           O  
ATOM   4145  CB  PRO A 544     194.663 175.036 149.593  1.00100.18           C  
ATOM   4146  CG  PRO A 544     194.143 173.810 150.262  1.00100.18           C  
ATOM   4147  CD  PRO A 544     195.349 173.031 150.691  1.00100.18           C  
ATOM   4148  N   LYS A 545     195.600 175.942 152.758  1.00105.95           N  
ATOM   4149  CA  LYS A 545     195.334 176.839 153.875  1.00105.95           C  
ATOM   4150  C   LYS A 545     196.408 177.915 153.977  1.00105.95           C  
ATOM   4151  O   LYS A 545     196.105 179.107 154.097  1.00105.95           O  
ATOM   4152  CB  LYS A 545     195.240 176.036 155.173  1.00105.95           C  
ATOM   4153  CG  LYS A 545     194.931 176.869 156.402  1.00105.95           C  
ATOM   4154  CD  LYS A 545     194.672 175.990 157.615  1.00105.95           C  
ATOM   4155  CE  LYS A 545     195.961 175.400 158.159  1.00105.95           C  
ATOM   4156  NZ  LYS A 545     195.735 174.656 159.429  1.00105.95           N  
ATOM   4157  N   SER A 546     197.674 177.506 153.928  1.00100.76           N  
ATOM   4158  CA  SER A 546     198.800 178.421 154.058  1.00100.76           C  
ATOM   4159  C   SER A 546     199.887 178.228 153.011  1.00100.76           C  
ATOM   4160  O   SER A 546     200.645 179.175 152.766  1.00100.76           O  
ATOM   4161  CB  SER A 546     199.435 178.296 155.452  1.00100.76           C  
ATOM   4162  OG  SER A 546     200.071 177.041 155.612  1.00100.76           O  
ATOM   4163  N   GLY A 547     199.994 177.059 152.388  1.00101.37           N  
ATOM   4164  CA  GLY A 547     201.116 176.753 151.527  1.00101.37           C  
ATOM   4165  C   GLY A 547     202.201 175.915 152.160  1.00101.37           C  
ATOM   4166  O   GLY A 547     203.274 175.770 151.563  1.00101.37           O  
ATOM   4167  N   GLU A 548     201.960 175.364 153.346  1.00104.19           N  
ATOM   4168  CA  GLU A 548     202.836 174.575 154.202  1.00104.19           C  
ATOM   4169  C   GLU A 548     202.760 173.098 153.814  1.00104.19           C  
ATOM   4170  O   GLU A 548     201.690 172.609 153.439  1.00104.19           O  
ATOM   4171  CB  GLU A 548     202.440 174.758 155.667  1.00104.19           C  
ATOM   4172  CG  GLU A 548     203.492 174.363 156.691  1.00104.19           C  
ATOM   4173  CD  GLU A 548     203.473 172.883 157.004  1.00104.19           C  
ATOM   4174  OE1 GLU A 548     202.392 172.269 156.885  1.00104.19           O  
ATOM   4175  OE2 GLU A 548     204.534 172.334 157.368  1.00104.19           O  
ATOM   4176  N   PRO A 549     203.881 172.373 153.892  1.00100.24           N  
ATOM   4177  CA  PRO A 549     203.855 170.929 153.612  1.00100.24           C  
ATOM   4178  C   PRO A 549     203.150 170.128 154.693  1.00100.24           C  
ATOM   4179  O   PRO A 549     203.629 170.041 155.828  1.00100.24           O  
ATOM   4180  CB  PRO A 549     205.343 170.560 153.526  1.00100.24           C  
ATOM   4181  CG  PRO A 549     206.047 171.638 154.285  1.00100.24           C  
ATOM   4182  CD  PRO A 549     205.257 172.881 154.020  1.00100.24           C  
ATOM   4183  N   ILE A 550     202.024 169.515 154.340  1.00 94.45           N  
ATOM   4184  CA  ILE A 550     201.128 168.933 155.333  1.00 94.45           C  
ATOM   4185  C   ILE A 550     201.466 167.471 155.609  1.00 94.45           C  
ATOM   4186  O   ILE A 550     201.369 167.015 156.751  1.00 94.45           O  
ATOM   4187  CB  ILE A 550     199.662 169.108 154.881  1.00 94.45           C  
ATOM   4188  CG1 ILE A 550     198.697 168.614 155.962  1.00 94.45           C  
ATOM   4189  CG2 ILE A 550     199.412 168.420 153.544  1.00 94.45           C  
ATOM   4190  CD1 ILE A 550     198.766 169.409 157.248  1.00 94.45           C  
ATOM   4191  N   ILE A 551     201.872 166.709 154.596  1.00 88.25           N  
ATOM   4192  CA  ILE A 551     202.321 165.340 154.825  1.00 88.25           C  
ATOM   4193  C   ILE A 551     203.777 165.373 155.272  1.00 88.25           C  
ATOM   4194  O   ILE A 551     204.605 166.084 154.690  1.00 88.25           O  
ATOM   4195  CB  ILE A 551     202.121 164.479 153.565  1.00 88.25           C  
ATOM   4196  CG1 ILE A 551     202.787 165.112 152.336  1.00 88.25           C  
ATOM   4197  CG2 ILE A 551     200.639 164.247 153.309  1.00 88.25           C  
ATOM   4198  CD1 ILE A 551     204.148 164.538 151.995  1.00 88.25           C  
ATOM   4199  N   ALA A 552     204.087 164.631 156.330  1.00 90.21           N  
ATOM   4200  CA  ALA A 552     205.417 164.667 156.926  1.00 90.21           C  
ATOM   4201  C   ALA A 552     205.669 163.356 157.664  1.00 90.21           C  
ATOM   4202  O   ALA A 552     204.884 162.406 157.571  1.00 90.21           O  
ATOM   4203  CB  ALA A 552     205.561 165.877 157.853  1.00 90.21           C  
ATOM   4204  N   ALA A 553     206.780 163.310 158.396  1.00 97.81           N  
ATOM   4205  CA  ALA A 553     207.035 162.220 159.328  1.00 97.81           C  
ATOM   4206  C   ALA A 553     206.155 162.401 160.559  1.00 97.81           C  
ATOM   4207  O   ALA A 553     206.072 163.500 161.117  1.00 97.81           O  
ATOM   4208  CB  ALA A 553     208.511 162.193 159.718  1.00 97.81           C  
ATOM   4209  N   THR A 554     205.492 161.328 160.980  1.00102.88           N  
ATOM   4210  CA  THR A 554     204.659 161.371 162.172  1.00102.88           C  
ATOM   4211  C   THR A 554     205.455 161.056 163.440  1.00102.88           C  
ATOM   4212  O   THR A 554     206.684 160.947 163.434  1.00102.88           O  
ATOM   4213  CB  THR A 554     203.478 160.417 162.015  1.00102.88           C  
ATOM   4214  OG1 THR A 554     203.960 159.070 161.926  1.00102.88           O  
ATOM   4215  CG2 THR A 554     202.689 160.752 160.758  1.00102.88           C  
ATOM   4216  N   GLN A 555     204.724 160.891 164.544  1.00111.63           N  
ATOM   4217  CA  GLN A 555     205.222 160.983 165.914  1.00111.63           C  
ATOM   4218  C   GLN A 555     206.302 159.974 166.300  1.00111.63           C  
ATOM   4219  O   GLN A 555     206.770 159.991 167.443  1.00111.63           O  
ATOM   4220  CB  GLN A 555     204.046 160.859 166.885  1.00111.63           C  
ATOM   4221  CG  GLN A 555     203.289 159.549 166.781  1.00111.63           C  
ATOM   4222  CD  GLN A 555     203.805 158.511 167.753  1.00111.63           C  
ATOM   4223  OE1 GLN A 555     204.193 158.835 168.874  1.00111.63           O  
ATOM   4224  NE2 GLN A 555     203.823 157.256 167.324  1.00111.63           N  
ATOM   4225  N   ASP A 556     206.706 159.087 165.392  1.00102.62           N  
ATOM   4226  CA  ASP A 556     207.890 158.279 165.668  1.00102.62           C  
ATOM   4227  C   ASP A 556     208.848 158.108 164.500  1.00102.62           C  
ATOM   4228  O   ASP A 556     209.932 157.556 164.709  1.00102.62           O  
ATOM   4229  CB  ASP A 556     207.478 156.887 166.172  1.00102.62           C  
ATOM   4230  CG  ASP A 556     206.562 156.163 165.207  1.00102.62           C  
ATOM   4231  OD1 ASP A 556     206.151 156.773 164.198  1.00102.62           O  
ATOM   4232  OD2 ASP A 556     206.255 154.979 165.459  1.00102.62           O  
ATOM   4233  N   PHE A 557     208.504 158.544 163.289  1.00 93.52           N  
ATOM   4234  CA  PHE A 557     209.504 158.620 162.232  1.00 93.52           C  
ATOM   4235  C   PHE A 557     210.561 159.681 162.516  1.00 93.52           C  
ATOM   4236  O   PHE A 557     211.674 159.588 161.986  1.00 93.52           O  
ATOM   4237  CB  PHE A 557     208.831 158.885 160.885  1.00 93.52           C  
ATOM   4238  CG  PHE A 557     208.095 157.698 160.332  1.00 93.52           C  
ATOM   4239  CD1 PHE A 557     208.418 156.414 160.741  1.00 93.52           C  
ATOM   4240  CD2 PHE A 557     207.086 157.864 159.398  1.00 93.52           C  
ATOM   4241  CE1 PHE A 557     207.743 155.319 160.234  1.00 93.52           C  
ATOM   4242  CE2 PHE A 557     206.409 156.773 158.885  1.00 93.52           C  
ATOM   4243  CZ  PHE A 557     206.738 155.499 159.304  1.00 93.52           C  
ATOM   4244  N   ILE A 558     210.237 160.683 163.335  1.00 98.18           N  
ATOM   4245  CA  ILE A 558     211.252 161.614 163.823  1.00 98.18           C  
ATOM   4246  C   ILE A 558     212.234 160.902 164.747  1.00 98.18           C  
ATOM   4247  O   ILE A 558     213.453 160.957 164.542  1.00 98.18           O  
ATOM   4248  CB  ILE A 558     210.592 162.818 164.521  1.00 98.18           C  
ATOM   4249  CG1 ILE A 558     210.009 163.790 163.493  1.00 98.18           C  
ATOM   4250  CG2 ILE A 558     211.592 163.529 165.423  1.00 98.18           C  
ATOM   4251  CD1 ILE A 558     208.538 163.584 163.219  1.00 98.18           C  
ATOM   4252  N   THR A 559     211.724 160.217 165.773  1.00 91.40           N  
ATOM   4253  CA  THR A 559     212.595 159.614 166.775  1.00 91.40           C  
ATOM   4254  C   THR A 559     213.342 158.392 166.258  1.00 91.40           C  
ATOM   4255  O   THR A 559     214.265 157.925 166.933  1.00 91.40           O  
ATOM   4256  CB  THR A 559     211.794 159.231 168.023  1.00 91.40           C  
ATOM   4257  OG1 THR A 559     212.695 158.885 169.083  1.00 91.40           O  
ATOM   4258  CG2 THR A 559     210.888 158.049 167.735  1.00 91.40           C  
ATOM   4259  N   GLY A 560     212.977 157.866 165.092  1.00 89.21           N  
ATOM   4260  CA  GLY A 560     213.830 156.902 164.428  1.00 89.21           C  
ATOM   4261  C   GLY A 560     214.995 157.607 163.767  1.00 89.21           C  
ATOM   4262  O   GLY A 560     216.152 157.205 163.927  1.00 89.21           O  
ATOM   4263  N   SER A 561     214.695 158.667 163.020  1.00 93.29           N  
ATOM   4264  CA  SER A 561     215.707 159.453 162.328  1.00 93.29           C  
ATOM   4265  C   SER A 561     216.441 160.412 163.257  1.00 93.29           C  
ATOM   4266  O   SER A 561     217.366 161.099 162.810  1.00 93.29           O  
ATOM   4267  CB  SER A 561     215.071 160.235 161.175  1.00 93.29           C  
ATOM   4268  OG  SER A 561     214.168 161.214 161.658  1.00 93.29           O  
ATOM   4269  N   TYR A 562     216.054 160.474 164.532  1.00 90.09           N  
ATOM   4270  CA  TYR A 562     216.779 161.250 165.531  1.00 90.09           C  
ATOM   4271  C   TYR A 562     217.923 160.471 166.168  1.00 90.09           C  
ATOM   4272  O   TYR A 562     219.006 161.029 166.375  1.00 90.09           O  
ATOM   4273  CB  TYR A 562     215.819 161.734 166.620  1.00 90.09           C  
ATOM   4274  CG  TYR A 562     216.490 162.530 167.716  1.00 90.09           C  
ATOM   4275  CD1 TYR A 562     216.934 163.826 167.489  1.00 90.09           C  
ATOM   4276  CD2 TYR A 562     216.684 161.983 168.978  1.00 90.09           C  
ATOM   4277  CE1 TYR A 562     217.548 164.557 168.489  1.00 90.09           C  
ATOM   4278  CE2 TYR A 562     217.298 162.706 169.984  1.00 90.09           C  
ATOM   4279  CZ  TYR A 562     217.727 163.992 169.734  1.00 90.09           C  
ATOM   4280  OH  TYR A 562     218.339 164.713 170.733  1.00 90.09           O  
ATOM   4281  N   LEU A 563     217.711 159.192 166.490  1.00 85.10           N  
ATOM   4282  CA  LEU A 563     218.786 158.409 167.087  1.00 85.10           C  
ATOM   4283  C   LEU A 563     219.880 158.087 166.080  1.00 85.10           C  
ATOM   4284  O   LEU A 563     221.015 157.809 166.482  1.00 85.10           O  
ATOM   4285  CB  LEU A 563     218.229 157.115 167.681  1.00 85.10           C  
ATOM   4286  CG  LEU A 563     217.237 157.266 168.836  1.00 85.10           C  
ATOM   4287  CD1 LEU A 563     216.751 155.904 169.308  1.00 85.10           C  
ATOM   4288  CD2 LEU A 563     217.868 158.043 169.979  1.00 85.10           C  
ATOM   4289  N   ILE A 564     219.564 158.119 164.785  1.00 86.80           N  
ATOM   4290  CA  ILE A 564     220.591 157.968 163.760  1.00 86.80           C  
ATOM   4291  C   ILE A 564     221.476 159.206 163.712  1.00 86.80           C  
ATOM   4292  O   ILE A 564     222.709 159.112 163.724  1.00 86.80           O  
ATOM   4293  CB  ILE A 564     219.946 157.683 162.392  1.00 86.80           C  
ATOM   4294  CG1 ILE A 564     219.232 156.332 162.413  1.00 86.80           C  
ATOM   4295  CG2 ILE A 564     220.994 157.721 161.289  1.00 86.80           C  
ATOM   4296  CD1 ILE A 564     218.402 156.065 161.183  1.00 86.80           C  
ATOM   4297  N   SER A 565     220.858 160.386 163.669  1.00 91.26           N  
ATOM   4298  CA  SER A 565     221.571 161.655 163.593  1.00 91.26           C  
ATOM   4299  C   SER A 565     222.078 162.148 164.942  1.00 91.26           C  
ATOM   4300  O   SER A 565     222.480 163.312 165.042  1.00 91.26           O  
ATOM   4301  CB  SER A 565     220.672 162.722 162.966  1.00 91.26           C  
ATOM   4302  OG  SER A 565     219.532 162.965 163.771  1.00 91.26           O  
ATOM   4303  N   HIS A 566     222.072 161.309 165.974  1.00 92.97           N  
ATOM   4304  CA  HIS A 566     222.677 161.703 167.236  1.00 92.97           C  
ATOM   4305  C   HIS A 566     224.190 161.786 167.075  1.00 92.97           C  
ATOM   4306  O   HIS A 566     224.792 161.058 166.281  1.00 92.97           O  
ATOM   4307  CB  HIS A 566     222.313 160.712 168.342  1.00 92.97           C  
ATOM   4308  CG  HIS A 566     222.454 161.270 169.724  1.00 92.97           C  
ATOM   4309  ND1 HIS A 566     222.475 160.475 170.849  1.00 92.97           N  
ATOM   4310  CD2 HIS A 566     222.582 162.545 170.161  1.00 92.97           C  
ATOM   4311  CE1 HIS A 566     222.609 161.236 171.921  1.00 92.97           C  
ATOM   4312  NE2 HIS A 566     222.676 162.496 171.531  1.00 92.97           N  
ATOM   4313  N   LYS A 567     224.808 162.691 167.837  1.00 91.65           N  
ATOM   4314  CA  LYS A 567     226.206 163.019 167.585  1.00 91.65           C  
ATOM   4315  C   LYS A 567     227.145 161.884 167.970  1.00 91.65           C  
ATOM   4316  O   LYS A 567     228.242 161.788 167.410  1.00 91.65           O  
ATOM   4317  CB  LYS A 567     226.581 164.296 168.338  1.00 91.65           C  
ATOM   4318  CG  LYS A 567     227.916 164.901 167.935  1.00 91.65           C  
ATOM   4319  CD  LYS A 567     228.182 166.190 168.697  1.00 91.65           C  
ATOM   4320  CE  LYS A 567     227.275 167.310 168.213  1.00 91.65           C  
ATOM   4321  NZ  LYS A 567     227.608 168.615 168.850  1.00 91.65           N  
ATOM   4322  N   ASP A 568     226.739 161.019 168.897  1.00 93.85           N  
ATOM   4323  CA  ASP A 568     227.546 159.875 169.313  1.00 93.85           C  
ATOM   4324  C   ASP A 568     227.090 158.588 168.638  1.00 93.85           C  
ATOM   4325  O   ASP A 568     227.079 157.522 169.260  1.00 93.85           O  
ATOM   4326  CB  ASP A 568     227.513 159.730 170.832  1.00 93.85           C  
ATOM   4327  CG  ASP A 568     226.101 159.700 171.385  1.00 93.85           C  
ATOM   4328  OD1 ASP A 568     225.149 159.929 170.610  1.00 93.85           O  
ATOM   4329  OD2 ASP A 568     225.943 159.447 172.598  1.00 93.85           O  
ATOM   4330  N   SER A 569     226.700 158.656 167.368  1.00 93.86           N  
ATOM   4331  CA  SER A 569     226.297 157.481 166.598  1.00 93.86           C  
ATOM   4332  C   SER A 569     227.341 157.214 165.518  1.00 93.86           C  
ATOM   4333  O   SER A 569     227.377 157.902 164.494  1.00 93.86           O  
ATOM   4334  CB  SER A 569     224.910 157.681 165.993  1.00 93.86           C  
ATOM   4335  OG  SER A 569     224.899 158.771 165.089  1.00 93.86           O  
ATOM   4336  N   PHE A 570     228.187 156.215 165.749  1.00 85.23           N  
ATOM   4337  CA  PHE A 570     229.300 155.903 164.864  1.00 85.23           C  
ATOM   4338  C   PHE A 570     229.128 154.492 164.319  1.00 85.23           C  
ATOM   4339  O   PHE A 570     228.638 153.602 165.022  1.00 85.23           O  
ATOM   4340  CB  PHE A 570     230.643 156.036 165.589  1.00 85.23           C  
ATOM   4341  CG  PHE A 570     231.036 157.457 165.876  1.00 85.23           C  
ATOM   4342  CD1 PHE A 570     230.531 158.497 165.112  1.00 85.23           C  
ATOM   4343  CD2 PHE A 570     231.911 157.754 166.908  1.00 85.23           C  
ATOM   4344  CE1 PHE A 570     230.889 159.806 165.373  1.00 85.23           C  
ATOM   4345  CE2 PHE A 570     232.273 159.062 167.174  1.00 85.23           C  
ATOM   4346  CZ  PHE A 570     231.762 160.089 166.405  1.00 85.23           C  
ATOM   4347  N   TYR A 571     229.528 154.292 163.065  1.00 85.66           N  
ATOM   4348  CA  TYR A 571     229.274 153.039 162.370  1.00 85.66           C  
ATOM   4349  C   TYR A 571     230.503 152.626 161.575  1.00 85.66           C  
ATOM   4350  O   TYR A 571     231.194 153.471 161.000  1.00 85.66           O  
ATOM   4351  CB  TYR A 571     228.064 153.155 161.434  1.00 85.66           C  
ATOM   4352  CG  TYR A 571     226.766 153.466 162.144  1.00 85.66           C  
ATOM   4353  CD1 TYR A 571     226.046 152.467 162.784  1.00 85.66           C  
ATOM   4354  CD2 TYR A 571     226.260 154.759 162.172  1.00 85.66           C  
ATOM   4355  CE1 TYR A 571     224.858 152.745 163.433  1.00 85.66           C  
ATOM   4356  CE2 TYR A 571     225.074 155.048 162.819  1.00 85.66           C  
ATOM   4357  CZ  TYR A 571     224.377 154.037 163.448  1.00 85.66           C  
ATOM   4358  OH  TYR A 571     223.195 154.320 164.093  1.00 85.66           O  
ATOM   4359  N   ASP A 572     230.768 151.322 161.549  1.00 87.59           N  
ATOM   4360  CA  ASP A 572     231.732 150.750 160.624  1.00 87.59           C  
ATOM   4361  C   ASP A 572     231.116 150.636 159.231  1.00 87.59           C  
ATOM   4362  O   ASP A 572     229.977 151.046 158.989  1.00 87.59           O  
ATOM   4363  CB  ASP A 572     232.214 149.391 161.130  1.00 87.59           C  
ATOM   4364  CG  ASP A 572     231.071 148.458 161.475  1.00 87.59           C  
ATOM   4365  OD1 ASP A 572     229.917 148.929 161.545  1.00 87.59           O  
ATOM   4366  OD2 ASP A 572     231.327 147.252 161.679  1.00 87.59           O  
ATOM   4367  N   ARG A 573     231.879 150.066 158.297  1.00 81.78           N  
ATOM   4368  CA  ARG A 573     231.354 149.853 156.952  1.00 81.78           C  
ATOM   4369  C   ARG A 573     230.291 148.761 156.940  1.00 81.78           C  
ATOM   4370  O   ARG A 573     229.294 148.866 156.215  1.00 81.78           O  
ATOM   4371  CB  ARG A 573     232.493 149.509 155.990  1.00 81.78           C  
ATOM   4372  CG  ARG A 573     232.052 149.326 154.546  1.00 81.78           C  
ATOM   4373  CD  ARG A 573     233.219 148.935 153.653  1.00 81.78           C  
ATOM   4374  NE  ARG A 573     234.162 150.034 153.468  1.00 81.78           N  
ATOM   4375  CZ  ARG A 573     234.043 150.969 152.531  1.00 81.78           C  
ATOM   4376  NH1 ARG A 573     233.026 150.934 151.682  1.00 81.78           N  
ATOM   4377  NH2 ARG A 573     234.947 151.934 152.435  1.00 81.78           N  
ATOM   4378  N   ALA A 574     230.490 147.702 157.730  1.00 78.58           N  
ATOM   4379  CA  ALA A 574     229.594 146.550 157.675  1.00 78.58           C  
ATOM   4380  C   ALA A 574     228.175 146.926 158.086  1.00 78.58           C  
ATOM   4381  O   ALA A 574     227.202 146.390 157.542  1.00 78.58           O  
ATOM   4382  CB  ALA A 574     230.128 145.425 158.560  1.00 78.58           C  
ATOM   4383  N   THR A 575     228.035 147.844 159.042  1.00 83.27           N  
ATOM   4384  CA  THR A 575     226.717 148.328 159.434  1.00 83.27           C  
ATOM   4385  C   THR A 575     226.235 149.483 158.566  1.00 83.27           C  
ATOM   4386  O   THR A 575     225.029 149.602 158.320  1.00 83.27           O  
ATOM   4387  CB  THR A 575     226.730 148.760 160.906  1.00 83.27           C  
ATOM   4388  OG1 THR A 575     227.235 147.690 161.714  1.00 83.27           O  
ATOM   4389  CG2 THR A 575     225.328 149.119 161.379  1.00 83.27           C  
ATOM   4390  N   LEU A 576     227.150 150.326 158.078  1.00 79.78           N  
ATOM   4391  CA  LEU A 576     226.755 151.379 157.148  1.00 79.78           C  
ATOM   4392  C   LEU A 576     226.222 150.789 155.849  1.00 79.78           C  
ATOM   4393  O   LEU A 576     225.341 151.379 155.213  1.00 79.78           O  
ATOM   4394  CB  LEU A 576     227.941 152.312 156.882  1.00 79.78           C  
ATOM   4395  CG  LEU A 576     227.749 153.607 156.082  1.00 79.78           C  
ATOM   4396  CD1 LEU A 576     227.843 153.383 154.575  1.00 79.78           C  
ATOM   4397  CD2 LEU A 576     226.428 154.269 156.448  1.00 79.78           C  
ATOM   4398  N   THR A 577     226.744 149.631 155.443  1.00 80.84           N  
ATOM   4399  CA  THR A 577     226.177 148.912 154.307  1.00 80.84           C  
ATOM   4400  C   THR A 577     224.749 148.466 154.598  1.00 80.84           C  
ATOM   4401  O   THR A 577     223.847 148.648 153.772  1.00 80.84           O  
ATOM   4402  CB  THR A 577     227.058 147.711 153.960  1.00 80.84           C  
ATOM   4403  OG1 THR A 577     228.285 148.168 153.376  1.00 80.84           O  
ATOM   4404  CG2 THR A 577     226.346 146.788 152.990  1.00 80.84           C  
ATOM   4405  N   GLN A 578     224.523 147.882 155.778  1.00 84.39           N  
ATOM   4406  CA  GLN A 578     223.221 147.295 156.077  1.00 84.39           C  
ATOM   4407  C   GLN A 578     222.154 148.362 156.287  1.00 84.39           C  
ATOM   4408  O   GLN A 578     220.993 148.155 155.914  1.00 84.39           O  
ATOM   4409  CB  GLN A 578     223.320 146.391 157.307  1.00 84.39           C  
ATOM   4410  CG  GLN A 578     222.024 145.679 157.665  1.00 84.39           C  
ATOM   4411  CD  GLN A 578     221.420 144.934 156.490  1.00 84.39           C  
ATOM   4412  OE1 GLN A 578     220.389 145.334 155.949  1.00 84.39           O  
ATOM   4413  NE2 GLN A 578     222.062 143.844 156.087  1.00 84.39           N  
ATOM   4414  N   LEU A 579     222.520 149.504 156.871  1.00 82.03           N  
ATOM   4415  CA  LEU A 579     221.559 150.591 157.020  1.00 82.03           C  
ATOM   4416  C   LEU A 579     221.200 151.188 155.665  1.00 82.03           C  
ATOM   4417  O   LEU A 579     220.023 151.430 155.372  1.00 82.03           O  
ATOM   4418  CB  LEU A 579     222.123 151.665 157.952  1.00 82.03           C  
ATOM   4419  CG  LEU A 579     222.327 151.257 159.412  1.00 82.03           C  
ATOM   4420  CD1 LEU A 579     222.897 152.412 160.224  1.00 82.03           C  
ATOM   4421  CD2 LEU A 579     221.027 150.758 160.019  1.00 82.03           C  
ATOM   4422  N   LEU A 580     222.207 151.434 154.823  1.00 84.11           N  
ATOM   4423  CA  LEU A 580     221.961 151.991 153.499  1.00 84.11           C  
ATOM   4424  C   LEU A 580     221.237 151.014 152.582  1.00 84.11           C  
ATOM   4425  O   LEU A 580     220.586 151.446 151.625  1.00 84.11           O  
ATOM   4426  CB  LEU A 580     223.287 152.415 152.865  1.00 84.11           C  
ATOM   4427  CG  LEU A 580     223.255 153.246 151.582  1.00 84.11           C  
ATOM   4428  CD1 LEU A 580     222.657 154.615 151.840  1.00 84.11           C  
ATOM   4429  CD2 LEU A 580     224.655 153.371 151.007  1.00 84.11           C  
ATOM   4430  N   SER A 581     221.327 149.713 152.857  1.00 88.31           N  
ATOM   4431  CA  SER A 581     220.598 148.707 152.095  1.00 88.31           C  
ATOM   4432  C   SER A 581     219.149 148.544 152.533  1.00 88.31           C  
ATOM   4433  O   SER A 581     218.386 147.869 151.835  1.00 88.31           O  
ATOM   4434  CB  SER A 581     221.311 147.356 152.194  1.00 88.31           C  
ATOM   4435  OG  SER A 581     220.594 146.349 151.503  1.00 88.31           O  
ATOM   4436  N   MET A 582     218.746 149.136 153.658  1.00 90.37           N  
ATOM   4437  CA  MET A 582     217.369 149.024 154.118  1.00 90.37           C  
ATOM   4438  C   MET A 582     216.508 150.241 153.806  1.00 90.37           C  
ATOM   4439  O   MET A 582     215.283 150.156 153.943  1.00 90.37           O  
ATOM   4440  CB  MET A 582     217.336 148.764 155.630  1.00 90.37           C  
ATOM   4441  CG  MET A 582     217.788 147.371 156.033  1.00 90.37           C  
ATOM   4442  SD  MET A 582     217.543 147.046 157.789  1.00 90.37           S  
ATOM   4443  CE  MET A 582     218.871 148.012 158.503  1.00 90.37           C  
ATOM   4444  N   MET A 583     217.098 151.366 153.397  1.00 91.40           N  
ATOM   4445  CA  MET A 583     216.273 152.478 152.942  1.00 91.40           C  
ATOM   4446  C   MET A 583     215.700 152.254 151.549  1.00 91.40           C  
ATOM   4447  O   MET A 583     214.685 152.868 151.205  1.00 91.40           O  
ATOM   4448  CB  MET A 583     217.075 153.782 152.957  1.00 91.40           C  
ATOM   4449  CG  MET A 583     218.312 153.767 152.074  1.00 91.40           C  
ATOM   4450  SD  MET A 583     219.135 155.370 152.003  1.00 91.40           S  
ATOM   4451  CE  MET A 583     219.681 155.559 153.697  1.00 91.40           C  
ATOM   4452  N   SER A 584     216.322 151.394 150.749  1.00 94.54           N  
ATOM   4453  CA  SER A 584     215.758 150.871 149.516  1.00 94.54           C  
ATOM   4454  C   SER A 584     215.503 149.373 149.667  1.00 94.54           C  
ATOM   4455  O   SER A 584     215.663 148.797 150.750  1.00 94.54           O  
ATOM   4456  CB  SER A 584     216.689 151.177 148.341  1.00 94.54           C  
ATOM   4457  OG  SER A 584     217.897 150.444 148.442  1.00 94.54           O  
ATOM   4458  N   ASP A 585     215.102 148.735 148.569  1.00104.01           N  
ATOM   4459  CA  ASP A 585     214.971 147.281 148.513  1.00104.01           C  
ATOM   4460  C   ASP A 585     216.134 146.652 147.757  1.00104.01           C  
ATOM   4461  O   ASP A 585     215.961 145.679 147.016  1.00104.01           O  
ATOM   4462  CB  ASP A 585     213.640 146.890 147.878  1.00104.01           C  
ATOM   4463  CG  ASP A 585     212.459 147.162 148.788  1.00104.01           C  
ATOM   4464  OD1 ASP A 585     212.637 147.124 150.024  1.00104.01           O  
ATOM   4465  OD2 ASP A 585     211.352 147.414 148.268  1.00104.01           O  
ATOM   4466  N   GLY A 586     217.334 147.199 147.935  1.00102.71           N  
ATOM   4467  CA  GLY A 586     218.497 146.746 147.197  1.00102.71           C  
ATOM   4468  C   GLY A 586     218.470 147.060 145.718  1.00102.71           C  
ATOM   4469  O   GLY A 586     219.015 146.290 144.922  1.00102.71           O  
ATOM   4470  N   ILE A 587     217.854 148.172 145.325  1.00 98.92           N  
ATOM   4471  CA  ILE A 587     217.680 148.514 143.922  1.00 98.92           C  
ATOM   4472  C   ILE A 587     218.491 149.744 143.532  1.00 98.92           C  
ATOM   4473  O   ILE A 587     219.114 149.767 142.469  1.00 98.92           O  
ATOM   4474  CB  ILE A 587     216.185 148.714 143.591  1.00 98.92           C  
ATOM   4475  CG1 ILE A 587     215.368 147.509 144.060  1.00 98.92           C  
ATOM   4476  CG2 ILE A 587     215.993 148.946 142.100  1.00 98.92           C  
ATOM   4477  CD1 ILE A 587     215.793 146.200 143.430  1.00 98.92           C  
ATOM   4478  N   GLU A 588     218.502 150.770 144.378  1.00 96.96           N  
ATOM   4479  CA  GLU A 588     219.218 152.001 144.072  1.00 96.96           C  
ATOM   4480  C   GLU A 588     220.717 151.823 144.277  1.00 96.96           C  
ATOM   4481  O   GLU A 588     221.156 151.287 145.300  1.00 96.96           O  
ATOM   4482  CB  GLU A 588     218.699 153.145 144.943  1.00 96.96           C  
ATOM   4483  CG  GLU A 588     219.324 154.497 144.634  1.00 96.96           C  
ATOM   4484  CD  GLU A 588     218.923 155.030 143.271  1.00 96.96           C  
ATOM   4485  OE1 GLU A 588     217.827 154.676 142.790  1.00 96.96           O  
ATOM   4486  OE2 GLU A 588     219.706 155.805 142.682  1.00 96.96           O  
ATOM   4487  N   HIS A 589     221.501 152.272 143.299  1.00 88.03           N  
ATOM   4488  CA  HIS A 589     222.951 152.141 143.344  1.00 88.03           C  
ATOM   4489  C   HIS A 589     223.525 153.325 144.111  1.00 88.03           C  
ATOM   4490  O   HIS A 589     223.213 154.481 143.804  1.00 88.03           O  
ATOM   4491  CB  HIS A 589     223.536 152.080 141.933  1.00 88.03           C  
ATOM   4492  CG  HIS A 589     225.029 151.969 141.901  1.00 88.03           C  
ATOM   4493  ND1 HIS A 589     225.857 153.070 141.847  1.00 88.03           N  
ATOM   4494  CD2 HIS A 589     225.843 150.887 141.915  1.00 88.03           C  
ATOM   4495  CE1 HIS A 589     227.116 152.670 141.829  1.00 88.03           C  
ATOM   4496  NE2 HIS A 589     227.135 151.350 141.870  1.00 88.03           N  
ATOM   4497  N   PHE A 590     224.362 153.039 145.101  1.00 86.16           N  
ATOM   4498  CA  PHE A 590     224.955 154.068 145.940  1.00 86.16           C  
ATOM   4499  C   PHE A 590     226.456 154.176 145.697  1.00 86.16           C  
ATOM   4500  O   PHE A 590     227.077 153.329 145.049  1.00 86.16           O  
ATOM   4501  CB  PHE A 590     224.681 153.778 147.420  1.00 86.16           C  
ATOM   4502  CG  PHE A 590     223.226 153.824 147.788  1.00 86.16           C  
ATOM   4503  CD1 PHE A 590     222.595 155.032 148.031  1.00 86.16           C  
ATOM   4504  CD2 PHE A 590     222.490 152.655 147.893  1.00 86.16           C  
ATOM   4505  CE1 PHE A 590     221.256 155.074 148.372  1.00 86.16           C  
ATOM   4506  CE2 PHE A 590     221.151 152.690 148.232  1.00 86.16           C  
ATOM   4507  CZ  PHE A 590     220.533 153.901 148.472  1.00 86.16           C  
ATOM   4508  N   ASP A 591     227.031 155.248 146.239  1.00 84.44           N  
ATOM   4509  CA  ASP A 591     228.473 155.427 146.319  1.00 84.44           C  
ATOM   4510  C   ASP A 591     228.823 155.924 147.714  1.00 84.44           C  
ATOM   4511  O   ASP A 591     228.148 156.803 148.256  1.00 84.44           O  
ATOM   4512  CB  ASP A 591     228.988 156.402 145.249  1.00 84.44           C  
ATOM   4513  CG  ASP A 591     228.183 157.687 145.186  1.00 84.44           C  
ATOM   4514  OD1 ASP A 591     227.155 157.787 145.886  1.00 84.44           O  
ATOM   4515  OD2 ASP A 591     228.581 158.600 144.432  1.00 84.44           O  
ATOM   4516  N   ILE A 592     229.872 155.352 148.293  1.00 76.84           N  
ATOM   4517  CA  ILE A 592     230.192 155.545 149.704  1.00 76.84           C  
ATOM   4518  C   ILE A 592     231.161 156.718 149.820  1.00 76.84           C  
ATOM   4519  O   ILE A 592     232.242 156.673 149.212  1.00 76.84           O  
ATOM   4520  CB  ILE A 592     230.793 154.276 150.320  1.00 76.84           C  
ATOM   4521  CG1 ILE A 592     229.875 153.079 150.070  1.00 76.84           C  
ATOM   4522  CG2 ILE A 592     231.026 154.466 151.810  1.00 76.84           C  
ATOM   4523  CD1 ILE A 592     228.497 153.231 150.674  1.00 76.84           C  
ATOM   4524  N   PRO A 593     230.826 157.765 150.569  1.00 75.82           N  
ATOM   4525  CA  PRO A 593     231.801 158.819 150.859  1.00 75.82           C  
ATOM   4526  C   PRO A 593     232.856 158.319 151.828  1.00 75.82           C  
ATOM   4527  O   PRO A 593     232.627 157.340 152.554  1.00 75.82           O  
ATOM   4528  CB  PRO A 593     230.943 159.927 151.484  1.00 75.82           C  
ATOM   4529  CG  PRO A 593     229.807 159.195 152.112  1.00 75.82           C  
ATOM   4530  CD  PRO A 593     229.525 158.017 151.215  1.00 75.82           C  
ATOM   4531  N   PRO A 594     234.030 158.956 151.867  1.00 74.54           N  
ATOM   4532  CA  PRO A 594     235.058 158.521 152.810  1.00 74.54           C  
ATOM   4533  C   PRO A 594     234.622 158.756 154.244  1.00 74.54           C  
ATOM   4534  O   PRO A 594     233.884 159.713 154.536  1.00 74.54           O  
ATOM   4535  CB  PRO A 594     236.270 159.395 152.440  1.00 74.54           C  
ATOM   4536  CG  PRO A 594     235.689 160.575 151.739  1.00 74.54           C  
ATOM   4537  CD  PRO A 594     234.493 160.057 151.006  1.00 74.54           C  
ATOM   4538  N   PRO A 595     235.050 157.907 155.175  1.00 80.12           N  
ATOM   4539  CA  PRO A 595     234.556 157.994 156.553  1.00 80.12           C  
ATOM   4540  C   PRO A 595     235.144 159.190 157.289  1.00 80.12           C  
ATOM   4541  O   PRO A 595     236.117 159.814 156.860  1.00 80.12           O  
ATOM   4542  CB  PRO A 595     235.017 156.673 157.174  1.00 80.12           C  
ATOM   4543  CG  PRO A 595     236.251 156.329 156.411  1.00 80.12           C  
ATOM   4544  CD  PRO A 595     236.002 156.796 154.999  1.00 80.12           C  
ATOM   4545  N   ALA A 596     234.524 159.508 158.427  1.00 83.47           N  
ATOM   4546  CA  ALA A 596     234.966 160.646 159.227  1.00 83.47           C  
ATOM   4547  C   ALA A 596     236.253 160.313 159.975  1.00 83.47           C  
ATOM   4548  O   ALA A 596     237.305 160.909 159.722  1.00 83.47           O  
ATOM   4549  CB  ALA A 596     233.863 161.067 160.201  1.00 83.47           C  
ATOM   4550  N   ILE A 597     236.186 159.361 160.902  1.00 92.63           N  
ATOM   4551  CA  ILE A 597     237.359 158.950 161.665  1.00 92.63           C  
ATOM   4552  C   ILE A 597     238.133 157.943 160.826  1.00 92.63           C  
ATOM   4553  O   ILE A 597     237.555 156.986 160.298  1.00 92.63           O  
ATOM   4554  CB  ILE A 597     236.949 158.355 163.021  1.00 92.63           C  
ATOM   4555  CG1 ILE A 597     236.075 159.345 163.791  1.00 92.63           C  
ATOM   4556  CG2 ILE A 597     238.179 157.982 163.834  1.00 92.63           C  
ATOM   4557  CD1 ILE A 597     236.743 160.673 164.049  1.00 92.63           C  
ATOM   4558  N   MET A 598     239.443 158.152 160.695  1.00 96.40           N  
ATOM   4559  CA  MET A 598     240.183 157.387 159.700  1.00 96.40           C  
ATOM   4560  C   MET A 598     241.437 156.693 160.220  1.00 96.40           C  
ATOM   4561  O   MET A 598     241.768 155.599 159.751  1.00 96.40           O  
ATOM   4562  CB  MET A 598     240.560 158.306 158.534  1.00 96.40           C  
ATOM   4563  CG  MET A 598     241.146 157.589 157.331  1.00 96.40           C  
ATOM   4564  SD  MET A 598     241.479 158.708 155.958  1.00 96.40           S  
ATOM   4565  CE  MET A 598     239.815 159.059 155.397  1.00 96.40           C  
ATOM   4566  N   LYS A 599     242.146 157.291 161.180  1.00 87.94           N  
ATOM   4567  CA  LYS A 599     243.441 156.692 161.488  1.00 87.94           C  
ATOM   4568  C   LYS A 599     243.344 155.420 162.330  1.00 87.94           C  
ATOM   4569  O   LYS A 599     243.938 154.405 161.943  1.00 87.94           O  
ATOM   4570  CB  LYS A 599     244.355 157.704 162.186  1.00 87.94           C  
ATOM   4571  CG  LYS A 599     245.824 157.302 162.178  1.00 87.94           C  
ATOM   4572  CD  LYS A 599     246.249 156.689 163.502  1.00 87.94           C  
ATOM   4573  CE  LYS A 599     247.705 156.260 163.464  1.00 87.94           C  
ATOM   4574  NZ  LYS A 599     247.933 155.163 162.484  1.00 87.94           N  
ATOM   4575  N   PRO A 600     242.632 155.403 163.481  1.00 89.06           N  
ATOM   4576  CA  PRO A 600     242.586 154.151 164.250  1.00 89.06           C  
ATOM   4577  C   PRO A 600     241.830 153.067 163.501  1.00 89.06           C  
ATOM   4578  O   PRO A 600     242.351 151.975 163.253  1.00 89.06           O  
ATOM   4579  CB  PRO A 600     241.861 154.554 165.543  1.00 89.06           C  
ATOM   4580  CG  PRO A 600     241.996 156.043 165.610  1.00 89.06           C  
ATOM   4581  CD  PRO A 600     241.911 156.478 164.182  1.00 89.06           C  
ATOM   4582  N   TYR A 601     240.591 153.384 163.132  1.00 94.35           N  
ATOM   4583  CA  TYR A 601     239.777 152.582 162.234  1.00 94.35           C  
ATOM   4584  C   TYR A 601     239.010 153.537 161.330  1.00 94.35           C  
ATOM   4585  O   TYR A 601     239.135 154.760 161.441  1.00 94.35           O  
ATOM   4586  CB  TYR A 601     238.831 151.656 163.011  1.00 94.35           C  
ATOM   4587  CG  TYR A 601     239.498 150.888 164.131  1.00 94.35           C  
ATOM   4588  CD1 TYR A 601     240.292 149.779 163.865  1.00 94.35           C  
ATOM   4589  CD2 TYR A 601     239.333 151.271 165.456  1.00 94.35           C  
ATOM   4590  CE1 TYR A 601     240.902 149.074 164.885  1.00 94.35           C  
ATOM   4591  CE2 TYR A 601     239.939 150.572 166.483  1.00 94.35           C  
ATOM   4592  CZ  TYR A 601     240.722 149.475 166.192  1.00 94.35           C  
ATOM   4593  OH  TYR A 601     241.329 148.776 167.210  1.00 94.35           O  
ATOM   4594  N   TYR A 602     238.208 152.982 160.427  1.00 91.07           N  
ATOM   4595  CA  TYR A 602     237.368 153.784 159.547  1.00 91.07           C  
ATOM   4596  C   TYR A 602     235.975 153.844 160.161  1.00 91.07           C  
ATOM   4597  O   TYR A 602     235.321 152.807 160.326  1.00 91.07           O  
ATOM   4598  CB  TYR A 602     237.324 153.213 158.129  1.00 91.07           C  
ATOM   4599  CG  TYR A 602     238.683 153.095 157.478  1.00 91.07           C  
ATOM   4600  CD1 TYR A 602     239.422 154.230 157.166  1.00 91.07           C  
ATOM   4601  CD2 TYR A 602     239.217 151.857 157.150  1.00 91.07           C  
ATOM   4602  CE1 TYR A 602     240.664 154.133 156.570  1.00 91.07           C  
ATOM   4603  CE2 TYR A 602     240.456 151.752 156.546  1.00 91.07           C  
ATOM   4604  CZ  TYR A 602     241.176 152.893 156.260  1.00 91.07           C  
ATOM   4605  OH  TYR A 602     242.408 152.793 155.656  1.00 91.07           O  
ATOM   4606  N   LEU A 603     235.523 155.050 160.499  1.00 86.39           N  
ATOM   4607  CA  LEU A 603     234.221 155.248 161.126  1.00 86.39           C  
ATOM   4608  C   LEU A 603     233.440 156.295 160.350  1.00 86.39           C  
ATOM   4609  O   LEU A 603     233.890 157.438 160.216  1.00 86.39           O  
ATOM   4610  CB  LEU A 603     234.367 155.677 162.591  1.00 86.39           C  
ATOM   4611  CG  LEU A 603     234.531 154.608 163.678  1.00 86.39           C  
ATOM   4612  CD1 LEU A 603     233.343 153.653 163.679  1.00 86.39           C  
ATOM   4613  CD2 LEU A 603     235.846 153.848 163.554  1.00 86.39           C  
ATOM   4614  N   TRP A 604     232.275 155.905 159.846  1.00 79.74           N  
ATOM   4615  CA  TRP A 604     231.288 156.852 159.359  1.00 79.74           C  
ATOM   4616  C   TRP A 604     230.439 157.368 160.517  1.00 79.74           C  
ATOM   4617  O   TRP A 604     230.361 156.757 161.586  1.00 79.74           O  
ATOM   4618  CB  TRP A 604     230.403 156.203 158.295  1.00 79.74           C  
ATOM   4619  CG  TRP A 604     231.096 156.019 156.980  1.00 79.74           C  
ATOM   4620  CD1 TRP A 604     231.042 156.850 155.900  1.00 79.74           C  
ATOM   4621  CD2 TRP A 604     231.960 154.937 156.610  1.00 79.74           C  
ATOM   4622  NE1 TRP A 604     231.814 156.351 154.878  1.00 79.74           N  
ATOM   4623  CE2 TRP A 604     232.388 155.177 155.290  1.00 79.74           C  
ATOM   4624  CE3 TRP A 604     232.411 153.788 157.267  1.00 79.74           C  
ATOM   4625  CZ2 TRP A 604     233.246 154.311 154.614  1.00 79.74           C  
ATOM   4626  CZ3 TRP A 604     233.261 152.930 156.594  1.00 79.74           C  
ATOM   4627  CH2 TRP A 604     233.669 153.196 155.281  1.00 79.74           C  
ATOM   4628  N   THR A 605     229.797 158.509 160.295  1.00 82.32           N  
ATOM   4629  CA  THR A 605     228.976 159.139 161.317  1.00 82.32           C  
ATOM   4630  C   THR A 605     227.499 158.903 161.022  1.00 82.32           C  
ATOM   4631  O   THR A 605     227.123 158.358 159.982  1.00 82.32           O  
ATOM   4632  CB  THR A 605     229.273 160.640 161.400  1.00 82.32           C  
ATOM   4633  OG1 THR A 605     228.550 161.213 162.497  1.00 82.32           O  
ATOM   4634  CG2 THR A 605     228.863 161.336 160.111  1.00 82.32           C  
ATOM   4635  N   GLY A 606     226.654 159.326 161.960  1.00 86.44           N  
ATOM   4636  CA  GLY A 606     225.228 159.110 161.814  1.00 86.44           C  
ATOM   4637  C   GLY A 606     224.530 160.182 161.004  1.00 86.44           C  
ATOM   4638  O   GLY A 606     223.314 160.362 161.113  1.00 86.44           O  
ATOM   4639  N   LYS A 607     225.290 160.896 160.184  1.00 84.49           N  
ATOM   4640  CA  LYS A 607     224.772 162.001 159.389  1.00 84.49           C  
ATOM   4641  C   LYS A 607     225.041 161.829 157.905  1.00 84.49           C  
ATOM   4642  O   LYS A 607     224.211 162.218 157.079  1.00 84.49           O  
ATOM   4643  CB  LYS A 607     225.385 163.322 159.875  1.00 84.49           C  
ATOM   4644  CG  LYS A 607     224.911 163.746 161.257  1.00 84.49           C  
ATOM   4645  CD  LYS A 607     225.603 165.018 161.715  1.00 84.49           C  
ATOM   4646  CE  LYS A 607     225.008 165.533 163.015  1.00 84.49           C  
ATOM   4647  NZ  LYS A 607     225.234 164.588 164.144  1.00 84.49           N  
ATOM   4648  N   GLN A 608     226.190 161.250 157.550  1.00 86.73           N  
ATOM   4649  CA  GLN A 608     226.479 160.922 156.158  1.00 86.73           C  
ATOM   4650  C   GLN A 608     225.532 159.856 155.625  1.00 86.73           C  
ATOM   4651  O   GLN A 608     225.177 159.879 154.440  1.00 86.73           O  
ATOM   4652  CB  GLN A 608     227.932 160.467 156.020  1.00 86.73           C  
ATOM   4653  CG  GLN A 608     228.949 161.551 156.345  1.00 86.73           C  
ATOM   4654  CD  GLN A 608     230.368 161.021 156.414  1.00 86.73           C  
ATOM   4655  OE1 GLN A 608     230.602 159.822 156.270  1.00 86.73           O  
ATOM   4656  NE2 GLN A 608     231.324 161.916 156.637  1.00 86.73           N  
ATOM   4657  N   VAL A 609     225.118 158.916 156.478  1.00 82.90           N  
ATOM   4658  CA  VAL A 609     224.069 157.971 156.104  1.00 82.90           C  
ATOM   4659  C   VAL A 609     222.756 158.698 155.833  1.00 82.90           C  
ATOM   4660  O   VAL A 609     221.992 158.312 154.939  1.00 82.90           O  
ATOM   4661  CB  VAL A 609     223.915 156.891 157.193  1.00 82.90           C  
ATOM   4662  CG1 VAL A 609     223.678 157.527 158.558  1.00 82.90           C  
ATOM   4663  CG2 VAL A 609     222.793 155.924 156.841  1.00 82.90           C  
ATOM   4664  N   PHE A 610     222.474 159.767 156.582  1.00 88.70           N  
ATOM   4665  CA  PHE A 610     221.293 160.564 156.275  1.00 88.70           C  
ATOM   4666  C   PHE A 610     221.497 161.431 155.041  1.00 88.70           C  
ATOM   4667  O   PHE A 610     220.515 161.808 154.391  1.00 88.70           O  
ATOM   4668  CB  PHE A 610     220.921 161.448 157.467  1.00 88.70           C  
ATOM   4669  CG  PHE A 610     219.553 162.063 157.362  1.00 88.70           C  
ATOM   4670  CD1 PHE A 610     218.422 161.325 157.666  1.00 88.70           C  
ATOM   4671  CD2 PHE A 610     219.399 163.374 156.942  1.00 88.70           C  
ATOM   4672  CE1 PHE A 610     217.162 161.886 157.566  1.00 88.70           C  
ATOM   4673  CE2 PHE A 610     218.142 163.941 156.838  1.00 88.70           C  
ATOM   4674  CZ  PHE A 610     217.022 163.196 157.150  1.00 88.70           C  
ATOM   4675  N   SER A 611     222.746 161.757 154.707  1.00 87.92           N  
ATOM   4676  CA  SER A 611     223.036 162.503 153.489  1.00 87.92           C  
ATOM   4677  C   SER A 611     222.809 161.677 152.230  1.00 87.92           C  
ATOM   4678  O   SER A 611     222.600 162.252 151.156  1.00 87.92           O  
ATOM   4679  CB  SER A 611     224.477 163.015 153.519  1.00 87.92           C  
ATOM   4680  OG  SER A 611     224.687 163.882 154.620  1.00 87.92           O  
ATOM   4681  N   LEU A 612     222.845 160.347 152.336  1.00 79.45           N  
ATOM   4682  CA  LEU A 612     222.706 159.499 151.158  1.00 79.45           C  
ATOM   4683  C   LEU A 612     221.253 159.244 150.770  1.00 79.45           C  
ATOM   4684  O   LEU A 612     220.976 158.991 149.593  1.00 79.45           O  
ATOM   4685  CB  LEU A 612     223.428 158.171 151.387  1.00 79.45           C  
ATOM   4686  CG  LEU A 612     224.955 158.255 151.451  1.00 79.45           C  
ATOM   4687  CD1 LEU A 612     225.564 156.899 151.771  1.00 79.45           C  
ATOM   4688  CD2 LEU A 612     225.520 158.808 150.150  1.00 79.45           C  
ATOM   4689  N   LEU A 613     220.315 159.298 151.720  1.00 82.30           N  
ATOM   4690  CA  LEU A 613     218.914 159.134 151.343  1.00 82.30           C  
ATOM   4691  C   LEU A 613     218.385 160.333 150.567  1.00 82.30           C  
ATOM   4692  O   LEU A 613     217.364 160.210 149.882  1.00 82.30           O  
ATOM   4693  CB  LEU A 613     218.052 158.868 152.580  1.00 82.30           C  
ATOM   4694  CG  LEU A 613     218.039 159.858 153.746  1.00 82.30           C  
ATOM   4695  CD1 LEU A 613     216.973 160.930 153.565  1.00 82.30           C  
ATOM   4696  CD2 LEU A 613     217.830 159.108 155.051  1.00 82.30           C  
ATOM   4697  N   ILE A 614     219.051 161.482 150.660  1.00 73.89           N  
ATOM   4698  CA  ILE A 614     218.706 162.622 149.816  1.00 73.89           C  
ATOM   4699  C   ILE A 614     219.308 162.446 148.428  1.00 73.89           C  
ATOM   4700  O   ILE A 614     218.596 162.402 147.418  1.00 73.89           O  
ATOM   4701  CB  ILE A 614     219.165 163.939 150.469  1.00 73.89           C  
ATOM   4702  CG1 ILE A 614     218.541 164.091 151.857  1.00 73.89           C  
ATOM   4703  CG2 ILE A 614     218.810 165.125 149.584  1.00 73.89           C  
ATOM   4704  CD1 ILE A 614     219.173 165.180 152.695  1.00 73.89           C  
ATOM   4705  N   LYS A 615     220.632 162.348 148.367  1.00 78.40           N  
ATOM   4706  CA  LYS A 615     221.375 162.222 147.113  1.00 78.40           C  
ATOM   4707  C   LYS A 615     222.049 160.858 147.116  1.00 78.40           C  
ATOM   4708  O   LYS A 615     223.118 160.692 147.729  1.00 78.40           O  
ATOM   4709  CB  LYS A 615     222.408 163.338 146.968  1.00 78.40           C  
ATOM   4710  CG  LYS A 615     223.134 163.346 145.633  1.00 78.40           C  
ATOM   4711  CD  LYS A 615     223.918 164.632 145.438  1.00 78.40           C  
ATOM   4712  CE  LYS A 615     225.153 164.666 146.323  1.00 78.40           C  
ATOM   4713  NZ  LYS A 615     226.168 163.662 145.900  1.00 78.40           N  
ATOM   4714  N   PRO A 616     221.469 159.850 146.456  1.00 79.72           N  
ATOM   4715  CA  PRO A 616     222.103 158.522 146.477  1.00 79.72           C  
ATOM   4716  C   PRO A 616     223.421 158.473 145.727  1.00 79.72           C  
ATOM   4717  O   PRO A 616     224.342 157.768 146.158  1.00 79.72           O  
ATOM   4718  CB  PRO A 616     221.043 157.620 145.828  1.00 79.72           C  
ATOM   4719  CG  PRO A 616     220.210 158.548 145.003  1.00 79.72           C  
ATOM   4720  CD  PRO A 616     220.166 159.834 145.771  1.00 79.72           C  
ATOM   4721  N   ASN A 617     223.544 159.200 144.621  1.00 80.28           N  
ATOM   4722  CA  ASN A 617     224.780 159.212 143.849  1.00 80.28           C  
ATOM   4723  C   ASN A 617     224.789 160.455 142.968  1.00 80.28           C  
ATOM   4724  O   ASN A 617     223.893 161.300 143.038  1.00 80.28           O  
ATOM   4725  CB  ASN A 617     224.927 157.933 143.018  1.00 80.28           C  
ATOM   4726  CG  ASN A 617     223.665 157.585 142.253  1.00 80.28           C  
ATOM   4727  OD1 ASN A 617     222.683 158.327 142.279  1.00 80.28           O  
ATOM   4728  ND2 ASN A 617     223.685 156.449 141.565  1.00 80.28           N  
ATOM   4729  N   HIS A 618     225.824 160.558 142.131  1.00 76.71           N  
ATOM   4730  CA  HIS A 618     225.968 161.718 141.258  1.00 76.71           C  
ATOM   4731  C   HIS A 618     224.908 161.739 140.165  1.00 76.71           C  
ATOM   4732  O   HIS A 618     224.571 162.811 139.650  1.00 76.71           O  
ATOM   4733  CB  HIS A 618     227.365 161.735 140.639  1.00 76.71           C  
ATOM   4734  CG  HIS A 618     227.678 160.520 139.822  1.00 76.71           C  
ATOM   4735  ND1 HIS A 618     227.350 160.415 138.488  1.00 76.71           N  
ATOM   4736  CD2 HIS A 618     228.285 159.356 140.153  1.00 76.71           C  
ATOM   4737  CE1 HIS A 618     227.743 159.240 138.031  1.00 76.71           C  
ATOM   4738  NE2 HIS A 618     228.314 158.578 139.021  1.00 76.71           N  
ATOM   4739  N   ASN A 619     224.374 160.572 139.798  1.00 79.24           N  
ATOM   4740  CA  ASN A 619     223.334 160.506 138.779  1.00 79.24           C  
ATOM   4741  C   ASN A 619     221.998 161.061 139.256  1.00 79.24           C  
ATOM   4742  O   ASN A 619     221.149 161.386 138.420  1.00 79.24           O  
ATOM   4743  CB  ASN A 619     223.151 159.062 138.310  1.00 79.24           C  
ATOM   4744  CG  ASN A 619     224.323 158.563 137.488  1.00 79.24           C  
ATOM   4745  OD1 ASN A 619     224.856 159.283 136.644  1.00 79.24           O  
ATOM   4746  ND2 ASN A 619     224.732 157.323 137.733  1.00 79.24           N  
ATOM   4747  N   SER A 620     221.787 161.179 140.561  1.00 81.52           N  
ATOM   4748  CA  SER A 620     220.584 161.852 141.034  1.00 81.52           C  
ATOM   4749  C   SER A 620     220.757 163.365 140.946  1.00 81.52           C  
ATOM   4750  O   SER A 620     221.757 163.899 141.435  1.00 81.52           O  
ATOM   4751  CB  SER A 620     220.270 161.446 142.471  1.00 81.52           C  
ATOM   4752  OG  SER A 620     221.264 161.921 143.362  1.00 81.52           O  
ATOM   4753  N   PRO A 621     219.809 164.082 140.335  1.00 83.40           N  
ATOM   4754  CA  PRO A 621     219.978 165.529 140.134  1.00 83.40           C  
ATOM   4755  C   PRO A 621     219.759 166.366 141.383  1.00 83.40           C  
ATOM   4756  O   PRO A 621     219.977 167.584 141.332  1.00 83.40           O  
ATOM   4757  CB  PRO A 621     218.923 165.848 139.070  1.00 83.40           C  
ATOM   4758  CG  PRO A 621     217.840 164.857 139.340  1.00 83.40           C  
ATOM   4759  CD  PRO A 621     218.537 163.591 139.774  1.00 83.40           C  
ATOM   4760  N   VAL A 622     219.341 165.763 142.492  1.00 80.80           N  
ATOM   4761  CA  VAL A 622     218.932 166.519 143.672  1.00 80.80           C  
ATOM   4762  C   VAL A 622     220.160 167.038 144.411  1.00 80.80           C  
ATOM   4763  O   VAL A 622     221.024 166.261 144.831  1.00 80.80           O  
ATOM   4764  CB  VAL A 622     218.059 165.659 144.597  1.00 80.80           C  
ATOM   4765  CG1 VAL A 622     217.680 166.441 145.847  1.00 80.80           C  
ATOM   4766  CG2 VAL A 622     216.817 165.180 143.861  1.00 80.80           C  
ATOM   4767  N   VAL A 623     220.235 168.358 144.567  1.00 84.41           N  
ATOM   4768  CA  VAL A 623     221.208 169.011 145.438  1.00 84.41           C  
ATOM   4769  C   VAL A 623     220.553 170.267 146.001  1.00 84.41           C  
ATOM   4770  O   VAL A 623     219.989 171.071 145.253  1.00 84.41           O  
ATOM   4771  CB  VAL A 623     222.527 169.335 144.701  1.00 84.41           C  
ATOM   4772  CG1 VAL A 623     222.267 170.125 143.423  1.00 84.41           C  
ATOM   4773  CG2 VAL A 623     223.474 170.095 145.617  1.00 84.41           C  
ATOM   4774  N   ILE A 624     220.606 170.429 147.324  1.00 91.10           N  
ATOM   4775  CA  ILE A 624     219.834 171.458 148.008  1.00 91.10           C  
ATOM   4776  C   ILE A 624     220.729 172.215 148.983  1.00 91.10           C  
ATOM   4777  O   ILE A 624     221.844 171.800 149.300  1.00 91.10           O  
ATOM   4778  CB  ILE A 624     218.612 170.874 148.749  1.00 91.10           C  
ATOM   4779  CG1 ILE A 624     219.050 169.779 149.724  1.00 91.10           C  
ATOM   4780  CG2 ILE A 624     217.588 170.339 147.759  1.00 91.10           C  
ATOM   4781  CD1 ILE A 624     217.948 169.307 150.648  1.00 91.10           C  
ATOM   4782  N   ASN A 625     220.209 173.348 149.455  1.00103.71           N  
ATOM   4783  CA  ASN A 625     220.880 174.218 150.412  1.00103.71           C  
ATOM   4784  C   ASN A 625     219.825 174.782 151.350  1.00103.71           C  
ATOM   4785  O   ASN A 625     218.796 175.286 150.888  1.00103.71           O  
ATOM   4786  CB  ASN A 625     221.639 175.349 149.709  1.00103.71           C  
ATOM   4787  CG  ASN A 625     222.739 174.836 148.800  1.00103.71           C  
ATOM   4788  OD1 ASN A 625     222.663 174.967 147.579  1.00103.71           O  
ATOM   4789  ND2 ASN A 625     223.771 174.248 149.394  1.00103.71           N  
ATOM   4790  N   LEU A 626     220.073 174.703 152.656  1.00107.25           N  
ATOM   4791  CA  LEU A 626     219.049 175.071 153.625  1.00107.25           C  
ATOM   4792  C   LEU A 626     219.683 175.344 154.982  1.00107.25           C  
ATOM   4793  O   LEU A 626     220.626 174.659 155.387  1.00107.25           O  
ATOM   4794  CB  LEU A 626     217.990 173.966 153.747  1.00107.25           C  
ATOM   4795  CG  LEU A 626     216.791 174.196 154.672  1.00107.25           C  
ATOM   4796  CD1 LEU A 626     215.532 173.619 154.053  1.00107.25           C  
ATOM   4797  CD2 LEU A 626     217.030 173.575 156.041  1.00107.25           C  
ATOM   4798  N   ASP A 627     219.147 176.349 155.672  1.00107.87           N  
ATOM   4799  CA  ASP A 627     219.510 176.688 157.042  1.00107.87           C  
ATOM   4800  C   ASP A 627     218.232 176.729 157.865  1.00107.87           C  
ATOM   4801  O   ASP A 627     217.248 177.349 157.448  1.00107.87           O  
ATOM   4802  CB  ASP A 627     220.238 178.034 157.114  1.00107.87           C  
ATOM   4803  CG  ASP A 627     221.487 178.071 156.254  1.00107.87           C  
ATOM   4804  OD1 ASP A 627     222.095 177.002 156.036  1.00107.87           O  
ATOM   4805  OD2 ASP A 627     221.861 179.171 155.796  1.00107.87           O  
ATOM   4806  N   ALA A 628     218.239 176.077 159.027  1.00104.17           N  
ATOM   4807  CA  ALA A 628     217.031 176.012 159.837  1.00104.17           C  
ATOM   4808  C   ALA A 628     217.382 175.856 161.310  1.00104.17           C  
ATOM   4809  O   ALA A 628     218.511 175.520 161.675  1.00104.17           O  
ATOM   4810  CB  ALA A 628     216.120 174.863 159.391  1.00104.17           C  
ATOM   4811  N   LYS A 629     216.381 176.113 162.148  1.00110.02           N  
ATOM   4812  CA  LYS A 629     216.489 176.063 163.599  1.00110.02           C  
ATOM   4813  C   LYS A 629     215.686 174.883 164.131  1.00110.02           C  
ATOM   4814  O   LYS A 629     214.584 174.605 163.648  1.00110.02           O  
ATOM   4815  CB  LYS A 629     215.984 177.368 164.224  1.00110.02           C  
ATOM   4816  CG  LYS A 629     216.181 177.469 165.724  1.00110.02           C  
ATOM   4817  CD  LYS A 629     215.497 178.708 166.281  1.00110.02           C  
ATOM   4818  CE  LYS A 629     216.255 179.972 165.907  1.00110.02           C  
ATOM   4819  NZ  LYS A 629     215.672 181.182 166.550  1.00110.02           N  
ATOM   4820  N   ASN A 630     216.237 174.190 165.127  1.00116.26           N  
ATOM   4821  CA  ASN A 630     215.551 173.042 165.699  1.00116.26           C  
ATOM   4822  C   ASN A 630     214.414 173.494 166.615  1.00116.26           C  
ATOM   4823  O   ASN A 630     214.120 174.685 166.754  1.00116.26           O  
ATOM   4824  CB  ASN A 630     216.534 172.157 166.463  1.00116.26           C  
ATOM   4825  CG  ASN A 630     217.367 171.284 165.549  1.00116.26           C  
ATOM   4826  OD1 ASN A 630     216.903 170.848 164.497  1.00116.26           O  
ATOM   4827  ND2 ASN A 630     218.599 171.008 165.956  1.00116.26           N  
ATOM   4828  N   LYS A 631     213.763 172.518 167.254  1.00108.55           N  
ATOM   4829  CA  LYS A 631     212.684 172.829 168.185  1.00108.55           C  
ATOM   4830  C   LYS A 631     213.200 173.391 169.505  1.00108.55           C  
ATOM   4831  O   LYS A 631     212.523 174.218 170.127  1.00108.55           O  
ATOM   4832  CB  LYS A 631     211.839 171.579 168.435  1.00108.55           C  
ATOM   4833  CG  LYS A 631     210.576 171.824 169.245  1.00108.55           C  
ATOM   4834  CD  LYS A 631     209.571 172.651 168.459  1.00108.55           C  
ATOM   4835  CE  LYS A 631     208.305 172.893 169.264  1.00108.55           C  
ATOM   4836  NZ  LYS A 631     207.560 171.628 169.512  1.00108.55           N  
ATOM   4837  N   VAL A 632     214.386 172.973 169.947  1.00115.00           N  
ATOM   4838  CA  VAL A 632     214.898 173.410 171.242  1.00115.00           C  
ATOM   4839  C   VAL A 632     215.854 174.587 171.079  1.00115.00           C  
ATOM   4840  O   VAL A 632     215.552 175.703 171.517  1.00115.00           O  
ATOM   4841  CB  VAL A 632     215.560 172.240 171.997  1.00115.00           C  
ATOM   4842  CG1 VAL A 632     214.496 171.376 172.650  1.00115.00           C  
ATOM   4843  CG2 VAL A 632     216.393 171.383 171.050  1.00115.00           C  
ATOM   4844  N   PHE A 633     217.002 174.352 170.439  1.00127.92           N  
ATOM   4845  CA  PHE A 633     217.952 175.401 170.064  1.00127.92           C  
ATOM   4846  C   PHE A 633     218.362 176.233 171.284  1.00127.92           C  
ATOM   4847  O   PHE A 633     217.984 177.395 171.444  1.00127.92           O  
ATOM   4848  CB  PHE A 633     217.377 176.290 168.953  1.00127.92           C  
ATOM   4849  CG  PHE A 633     218.353 177.303 168.424  1.00127.92           C  
ATOM   4850  CD1 PHE A 633     219.454 176.900 167.687  1.00127.92           C  
ATOM   4851  CD2 PHE A 633     218.170 178.656 168.661  1.00127.92           C  
ATOM   4852  CE1 PHE A 633     220.356 177.825 167.199  1.00127.92           C  
ATOM   4853  CE2 PHE A 633     219.068 179.587 168.174  1.00127.92           C  
ATOM   4854  CZ  PHE A 633     220.162 179.171 167.442  1.00127.92           C  
ATOM   4855  N   VAL A 634     219.136 175.599 172.155  1.00136.23           N  
ATOM   4856  CA  VAL A 634     219.753 176.359 173.250  1.00136.23           C  
ATOM   4857  C   VAL A 634     220.799 177.307 172.668  1.00136.23           C  
ATOM   4858  O   VAL A 634     221.646 176.877 171.864  1.00136.23           O  
ATOM   4859  CB  VAL A 634     220.361 175.410 174.292  1.00136.23           C  
ATOM   4860  CG1 VAL A 634     221.402 174.486 173.671  1.00136.23           C  
ATOM   4861  CG2 VAL A 634     220.964 176.201 175.445  1.00136.23           C  
ATOM   4862  N   PRO A 635     220.758 178.595 172.996  1.00141.53           N  
ATOM   4863  CA  PRO A 635     221.551 179.572 172.247  1.00141.53           C  
ATOM   4864  C   PRO A 635     223.015 179.529 172.643  1.00141.53           C  
ATOM   4865  O   PRO A 635     223.354 179.241 173.801  1.00141.53           O  
ATOM   4866  CB  PRO A 635     220.916 180.915 172.641  1.00141.53           C  
ATOM   4867  CG  PRO A 635     219.542 180.565 173.113  1.00141.53           C  
ATOM   4868  CD  PRO A 635     219.709 179.243 173.800  1.00141.53           C  
ATOM   4869  N   PRO A 636     223.912 179.811 171.699  1.00150.79           N  
ATOM   4870  CA  PRO A 636     225.336 179.965 172.028  1.00150.79           C  
ATOM   4871  C   PRO A 636     225.614 181.260 172.774  1.00150.79           C  
ATOM   4872  O   PRO A 636     224.690 181.935 173.240  1.00150.79           O  
ATOM   4873  CB  PRO A 636     226.019 179.957 170.653  1.00150.79           C  
ATOM   4874  CG  PRO A 636     225.023 179.335 169.724  1.00150.79           C  
ATOM   4875  CD  PRO A 636     223.687 179.755 170.246  1.00150.79           C  
ATOM   4876  N   LYS A 637     226.897 181.612 172.891  1.00154.77           N  
ATOM   4877  CA  LYS A 637     227.312 182.822 173.592  1.00154.77           C  
ATOM   4878  C   LYS A 637     226.765 184.088 172.942  1.00154.77           C  
ATOM   4879  O   LYS A 637     226.869 185.167 173.538  1.00154.77           O  
ATOM   4880  CB  LYS A 637     228.840 182.897 173.666  1.00154.77           C  
ATOM   4881  CG  LYS A 637     229.458 182.126 174.827  1.00154.77           C  
ATOM   4882  CD  LYS A 637     229.474 180.627 174.572  1.00154.77           C  
ATOM   4883  CE  LYS A 637     230.089 179.875 175.741  1.00154.77           C  
ATOM   4884  NZ  LYS A 637     229.981 178.400 175.570  1.00154.77           N  
ATOM   4885  N   SER A 638     226.199 183.981 171.741  1.00162.63           N  
ATOM   4886  CA  SER A 638     225.209 184.870 171.145  1.00162.63           C  
ATOM   4887  C   SER A 638     225.817 186.169 170.621  1.00162.63           C  
ATOM   4888  O   SER A 638     225.107 186.939 169.973  1.00162.63           O  
ATOM   4889  CB  SER A 638     224.054 185.218 172.104  1.00162.63           C  
ATOM   4890  OG  SER A 638     223.331 184.057 172.475  1.00162.63           O  
ATOM   4891  N   LYS A 639     227.085 186.446 170.869  1.00164.08           N  
ATOM   4892  CA  LYS A 639     227.685 187.634 170.271  1.00164.08           C  
ATOM   4893  C   LYS A 639     228.950 187.312 169.492  1.00164.08           C  
ATOM   4894  O   LYS A 639     229.158 187.875 168.414  1.00164.08           O  
ATOM   4895  CB  LYS A 639     227.990 188.683 171.355  1.00164.08           C  
ATOM   4896  CG  LYS A 639     226.758 189.215 172.072  1.00164.08           C  
ATOM   4897  CD  LYS A 639     225.862 189.994 171.121  1.00164.08           C  
ATOM   4898  CE  LYS A 639     224.626 190.524 171.830  1.00164.08           C  
ATOM   4899  NZ  LYS A 639     223.672 189.434 172.174  1.00164.08           N  
ATOM   4900  N   SER A 640     229.799 186.424 170.007  1.00165.56           N  
ATOM   4901  CA  SER A 640     230.973 185.986 169.262  1.00165.56           C  
ATOM   4902  C   SER A 640     230.693 184.710 168.477  1.00165.56           C  
ATOM   4903  O   SER A 640     231.096 184.591 167.315  1.00165.56           O  
ATOM   4904  CB  SER A 640     232.153 185.770 170.212  1.00165.56           C  
ATOM   4905  OG  SER A 640     232.538 186.986 170.829  1.00165.56           O  
ATOM   4906  N   LEU A 641     230.005 183.759 169.100  1.00157.31           N  
ATOM   4907  CA  LEU A 641     229.676 182.486 168.471  1.00157.31           C  
ATOM   4908  C   LEU A 641     228.444 182.642 167.585  1.00157.31           C  
ATOM   4909  O   LEU A 641     227.461 183.258 168.008  1.00157.31           O  
ATOM   4910  CB  LEU A 641     229.423 181.413 169.530  1.00157.31           C  
ATOM   4911  CG  LEU A 641     230.628 180.702 170.153  1.00157.31           C  
ATOM   4912  CD1 LEU A 641     231.418 181.632 171.064  1.00157.31           C  
ATOM   4913  CD2 LEU A 641     230.179 179.465 170.917  1.00157.31           C  
ATOM   4914  N   PRO A 642     228.456 182.108 166.363  1.00141.98           N  
ATOM   4915  CA  PRO A 642     227.233 182.124 165.549  1.00141.98           C  
ATOM   4916  C   PRO A 642     226.271 181.027 165.975  1.00141.98           C  
ATOM   4917  O   PRO A 642     226.504 180.355 166.985  1.00141.98           O  
ATOM   4918  CB  PRO A 642     227.759 181.899 164.128  1.00141.98           C  
ATOM   4919  CG  PRO A 642     228.995 181.086 164.330  1.00141.98           C  
ATOM   4920  CD  PRO A 642     229.609 181.570 165.620  1.00141.98           C  
ATOM   4921  N   ASN A 643     225.187 180.832 165.219  1.00127.83           N  
ATOM   4922  CA  ASN A 643     224.144 179.912 165.658  1.00127.83           C  
ATOM   4923  C   ASN A 643     224.598 178.458 165.638  1.00127.83           C  
ATOM   4924  O   ASN A 643     224.029 177.636 166.364  1.00127.83           O  
ATOM   4925  CB  ASN A 643     222.897 180.074 164.786  1.00127.83           C  
ATOM   4926  CG  ASN A 643     222.219 181.415 164.982  1.00127.83           C  
ATOM   4927  OD1 ASN A 643     222.097 181.904 166.106  1.00127.83           O  
ATOM   4928  ND2 ASN A 643     221.771 182.018 163.887  1.00127.83           N  
ATOM   4929  N   GLU A 644     225.605 178.123 164.827  1.00132.95           N  
ATOM   4930  CA  GLU A 644     226.011 176.728 164.689  1.00132.95           C  
ATOM   4931  C   GLU A 644     226.664 176.194 165.958  1.00132.95           C  
ATOM   4932  O   GLU A 644     226.496 175.014 166.289  1.00132.95           O  
ATOM   4933  CB  GLU A 644     226.961 176.569 163.501  1.00132.95           C  
ATOM   4934  CG  GLU A 644     226.321 176.831 162.146  1.00132.95           C  
ATOM   4935  CD  GLU A 644     226.319 178.299 161.770  1.00132.95           C  
ATOM   4936  OE1 GLU A 644     226.832 179.118 162.561  1.00132.95           O  
ATOM   4937  OE2 GLU A 644     225.805 178.635 160.682  1.00132.95           O  
ATOM   4938  N   MET A 645     227.405 177.034 166.677  1.00145.02           N  
ATOM   4939  CA  MET A 645     228.204 176.579 167.816  1.00145.02           C  
ATOM   4940  C   MET A 645     227.372 176.553 169.100  1.00145.02           C  
ATOM   4941  O   MET A 645     227.707 177.165 170.114  1.00145.02           O  
ATOM   4942  CB  MET A 645     229.441 177.455 167.971  1.00145.02           C  
ATOM   4943  CG  MET A 645     230.401 177.368 166.796  1.00145.02           C  
ATOM   4944  SD  MET A 645     231.052 175.702 166.569  1.00145.02           S  
ATOM   4945  CE  MET A 645     231.881 175.873 164.991  1.00145.02           C  
ATOM   4946  N   SER A 646     226.264 175.820 169.039  1.00136.93           N  
ATOM   4947  CA  SER A 646     225.387 175.676 170.189  1.00136.93           C  
ATOM   4948  C   SER A 646     225.981 174.677 171.181  1.00136.93           C  
ATOM   4949  O   SER A 646     226.963 173.986 170.898  1.00136.93           O  
ATOM   4950  CB  SER A 646     223.992 175.236 169.749  1.00136.93           C  
ATOM   4951  OG  SER A 646     224.014 173.919 169.227  1.00136.93           O  
ATOM   4952  N   GLN A 647     225.370 174.603 172.366  1.00138.10           N  
ATOM   4953  CA  GLN A 647     225.814 173.616 173.344  1.00138.10           C  
ATOM   4954  C   GLN A 647     225.383 172.214 172.932  1.00138.10           C  
ATOM   4955  O   GLN A 647     226.148 171.254 173.077  1.00138.10           O  
ATOM   4956  CB  GLN A 647     225.273 173.964 174.731  1.00138.10           C  
ATOM   4957  CG  GLN A 647     225.862 175.233 175.333  1.00138.10           C  
ATOM   4958  CD  GLN A 647     225.182 176.493 174.833  1.00138.10           C  
ATOM   4959  OE1 GLN A 647     224.104 176.437 174.241  1.00138.10           O  
ATOM   4960  NE2 GLN A 647     225.811 177.639 175.069  1.00138.10           N  
ATOM   4961  N   ASN A 648     224.164 172.079 172.418  1.00131.59           N  
ATOM   4962  CA  ASN A 648     223.730 170.869 171.740  1.00131.59           C  
ATOM   4963  C   ASN A 648     224.141 170.954 170.270  1.00131.59           C  
ATOM   4964  O   ASN A 648     224.943 171.804 169.875  1.00131.59           O  
ATOM   4965  CB  ASN A 648     222.225 170.669 171.916  1.00131.59           C  
ATOM   4966  CG  ASN A 648     221.411 171.846 171.404  1.00131.59           C  
ATOM   4967  OD1 ASN A 648     221.958 172.828 170.903  1.00131.59           O  
ATOM   4968  ND2 ASN A 648     220.093 171.748 171.529  1.00131.59           N  
ATOM   4969  N   ASP A 649     223.593 170.067 169.437  1.00122.00           N  
ATOM   4970  CA  ASP A 649     223.855 170.157 168.005  1.00122.00           C  
ATOM   4971  C   ASP A 649     223.102 171.334 167.394  1.00122.00           C  
ATOM   4972  O   ASP A 649     223.658 172.084 166.582  1.00122.00           O  
ATOM   4973  CB  ASP A 649     223.477 168.842 167.324  1.00122.00           C  
ATOM   4974  CG  ASP A 649     224.138 168.674 165.972  1.00122.00           C  
ATOM   4975  OD1 ASP A 649     224.847 169.604 165.533  1.00122.00           O  
ATOM   4976  OD2 ASP A 649     223.956 167.607 165.350  1.00122.00           O  
ATOM   4977  N   GLY A 650     221.842 171.508 167.778  1.00117.16           N  
ATOM   4978  CA  GLY A 650     221.122 172.751 167.540  1.00117.16           C  
ATOM   4979  C   GLY A 650     220.935 173.118 166.079  1.00117.16           C  
ATOM   4980  O   GLY A 650     220.258 172.417 165.317  1.00117.16           O  
ATOM   4981  N   PHE A 651     221.546 174.230 165.674  1.00114.72           N  
ATOM   4982  CA  PHE A 651     221.286 174.802 164.359  1.00114.72           C  
ATOM   4983  C   PHE A 651     221.862 173.921 163.256  1.00114.72           C  
ATOM   4984  O   PHE A 651     223.026 173.513 163.313  1.00114.72           O  
ATOM   4985  CB  PHE A 651     221.875 176.210 164.279  1.00114.72           C  
ATOM   4986  CG  PHE A 651     221.314 177.042 163.161  1.00114.72           C  
ATOM   4987  CD1 PHE A 651     220.109 177.707 163.319  1.00114.72           C  
ATOM   4988  CD2 PHE A 651     221.990 177.167 161.960  1.00114.72           C  
ATOM   4989  CE1 PHE A 651     219.585 178.477 162.298  1.00114.72           C  
ATOM   4990  CE2 PHE A 651     221.471 177.937 160.934  1.00114.72           C  
ATOM   4991  CZ  PHE A 651     220.267 178.592 161.104  1.00114.72           C  
ATOM   4992  N   VAL A 652     221.038 173.631 162.249  1.00103.05           N  
ATOM   4993  CA  VAL A 652     221.338 172.623 161.238  1.00103.05           C  
ATOM   4994  C   VAL A 652     221.772 173.310 159.950  1.00103.05           C  
ATOM   4995  O   VAL A 652     221.181 174.314 159.530  1.00103.05           O  
ATOM   4996  CB  VAL A 652     220.124 171.699 161.001  1.00103.05           C  
ATOM   4997  CG1 VAL A 652     218.905 172.498 160.559  1.00103.05           C  
ATOM   4998  CG2 VAL A 652     220.458 170.624 159.978  1.00103.05           C  
ATOM   4999  N   ILE A 653     222.829 172.782 159.335  1.00 98.69           N  
ATOM   5000  CA  ILE A 653     223.391 173.313 158.100  1.00 98.69           C  
ATOM   5001  C   ILE A 653     223.561 172.155 157.129  1.00 98.69           C  
ATOM   5002  O   ILE A 653     224.160 171.132 157.481  1.00 98.69           O  
ATOM   5003  CB  ILE A 653     224.739 174.022 158.334  1.00 98.69           C  
ATOM   5004  CG1 ILE A 653     224.578 175.187 159.312  1.00 98.69           C  
ATOM   5005  CG2 ILE A 653     225.323 174.509 157.015  1.00 98.69           C  
ATOM   5006  CD1 ILE A 653     223.715 176.308 158.785  1.00 98.69           C  
ATOM   5007  N   ILE A 654     223.034 172.306 155.916  1.00 97.74           N  
ATOM   5008  CA  ILE A 654     223.344 171.400 154.817  1.00 97.74           C  
ATOM   5009  C   ILE A 654     223.792 172.219 153.614  1.00 97.74           C  
ATOM   5010  O   ILE A 654     223.156 173.219 153.262  1.00 97.74           O  
ATOM   5011  CB  ILE A 654     222.150 170.487 154.464  1.00 97.74           C  
ATOM   5012  CG1 ILE A 654     220.868 171.289 154.226  1.00 97.74           C  
ATOM   5013  CG2 ILE A 654     221.925 169.464 155.561  1.00 97.74           C  
ATOM   5014  CD1 ILE A 654     220.534 171.480 152.765  1.00 97.74           C  
ATOM   5015  N   ARG A 655     224.899 171.803 153.002  1.00 96.41           N  
ATOM   5016  CA  ARG A 655     225.465 172.464 151.832  1.00 96.41           C  
ATOM   5017  C   ARG A 655     225.850 171.383 150.835  1.00 96.41           C  
ATOM   5018  O   ARG A 655     226.666 170.512 151.152  1.00 96.41           O  
ATOM   5019  CB  ARG A 655     226.681 173.322 152.201  1.00 96.41           C  
ATOM   5020  CG  ARG A 655     226.393 174.418 153.219  1.00 96.41           C  
ATOM   5021  CD  ARG A 655     225.482 175.491 152.642  1.00 96.41           C  
ATOM   5022  NE  ARG A 655     225.141 176.511 153.630  1.00 96.41           N  
ATOM   5023  CZ  ARG A 655     225.857 177.609 153.850  1.00 96.41           C  
ATOM   5024  NH1 ARG A 655     226.958 177.838 153.148  1.00 96.41           N  
ATOM   5025  NH2 ARG A 655     225.469 178.482 154.770  1.00 96.41           N  
ATOM   5026  N   GLY A 656     225.268 171.435 149.640  1.00 91.08           N  
ATOM   5027  CA  GLY A 656     225.539 170.411 148.649  1.00 91.08           C  
ATOM   5028  C   GLY A 656     224.935 169.069 148.995  1.00 91.08           C  
ATOM   5029  O   GLY A 656     225.434 168.034 148.544  1.00 91.08           O  
ATOM   5030  N   SER A 657     223.860 169.070 149.786  1.00 85.42           N  
ATOM   5031  CA  SER A 657     223.166 167.859 150.228  1.00 85.42           C  
ATOM   5032  C   SER A 657     224.091 166.925 151.007  1.00 85.42           C  
ATOM   5033  O   SER A 657     224.229 165.741 150.695  1.00 85.42           O  
ATOM   5034  CB  SER A 657     222.521 167.131 149.045  1.00 85.42           C  
ATOM   5035  OG  SER A 657     221.514 167.926 148.446  1.00 85.42           O  
ATOM   5036  N   GLN A 658     224.731 167.476 152.037  1.00 91.69           N  
ATOM   5037  CA  GLN A 658     225.358 166.684 153.084  1.00 91.69           C  
ATOM   5038  C   GLN A 658     225.018 167.328 154.418  1.00 91.69           C  
ATOM   5039  O   GLN A 658     224.995 168.557 154.527  1.00 91.69           O  
ATOM   5040  CB  GLN A 658     226.882 166.596 152.917  1.00 91.69           C  
ATOM   5041  CG  GLN A 658     227.347 165.787 151.716  1.00 91.69           C  
ATOM   5042  CD  GLN A 658     227.410 166.610 150.446  1.00 91.69           C  
ATOM   5043  OE1 GLN A 658     227.465 167.839 150.493  1.00 91.69           O  
ATOM   5044  NE2 GLN A 658     227.406 165.937 149.302  1.00 91.69           N  
ATOM   5045  N   ILE A 659     224.754 166.503 155.431  1.00 87.88           N  
ATOM   5046  CA  ILE A 659     224.538 167.036 156.769  1.00 87.88           C  
ATOM   5047  C   ILE A 659     225.846 167.608 157.297  1.00 87.88           C  
ATOM   5048  O   ILE A 659     226.876 166.922 157.317  1.00 87.88           O  
ATOM   5049  CB  ILE A 659     223.992 165.945 157.702  1.00 87.88           C  
ATOM   5050  CG1 ILE A 659     222.750 165.287 157.097  1.00 87.88           C  
ATOM   5051  CG2 ILE A 659     223.661 166.532 159.064  1.00 87.88           C  
ATOM   5052  CD1 ILE A 659     221.559 166.207 156.987  1.00 87.88           C  
ATOM   5053  N   LEU A 660     225.816 168.871 157.729  1.00 89.78           N  
ATOM   5054  CA  LEU A 660     226.995 169.485 158.320  1.00 89.78           C  
ATOM   5055  C   LEU A 660     226.831 169.827 159.793  1.00 89.78           C  
ATOM   5056  O   LEU A 660     227.838 169.960 160.495  1.00 89.78           O  
ATOM   5057  CB  LEU A 660     227.377 170.760 157.553  1.00 89.78           C  
ATOM   5058  CG  LEU A 660     227.677 170.576 156.064  1.00 89.78           C  
ATOM   5059  CD1 LEU A 660     228.019 171.908 155.414  1.00 89.78           C  
ATOM   5060  CD2 LEU A 660     228.798 169.569 155.859  1.00 89.78           C  
ATOM   5061  N   SER A 661     225.598 169.968 160.272  1.00103.13           N  
ATOM   5062  CA  SER A 661     225.324 170.217 161.681  1.00103.13           C  
ATOM   5063  C   SER A 661     223.887 169.799 161.964  1.00103.13           C  
ATOM   5064  O   SER A 661     223.178 169.304 161.083  1.00103.13           O  
ATOM   5065  CB  SER A 661     225.569 171.685 162.044  1.00103.13           C  
ATOM   5066  OG  SER A 661     224.655 172.536 161.374  1.00103.13           O  
ATOM   5067  N   GLY A 662     223.463 169.995 163.209  1.00106.89           N  
ATOM   5068  CA  GLY A 662     222.065 169.863 163.568  1.00106.89           C  
ATOM   5069  C   GLY A 662     221.532 168.446 163.624  1.00106.89           C  
ATOM   5070  O   GLY A 662     222.169 167.506 163.138  1.00106.89           O  
ATOM   5071  N   VAL A 663     220.351 168.289 164.218  1.00104.41           N  
ATOM   5072  CA  VAL A 663     219.627 167.024 164.214  1.00104.41           C  
ATOM   5073  C   VAL A 663     218.258 167.264 163.593  1.00104.41           C  
ATOM   5074  O   VAL A 663     217.932 168.392 163.207  1.00104.41           O  
ATOM   5075  CB  VAL A 663     219.500 166.440 165.632  1.00104.41           C  
ATOM   5076  CG1 VAL A 663     220.875 166.124 166.203  1.00104.41           C  
ATOM   5077  CG2 VAL A 663     218.749 167.405 166.537  1.00104.41           C  
ATOM   5078  N   MET A 664     217.448 166.214 163.490  1.00102.92           N  
ATOM   5079  CA  MET A 664     216.112 166.310 162.912  1.00102.92           C  
ATOM   5080  C   MET A 664     215.095 166.017 164.008  1.00102.92           C  
ATOM   5081  O   MET A 664     214.956 164.869 164.444  1.00102.92           O  
ATOM   5082  CB  MET A 664     215.953 165.347 161.738  1.00102.92           C  
ATOM   5083  CG  MET A 664     216.630 165.812 160.461  1.00102.92           C  
ATOM   5084  SD  MET A 664     218.411 165.553 160.505  1.00102.92           S  
ATOM   5085  CE  MET A 664     218.482 163.771 160.358  1.00102.92           C  
ATOM   5086  N   ASP A 665     214.388 167.053 164.446  1.00112.38           N  
ATOM   5087  CA  ASP A 665     213.474 166.963 165.580  1.00112.38           C  
ATOM   5088  C   ASP A 665     212.161 167.665 165.247  1.00112.38           C  
ATOM   5089  O   ASP A 665     211.705 168.557 165.964  1.00112.38           O  
ATOM   5090  CB  ASP A 665     214.113 167.532 166.847  1.00112.38           C  
ATOM   5091  CG  ASP A 665     214.625 168.948 166.662  1.00112.38           C  
ATOM   5092  OD1 ASP A 665     214.525 169.484 165.538  1.00112.38           O  
ATOM   5093  OD2 ASP A 665     215.126 169.526 167.648  1.00112.38           O  
ATOM   5094  N   LYS A 666     211.549 167.276 164.128  1.00105.83           N  
ATOM   5095  CA  LYS A 666     210.181 167.585 163.729  1.00105.83           C  
ATOM   5096  C   LYS A 666     210.070 169.034 163.232  1.00105.83           C  
ATOM   5097  O   LYS A 666     209.059 169.387 162.622  1.00105.83           O  
ATOM   5098  CB  LYS A 666     209.158 167.322 164.858  1.00105.83           C  
ATOM   5099  CG  LYS A 666     207.725 167.806 164.660  1.00105.83           C  
ATOM   5100  CD  LYS A 666     207.041 167.073 163.516  1.00105.83           C  
ATOM   5101  CE  LYS A 666     205.574 167.460 163.410  1.00105.83           C  
ATOM   5102  NZ  LYS A 666     205.397 168.894 163.055  1.00105.83           N  
ATOM   5103  N   SER A 667     211.104 169.859 163.396  1.00102.66           N  
ATOM   5104  CA  SER A 667     211.151 171.174 162.773  1.00102.66           C  
ATOM   5105  C   SER A 667     212.029 171.209 161.529  1.00102.66           C  
ATOM   5106  O   SER A 667     212.101 172.248 160.866  1.00102.66           O  
ATOM   5107  CB  SER A 667     211.643 172.219 163.780  1.00102.66           C  
ATOM   5108  OG  SER A 667     211.696 173.508 163.193  1.00102.66           O  
ATOM   5109  N   VAL A 668     212.695 170.105 161.200  1.00 91.76           N  
ATOM   5110  CA  VAL A 668     213.621 170.048 160.081  1.00 91.76           C  
ATOM   5111  C   VAL A 668     213.083 169.160 158.966  1.00 91.76           C  
ATOM   5112  O   VAL A 668     213.274 169.452 157.784  1.00 91.76           O  
ATOM   5113  CB  VAL A 668     215.014 169.570 160.544  1.00 91.76           C  
ATOM   5114  CG1 VAL A 668     215.987 169.528 159.375  1.00 91.76           C  
ATOM   5115  CG2 VAL A 668     215.541 170.475 161.641  1.00 91.76           C  
ATOM   5116  N   LEU A 669     212.393 168.081 159.333  1.00 91.51           N  
ATOM   5117  CA  LEU A 669     211.869 167.109 158.390  1.00 91.51           C  
ATOM   5118  C   LEU A 669     210.367 166.920 158.526  1.00 91.51           C  
ATOM   5119  O   LEU A 669     209.756 166.292 157.654  1.00 91.51           O  
ATOM   5120  CB  LEU A 669     212.564 165.749 158.571  1.00 91.51           C  
ATOM   5121  CG  LEU A 669     212.026 164.841 159.682  1.00 91.51           C  
ATOM   5122  CD1 LEU A 669     212.503 163.410 159.482  1.00 91.51           C  
ATOM   5123  CD2 LEU A 669     212.411 165.347 161.065  1.00 91.51           C  
ATOM   5124  N   GLY A 670     209.765 167.441 159.587  1.00102.93           N  
ATOM   5125  CA  GLY A 670     208.380 167.187 159.926  1.00102.93           C  
ATOM   5126  C   GLY A 670     207.427 168.230 159.386  1.00102.93           C  
ATOM   5127  O   GLY A 670     207.646 168.826 158.327  1.00102.93           O  
ATOM   5128  N   ASP A 671     206.352 168.450 160.135  1.00107.97           N  
ATOM   5129  CA  ASP A 671     205.201 169.223 159.704  1.00107.97           C  
ATOM   5130  C   ASP A 671     205.231 170.602 160.364  1.00107.97           C  
ATOM   5131  O   ASP A 671     206.097 170.909 161.187  1.00107.97           O  
ATOM   5132  CB  ASP A 671     203.910 168.466 160.034  1.00107.97           C  
ATOM   5133  CG  ASP A 671     202.708 168.990 159.270  1.00107.97           C  
ATOM   5134  OD1 ASP A 671     202.855 169.990 158.538  1.00107.97           O  
ATOM   5135  OD2 ASP A 671     201.615 168.402 159.403  1.00107.97           O  
ATOM   5136  N   GLY A 672     204.270 171.444 159.993  1.00106.70           N  
ATOM   5137  CA  GLY A 672     204.078 172.710 160.672  1.00106.70           C  
ATOM   5138  C   GLY A 672     204.977 173.831 160.192  1.00106.70           C  
ATOM   5139  O   GLY A 672     204.479 174.878 159.766  1.00106.70           O  
ATOM   5140  N   LYS A 673     206.292 173.642 160.253  1.00 98.96           N  
ATOM   5141  CA  LYS A 673     207.210 174.694 159.840  1.00 98.96           C  
ATOM   5142  C   LYS A 673     207.435 174.659 158.333  1.00 98.96           C  
ATOM   5143  O   LYS A 673     207.464 173.591 157.716  1.00 98.96           O  
ATOM   5144  CB  LYS A 673     208.546 174.558 160.571  1.00 98.96           C  
ATOM   5145  CG  LYS A 673     208.599 175.261 161.921  1.00 98.96           C  
ATOM   5146  CD  LYS A 673     207.871 174.476 163.002  1.00 98.96           C  
ATOM   5147  CE  LYS A 673     208.009 175.152 164.357  1.00 98.96           C  
ATOM   5148  NZ  LYS A 673     207.256 174.433 165.421  1.00 98.96           N  
ATOM   5149  N   LYS A 674     207.592 175.848 157.747  1.00 97.89           N  
ATOM   5150  CA  LYS A 674     207.728 175.965 156.298  1.00 97.89           C  
ATOM   5151  C   LYS A 674     209.086 175.466 155.816  1.00 97.89           C  
ATOM   5152  O   LYS A 674     209.182 174.835 154.757  1.00 97.89           O  
ATOM   5153  CB  LYS A 674     207.510 177.417 155.870  1.00 97.89           C  
ATOM   5154  CG  LYS A 674     207.579 177.647 154.369  1.00 97.89           C  
ATOM   5155  CD  LYS A 674     206.448 176.936 153.643  1.00 97.89           C  
ATOM   5156  CE  LYS A 674     205.095 177.505 154.037  1.00 97.89           C  
ATOM   5157  NZ  LYS A 674     204.930 178.917 153.594  1.00 97.89           N  
ATOM   5158  N   HIS A 675     210.142 175.734 156.580  1.00 97.88           N  
ATOM   5159  CA  HIS A 675     211.516 175.523 156.122  1.00 97.88           C  
ATOM   5160  C   HIS A 675     212.004 174.112 156.456  1.00 97.88           C  
ATOM   5161  O   HIS A 675     213.023 173.908 157.116  1.00 97.88           O  
ATOM   5162  CB  HIS A 675     212.432 176.582 156.724  1.00 97.88           C  
ATOM   5163  CG  HIS A 675     212.293 176.726 158.208  1.00 97.88           C  
ATOM   5164  ND1 HIS A 675     212.949 175.906 159.101  1.00 97.88           N  
ATOM   5165  CD2 HIS A 675     211.571 177.593 158.956  1.00 97.88           C  
ATOM   5166  CE1 HIS A 675     212.637 176.262 160.334  1.00 97.88           C  
ATOM   5167  NE2 HIS A 675     211.803 177.284 160.274  1.00 97.88           N  
ATOM   5168  N   SER A 676     211.252 173.125 155.981  1.00 94.16           N  
ATOM   5169  CA  SER A 676     211.577 171.726 156.212  1.00 94.16           C  
ATOM   5170  C   SER A 676     212.273 171.126 154.992  1.00 94.16           C  
ATOM   5171  O   SER A 676     212.272 171.692 153.897  1.00 94.16           O  
ATOM   5172  CB  SER A 676     210.314 170.930 156.553  1.00 94.16           C  
ATOM   5173  OG  SER A 676     209.470 170.800 155.423  1.00 94.16           O  
ATOM   5174  N   VAL A 677     212.880 169.957 155.205  1.00 85.79           N  
ATOM   5175  CA  VAL A 677     213.674 169.317 154.159  1.00 85.79           C  
ATOM   5176  C   VAL A 677     212.775 168.824 153.031  1.00 85.79           C  
ATOM   5177  O   VAL A 677     213.041 169.065 151.848  1.00 85.79           O  
ATOM   5178  CB  VAL A 677     214.520 168.175 154.749  1.00 85.79           C  
ATOM   5179  CG1 VAL A 677     215.105 167.316 153.638  1.00 85.79           C  
ATOM   5180  CG2 VAL A 677     215.626 168.735 155.630  1.00 85.79           C  
ATOM   5181  N   PHE A 678     211.693 168.126 153.384  1.00 88.37           N  
ATOM   5182  CA  PHE A 678     210.764 167.594 152.393  1.00 88.37           C  
ATOM   5183  C   PHE A 678     210.014 168.691 151.650  1.00 88.37           C  
ATOM   5184  O   PHE A 678     209.535 168.452 150.536  1.00 88.37           O  
ATOM   5185  CB  PHE A 678     209.771 166.648 153.069  1.00 88.37           C  
ATOM   5186  CG  PHE A 678     210.396 165.381 153.584  1.00 88.37           C  
ATOM   5187  CD1 PHE A 678     211.582 164.909 153.047  1.00 88.37           C  
ATOM   5188  CD2 PHE A 678     209.802 164.669 154.613  1.00 88.37           C  
ATOM   5189  CE1 PHE A 678     212.161 163.747 153.521  1.00 88.37           C  
ATOM   5190  CE2 PHE A 678     210.376 163.506 155.092  1.00 88.37           C  
ATOM   5191  CZ  PHE A 678     211.558 163.045 154.546  1.00 88.37           C  
ATOM   5192  N   TYR A 679     209.898 169.882 152.240  1.00 90.00           N  
ATOM   5193  CA  TYR A 679     209.375 171.030 151.506  1.00 90.00           C  
ATOM   5194  C   TYR A 679     210.299 171.425 150.360  1.00 90.00           C  
ATOM   5195  O   TYR A 679     209.833 171.801 149.278  1.00 90.00           O  
ATOM   5196  CB  TYR A 679     209.172 172.206 152.463  1.00 90.00           C  
ATOM   5197  CG  TYR A 679     208.754 173.492 151.789  1.00 90.00           C  
ATOM   5198  CD1 TYR A 679     207.461 173.662 151.316  1.00 90.00           C  
ATOM   5199  CD2 TYR A 679     209.654 174.539 151.631  1.00 90.00           C  
ATOM   5200  CE1 TYR A 679     207.074 174.839 150.705  1.00 90.00           C  
ATOM   5201  CE2 TYR A 679     209.277 175.718 151.019  1.00 90.00           C  
ATOM   5202  CZ  TYR A 679     207.986 175.863 150.559  1.00 90.00           C  
ATOM   5203  OH  TYR A 679     207.606 177.035 149.946  1.00 90.00           O  
ATOM   5204  N   THR A 680     211.613 171.345 150.576  1.00 85.72           N  
ATOM   5205  CA  THR A 680     212.564 171.946 149.646  1.00 85.72           C  
ATOM   5206  C   THR A 680     212.777 171.075 148.412  1.00 85.72           C  
ATOM   5207  O   THR A 680     212.893 171.595 147.296  1.00 85.72           O  
ATOM   5208  CB  THR A 680     213.896 172.204 150.352  1.00 85.72           C  
ATOM   5209  OG1 THR A 680     213.667 173.000 151.521  1.00 85.72           O  
ATOM   5210  CG2 THR A 680     214.858 172.939 149.430  1.00 85.72           C  
ATOM   5211  N   ILE A 681     212.824 169.752 148.587  1.00 85.99           N  
ATOM   5212  CA  ILE A 681     212.894 168.861 147.433  1.00 85.99           C  
ATOM   5213  C   ILE A 681     211.601 168.912 146.628  1.00 85.99           C  
ATOM   5214  O   ILE A 681     211.611 168.702 145.409  1.00 85.99           O  
ATOM   5215  CB  ILE A 681     213.220 167.427 147.889  1.00 85.99           C  
ATOM   5216  CG1 ILE A 681     212.216 166.964 148.947  1.00 85.99           C  
ATOM   5217  CG2 ILE A 681     214.640 167.350 148.427  1.00 85.99           C  
ATOM   5218  CD1 ILE A 681     212.327 165.499 149.297  1.00 85.99           C  
ATOM   5219  N   LEU A 682     210.473 169.189 147.286  1.00 88.44           N  
ATOM   5220  CA  LEU A 682     209.245 169.498 146.562  1.00 88.44           C  
ATOM   5221  C   LEU A 682     209.370 170.811 145.799  1.00 88.44           C  
ATOM   5222  O   LEU A 682     208.809 170.951 144.706  1.00 88.44           O  
ATOM   5223  CB  LEU A 682     208.064 169.541 147.538  1.00 88.44           C  
ATOM   5224  CG  LEU A 682     206.630 169.769 147.037  1.00 88.44           C  
ATOM   5225  CD1 LEU A 682     206.283 171.253 146.923  1.00 88.44           C  
ATOM   5226  CD2 LEU A 682     206.386 169.050 145.715  1.00 88.44           C  
ATOM   5227  N   ARG A 683     210.103 171.776 146.357  1.00 97.59           N  
ATOM   5228  CA  ARG A 683     210.155 173.116 145.782  1.00 97.59           C  
ATOM   5229  C   ARG A 683     210.979 173.152 144.499  1.00 97.59           C  
ATOM   5230  O   ARG A 683     210.539 173.709 143.486  1.00 97.59           O  
ATOM   5231  CB  ARG A 683     210.715 174.101 146.809  1.00 97.59           C  
ATOM   5232  CG  ARG A 683     210.819 175.528 146.302  1.00 97.59           C  
ATOM   5233  CD  ARG A 683     209.465 176.067 145.874  1.00 97.59           C  
ATOM   5234  NE  ARG A 683     208.503 176.082 146.972  1.00 97.59           N  
ATOM   5235  CZ  ARG A 683     207.188 176.179 146.806  1.00 97.59           C  
ATOM   5236  NH1 ARG A 683     206.679 176.259 145.586  1.00 97.59           N  
ATOM   5237  NH2 ARG A 683     206.381 176.188 147.858  1.00 97.59           N  
ATOM   5238  N   ASP A 684     212.175 172.565 144.516  1.00 92.48           N  
ATOM   5239  CA  ASP A 684     213.137 172.759 143.440  1.00 92.48           C  
ATOM   5240  C   ASP A 684     213.368 171.520 142.585  1.00 92.48           C  
ATOM   5241  O   ASP A 684     214.193 171.570 141.667  1.00 92.48           O  
ATOM   5242  CB  ASP A 684     214.479 173.232 144.014  1.00 92.48           C  
ATOM   5243  CG  ASP A 684     214.382 174.591 144.676  1.00 92.48           C  
ATOM   5244  OD1 ASP A 684     213.545 175.407 144.238  1.00 92.48           O  
ATOM   5245  OD2 ASP A 684     215.145 174.845 145.632  1.00 92.48           O  
ATOM   5246  N   TYR A 685     212.671 170.411 142.852  1.00 80.84           N  
ATOM   5247  CA  TYR A 685     212.879 169.213 142.046  1.00 80.84           C  
ATOM   5248  C   TYR A 685     211.572 168.500 141.713  1.00 80.84           C  
ATOM   5249  O   TYR A 685     211.588 167.296 141.429  1.00 80.84           O  
ATOM   5250  CB  TYR A 685     213.838 168.248 142.750  1.00 80.84           C  
ATOM   5251  CG  TYR A 685     215.232 168.809 142.900  1.00 80.84           C  
ATOM   5252  CD1 TYR A 685     216.119 168.804 141.833  1.00 80.84           C  
ATOM   5253  CD2 TYR A 685     215.656 169.358 144.103  1.00 80.84           C  
ATOM   5254  CE1 TYR A 685     217.392 169.321 141.960  1.00 80.84           C  
ATOM   5255  CE2 TYR A 685     216.928 169.878 144.240  1.00 80.84           C  
ATOM   5256  CZ  TYR A 685     217.791 169.856 143.165  1.00 80.84           C  
ATOM   5257  OH  TYR A 685     219.059 170.372 143.293  1.00 80.84           O  
ATOM   5258  N   GLY A 686     210.447 169.209 141.739  1.00 82.90           N  
ATOM   5259  CA  GLY A 686     209.179 168.651 141.338  1.00 82.90           C  
ATOM   5260  C   GLY A 686     208.573 167.766 142.406  1.00 82.90           C  
ATOM   5261  O   GLY A 686     209.173 167.516 143.456  1.00 82.90           O  
ATOM   5262  N   PRO A 687     207.357 167.270 142.154  1.00 80.43           N  
ATOM   5263  CA  PRO A 687     206.719 166.376 143.130  1.00 80.43           C  
ATOM   5264  C   PRO A 687     207.223 164.945 143.080  1.00 80.43           C  
ATOM   5265  O   PRO A 687     207.110 164.235 144.088  1.00 80.43           O  
ATOM   5266  CB  PRO A 687     205.237 166.444 142.744  1.00 80.43           C  
ATOM   5267  CG  PRO A 687     205.257 166.731 141.280  1.00 80.43           C  
ATOM   5268  CD  PRO A 687     206.454 167.616 141.043  1.00 80.43           C  
ATOM   5269  N   GLN A 688     207.768 164.499 141.946  1.00 81.35           N  
ATOM   5270  CA  GLN A 688     208.111 163.088 141.792  1.00 81.35           C  
ATOM   5271  C   GLN A 688     209.288 162.702 142.680  1.00 81.35           C  
ATOM   5272  O   GLN A 688     209.252 161.672 143.364  1.00 81.35           O  
ATOM   5273  CB  GLN A 688     208.417 162.780 140.326  1.00 81.35           C  
ATOM   5274  CG  GLN A 688     208.739 161.320 140.052  1.00 81.35           C  
ATOM   5275  CD  GLN A 688     207.618 160.387 140.465  1.00 81.35           C  
ATOM   5276  OE1 GLN A 688     207.711 159.696 141.479  1.00 81.35           O  
ATOM   5277  NE2 GLN A 688     206.548 160.362 139.678  1.00 81.35           N  
ATOM   5278  N   GLU A 689     210.343 163.520 142.684  1.00 85.49           N  
ATOM   5279  CA  GLU A 689     211.479 163.265 143.560  1.00 85.49           C  
ATOM   5280  C   GLU A 689     211.174 163.563 145.022  1.00 85.49           C  
ATOM   5281  O   GLU A 689     211.892 163.075 145.901  1.00 85.49           O  
ATOM   5282  CB  GLU A 689     212.686 164.087 143.106  1.00 85.49           C  
ATOM   5283  CG  GLU A 689     213.216 163.704 141.732  1.00 85.49           C  
ATOM   5284  CD  GLU A 689     213.834 162.320 141.709  1.00 85.49           C  
ATOM   5285  OE1 GLU A 689     214.392 161.897 142.743  1.00 85.49           O  
ATOM   5286  OE2 GLU A 689     213.762 161.654 140.655  1.00 85.49           O  
ATOM   5287  N   ALA A 690     210.135 164.352 145.305  1.00 82.99           N  
ATOM   5288  CA  ALA A 690     209.781 164.623 146.694  1.00 82.99           C  
ATOM   5289  C   ALA A 690     209.241 163.375 147.382  1.00 82.99           C  
ATOM   5290  O   ALA A 690     209.631 163.060 148.513  1.00 82.99           O  
ATOM   5291  CB  ALA A 690     208.762 165.760 146.763  1.00 82.99           C  
ATOM   5292  N   ALA A 691     208.339 162.649 146.717  1.00 83.65           N  
ATOM   5293  CA  ALA A 691     207.853 161.395 147.282  1.00 83.65           C  
ATOM   5294  C   ALA A 691     208.935 160.322 147.265  1.00 83.65           C  
ATOM   5295  O   ALA A 691     209.017 159.500 148.185  1.00 83.65           O  
ATOM   5296  CB  ALA A 691     206.614 160.922 146.523  1.00 83.65           C  
ATOM   5297  N   ASN A 692     209.773 160.315 146.225  1.00 84.29           N  
ATOM   5298  CA  ASN A 692     210.795 159.284 146.087  1.00 84.29           C  
ATOM   5299  C   ASN A 692     211.889 159.394 147.141  1.00 84.29           C  
ATOM   5300  O   ASN A 692     212.585 158.406 147.397  1.00 84.29           O  
ATOM   5301  CB  ASN A 692     211.415 159.339 144.690  1.00 84.29           C  
ATOM   5302  CG  ASN A 692     210.472 158.836 143.615  1.00 84.29           C  
ATOM   5303  OD1 ASN A 692     209.832 157.796 143.772  1.00 84.29           O  
ATOM   5304  ND2 ASN A 692     210.381 159.573 142.514  1.00 84.29           N  
ATOM   5305  N   ALA A 693     212.061 160.565 147.752  1.00 83.39           N  
ATOM   5306  CA  ALA A 693     213.083 160.741 148.773  1.00 83.39           C  
ATOM   5307  C   ALA A 693     212.580 160.493 150.188  1.00 83.39           C  
ATOM   5308  O   ALA A 693     213.394 160.214 151.075  1.00 83.39           O  
ATOM   5309  CB  ALA A 693     213.677 162.150 148.689  1.00 83.39           C  
ATOM   5310  N   MET A 694     211.273 160.585 150.427  1.00 88.96           N  
ATOM   5311  CA  MET A 694     210.754 160.447 151.782  1.00 88.96           C  
ATOM   5312  C   MET A 694     210.222 159.055 152.091  1.00 88.96           C  
ATOM   5313  O   MET A 694     210.219 158.655 153.259  1.00 88.96           O  
ATOM   5314  CB  MET A 694     209.652 161.482 152.037  1.00 88.96           C  
ATOM   5315  CG  MET A 694     208.370 161.259 151.257  1.00 88.96           C  
ATOM   5316  SD  MET A 694     207.117 162.481 151.687  1.00 88.96           S  
ATOM   5317  CE  MET A 694     206.765 162.028 153.384  1.00 88.96           C  
ATOM   5318  N   ASN A 695     209.769 158.302 151.084  1.00 80.51           N  
ATOM   5319  CA  ASN A 695     209.486 156.889 151.305  1.00 80.51           C  
ATOM   5320  C   ASN A 695     210.760 156.076 151.492  1.00 80.51           C  
ATOM   5321  O   ASN A 695     210.712 154.994 152.085  1.00 80.51           O  
ATOM   5322  CB  ASN A 695     208.661 156.320 150.148  1.00 80.51           C  
ATOM   5323  CG  ASN A 695     209.336 156.497 148.800  1.00 80.51           C  
ATOM   5324  OD1 ASN A 695     210.447 157.019 148.708  1.00 80.51           O  
ATOM   5325  ND2 ASN A 695     208.663 156.057 147.742  1.00 80.51           N  
ATOM   5326  N   ARG A 696     211.893 156.578 150.993  1.00 82.04           N  
ATOM   5327  CA  ARG A 696     213.187 155.990 151.321  1.00 82.04           C  
ATOM   5328  C   ARG A 696     213.504 156.120 152.805  1.00 82.04           C  
ATOM   5329  O   ARG A 696     214.171 155.250 153.376  1.00 82.04           O  
ATOM   5330  CB  ARG A 696     214.280 156.647 150.477  1.00 82.04           C  
ATOM   5331  CG  ARG A 696     215.635 155.968 150.561  1.00 82.04           C  
ATOM   5332  CD  ARG A 696     216.636 156.608 149.614  1.00 82.04           C  
ATOM   5333  NE  ARG A 696     216.207 156.522 148.221  1.00 82.04           N  
ATOM   5334  CZ  ARG A 696     215.950 157.575 147.452  1.00 82.04           C  
ATOM   5335  NH1 ARG A 696     216.097 158.802 147.934  1.00 82.04           N  
ATOM   5336  NH2 ARG A 696     215.562 157.402 146.196  1.00 82.04           N  
ATOM   5337  N   MET A 697     213.031 157.191 153.446  1.00 82.10           N  
ATOM   5338  CA  MET A 697     213.097 157.272 154.902  1.00 82.10           C  
ATOM   5339  C   MET A 697     212.143 156.283 155.560  1.00 82.10           C  
ATOM   5340  O   MET A 697     212.507 155.624 156.541  1.00 82.10           O  
ATOM   5341  CB  MET A 697     212.791 158.697 155.361  1.00 82.10           C  
ATOM   5342  CG  MET A 697     212.872 158.894 156.866  1.00 82.10           C  
ATOM   5343  SD  MET A 697     212.181 160.473 157.392  1.00 82.10           S  
ATOM   5344  CE  MET A 697     210.430 160.166 157.174  1.00 82.10           C  
ATOM   5345  N   ALA A 698     210.917 156.171 155.042  1.00 80.16           N  
ATOM   5346  CA  ALA A 698     209.916 155.333 155.695  1.00 80.16           C  
ATOM   5347  C   ALA A 698     210.313 153.863 155.657  1.00 80.16           C  
ATOM   5348  O   ALA A 698     210.101 153.132 156.632  1.00 80.16           O  
ATOM   5349  CB  ALA A 698     208.550 155.539 155.042  1.00 80.16           C  
ATOM   5350  N   LYS A 699     210.888 153.409 154.541  1.00 82.69           N  
ATOM   5351  CA  LYS A 699     211.349 152.029 154.455  1.00 82.69           C  
ATOM   5352  C   LYS A 699     212.567 151.772 155.333  1.00 82.69           C  
ATOM   5353  O   LYS A 699     212.855 150.613 155.649  1.00 82.69           O  
ATOM   5354  CB  LYS A 699     211.669 151.671 153.003  1.00 82.69           C  
ATOM   5355  CG  LYS A 699     210.451 151.624 152.094  1.00 82.69           C  
ATOM   5356  CD  LYS A 699     210.833 151.232 150.676  1.00 82.69           C  
ATOM   5357  CE  LYS A 699     209.621 151.241 149.758  1.00 82.69           C  
ATOM   5358  NZ  LYS A 699     208.650 150.168 150.109  1.00 82.69           N  
ATOM   5359  N   LEU A 700     213.285 152.823 155.730  1.00 79.49           N  
ATOM   5360  CA  LEU A 700     214.429 152.695 156.629  1.00 79.49           C  
ATOM   5361  C   LEU A 700     214.000 152.717 158.094  1.00 79.49           C  
ATOM   5362  O   LEU A 700     214.261 151.767 158.839  1.00 79.49           O  
ATOM   5363  CB  LEU A 700     215.449 153.805 156.345  1.00 79.49           C  
ATOM   5364  CG  LEU A 700     216.654 153.886 157.286  1.00 79.49           C  
ATOM   5365  CD1 LEU A 700     217.935 154.098 156.502  1.00 79.49           C  
ATOM   5366  CD2 LEU A 700     216.469 155.007 158.297  1.00 79.49           C  
ATOM   5367  N   CYS A 701     213.343 153.801 158.518  1.00 81.96           N  
ATOM   5368  CA  CYS A 701     213.038 153.989 159.932  1.00 81.96           C  
ATOM   5369  C   CYS A 701     212.054 152.955 160.459  1.00 81.96           C  
ATOM   5370  O   CYS A 701     212.011 152.723 161.671  1.00 81.96           O  
ATOM   5371  CB  CYS A 701     212.486 155.396 160.167  1.00 81.96           C  
ATOM   5372  SG  CYS A 701     213.714 156.715 160.032  1.00 81.96           S  
ATOM   5373  N   ALA A 702     211.264 152.333 159.584  1.00 82.77           N  
ATOM   5374  CA  ALA A 702     210.476 151.177 159.996  1.00 82.77           C  
ATOM   5375  C   ALA A 702     211.374 149.986 160.305  1.00 82.77           C  
ATOM   5376  O   ALA A 702     211.309 149.410 161.397  1.00 82.77           O  
ATOM   5377  CB  ALA A 702     209.457 150.822 158.913  1.00 82.77           C  
ATOM   5378  N   ARG A 703     212.231 149.610 159.353  1.00 81.87           N  
ATOM   5379  CA  ARG A 703     213.089 148.443 159.519  1.00 81.87           C  
ATOM   5380  C   ARG A 703     214.222 148.665 160.514  1.00 81.87           C  
ATOM   5381  O   ARG A 703     214.804 147.684 160.990  1.00 81.87           O  
ATOM   5382  CB  ARG A 703     213.684 148.031 158.171  1.00 81.87           C  
ATOM   5383  CG  ARG A 703     212.690 147.439 157.185  1.00 81.87           C  
ATOM   5384  CD  ARG A 703     213.392 147.051 155.891  1.00 81.87           C  
ATOM   5385  NE  ARG A 703     212.483 146.450 154.919  1.00 81.87           N  
ATOM   5386  CZ  ARG A 703     211.840 147.133 153.978  1.00 81.87           C  
ATOM   5387  NH1 ARG A 703     212.000 148.445 153.881  1.00 81.87           N  
ATOM   5388  NH2 ARG A 703     211.033 146.504 153.134  1.00 81.87           N  
ATOM   5389  N   PHE A 704     214.553 149.914 160.845  1.00 82.26           N  
ATOM   5390  CA  PHE A 704     215.761 150.160 161.634  1.00 82.26           C  
ATOM   5391  C   PHE A 704     215.529 149.964 163.130  1.00 82.26           C  
ATOM   5392  O   PHE A 704     216.076 149.037 163.735  1.00 82.26           O  
ATOM   5393  CB  PHE A 704     216.289 151.572 161.356  1.00 82.26           C  
ATOM   5394  CG  PHE A 704     217.318 152.035 162.347  1.00 82.26           C  
ATOM   5395  CD1 PHE A 704     218.549 151.407 162.433  1.00 82.26           C  
ATOM   5396  CD2 PHE A 704     217.049 153.091 163.202  1.00 82.26           C  
ATOM   5397  CE1 PHE A 704     219.496 151.828 163.347  1.00 82.26           C  
ATOM   5398  CE2 PHE A 704     217.992 153.516 164.119  1.00 82.26           C  
ATOM   5399  CZ  PHE A 704     219.217 152.884 164.191  1.00 82.26           C  
ATOM   5400  N   LEU A 705     214.720 150.827 163.747  1.00 84.45           N  
ATOM   5401  CA  LEU A 705     214.852 151.012 165.187  1.00 84.45           C  
ATOM   5402  C   LEU A 705     214.155 149.925 165.994  1.00 84.45           C  
ATOM   5403  O   LEU A 705     214.325 149.881 167.217  1.00 84.45           O  
ATOM   5404  CB  LEU A 705     214.311 152.385 165.602  1.00 84.45           C  
ATOM   5405  CG  LEU A 705     212.831 152.511 165.973  1.00 84.45           C  
ATOM   5406  CD1 LEU A 705     212.564 153.853 166.640  1.00 84.45           C  
ATOM   5407  CD2 LEU A 705     211.926 152.322 164.769  1.00 84.45           C  
ATOM   5408  N   GLY A 706     213.385 149.049 165.346  1.00 88.91           N  
ATOM   5409  CA  GLY A 706     213.013 147.789 165.962  1.00 88.91           C  
ATOM   5410  C   GLY A 706     214.170 146.833 166.154  1.00 88.91           C  
ATOM   5411  O   GLY A 706     214.050 145.879 166.928  1.00 88.91           O  
ATOM   5412  N   ASN A 707     215.288 147.068 165.465  1.00 90.04           N  
ATOM   5413  CA  ASN A 707     216.515 146.316 165.684  1.00 90.04           C  
ATOM   5414  C   ASN A 707     217.557 147.078 166.491  1.00 90.04           C  
ATOM   5415  O   ASN A 707     218.536 146.468 166.934  1.00 90.04           O  
ATOM   5416  CB  ASN A 707     217.120 145.901 164.338  1.00 90.04           C  
ATOM   5417  CG  ASN A 707     216.117 145.200 163.445  1.00 90.04           C  
ATOM   5418  OD1 ASN A 707     215.270 144.444 163.919  1.00 90.04           O  
ATOM   5419  ND2 ASN A 707     216.206 145.450 162.143  1.00 90.04           N  
ATOM   5420  N   ARG A 708     217.381 148.383 166.689  1.00 85.58           N  
ATOM   5421  CA  ARG A 708     218.226 149.121 167.620  1.00 85.58           C  
ATOM   5422  C   ARG A 708     217.673 149.052 169.039  1.00 85.58           C  
ATOM   5423  O   ARG A 708     218.416 148.776 169.987  1.00 85.58           O  
ATOM   5424  CB  ARG A 708     218.367 150.580 167.171  1.00 85.58           C  
ATOM   5425  CG  ARG A 708     219.477 151.337 167.886  1.00 85.58           C  
ATOM   5426  CD  ARG A 708     218.956 152.186 169.033  1.00 85.58           C  
ATOM   5427  NE  ARG A 708     220.047 152.852 169.738  1.00 85.58           N  
ATOM   5428  CZ  ARG A 708     219.912 153.496 170.892  1.00 85.58           C  
ATOM   5429  NH1 ARG A 708     218.724 153.577 171.476  1.00 85.58           N  
ATOM   5430  NH2 ARG A 708     220.965 154.067 171.458  1.00 85.58           N  
ATOM   5431  N   GLY A 709     216.376 149.299 169.197  1.00 86.24           N  
ATOM   5432  CA  GLY A 709     215.722 149.166 170.482  1.00 86.24           C  
ATOM   5433  C   GLY A 709     215.448 150.477 171.188  1.00 86.24           C  
ATOM   5434  O   GLY A 709     216.296 151.374 171.217  1.00 86.24           O  
ATOM   5435  N   PHE A 710     214.254 150.589 171.766  1.00 85.89           N  
ATOM   5436  CA  PHE A 710     213.822 151.796 172.460  1.00 85.89           C  
ATOM   5437  C   PHE A 710     212.621 151.430 173.316  1.00 85.89           C  
ATOM   5438  O   PHE A 710     211.688 150.786 172.827  1.00 85.89           O  
ATOM   5439  CB  PHE A 710     213.464 152.911 171.471  1.00 85.89           C  
ATOM   5440  CG  PHE A 710     212.979 154.172 172.129  1.00 85.89           C  
ATOM   5441  CD1 PHE A 710     213.852 154.979 172.838  1.00 85.89           C  
ATOM   5442  CD2 PHE A 710     211.650 154.549 172.037  1.00 85.89           C  
ATOM   5443  CE1 PHE A 710     213.409 156.140 173.443  1.00 85.89           C  
ATOM   5444  CE2 PHE A 710     211.200 155.709 172.640  1.00 85.89           C  
ATOM   5445  CZ  PHE A 710     212.081 156.505 173.344  1.00 85.89           C  
ATOM   5446  N   SER A 711     212.643 151.836 174.583  1.00 93.82           N  
ATOM   5447  CA  SER A 711     211.574 151.483 175.505  1.00 93.82           C  
ATOM   5448  C   SER A 711     211.437 152.567 176.565  1.00 93.82           C  
ATOM   5449  O   SER A 711     212.144 153.579 176.551  1.00 93.82           O  
ATOM   5450  CB  SER A 711     211.830 150.114 176.143  1.00 93.82           C  
ATOM   5451  OG  SER A 711     211.794 149.086 175.170  1.00 93.82           O  
ATOM   5452  N   ILE A 712     210.510 152.336 177.492  1.00105.78           N  
ATOM   5453  CA  ILE A 712     210.209 153.268 178.571  1.00105.78           C  
ATOM   5454  C   ILE A 712     209.826 152.442 179.789  1.00105.78           C  
ATOM   5455  O   ILE A 712     209.353 151.310 179.666  1.00105.78           O  
ATOM   5456  CB  ILE A 712     209.084 154.254 178.172  1.00105.78           C  
ATOM   5457  CG1 ILE A 712     209.015 155.432 179.145  1.00105.78           C  
ATOM   5458  CG2 ILE A 712     207.744 153.541 178.103  1.00105.78           C  
ATOM   5459  CD1 ILE A 712     208.056 156.514 178.708  1.00105.78           C  
ATOM   5460  N   GLY A 713     210.034 153.006 180.968  1.00131.00           N  
ATOM   5461  CA  GLY A 713     209.732 152.290 182.183  1.00131.00           C  
ATOM   5462  C   GLY A 713     209.637 153.198 183.385  1.00131.00           C  
ATOM   5463  O   GLY A 713     209.380 154.397 183.265  1.00131.00           O  
ATOM   5464  N   ILE A 714     209.855 152.605 184.558  1.00137.41           N  
ATOM   5465  CA  ILE A 714     209.713 153.341 185.809  1.00137.41           C  
ATOM   5466  C   ILE A 714     210.944 154.195 186.086  1.00137.41           C  
ATOM   5467  O   ILE A 714     210.827 155.372 186.444  1.00137.41           O  
ATOM   5468  CB  ILE A 714     209.429 152.367 186.968  1.00137.41           C  
ATOM   5469  CG1 ILE A 714     208.095 151.651 186.746  1.00137.41           C  
ATOM   5470  CG2 ILE A 714     209.423 153.104 188.298  1.00137.41           C  
ATOM   5471  CD1 ILE A 714     206.911 152.588 186.654  1.00137.41           C  
ATOM   5472  N   ASN A 715     212.140 153.623 185.916  1.00141.06           N  
ATOM   5473  CA  ASN A 715     213.359 154.349 186.265  1.00141.06           C  
ATOM   5474  C   ASN A 715     213.557 155.599 185.418  1.00141.06           C  
ATOM   5475  O   ASN A 715     214.157 156.572 185.889  1.00141.06           O  
ATOM   5476  CB  ASN A 715     214.576 153.435 186.129  1.00141.06           C  
ATOM   5477  CG  ASN A 715     214.570 152.305 187.132  1.00141.06           C  
ATOM   5478  OD1 ASN A 715     214.733 151.140 186.772  1.00141.06           O  
ATOM   5479  ND2 ASN A 715     214.372 152.641 188.401  1.00141.06           N  
ATOM   5480  N   ASP A 716     213.071 155.602 184.177  1.00139.51           N  
ATOM   5481  CA  ASP A 716     213.109 156.803 183.355  1.00139.51           C  
ATOM   5482  C   ASP A 716     211.782 157.556 183.351  1.00139.51           C  
ATOM   5483  O   ASP A 716     211.500 158.296 182.403  1.00139.51           O  
ATOM   5484  CB  ASP A 716     213.530 156.452 181.926  1.00139.51           C  
ATOM   5485  CG  ASP A 716     212.696 155.338 181.328  1.00139.51           C  
ATOM   5486  OD1 ASP A 716     211.895 154.731 182.067  1.00139.51           O  
ATOM   5487  OD2 ASP A 716     212.842 155.067 180.117  1.00139.51           O  
ATOM   5488  N   VAL A 717     210.964 157.388 184.390  1.00144.14           N  
ATOM   5489  CA  VAL A 717     209.817 158.263 184.612  1.00144.14           C  
ATOM   5490  C   VAL A 717     209.762 158.657 186.083  1.00144.14           C  
ATOM   5491  O   VAL A 717     209.029 159.576 186.466  1.00144.14           O  
ATOM   5492  CB  VAL A 717     208.504 157.589 184.171  1.00144.14           C  
ATOM   5493  CG1 VAL A 717     208.024 156.608 185.231  1.00144.14           C  
ATOM   5494  CG2 VAL A 717     207.438 158.634 183.867  1.00144.14           C  
ATOM   5495  N   THR A 718     210.543 157.970 186.914  1.00159.74           N  
ATOM   5496  CA  THR A 718     210.519 158.231 188.344  1.00159.74           C  
ATOM   5497  C   THR A 718     211.316 159.487 188.693  1.00159.74           C  
ATOM   5498  O   THR A 718     212.233 159.877 187.965  1.00159.74           O  
ATOM   5499  CB  THR A 718     211.082 157.037 189.114  1.00159.74           C  
ATOM   5500  OG1 THR A 718     210.897 157.235 190.521  1.00159.74           O  
ATOM   5501  CG2 THR A 718     212.566 156.860 188.827  1.00159.74           C  
ATOM   5502  N   PRO A 719     210.967 160.143 189.797  1.00173.46           N  
ATOM   5503  CA  PRO A 719     211.853 161.169 190.354  1.00173.46           C  
ATOM   5504  C   PRO A 719     213.117 160.546 190.924  1.00173.46           C  
ATOM   5505  O   PRO A 719     213.085 159.473 191.530  1.00173.46           O  
ATOM   5506  CB  PRO A 719     211.002 161.819 191.453  1.00173.46           C  
ATOM   5507  CG  PRO A 719     209.959 160.795 191.780  1.00173.46           C  
ATOM   5508  CD  PRO A 719     209.662 160.119 190.479  1.00173.46           C  
ATOM   5509  N   ALA A 720     214.240 161.232 190.718  1.00199.29           N  
ATOM   5510  CA  ALA A 720     215.551 160.733 191.106  1.00199.29           C  
ATOM   5511  C   ALA A 720     215.907 161.109 192.538  1.00199.29           C  
ATOM   5512  O   ALA A 720     217.095 161.213 192.869  1.00199.29           O  
ATOM   5513  CB  ALA A 720     216.621 161.249 190.142  1.00199.29           C  
ATOM   5514  N   ASP A 721     214.894 161.349 193.375  1.00224.68           N  
ATOM   5515  CA  ASP A 721     215.010 161.501 194.822  1.00224.68           C  
ATOM   5516  C   ASP A 721     215.641 162.837 195.194  1.00224.68           C  
ATOM   5517  O   ASP A 721     215.682 163.200 196.373  1.00224.68           O  
ATOM   5518  CB  ASP A 721     215.807 160.341 195.429  1.00224.68           C  
ATOM   5519  CG  ASP A 721     215.621 160.226 196.929  1.00224.68           C  
ATOM   5520  OD1 ASP A 721     214.544 159.765 197.362  1.00224.68           O  
ATOM   5521  OD2 ASP A 721     216.552 160.597 197.674  1.00224.68           O  
ATOM   5522  N   ASP A 722     216.131 163.580 194.202  1.00226.98           N  
ATOM   5523  CA  ASP A 722     216.525 164.964 194.420  1.00226.98           C  
ATOM   5524  C   ASP A 722     215.414 165.944 194.072  1.00226.98           C  
ATOM   5525  O   ASP A 722     215.427 167.079 194.561  1.00226.98           O  
ATOM   5526  CB  ASP A 722     217.776 165.296 193.601  1.00226.98           C  
ATOM   5527  CG  ASP A 722     219.011 164.576 194.107  1.00226.98           C  
ATOM   5528  OD1 ASP A 722     219.082 164.296 195.322  1.00226.98           O  
ATOM   5529  OD2 ASP A 722     219.912 164.289 193.290  1.00226.98           O  
ATOM   5530  N   LEU A 723     214.459 165.526 193.241  1.00228.29           N  
ATOM   5531  CA  LEU A 723     213.185 166.212 193.066  1.00228.29           C  
ATOM   5532  C   LEU A 723     212.221 165.998 194.226  1.00228.29           C  
ATOM   5533  O   LEU A 723     211.203 166.695 194.295  1.00228.29           O  
ATOM   5534  CB  LEU A 723     212.516 165.764 191.762  1.00228.29           C  
ATOM   5535  CG  LEU A 723     212.901 166.480 190.462  1.00228.29           C  
ATOM   5536  CD1 LEU A 723     212.567 167.963 190.546  1.00228.29           C  
ATOM   5537  CD2 LEU A 723     214.368 166.272 190.107  1.00228.29           C  
ATOM   5538  N   LYS A 724     212.506 165.061 195.132  1.00238.14           N  
ATOM   5539  CA  LYS A 724     211.588 164.805 196.237  1.00238.14           C  
ATOM   5540  C   LYS A 724     211.754 165.824 197.359  1.00238.14           C  
ATOM   5541  O   LYS A 724     210.766 166.399 197.828  1.00238.14           O  
ATOM   5542  CB  LYS A 724     211.794 163.385 196.771  1.00238.14           C  
ATOM   5543  CG  LYS A 724     210.791 162.973 197.837  1.00238.14           C  
ATOM   5544  CD  LYS A 724     211.025 161.543 198.297  1.00238.14           C  
ATOM   5545  CE  LYS A 724     210.102 160.572 197.579  1.00238.14           C  
ATOM   5546  NZ  LYS A 724     210.567 160.278 196.195  1.00238.14           N  
ATOM   5547  N   GLN A 725     212.989 166.065 197.805  1.00244.29           N  
ATOM   5548  CA  GLN A 725     213.187 167.043 198.868  1.00244.29           C  
ATOM   5549  C   GLN A 725     213.042 168.473 198.368  1.00244.29           C  
ATOM   5550  O   GLN A 725     212.829 169.380 199.179  1.00244.29           O  
ATOM   5551  CB  GLN A 725     214.558 166.863 199.523  1.00244.29           C  
ATOM   5552  CG  GLN A 725     214.721 165.564 200.295  1.00244.29           C  
ATOM   5553  CD  GLN A 725     215.417 164.491 199.486  1.00244.29           C  
ATOM   5554  OE1 GLN A 725     216.143 164.790 198.539  1.00244.29           O  
ATOM   5555  NE2 GLN A 725     215.202 163.234 199.855  1.00244.29           N  
ATOM   5556  N   LYS A 726     213.153 168.696 197.057  1.00242.53           N  
ATOM   5557  CA  LYS A 726     213.035 170.046 196.519  1.00242.53           C  
ATOM   5558  C   LYS A 726     211.580 170.435 196.287  1.00242.53           C  
ATOM   5559  O   LYS A 726     211.191 171.578 196.553  1.00242.53           O  
ATOM   5560  CB  LYS A 726     213.833 170.165 195.220  1.00242.53           C  
ATOM   5561  CG  LYS A 726     213.904 171.579 194.667  1.00242.53           C  
ATOM   5562  CD  LYS A 726     214.834 171.658 193.468  1.00242.53           C  
ATOM   5563  CE  LYS A 726     214.826 173.051 192.859  1.00242.53           C  
ATOM   5564  NZ  LYS A 726     215.389 174.066 193.790  1.00242.53           N  
ATOM   5565  N   LYS A 727     210.763 169.500 195.796  1.00250.06           N  
ATOM   5566  CA  LYS A 727     209.348 169.788 195.587  1.00250.06           C  
ATOM   5567  C   LYS A 727     208.597 169.912 196.906  1.00250.06           C  
ATOM   5568  O   LYS A 727     207.674 170.726 197.016  1.00250.06           O  
ATOM   5569  CB  LYS A 727     208.719 168.706 194.705  1.00250.06           C  
ATOM   5570  CG  LYS A 727     207.243 168.915 194.388  1.00250.06           C  
ATOM   5571  CD  LYS A 727     206.350 168.043 195.259  1.00250.06           C  
ATOM   5572  CE  LYS A 727     206.497 166.574 194.899  1.00250.06           C  
ATOM   5573  NZ  LYS A 727     205.605 165.709 195.719  1.00250.06           N  
ATOM   5574  N   GLU A 728     208.977 169.127 197.917  1.00260.97           N  
ATOM   5575  CA  GLU A 728     208.236 169.106 199.172  1.00260.97           C  
ATOM   5576  C   GLU A 728     208.429 170.375 199.992  1.00260.97           C  
ATOM   5577  O   GLU A 728     207.682 170.588 200.953  1.00260.97           O  
ATOM   5578  CB  GLU A 728     208.645 167.891 200.007  1.00260.97           C  
ATOM   5579  CG  GLU A 728     210.046 167.980 200.588  1.00260.97           C  
ATOM   5580  CD  GLU A 728     210.502 166.676 201.210  1.00260.97           C  
ATOM   5581  OE1 GLU A 728     209.752 165.681 201.125  1.00260.97           O  
ATOM   5582  OE2 GLU A 728     211.610 166.645 201.786  1.00260.97           O  
ATOM   5583  N   GLU A 729     209.402 171.215 199.642  1.00273.91           N  
ATOM   5584  CA  GLU A 729     209.570 172.518 200.269  1.00273.91           C  
ATOM   5585  C   GLU A 729     209.189 173.682 199.369  1.00273.91           C  
ATOM   5586  O   GLU A 729     208.743 174.713 199.876  1.00273.91           O  
ATOM   5587  CB  GLU A 729     211.020 172.704 200.739  1.00273.91           C  
ATOM   5588  CG  GLU A 729     212.074 172.463 199.668  1.00273.91           C  
ATOM   5589  CD  GLU A 729     212.401 173.713 198.873  1.00273.91           C  
ATOM   5590  OE1 GLU A 729     212.139 174.825 199.377  1.00273.91           O  
ATOM   5591  OE2 GLU A 729     212.920 173.583 197.744  1.00273.91           O  
ATOM   5592  N   LEU A 730     209.350 173.547 198.051  1.00275.93           N  
ATOM   5593  CA  LEU A 730     209.093 174.664 197.151  1.00275.93           C  
ATOM   5594  C   LEU A 730     207.607 174.871 196.890  1.00275.93           C  
ATOM   5595  O   LEU A 730     207.201 175.992 196.564  1.00275.93           O  
ATOM   5596  CB  LEU A 730     209.838 174.448 195.829  1.00275.93           C  
ATOM   5597  CG  LEU A 730     210.049 175.641 194.891  1.00275.93           C  
ATOM   5598  CD1 LEU A 730     211.381 175.506 194.173  1.00275.93           C  
ATOM   5599  CD2 LEU A 730     208.922 175.756 193.878  1.00275.93           C  
ATOM   5600  N   VAL A 731     206.785 173.828 197.039  1.00286.97           N  
ATOM   5601  CA  VAL A 731     205.335 174.016 197.012  1.00286.97           C  
ATOM   5602  C   VAL A 731     204.801 174.526 198.338  1.00286.97           C  
ATOM   5603  O   VAL A 731     203.639 174.945 198.409  1.00286.97           O  
ATOM   5604  CB  VAL A 731     204.599 172.714 196.644  1.00286.97           C  
ATOM   5605  CG1 VAL A 731     205.130 172.155 195.332  1.00286.97           C  
ATOM   5606  CG2 VAL A 731     204.721 171.694 197.767  1.00286.97           C  
ATOM   5607  N   GLU A 732     205.620 174.504 199.391  1.00299.84           N  
ATOM   5608  CA  GLU A 732     205.293 175.164 200.646  1.00299.84           C  
ATOM   5609  C   GLU A 732     205.675 176.637 200.645  1.00299.84           C  
ATOM   5610  O   GLU A 732     205.098 177.416 201.413  1.00299.84           O  
ATOM   5611  CB  GLU A 732     205.995 174.447 201.808  1.00299.84           C  
ATOM   5612  CG  GLU A 732     205.621 174.946 203.197  1.00299.84           C  
ATOM   5613  CD  GLU A 732     204.159 174.721 203.527  1.00299.84           C  
ATOM   5614  OE1 GLU A 732     203.581 173.728 203.037  1.00299.84           O  
ATOM   5615  OE2 GLU A 732     203.586 175.538 204.278  1.00299.84           O  
ATOM   5616  N   ILE A 733     206.623 177.035 199.793  1.00300.40           N  
ATOM   5617  CA  ILE A 733     206.949 178.450 199.644  1.00300.40           C  
ATOM   5618  C   ILE A 733     205.743 179.222 199.126  1.00300.40           C  
ATOM   5619  O   ILE A 733     205.426 180.312 199.616  1.00300.40           O  
ATOM   5620  CB  ILE A 733     208.171 178.621 198.721  1.00300.40           C  
ATOM   5621  CG1 ILE A 733     209.402 177.955 199.339  1.00300.40           C  
ATOM   5622  CG2 ILE A 733     208.437 180.095 198.452  1.00300.40           C  
ATOM   5623  CD1 ILE A 733     209.805 178.537 200.676  1.00300.40           C  
ATOM   5624  N   ALA A 734     205.046 178.666 198.134  1.00307.53           N  
ATOM   5625  CA  ALA A 734     203.816 179.279 197.649  1.00307.53           C  
ATOM   5626  C   ALA A 734     202.659 179.109 198.624  1.00307.53           C  
ATOM   5627  O   ALA A 734     201.662 179.830 198.511  1.00307.53           O  
ATOM   5628  CB  ALA A 734     203.439 178.696 196.287  1.00307.53           C  
ATOM   5629  N   TYR A 735     202.765 178.178 199.575  1.00305.13           N  
ATOM   5630  CA  TYR A 735     201.692 177.990 200.545  1.00305.13           C  
ATOM   5631  C   TYR A 735     201.686 179.076 201.615  1.00305.13           C  
ATOM   5632  O   TYR A 735     200.619 179.598 201.958  1.00305.13           O  
ATOM   5633  CB  TYR A 735     201.802 176.609 201.193  1.00305.13           C  
ATOM   5634  CG  TYR A 735     201.237 175.486 200.350  1.00305.13           C  
ATOM   5635  CD1 TYR A 735     200.406 175.753 199.270  1.00305.13           C  
ATOM   5636  CD2 TYR A 735     201.528 174.160 200.640  1.00305.13           C  
ATOM   5637  CE1 TYR A 735     199.884 174.730 198.499  1.00305.13           C  
ATOM   5638  CE2 TYR A 735     201.013 173.131 199.875  1.00305.13           C  
ATOM   5639  CZ  TYR A 735     200.191 173.422 198.807  1.00305.13           C  
ATOM   5640  OH  TYR A 735     199.676 172.400 198.043  1.00305.13           O  
ATOM   5641  N   HIS A 736     202.853 179.434 202.158  1.00323.30           N  
ATOM   5642  CA  HIS A 736     202.872 180.441 203.212  1.00323.30           C  
ATOM   5643  C   HIS A 736     202.877 181.860 202.662  1.00323.30           C  
ATOM   5644  O   HIS A 736     202.501 182.791 203.383  1.00323.30           O  
ATOM   5645  CB  HIS A 736     204.078 180.243 204.135  1.00323.30           C  
ATOM   5646  CG  HIS A 736     205.383 180.665 203.536  1.00323.30           C  
ATOM   5647  ND1 HIS A 736     206.105 179.865 202.676  1.00323.30           N  
ATOM   5648  CD2 HIS A 736     206.101 181.804 203.681  1.00323.30           C  
ATOM   5649  CE1 HIS A 736     207.210 180.495 202.316  1.00323.30           C  
ATOM   5650  NE2 HIS A 736     207.230 181.674 202.911  1.00323.30           N  
ATOM   5651  N   LYS A 737     203.294 182.049 201.407  1.00326.60           N  
ATOM   5652  CA  LYS A 737     203.002 183.301 200.717  1.00326.60           C  
ATOM   5653  C   LYS A 737     201.501 183.479 200.531  1.00326.60           C  
ATOM   5654  O   LYS A 737     200.986 184.601 200.596  1.00326.60           O  
ATOM   5655  CB  LYS A 737     203.722 183.342 199.370  1.00326.60           C  
ATOM   5656  CG  LYS A 737     205.222 183.565 199.475  1.00326.60           C  
ATOM   5657  CD  LYS A 737     205.867 183.638 198.100  1.00326.60           C  
ATOM   5658  CE  LYS A 737     207.371 183.829 198.204  1.00326.60           C  
ATOM   5659  NZ  LYS A 737     208.017 183.887 196.863  1.00326.60           N  
ATOM   5660  N   CYS A 738     200.783 182.378 200.296  1.00341.20           N  
ATOM   5661  CA  CYS A 738     199.326 182.428 200.284  1.00341.20           C  
ATOM   5662  C   CYS A 738     198.764 182.654 201.681  1.00341.20           C  
ATOM   5663  O   CYS A 738     197.663 183.198 201.823  1.00341.20           O  
ATOM   5664  CB  CYS A 738     198.764 181.139 199.683  1.00341.20           C  
ATOM   5665  SG  CYS A 738     196.963 181.094 199.540  1.00341.20           S  
ATOM   5666  N   ASP A 739     199.501 182.250 202.718  1.00350.49           N  
ATOM   5667  CA  ASP A 739     198.976 182.339 204.077  1.00350.49           C  
ATOM   5668  C   ASP A 739     198.892 183.788 204.540  1.00350.49           C  
ATOM   5669  O   ASP A 739     197.912 184.185 205.179  1.00350.49           O  
ATOM   5670  CB  ASP A 739     199.844 181.518 205.031  1.00350.49           C  
ATOM   5671  CG  ASP A 739     199.136 181.195 206.332  1.00350.49           C  
ATOM   5672  OD1 ASP A 739     197.948 181.554 206.472  1.00350.49           O  
ATOM   5673  OD2 ASP A 739     199.768 180.581 207.218  1.00350.49           O  
ATOM   5674  N   GLU A 740     199.907 184.595 204.221  1.00358.70           N  
ATOM   5675  CA  GLU A 740     199.832 186.023 204.500  1.00358.70           C  
ATOM   5676  C   GLU A 740     198.904 186.748 203.535  1.00358.70           C  
ATOM   5677  O   GLU A 740     198.506 187.885 203.813  1.00358.70           O  
ATOM   5678  CB  GLU A 740     201.229 186.644 204.446  1.00358.70           C  
ATOM   5679  CG  GLU A 740     201.843 186.673 203.056  1.00358.70           C  
ATOM   5680  CD  GLU A 740     203.230 187.285 203.045  1.00358.70           C  
ATOM   5681  OE1 GLU A 740     203.727 187.654 204.130  1.00358.70           O  
ATOM   5682  OE2 GLU A 740     203.823 187.399 201.952  1.00358.70           O  
ATOM   5683  N   LEU A 741     198.551 186.119 202.414  1.00354.75           N  
ATOM   5684  CA  LEU A 741     197.640 186.716 201.448  1.00354.75           C  
ATOM   5685  C   LEU A 741     196.187 186.334 201.695  1.00354.75           C  
ATOM   5686  O   LEU A 741     195.285 187.019 201.199  1.00354.75           O  
ATOM   5687  CB  LEU A 741     198.047 186.308 200.027  1.00354.75           C  
ATOM   5688  CG  LEU A 741     197.344 186.977 198.843  1.00354.75           C  
ATOM   5689  CD1 LEU A 741     197.527 188.486 198.892  1.00354.75           C  
ATOM   5690  CD2 LEU A 741     197.851 186.413 197.525  1.00354.75           C  
ATOM   5691  N   ILE A 742     195.938 185.270 202.456  1.00351.78           N  
ATOM   5692  CA  ILE A 742     194.569 184.879 202.770  1.00351.78           C  
ATOM   5693  C   ILE A 742     194.091 185.475 204.094  1.00351.78           C  
ATOM   5694  O   ILE A 742     192.886 185.672 204.282  1.00351.78           O  
ATOM   5695  CB  ILE A 742     194.443 183.344 202.772  1.00351.78           C  
ATOM   5696  CG1 ILE A 742     192.972 182.924 202.754  1.00351.78           C  
ATOM   5697  CG2 ILE A 742     195.164 182.740 203.970  1.00351.78           C  
ATOM   5698  CD1 ILE A 742     192.224 183.373 201.518  1.00351.78           C  
ATOM   5699  N   THR A 743     195.006 185.780 205.013  1.00352.34           N  
ATOM   5700  CA  THR A 743     194.631 186.284 206.328  1.00352.34           C  
ATOM   5701  C   THR A 743     194.320 187.776 206.333  1.00352.34           C  
ATOM   5702  O   THR A 743     194.067 188.332 207.407  1.00352.34           O  
ATOM   5703  CB  THR A 743     195.737 185.990 207.346  1.00352.34           C  
ATOM   5704  OG1 THR A 743     196.991 186.477 206.851  1.00352.34           O  
ATOM   5705  CG2 THR A 743     195.839 184.494 207.608  1.00352.34           C  
ATOM   5706  N   LEU A 744     194.330 188.434 205.177  1.00353.71           N  
ATOM   5707  CA  LEU A 744     193.977 189.851 205.096  1.00353.71           C  
ATOM   5708  C   LEU A 744     192.490 190.045 204.805  1.00353.71           C  
ATOM   5709  O   LEU A 744     192.087 190.819 203.939  1.00353.71           O  
ATOM   5710  CB  LEU A 744     194.851 190.544 204.055  1.00353.71           C  
ATOM   5711  CG  LEU A 744     195.073 189.893 202.683  1.00353.71           C  
ATOM   5712  CD1 LEU A 744     194.043 190.318 201.643  1.00353.71           C  
ATOM   5713  CD2 LEU A 744     196.483 190.185 202.186  1.00353.71           C  
ATOM   5714  N   PHE A 745     191.656 189.350 205.575  1.00352.95           N  
ATOM   5715  CA  PHE A 745     190.212 189.554 205.571  1.00352.95           C  
ATOM   5716  C   PHE A 745     189.708 190.274 206.811  1.00352.95           C  
ATOM   5717  O   PHE A 745     188.772 191.071 206.718  1.00352.95           O  
ATOM   5718  CB  PHE A 745     189.485 188.209 205.425  1.00352.95           C  
ATOM   5719  CG  PHE A 745     189.704 187.264 206.576  1.00352.95           C  
ATOM   5720  CD1 PHE A 745     190.817 186.440 206.611  1.00352.95           C  
ATOM   5721  CD2 PHE A 745     188.788 187.187 207.613  1.00352.95           C  
ATOM   5722  CE1 PHE A 745     191.019 185.567 207.663  1.00352.95           C  
ATOM   5723  CE2 PHE A 745     188.985 186.316 208.669  1.00352.95           C  
ATOM   5724  CZ  PHE A 745     190.102 185.504 208.693  1.00352.95           C  
ATOM   5725  N   ASN A 746     190.306 190.010 207.975  1.00363.05           N  
ATOM   5726  CA  ASN A 746     189.987 190.790 209.165  1.00363.05           C  
ATOM   5727  C   ASN A 746     190.576 192.193 209.085  1.00363.05           C  
ATOM   5728  O   ASN A 746     189.966 193.149 209.577  1.00363.05           O  
ATOM   5729  CB  ASN A 746     190.493 190.070 210.416  1.00363.05           C  
ATOM   5730  CG  ASN A 746     189.712 190.443 211.665  1.00363.05           C  
ATOM   5731  OD1 ASN A 746     189.822 189.781 212.697  1.00363.05           O  
ATOM   5732  ND2 ASN A 746     188.917 191.503 211.575  1.00363.05           N  
ATOM   5733  N   LYS A 747     191.752 192.335 208.471  1.00365.06           N  
ATOM   5734  CA  LYS A 747     192.360 193.651 208.308  1.00365.06           C  
ATOM   5735  C   LYS A 747     191.679 194.441 207.196  1.00365.06           C  
ATOM   5736  O   LYS A 747     191.379 195.629 207.363  1.00365.06           O  
ATOM   5737  CB  LYS A 747     193.857 193.506 208.028  1.00365.06           C  
ATOM   5738  CG  LYS A 747     194.621 192.767 209.116  1.00365.06           C  
ATOM   5739  CD  LYS A 747     194.503 193.476 210.456  1.00365.06           C  
ATOM   5740  CE  LYS A 747     195.226 194.814 210.441  1.00365.06           C  
ATOM   5741  NZ  LYS A 747     196.695 194.648 210.266  1.00365.06           N  
ATOM   5742  N   GLY A 748     191.430 193.802 206.056  1.00363.59           N  
ATOM   5743  CA  GLY A 748     190.708 194.449 204.977  1.00363.59           C  
ATOM   5744  C   GLY A 748     191.599 195.041 203.905  1.00363.59           C  
ATOM   5745  O   GLY A 748     191.337 196.143 203.413  1.00363.59           O  
ATOM   5746  N   GLU A 749     192.653 194.322 203.531  1.00365.30           N  
ATOM   5747  CA  GLU A 749     193.563 194.794 202.498  1.00365.30           C  
ATOM   5748  C   GLU A 749     192.967 194.548 201.118  1.00365.30           C  
ATOM   5749  O   GLU A 749     192.362 193.503 200.863  1.00365.30           O  
ATOM   5750  CB  GLU A 749     194.918 194.096 202.621  1.00365.30           C  
ATOM   5751  CG  GLU A 749     196.041 194.752 201.829  1.00365.30           C  
ATOM   5752  CD  GLU A 749     196.132 194.239 200.405  1.00365.30           C  
ATOM   5753  OE1 GLU A 749     195.767 193.068 200.170  1.00365.30           O  
ATOM   5754  OE2 GLU A 749     196.568 195.006 199.521  1.00365.30           O  
ATOM   5755  N   LEU A 750     193.141 195.522 200.227  1.00384.46           N  
ATOM   5756  CA  LEU A 750     192.686 195.391 198.845  1.00384.46           C  
ATOM   5757  C   LEU A 750     193.600 196.228 197.962  1.00384.46           C  
ATOM   5758  O   LEU A 750     193.622 197.456 198.080  1.00384.46           O  
ATOM   5759  CB  LEU A 750     191.230 195.829 198.701  1.00384.46           C  
ATOM   5760  CG  LEU A 750     190.577 195.576 197.341  1.00384.46           C  
ATOM   5761  CD1 LEU A 750     190.475 194.084 197.063  1.00384.46           C  
ATOM   5762  CD2 LEU A 750     189.207 196.232 197.272  1.00384.46           C  
ATOM   5763  N   GLU A 751     194.354 195.562 197.084  1.00388.84           N  
ATOM   5764  CA  GLU A 751     195.359 196.260 196.289  1.00388.84           C  
ATOM   5765  C   GLU A 751     194.715 197.139 195.223  1.00388.84           C  
ATOM   5766  O   GLU A 751     195.285 198.170 194.848  1.00388.84           O  
ATOM   5767  CB  GLU A 751     196.317 195.251 195.652  1.00388.84           C  
ATOM   5768  CG  GLU A 751     197.652 195.838 195.206  1.00388.84           C  
ATOM   5769  CD  GLU A 751     197.589 196.484 193.837  1.00388.84           C  
ATOM   5770  OE1 GLU A 751     196.725 196.085 193.029  1.00388.84           O  
ATOM   5771  OE2 GLU A 751     198.405 197.391 193.567  1.00388.84           O  
ATOM   5772  N   THR A 752     193.537 196.748 194.731  1.00399.66           N  
ATOM   5773  CA  THR A 752     192.803 197.459 193.681  1.00399.66           C  
ATOM   5774  C   THR A 752     193.655 197.594 192.414  1.00399.66           C  
ATOM   5775  O   THR A 752     194.094 198.677 192.022  1.00399.66           O  
ATOM   5776  CB  THR A 752     192.318 198.832 194.169  1.00399.66           C  
ATOM   5777  OG1 THR A 752     193.443 199.685 194.421  1.00399.66           O  
ATOM   5778  CG2 THR A 752     191.502 198.687 195.446  1.00399.66           C  
ATOM   5779  N   GLN A 753     193.880 196.441 191.788  1.00400.85           N  
ATOM   5780  CA  GLN A 753     194.412 196.412 190.436  1.00400.85           C  
ATOM   5781  C   GLN A 753     193.470 197.146 189.482  1.00400.85           C  
ATOM   5782  O   GLN A 753     192.264 197.238 189.732  1.00400.85           O  
ATOM   5783  CB  GLN A 753     194.603 194.971 189.965  1.00400.85           C  
ATOM   5784  CG  GLN A 753     195.712 194.215 190.676  1.00400.85           C  
ATOM   5785  CD  GLN A 753     195.886 192.806 190.146  1.00400.85           C  
ATOM   5786  OE1 GLN A 753     195.131 192.356 189.285  1.00400.85           O  
ATOM   5787  NE2 GLN A 753     196.888 192.101 190.659  1.00400.85           N  
ATOM   5788  N   PRO A 754     193.994 197.679 188.379  1.00403.79           N  
ATOM   5789  CA  PRO A 754     193.117 198.215 187.327  1.00403.79           C  
ATOM   5790  C   PRO A 754     192.274 197.108 186.715  1.00403.79           C  
ATOM   5791  O   PRO A 754     192.796 196.157 186.129  1.00403.79           O  
ATOM   5792  CB  PRO A 754     194.104 198.807 186.314  1.00403.79           C  
ATOM   5793  CG  PRO A 754     195.334 199.095 187.111  1.00403.79           C  
ATOM   5794  CD  PRO A 754     195.411 197.994 188.129  1.00403.79           C  
ATOM   5795  N   GLY A 755     190.956 197.236 186.855  1.00403.89           N  
ATOM   5796  CA  GLY A 755     190.059 196.163 186.476  1.00403.89           C  
ATOM   5797  C   GLY A 755     188.943 195.914 187.470  1.00403.89           C  
ATOM   5798  O   GLY A 755     188.178 194.956 187.319  1.00403.89           O  
ATOM   5799  N   CYS A 756     188.844 196.770 188.490  1.00403.76           N  
ATOM   5800  CA  CYS A 756     187.698 196.815 189.401  1.00403.76           C  
ATOM   5801  C   CYS A 756     187.517 195.471 190.116  1.00403.76           C  
ATOM   5802  O   CYS A 756     186.567 194.719 189.885  1.00403.76           O  
ATOM   5803  CB  CYS A 756     186.423 197.223 188.653  1.00403.76           C  
ATOM   5804  SG  CYS A 756     186.457 198.900 187.979  1.00403.76           S  
ATOM   5805  N   ASN A 757     188.477 195.196 190.998  1.00399.03           N  
ATOM   5806  CA  ASN A 757     188.608 193.898 191.651  1.00399.03           C  
ATOM   5807  C   ASN A 757     187.386 193.548 192.492  1.00399.03           C  
ATOM   5808  O   ASN A 757     186.645 192.618 192.156  1.00399.03           O  
ATOM   5809  CB  ASN A 757     189.866 193.869 192.521  1.00399.03           C  
ATOM   5810  CG  ASN A 757     191.138 193.958 191.705  1.00399.03           C  
ATOM   5811  OD1 ASN A 757     191.859 194.952 191.770  1.00399.03           O  
ATOM   5812  ND2 ASN A 757     191.420 192.917 190.930  1.00399.03           N  
ATOM   5813  N   GLU A 758     187.168 194.291 193.577  1.00391.58           N  
ATOM   5814  CA  GLU A 758     186.036 194.090 194.482  1.00391.58           C  
ATOM   5815  C   GLU A 758     185.991 192.640 194.976  1.00391.58           C  
ATOM   5816  O   GLU A 758     185.126 191.841 194.614  1.00391.58           O  
ATOM   5817  CB  GLU A 758     184.721 194.495 193.806  1.00391.58           C  
ATOM   5818  CG  GLU A 758     183.521 194.548 194.743  1.00391.58           C  
ATOM   5819  CD  GLU A 758     183.627 195.658 195.771  1.00391.58           C  
ATOM   5820  OE1 GLU A 758     184.265 196.690 195.472  1.00391.58           O  
ATOM   5821  OE2 GLU A 758     183.072 195.499 196.878  1.00391.58           O  
ATOM   5822  N   GLU A 759     186.988 192.329 195.806  1.00372.78           N  
ATOM   5823  CA  GLU A 759     187.193 190.998 196.380  1.00372.78           C  
ATOM   5824  C   GLU A 759     187.475 189.974 195.277  1.00372.78           C  
ATOM   5825  O   GLU A 759     186.722 189.025 195.049  1.00372.78           O  
ATOM   5826  CB  GLU A 759     185.997 190.585 197.250  1.00372.78           C  
ATOM   5827  CG  GLU A 759     186.193 189.302 198.052  1.00372.78           C  
ATOM   5828  CD  GLU A 759     187.250 189.438 199.131  1.00372.78           C  
ATOM   5829  OE1 GLU A 759     187.490 190.572 199.596  1.00372.78           O  
ATOM   5830  OE2 GLU A 759     187.839 188.407 199.519  1.00372.78           O  
ATOM   5831  N   GLN A 760     188.584 190.205 194.572  1.00375.63           N  
ATOM   5832  CA  GLN A 760     189.260 189.156 193.824  1.00375.63           C  
ATOM   5833  C   GLN A 760     190.776 189.275 193.877  1.00375.63           C  
ATOM   5834  O   GLN A 760     191.460 188.497 193.205  1.00375.63           O  
ATOM   5835  CB  GLN A 760     188.801 189.149 192.356  1.00375.63           C  
ATOM   5836  CG  GLN A 760     189.258 190.354 191.555  1.00375.63           C  
ATOM   5837  CD  GLN A 760     188.777 190.316 190.118  1.00375.63           C  
ATOM   5838  OE1 GLN A 760     188.129 189.359 189.693  1.00375.63           O  
ATOM   5839  NE2 GLN A 760     189.093 191.360 189.360  1.00375.63           N  
ATOM   5840  N   THR A 761     191.322 190.221 194.645  1.00378.40           N  
ATOM   5841  CA  THR A 761     192.771 190.352 194.753  1.00378.40           C  
ATOM   5842  C   THR A 761     193.394 189.165 195.476  1.00378.40           C  
ATOM   5843  O   THR A 761     194.502 188.742 195.127  1.00378.40           O  
ATOM   5844  CB  THR A 761     193.124 191.658 195.468  1.00378.40           C  
ATOM   5845  OG1 THR A 761     192.526 192.760 194.774  1.00378.40           O  
ATOM   5846  CG2 THR A 761     194.632 191.860 195.512  1.00378.40           C  
ATOM   5847  N   LEU A 762     192.700 188.603 196.466  1.00363.23           N  
ATOM   5848  CA  LEU A 762     193.080 187.319 197.036  1.00363.23           C  
ATOM   5849  C   LEU A 762     192.518 186.136 196.251  1.00363.23           C  
ATOM   5850  O   LEU A 762     192.522 185.009 196.758  1.00363.23           O  
ATOM   5851  CB  LEU A 762     192.650 187.250 198.506  1.00363.23           C  
ATOM   5852  CG  LEU A 762     191.178 187.452 198.882  1.00363.23           C  
ATOM   5853  CD1 LEU A 762     190.390 186.148 198.856  1.00363.23           C  
ATOM   5854  CD2 LEU A 762     191.069 188.117 200.247  1.00363.23           C  
ATOM   5855  N   GLU A 763     192.046 186.367 195.030  1.00356.44           N  
ATOM   5856  CA  GLU A 763     191.612 185.298 194.140  1.00356.44           C  
ATOM   5857  C   GLU A 763     192.390 185.269 192.835  1.00356.44           C  
ATOM   5858  O   GLU A 763     192.790 184.193 192.384  1.00356.44           O  
ATOM   5859  CB  GLU A 763     190.108 185.434 193.843  1.00356.44           C  
ATOM   5860  CG  GLU A 763     189.485 184.233 193.141  1.00356.44           C  
ATOM   5861  CD  GLU A 763     189.553 184.328 191.628  1.00356.44           C  
ATOM   5862  OE1 GLU A 763     189.558 185.460 191.101  1.00356.44           O  
ATOM   5863  OE2 GLU A 763     189.599 183.270 190.966  1.00356.44           O  
ATOM   5864  N   ALA A 764     192.616 186.429 192.217  1.00339.94           N  
ATOM   5865  CA  ALA A 764     193.241 186.503 190.903  1.00339.94           C  
ATOM   5866  C   ALA A 764     194.762 186.486 190.967  1.00339.94           C  
ATOM   5867  O   ALA A 764     195.407 186.331 189.924  1.00339.94           O  
ATOM   5868  CB  ALA A 764     192.772 187.761 190.167  1.00339.94           C  
ATOM   5869  N   LYS A 765     195.345 186.639 192.155  1.00323.03           N  
ATOM   5870  CA  LYS A 765     196.793 186.615 192.317  1.00323.03           C  
ATOM   5871  C   LYS A 765     197.326 185.232 192.660  1.00323.03           C  
ATOM   5872  O   LYS A 765     198.432 184.881 192.230  1.00323.03           O  
ATOM   5873  CB  LYS A 765     197.219 187.612 193.399  1.00323.03           C  
ATOM   5874  CG  LYS A 765     198.724 187.776 193.538  1.00323.03           C  
ATOM   5875  CD  LYS A 765     199.075 188.867 194.536  1.00323.03           C  
ATOM   5876  CE  LYS A 765     200.575 188.931 194.774  1.00323.03           C  
ATOM   5877  NZ  LYS A 765     201.319 189.320 193.543  1.00323.03           N  
ATOM   5878  N   ILE A 766     196.570 184.440 193.422  1.00310.51           N  
ATOM   5879  CA  ILE A 766     197.045 183.116 193.808  1.00310.51           C  
ATOM   5880  C   ILE A 766     197.147 182.211 192.587  1.00310.51           C  
ATOM   5881  O   ILE A 766     198.056 181.377 192.488  1.00310.51           O  
ATOM   5882  CB  ILE A 766     196.125 182.516 194.888  1.00310.51           C  
ATOM   5883  CG1 ILE A 766     196.075 183.434 196.110  1.00310.51           C  
ATOM   5884  CG2 ILE A 766     196.599 181.129 195.291  1.00310.51           C  
ATOM   5885  CD1 ILE A 766     195.066 183.008 197.151  1.00310.51           C  
ATOM   5886  N   GLY A 767     196.232 182.371 191.629  1.00304.20           N  
ATOM   5887  CA  GLY A 767     196.366 181.673 190.363  1.00304.20           C  
ATOM   5888  C   GLY A 767     197.588 182.099 189.573  1.00304.20           C  
ATOM   5889  O   GLY A 767     198.098 181.335 188.749  1.00304.20           O  
ATOM   5890  N   GLY A 768     198.073 183.320 189.809  1.00298.57           N  
ATOM   5891  CA  GLY A 768     199.327 183.738 189.205  1.00298.57           C  
ATOM   5892  C   GLY A 768     200.539 183.071 189.828  1.00298.57           C  
ATOM   5893  O   GLY A 768     201.470 182.674 189.121  1.00298.57           O  
ATOM   5894  N   LEU A 769     200.548 182.937 191.156  1.00291.74           N  
ATOM   5895  CA  LEU A 769     201.681 182.309 191.827  1.00291.74           C  
ATOM   5896  C   LEU A 769     201.594 180.788 191.802  1.00291.74           C  
ATOM   5897  O   LEU A 769     202.630 180.114 191.857  1.00291.74           O  
ATOM   5898  CB  LEU A 769     201.790 182.818 193.268  1.00291.74           C  
ATOM   5899  CG  LEU A 769     200.631 182.584 194.242  1.00291.74           C  
ATOM   5900  CD1 LEU A 769     200.786 181.275 195.009  1.00291.74           C  
ATOM   5901  CD2 LEU A 769     200.497 183.758 195.203  1.00291.74           C  
ATOM   5902  N   LEU A 770     200.385 180.228 191.721  1.00283.97           N  
ATOM   5903  CA  LEU A 770     200.255 178.795 191.486  1.00283.97           C  
ATOM   5904  C   LEU A 770     200.631 178.407 190.063  1.00283.97           C  
ATOM   5905  O   LEU A 770     200.999 177.252 189.827  1.00283.97           O  
ATOM   5906  CB  LEU A 770     198.831 178.327 191.791  1.00283.97           C  
ATOM   5907  CG  LEU A 770     198.438 178.249 193.268  1.00283.97           C  
ATOM   5908  CD1 LEU A 770     196.960 177.925 193.412  1.00283.97           C  
ATOM   5909  CD2 LEU A 770     199.290 177.221 193.996  1.00283.97           C  
ATOM   5910  N   SER A 771     200.548 179.337 189.114  1.00281.99           N  
ATOM   5911  CA  SER A 771     201.091 179.121 187.781  1.00281.99           C  
ATOM   5912  C   SER A 771     202.567 179.482 187.682  1.00281.99           C  
ATOM   5913  O   SER A 771     203.138 179.403 186.589  1.00281.99           O  
ATOM   5914  CB  SER A 771     200.294 179.925 186.748  1.00281.99           C  
ATOM   5915  OG  SER A 771     200.827 179.756 185.446  1.00281.99           O  
ATOM   5916  N   LYS A 772     203.193 179.879 188.790  1.00270.00           N  
ATOM   5917  CA  LYS A 772     204.644 179.997 188.867  1.00270.00           C  
ATOM   5918  C   LYS A 772     205.285 178.695 189.333  1.00270.00           C  
ATOM   5919  O   LYS A 772     206.262 178.231 188.737  1.00270.00           O  
ATOM   5920  CB  LYS A 772     205.031 181.147 189.802  1.00270.00           C  
ATOM   5921  CG  LYS A 772     206.532 181.327 189.973  1.00270.00           C  
ATOM   5922  CD  LYS A 772     206.849 182.482 190.908  1.00270.00           C  
ATOM   5923  CE  LYS A 772     208.349 182.694 191.036  1.00270.00           C  
ATOM   5924  NZ  LYS A 772     209.012 181.564 191.744  1.00270.00           N  
ATOM   5925  N   VAL A 773     204.742 178.095 190.396  1.00261.18           N  
ATOM   5926  CA  VAL A 773     205.244 176.817 190.882  1.00261.18           C  
ATOM   5927  C   VAL A 773     204.925 175.690 189.909  1.00261.18           C  
ATOM   5928  O   VAL A 773     205.598 174.652 189.920  1.00261.18           O  
ATOM   5929  CB  VAL A 773     204.668 176.524 192.283  1.00261.18           C  
ATOM   5930  CG1 VAL A 773     203.165 176.289 192.210  1.00261.18           C  
ATOM   5931  CG2 VAL A 773     205.378 175.341 192.932  1.00261.18           C  
ATOM   5932  N   ARG A 774     203.926 175.875 189.045  1.00249.45           N  
ATOM   5933  CA  ARG A 774     203.564 174.834 188.092  1.00249.45           C  
ATOM   5934  C   ARG A 774     204.530 174.777 186.916  1.00249.45           C  
ATOM   5935  O   ARG A 774     204.732 173.703 186.337  1.00249.45           O  
ATOM   5936  CB  ARG A 774     202.130 175.064 187.603  1.00249.45           C  
ATOM   5937  CG  ARG A 774     201.560 173.974 186.708  1.00249.45           C  
ATOM   5938  CD  ARG A 774     201.565 174.400 185.247  1.00249.45           C  
ATOM   5939  NE  ARG A 774     200.894 173.427 184.392  1.00249.45           N  
ATOM   5940  CZ  ARG A 774     199.585 173.414 184.160  1.00249.45           C  
ATOM   5941  NH1 ARG A 774     198.802 174.325 184.720  1.00249.45           N  
ATOM   5942  NH2 ARG A 774     199.059 172.491 183.367  1.00249.45           N  
ATOM   5943  N   GLU A 775     205.141 175.905 186.552  1.00249.94           N  
ATOM   5944  CA  GLU A 775     206.121 175.928 185.474  1.00249.94           C  
ATOM   5945  C   GLU A 775     207.560 175.861 185.965  1.00249.94           C  
ATOM   5946  O   GLU A 775     208.432 175.398 185.223  1.00249.94           O  
ATOM   5947  CB  GLU A 775     205.942 177.189 184.619  1.00249.94           C  
ATOM   5948  CG  GLU A 775     206.009 178.493 185.400  1.00249.94           C  
ATOM   5949  CD  GLU A 775     207.412 179.065 185.465  1.00249.94           C  
ATOM   5950  OE1 GLU A 775     208.254 178.677 184.627  1.00249.94           O  
ATOM   5951  OE2 GLU A 775     207.673 179.901 186.355  1.00249.94           O  
ATOM   5952  N   GLU A 776     207.831 176.309 187.193  1.00244.59           N  
ATOM   5953  CA  GLU A 776     209.203 176.308 187.695  1.00244.59           C  
ATOM   5954  C   GLU A 776     209.681 174.889 187.975  1.00244.59           C  
ATOM   5955  O   GLU A 776     210.782 174.501 187.568  1.00244.59           O  
ATOM   5956  CB  GLU A 776     209.305 177.173 188.952  1.00244.59           C  
ATOM   5957  CG  GLU A 776     210.727 177.547 189.345  1.00244.59           C  
ATOM   5958  CD  GLU A 776     211.398 176.491 190.203  1.00244.59           C  
ATOM   5959  OE1 GLU A 776     210.679 175.750 190.906  1.00244.59           O  
ATOM   5960  OE2 GLU A 776     212.644 176.403 190.174  1.00244.59           O  
ATOM   5961  N   VAL A 777     208.865 174.100 188.678  1.00233.41           N  
ATOM   5962  CA  VAL A 777     209.274 172.753 189.060  1.00233.41           C  
ATOM   5963  C   VAL A 777     209.388 171.859 187.832  1.00233.41           C  
ATOM   5964  O   VAL A 777     210.228 170.951 187.789  1.00233.41           O  
ATOM   5965  CB  VAL A 777     208.295 172.173 190.098  1.00233.41           C  
ATOM   5966  CG1 VAL A 777     208.748 170.795 190.558  1.00233.41           C  
ATOM   5967  CG2 VAL A 777     208.163 173.116 191.284  1.00233.41           C  
ATOM   5968  N   GLY A 778     208.564 172.105 186.811  1.00229.29           N  
ATOM   5969  CA  GLY A 778     208.730 171.423 185.541  1.00229.29           C  
ATOM   5970  C   GLY A 778     209.995 171.795 184.797  1.00229.29           C  
ATOM   5971  O   GLY A 778     210.420 171.048 183.910  1.00229.29           O  
ATOM   5972  N   ASP A 779     210.606 172.930 185.135  1.00226.16           N  
ATOM   5973  CA  ASP A 779     211.890 173.294 184.553  1.00226.16           C  
ATOM   5974  C   ASP A 779     213.073 172.777 185.359  1.00226.16           C  
ATOM   5975  O   ASP A 779     214.192 172.739 184.834  1.00226.16           O  
ATOM   5976  CB  ASP A 779     211.999 174.816 184.414  1.00226.16           C  
ATOM   5977  CG  ASP A 779     210.983 175.388 183.445  1.00226.16           C  
ATOM   5978  OD1 ASP A 779     210.552 174.653 182.532  1.00226.16           O  
ATOM   5979  OD2 ASP A 779     210.617 176.572 183.596  1.00226.16           O  
ATOM   5980  N   VAL A 780     212.855 172.384 186.616  1.00219.46           N  
ATOM   5981  CA  VAL A 780     213.937 171.802 187.403  1.00219.46           C  
ATOM   5982  C   VAL A 780     214.301 170.425 186.864  1.00219.46           C  
ATOM   5983  O   VAL A 780     215.466 170.010 186.926  1.00219.46           O  
ATOM   5984  CB  VAL A 780     213.535 171.746 188.890  1.00219.46           C  
ATOM   5985  CG1 VAL A 780     214.653 171.154 189.731  1.00219.46           C  
ATOM   5986  CG2 VAL A 780     213.166 173.133 189.391  1.00219.46           C  
ATOM   5987  N   CYS A 781     213.322 169.704 186.315  1.00208.96           N  
ATOM   5988  CA  CYS A 781     213.551 168.330 185.877  1.00208.96           C  
ATOM   5989  C   CYS A 781     214.465 168.280 184.659  1.00208.96           C  
ATOM   5990  O   CYS A 781     215.295 167.373 184.537  1.00208.96           O  
ATOM   5991  CB  CYS A 781     212.218 167.646 185.578  1.00208.96           C  
ATOM   5992  SG  CYS A 781     211.142 167.444 187.017  1.00208.96           S  
ATOM   5993  N   ILE A 782     214.325 169.248 183.751  1.00203.79           N  
ATOM   5994  CA  ILE A 782     215.015 169.183 182.466  1.00203.79           C  
ATOM   5995  C   ILE A 782     216.526 169.271 182.651  1.00203.79           C  
ATOM   5996  O   ILE A 782     217.286 168.553 181.990  1.00203.79           O  
ATOM   5997  CB  ILE A 782     214.493 170.288 181.530  1.00203.79           C  
ATOM   5998  CG1 ILE A 782     212.975 170.183 181.379  1.00203.79           C  
ATOM   5999  CG2 ILE A 782     215.171 170.204 180.170  1.00203.79           C  
ATOM   6000  CD1 ILE A 782     212.509 168.872 180.786  1.00203.79           C  
ATOM   6001  N   ASN A 783     216.989 170.139 183.549  1.00204.93           N  
ATOM   6002  CA  ASN A 783     218.417 170.250 183.814  1.00204.93           C  
ATOM   6003  C   ASN A 783     218.918 169.263 184.861  1.00204.93           C  
ATOM   6004  O   ASN A 783     220.133 169.168 185.063  1.00204.93           O  
ATOM   6005  CB  ASN A 783     218.761 171.676 184.260  1.00204.93           C  
ATOM   6006  CG  ASN A 783     218.494 172.706 183.179  1.00204.93           C  
ATOM   6007  OD1 ASN A 783     217.621 173.562 183.323  1.00204.93           O  
ATOM   6008  ND2 ASN A 783     219.248 172.629 182.088  1.00204.93           N  
ATOM   6009  N   GLU A 784     218.024 168.531 185.529  1.00199.80           N  
ATOM   6010  CA  GLU A 784     218.413 167.590 186.574  1.00199.80           C  
ATOM   6011  C   GLU A 784     217.966 166.166 186.259  1.00199.80           C  
ATOM   6012  O   GLU A 784     217.822 165.349 187.175  1.00199.80           O  
ATOM   6013  CB  GLU A 784     217.868 168.029 187.934  1.00199.80           C  
ATOM   6014  CG  GLU A 784     218.425 169.355 188.425  1.00199.80           C  
ATOM   6015  CD  GLU A 784     217.867 169.755 189.776  1.00199.80           C  
ATOM   6016  OE1 GLU A 784     217.008 169.019 190.307  1.00199.80           O  
ATOM   6017  OE2 GLU A 784     218.287 170.804 190.309  1.00199.80           O  
ATOM   6018  N   LEU A 785     217.746 165.850 184.986  1.00174.84           N  
ATOM   6019  CA  LEU A 785     217.463 164.492 184.548  1.00174.84           C  
ATOM   6020  C   LEU A 785     218.547 164.032 183.585  1.00174.84           C  
ATOM   6021  O   LEU A 785     219.056 164.823 182.785  1.00174.84           O  
ATOM   6022  CB  LEU A 785     216.087 164.409 183.878  1.00174.84           C  
ATOM   6023  CG  LEU A 785     215.519 163.027 183.567  1.00174.84           C  
ATOM   6024  CD1 LEU A 785     215.341 162.228 184.847  1.00174.84           C  
ATOM   6025  CD2 LEU A 785     214.197 163.166 182.829  1.00174.84           C  
ATOM   6026  N   ASP A 786     218.890 162.748 183.659  1.00153.63           N  
ATOM   6027  CA  ASP A 786     219.949 162.213 182.820  1.00153.63           C  
ATOM   6028  C   ASP A 786     219.490 162.089 181.369  1.00153.63           C  
ATOM   6029  O   ASP A 786     218.296 162.108 181.057  1.00153.63           O  
ATOM   6030  CB  ASP A 786     220.406 160.850 183.342  1.00153.63           C  
ATOM   6031  CG  ASP A 786     219.261 159.864 183.482  1.00153.63           C  
ATOM   6032  OD1 ASP A 786     218.091 160.284 183.371  1.00153.63           O  
ATOM   6033  OD2 ASP A 786     219.533 158.665 183.703  1.00153.63           O  
ATOM   6034  N   ASN A 787     220.470 161.963 180.478  1.00134.44           N  
ATOM   6035  CA  ASN A 787     220.208 161.679 179.077  1.00134.44           C  
ATOM   6036  C   ASN A 787     219.786 160.223 178.887  1.00134.44           C  
ATOM   6037  O   ASN A 787     219.790 159.412 179.819  1.00134.44           O  
ATOM   6038  CB  ASN A 787     221.440 161.994 178.227  1.00134.44           C  
ATOM   6039  CG  ASN A 787     222.705 161.355 178.770  1.00134.44           C  
ATOM   6040  OD1 ASN A 787     222.669 160.602 179.744  1.00134.44           O  
ATOM   6041  ND2 ASN A 787     223.834 161.652 178.137  1.00134.44           N  
ATOM   6042  N   TRP A 788     219.407 159.906 177.647  1.00125.84           N  
ATOM   6043  CA  TRP A 788     218.818 158.613 177.287  1.00125.84           C  
ATOM   6044  C   TRP A 788     217.555 158.322 178.094  1.00125.84           C  
ATOM   6045  O   TRP A 788     217.284 157.180 178.472  1.00125.84           O  
ATOM   6046  CB  TRP A 788     219.834 157.477 177.430  1.00125.84           C  
ATOM   6047  CG  TRP A 788     221.022 157.637 176.535  1.00125.84           C  
ATOM   6048  CD1 TRP A 788     222.269 158.062 176.892  1.00125.84           C  
ATOM   6049  CD2 TRP A 788     221.066 157.409 175.121  1.00125.84           C  
ATOM   6050  NE1 TRP A 788     223.091 158.094 175.792  1.00125.84           N  
ATOM   6051  CE2 TRP A 788     222.376 157.700 174.692  1.00125.84           C  
ATOM   6052  CE3 TRP A 788     220.127 156.981 174.179  1.00125.84           C  
ATOM   6053  CZ2 TRP A 788     222.770 157.576 173.361  1.00125.84           C  
ATOM   6054  CZ3 TRP A 788     220.519 156.859 172.859  1.00125.84           C  
ATOM   6055  CH2 TRP A 788     221.829 157.154 172.462  1.00125.84           C  
ATOM   6056  N   ASN A 789     216.775 159.364 178.359  1.00122.75           N  
ATOM   6057  CA  ASN A 789     215.533 159.255 179.109  1.00122.75           C  
ATOM   6058  C   ASN A 789     214.381 159.456 178.133  1.00122.75           C  
ATOM   6059  O   ASN A 789     214.339 160.462 177.417  1.00122.75           O  
ATOM   6060  CB  ASN A 789     215.496 160.284 180.244  1.00122.75           C  
ATOM   6061  CG  ASN A 789     214.500 159.926 181.333  1.00122.75           C  
ATOM   6062  OD1 ASN A 789     214.802 160.034 182.519  1.00122.75           O  
ATOM   6063  ND2 ASN A 789     213.303 159.523 180.938  1.00122.75           N  
ATOM   6064  N   ALA A 790     213.451 158.499 178.104  1.00115.00           N  
ATOM   6065  CA  ALA A 790     212.528 158.393 176.979  1.00115.00           C  
ATOM   6066  C   ALA A 790     211.450 159.477 176.972  1.00115.00           C  
ATOM   6067  O   ALA A 790     211.148 160.014 175.899  1.00115.00           O  
ATOM   6068  CB  ALA A 790     211.882 157.003 176.952  1.00115.00           C  
ATOM   6069  N   PRO A 791     210.855 159.852 178.112  1.00117.63           N  
ATOM   6070  CA  PRO A 791     210.037 161.076 178.118  1.00117.63           C  
ATOM   6071  C   PRO A 791     210.838 162.346 177.902  1.00117.63           C  
ATOM   6072  O   PRO A 791     210.249 163.370 177.533  1.00117.63           O  
ATOM   6073  CB  PRO A 791     209.388 161.062 179.509  1.00117.63           C  
ATOM   6074  CG  PRO A 791     209.356 159.636 179.886  1.00117.63           C  
ATOM   6075  CD  PRO A 791     210.631 159.061 179.336  1.00117.63           C  
ATOM   6076  N   LEU A 792     212.154 162.320 178.115  1.00116.10           N  
ATOM   6077  CA  LEU A 792     212.983 163.464 177.756  1.00116.10           C  
ATOM   6078  C   LEU A 792     213.305 163.480 176.266  1.00116.10           C  
ATOM   6079  O   LEU A 792     213.230 164.534 175.624  1.00116.10           O  
ATOM   6080  CB  LEU A 792     214.266 163.460 178.592  1.00116.10           C  
ATOM   6081  CG  LEU A 792     215.210 164.669 178.550  1.00116.10           C  
ATOM   6082  CD1 LEU A 792     216.217 164.577 177.406  1.00116.10           C  
ATOM   6083  CD2 LEU A 792     214.418 165.969 178.472  1.00116.10           C  
ATOM   6084  N   ILE A 793     213.668 162.327 175.699  1.00109.15           N  
ATOM   6085  CA  ILE A 793     214.206 162.310 174.343  1.00109.15           C  
ATOM   6086  C   ILE A 793     213.124 162.452 173.279  1.00109.15           C  
ATOM   6087  O   ILE A 793     213.435 162.818 172.138  1.00109.15           O  
ATOM   6088  CB  ILE A 793     215.021 161.024 174.116  1.00109.15           C  
ATOM   6089  CG1 ILE A 793     215.986 161.192 172.939  1.00109.15           C  
ATOM   6090  CG2 ILE A 793     214.100 159.832 173.892  1.00109.15           C  
ATOM   6091  CD1 ILE A 793     217.055 160.124 172.873  1.00109.15           C  
ATOM   6092  N   MET A 794     211.862 162.183 173.610  1.00119.36           N  
ATOM   6093  CA  MET A 794     210.758 162.444 172.697  1.00119.36           C  
ATOM   6094  C   MET A 794     210.023 163.739 173.013  1.00119.36           C  
ATOM   6095  O   MET A 794     209.089 164.097 172.290  1.00119.36           O  
ATOM   6096  CB  MET A 794     209.768 161.273 172.695  1.00119.36           C  
ATOM   6097  CG  MET A 794     208.907 161.162 173.940  1.00119.36           C  
ATOM   6098  SD  MET A 794     207.829 159.717 173.884  1.00119.36           S  
ATOM   6099  CE  MET A 794     209.008 158.389 174.115  1.00119.36           C  
ATOM   6100  N   ALA A 795     210.420 164.449 174.070  1.00117.26           N  
ATOM   6101  CA  ALA A 795     210.058 165.850 174.228  1.00117.26           C  
ATOM   6102  C   ALA A 795     211.141 166.809 173.760  1.00117.26           C  
ATOM   6103  O   ALA A 795     210.833 167.972 173.476  1.00117.26           O  
ATOM   6104  CB  ALA A 795     209.722 166.150 175.694  1.00117.26           C  
ATOM   6105  N   THR A 796     212.396 166.360 173.675  1.00117.41           N  
ATOM   6106  CA  THR A 796     213.412 167.156 172.995  1.00117.41           C  
ATOM   6107  C   THR A 796     213.086 167.303 171.515  1.00117.41           C  
ATOM   6108  O   THR A 796     213.322 168.360 170.918  1.00117.41           O  
ATOM   6109  CB  THR A 796     214.790 166.520 173.184  1.00117.41           C  
ATOM   6110  OG1 THR A 796     215.055 166.357 174.583  1.00117.41           O  
ATOM   6111  CG2 THR A 796     215.874 167.396 172.571  1.00117.41           C  
ATOM   6112  N   CYS A 797     212.531 166.256 170.910  1.00119.04           N  
ATOM   6113  CA  CYS A 797     211.979 166.339 169.569  1.00119.04           C  
ATOM   6114  C   CYS A 797     210.577 166.944 169.614  1.00119.04           C  
ATOM   6115  O   CYS A 797     210.056 167.305 170.673  1.00119.04           O  
ATOM   6116  CB  CYS A 797     211.961 164.959 168.916  1.00119.04           C  
ATOM   6117  SG  CYS A 797     213.589 164.194 168.741  1.00119.04           S  
ATOM   6118  N   GLY A 798     209.955 167.056 168.444  1.00127.53           N  
ATOM   6119  CA  GLY A 798     208.554 167.416 168.368  1.00127.53           C  
ATOM   6120  C   GLY A 798     207.688 166.228 168.003  1.00127.53           C  
ATOM   6121  O   GLY A 798     206.626 166.383 167.393  1.00127.53           O  
ATOM   6122  N   SER A 799     208.143 165.030 168.373  1.00126.98           N  
ATOM   6123  CA  SER A 799     207.450 163.792 168.037  1.00126.98           C  
ATOM   6124  C   SER A 799     206.085 163.734 168.710  1.00126.98           C  
ATOM   6125  O   SER A 799     205.049 163.766 168.037  1.00126.98           O  
ATOM   6126  CB  SER A 799     208.296 162.583 168.440  1.00126.98           C  
ATOM   6127  OG  SER A 799     208.378 162.465 169.850  1.00126.98           O  
ATOM   6128  N   LYS A 800     206.079 163.653 170.039  1.00133.07           N  
ATOM   6129  CA  LYS A 800     204.844 163.682 170.812  1.00133.07           C  
ATOM   6130  C   LYS A 800     205.192 164.045 172.246  1.00133.07           C  
ATOM   6131  O   LYS A 800     206.127 163.478 172.820  1.00133.07           O  
ATOM   6132  CB  LYS A 800     204.119 162.331 170.764  1.00133.07           C  
ATOM   6133  CG  LYS A 800     202.724 162.358 171.371  1.00133.07           C  
ATOM   6134  CD  LYS A 800     201.987 161.047 171.142  1.00133.07           C  
ATOM   6135  CE  LYS A 800     201.625 160.859 169.680  1.00133.07           C  
ATOM   6136  NZ  LYS A 800     200.675 161.900 169.201  1.00133.07           N  
ATOM   6137  N   GLY A 801     204.445 164.979 172.814  1.00158.57           N  
ATOM   6138  CA  GLY A 801     204.613 165.387 174.192  1.00158.57           C  
ATOM   6139  C   GLY A 801     205.032 166.838 174.288  1.00158.57           C  
ATOM   6140  O   GLY A 801     204.982 167.600 173.317  1.00158.57           O  
ATOM   6141  N   SER A 802     205.454 167.221 175.488  1.00171.39           N  
ATOM   6142  CA  SER A 802     205.925 168.574 175.754  1.00171.39           C  
ATOM   6143  C   SER A 802     206.794 168.533 177.004  1.00171.39           C  
ATOM   6144  O   SER A 802     207.011 167.474 177.598  1.00171.39           O  
ATOM   6145  CB  SER A 802     204.754 169.549 175.911  1.00171.39           C  
ATOM   6146  OG  SER A 802     204.014 169.271 177.087  1.00171.39           O  
ATOM   6147  N   THR A 803     207.294 169.703 177.401  1.00181.90           N  
ATOM   6148  CA  THR A 803     207.980 169.818 178.680  1.00181.90           C  
ATOM   6149  C   THR A 803     207.012 169.943 179.848  1.00181.90           C  
ATOM   6150  O   THR A 803     207.447 169.882 181.003  1.00181.90           O  
ATOM   6151  CB  THR A 803     208.929 171.019 178.669  1.00181.90           C  
ATOM   6152  OG1 THR A 803     209.709 171.026 179.871  1.00181.90           O  
ATOM   6153  CG2 THR A 803     208.142 172.318 178.573  1.00181.90           C  
ATOM   6154  N   LEU A 804     205.719 170.115 179.574  1.00186.37           N  
ATOM   6155  CA  LEU A 804     204.705 170.151 180.618  1.00186.37           C  
ATOM   6156  C   LEU A 804     204.072 168.786 180.848  1.00186.37           C  
ATOM   6157  O   LEU A 804     203.636 168.491 181.967  1.00186.37           O  
ATOM   6158  CB  LEU A 804     203.628 171.183 180.257  1.00186.37           C  
ATOM   6159  CG  LEU A 804     202.558 171.606 181.270  1.00186.37           C  
ATOM   6160  CD1 LEU A 804     201.356 170.669 181.258  1.00186.37           C  
ATOM   6161  CD2 LEU A 804     203.150 171.706 182.668  1.00186.37           C  
ATOM   6162  N   ASN A 805     204.023 167.945 179.812  1.00181.82           N  
ATOM   6163  CA  ASN A 805     203.415 166.625 179.946  1.00181.82           C  
ATOM   6164  C   ASN A 805     204.257 165.710 180.827  1.00181.82           C  
ATOM   6165  O   ASN A 805     203.717 164.967 181.655  1.00181.82           O  
ATOM   6166  CB  ASN A 805     203.207 166.002 178.566  1.00181.82           C  
ATOM   6167  CG  ASN A 805     202.115 166.693 177.774  1.00181.82           C  
ATOM   6168  OD1 ASN A 805     201.051 167.009 178.305  1.00181.82           O  
ATOM   6169  ND2 ASN A 805     202.375 166.932 176.493  1.00181.82           N  
ATOM   6170  N   VAL A 806     205.581 165.749 180.662  1.00176.49           N  
ATOM   6171  CA  VAL A 806     206.458 164.960 181.521  1.00176.49           C  
ATOM   6172  C   VAL A 806     206.495 165.533 182.932  1.00176.49           C  
ATOM   6173  O   VAL A 806     206.692 164.793 183.905  1.00176.49           O  
ATOM   6174  CB  VAL A 806     207.866 164.876 180.898  1.00176.49           C  
ATOM   6175  CG1 VAL A 806     208.467 166.266 180.733  1.00176.49           C  
ATOM   6176  CG2 VAL A 806     208.777 163.982 181.730  1.00176.49           C  
ATOM   6177  N   SER A 807     206.285 166.843 183.078  1.00188.24           N  
ATOM   6178  CA  SER A 807     206.358 167.457 184.399  1.00188.24           C  
ATOM   6179  C   SER A 807     205.176 167.053 185.270  1.00188.24           C  
ATOM   6180  O   SER A 807     205.316 166.947 186.494  1.00188.24           O  
ATOM   6181  CB  SER A 807     206.425 168.978 184.271  1.00188.24           C  
ATOM   6182  OG  SER A 807     205.201 169.501 183.788  1.00188.24           O  
ATOM   6183  N   GLN A 808     204.010 166.825 184.662  1.00191.93           N  
ATOM   6184  CA  GLN A 808     202.863 166.323 185.410  1.00191.93           C  
ATOM   6185  C   GLN A 808     203.000 164.849 185.760  1.00191.93           C  
ATOM   6186  O   GLN A 808     202.273 164.362 186.633  1.00191.93           O  
ATOM   6187  CB  GLN A 808     201.573 166.551 184.620  1.00191.93           C  
ATOM   6188  CG  GLN A 808     201.189 168.013 184.460  1.00191.93           C  
ATOM   6189  CD  GLN A 808     199.885 168.191 183.707  1.00191.93           C  
ATOM   6190  OE1 GLN A 808     199.308 167.227 183.204  1.00191.93           O  
ATOM   6191  NE2 GLN A 808     199.407 169.428 183.635  1.00191.93           N  
ATOM   6192  N   MET A 809     203.910 164.128 185.108  1.00188.37           N  
ATOM   6193  CA  MET A 809     204.102 162.714 185.394  1.00188.37           C  
ATOM   6194  C   MET A 809     205.125 162.448 186.490  1.00188.37           C  
ATOM   6195  O   MET A 809     205.113 161.356 187.069  1.00188.37           O  
ATOM   6196  CB  MET A 809     204.525 161.972 184.121  1.00188.37           C  
ATOM   6197  CG  MET A 809     203.452 161.923 183.045  1.00188.37           C  
ATOM   6198  SD  MET A 809     204.027 161.148 181.522  1.00188.37           S  
ATOM   6199  CE  MET A 809     204.172 159.441 182.045  1.00188.37           C  
ATOM   6200  N   VAL A 810     206.004 163.403 186.794  1.00188.52           N  
ATOM   6201  CA  VAL A 810     207.124 163.115 187.683  1.00188.52           C  
ATOM   6202  C   VAL A 810     207.161 164.070 188.873  1.00188.52           C  
ATOM   6203  O   VAL A 810     207.622 163.698 189.958  1.00188.52           O  
ATOM   6204  CB  VAL A 810     208.456 163.151 186.906  1.00188.52           C  
ATOM   6205  CG1 VAL A 810     208.760 164.557 186.405  1.00188.52           C  
ATOM   6206  CG2 VAL A 810     209.599 162.619 187.761  1.00188.52           C  
ATOM   6207  N   ALA A 811     206.669 165.298 188.698  1.00198.64           N  
ATOM   6208  CA  ALA A 811     206.845 166.322 189.725  1.00198.64           C  
ATOM   6209  C   ALA A 811     205.524 166.819 190.298  1.00198.64           C  
ATOM   6210  O   ALA A 811     205.295 166.679 191.504  1.00198.64           O  
ATOM   6211  CB  ALA A 811     207.657 167.492 189.155  1.00198.64           C  
ATOM   6212  N   VAL A 812     204.647 167.389 189.476  1.00210.15           N  
ATOM   6213  CA  VAL A 812     203.429 168.024 189.972  1.00210.15           C  
ATOM   6214  C   VAL A 812     202.476 168.195 188.797  1.00210.15           C  
ATOM   6215  O   VAL A 812     202.900 168.469 187.672  1.00210.15           O  
ATOM   6216  CB  VAL A 812     203.741 169.372 190.669  1.00210.15           C  
ATOM   6217  CG1 VAL A 812     204.351 170.365 189.687  1.00210.15           C  
ATOM   6218  CG2 VAL A 812     202.491 169.947 191.324  1.00210.15           C  
ATOM   6219  N   VAL A 813     201.177 168.041 189.068  1.00216.93           N  
ATOM   6220  CA  VAL A 813     200.170 168.082 188.011  1.00216.93           C  
ATOM   6221  C   VAL A 813     199.493 169.440 187.886  1.00216.93           C  
ATOM   6222  O   VAL A 813     198.687 169.632 186.960  1.00216.93           O  
ATOM   6223  CB  VAL A 813     199.099 166.990 188.221  1.00216.93           C  
ATOM   6224  CG1 VAL A 813     199.712 165.614 188.055  1.00216.93           C  
ATOM   6225  CG2 VAL A 813     198.469 167.129 189.593  1.00216.93           C  
ATOM   6226  N   GLY A 814     199.786 170.382 188.776  1.00238.28           N  
ATOM   6227  CA  GLY A 814     199.207 171.704 188.684  1.00238.28           C  
ATOM   6228  C   GLY A 814     197.798 171.774 189.246  1.00238.28           C  
ATOM   6229  O   GLY A 814     197.299 170.861 189.909  1.00238.28           O  
ATOM   6230  N   GLN A 815     197.151 172.902 188.964  1.00261.05           N  
ATOM   6231  CA  GLN A 815     195.822 173.209 189.473  1.00261.05           C  
ATOM   6232  C   GLN A 815     194.819 173.097 188.333  1.00261.05           C  
ATOM   6233  O   GLN A 815     195.025 173.676 187.262  1.00261.05           O  
ATOM   6234  CB  GLN A 815     195.783 174.610 190.088  1.00261.05           C  
ATOM   6235  CG  GLN A 815     194.517 174.916 190.873  1.00261.05           C  
ATOM   6236  CD  GLN A 815     193.439 175.555 190.021  1.00261.05           C  
ATOM   6237  OE1 GLN A 815     193.729 176.321 189.103  1.00261.05           O  
ATOM   6238  NE2 GLN A 815     192.185 175.238 190.321  1.00261.05           N  
ATOM   6239  N   GLN A 816     193.738 172.353 188.562  1.00263.38           N  
ATOM   6240  CA  GLN A 816     192.714 172.195 187.538  1.00263.38           C  
ATOM   6241  C   GLN A 816     191.910 173.480 187.382  1.00263.38           C  
ATOM   6242  O   GLN A 816     191.410 174.038 188.363  1.00263.38           O  
ATOM   6243  CB  GLN A 816     191.788 171.031 187.887  1.00263.38           C  
ATOM   6244  CG  GLN A 816     192.419 169.657 187.720  1.00263.38           C  
ATOM   6245  CD  GLN A 816     193.173 169.204 188.955  1.00263.38           C  
ATOM   6246  OE1 GLN A 816     193.007 169.765 190.038  1.00263.38           O  
ATOM   6247  NE2 GLN A 816     194.007 168.183 188.797  1.00263.38           N  
ATOM   6248  N   ILE A 817     191.779 173.942 186.141  1.00300.49           N  
ATOM   6249  CA  ILE A 817     190.943 175.086 185.799  1.00300.49           C  
ATOM   6250  C   ILE A 817     189.637 174.581 185.202  1.00300.49           C  
ATOM   6251  O   ILE A 817     189.586 173.515 184.576  1.00300.49           O  
ATOM   6252  CB  ILE A 817     191.676 176.044 184.832  1.00300.49           C  
ATOM   6253  CG1 ILE A 817     190.998 177.416 184.808  1.00300.49           C  
ATOM   6254  CG2 ILE A 817     191.754 175.451 183.430  1.00300.49           C  
ATOM   6255  CD1 ILE A 817     191.194 178.210 186.078  1.00300.49           C  
ATOM   6256  N   ILE A 818     188.562 175.338 185.413  1.00316.53           N  
ATOM   6257  CA  ILE A 818     187.243 175.000 184.883  1.00316.53           C  
ATOM   6258  C   ILE A 818     186.698 176.260 184.220  1.00316.53           C  
ATOM   6259  O   ILE A 818     186.107 177.117 184.888  1.00316.53           O  
ATOM   6260  CB  ILE A 818     186.288 174.493 185.969  1.00316.53           C  
ATOM   6261  CG1 ILE A 818     186.868 173.260 186.663  1.00316.53           C  
ATOM   6262  CG2 ILE A 818     184.926 174.167 185.371  1.00316.53           C  
ATOM   6263  CD1 ILE A 818     186.150 172.890 187.939  1.00316.53           C  
ATOM   6264  N   SER A 819     186.897 176.373 182.905  1.00327.93           N  
ATOM   6265  CA  SER A 819     186.361 177.467 182.091  1.00327.93           C  
ATOM   6266  C   SER A 819     186.774 178.831 182.639  1.00327.93           C  
ATOM   6267  O   SER A 819     185.980 179.774 182.671  1.00327.93           O  
ATOM   6268  CB  SER A 819     184.839 177.370 181.968  1.00327.93           C  
ATOM   6269  OG  SER A 819     184.205 177.653 183.204  1.00327.93           O  
ATOM   6270  N   GLY A 820     188.024 178.940 183.076  1.00329.25           N  
ATOM   6271  CA  GLY A 820     188.478 180.166 183.703  1.00329.25           C  
ATOM   6272  C   GLY A 820     188.040 180.317 185.142  1.00329.25           C  
ATOM   6273  O   GLY A 820     187.748 181.436 185.583  1.00329.25           O  
ATOM   6274  N   ASN A 821     187.983 179.220 185.894  1.00325.41           N  
ATOM   6275  CA  ASN A 821     187.627 179.278 187.303  1.00325.41           C  
ATOM   6276  C   ASN A 821     188.333 178.151 188.040  1.00325.41           C  
ATOM   6277  O   ASN A 821     188.380 177.017 187.556  1.00325.41           O  
ATOM   6278  CB  ASN A 821     186.109 179.182 187.500  1.00325.41           C  
ATOM   6279  CG  ASN A 821     185.678 179.544 188.908  1.00325.41           C  
ATOM   6280  OD1 ASN A 821     186.509 179.803 189.779  1.00325.41           O  
ATOM   6281  ND2 ASN A 821     184.371 179.576 189.134  1.00325.41           N  
ATOM   6282  N   ARG A 822     188.881 178.472 189.212  1.00318.21           N  
ATOM   6283  CA  ARG A 822     189.746 177.545 189.943  1.00318.21           C  
ATOM   6284  C   ARG A 822     188.909 176.677 190.888  1.00318.21           C  
ATOM   6285  O   ARG A 822     189.019 176.727 192.115  1.00318.21           O  
ATOM   6286  CB  ARG A 822     190.839 178.316 190.675  1.00318.21           C  
ATOM   6287  CG  ARG A 822     190.339 179.397 191.630  1.00318.21           C  
ATOM   6288  CD  ARG A 822     191.495 180.087 192.337  1.00318.21           C  
ATOM   6289  NE  ARG A 822     191.033 181.084 193.298  1.00318.21           N  
ATOM   6290  CZ  ARG A 822     190.781 180.827 194.577  1.00318.21           C  
ATOM   6291  NH1 ARG A 822     190.953 179.602 195.054  1.00318.21           N  
ATOM   6292  NH2 ARG A 822     190.364 181.795 195.381  1.00318.21           N  
ATOM   6293  N   VAL A 823     188.072 175.846 190.270  1.00304.19           N  
ATOM   6294  CA  VAL A 823     187.191 174.902 190.959  1.00304.19           C  
ATOM   6295  C   VAL A 823     186.312 175.630 191.971  1.00304.19           C  
ATOM   6296  O   VAL A 823     186.633 175.654 193.168  1.00304.19           O  
ATOM   6297  CB  VAL A 823     187.995 173.778 191.632  1.00304.19           C  
ATOM   6298  CG1 VAL A 823     187.060 172.697 192.158  1.00304.19           C  
ATOM   6299  CG2 VAL A 823     189.000 173.188 190.653  1.00304.19           C  
ATOM   6300  N   PRO A 824     185.214 176.249 191.539  1.00312.09           N  
ATOM   6301  CA  PRO A 824     184.355 176.987 192.473  1.00312.09           C  
ATOM   6302  C   PRO A 824     183.721 176.069 193.508  1.00312.09           C  
ATOM   6303  O   PRO A 824     183.750 174.840 193.408  1.00312.09           O  
ATOM   6304  CB  PRO A 824     183.299 177.616 191.560  1.00312.09           C  
ATOM   6305  CG  PRO A 824     183.237 176.699 190.384  1.00312.09           C  
ATOM   6306  CD  PRO A 824     184.643 176.201 190.181  1.00312.09           C  
ATOM   6307  N   ASP A 825     183.137 176.696 194.526  1.00303.93           N  
ATOM   6308  CA  ASP A 825     182.663 175.973 195.697  1.00303.93           C  
ATOM   6309  C   ASP A 825     181.456 175.107 195.351  1.00303.93           C  
ATOM   6310  O   ASP A 825     180.646 175.445 194.484  1.00303.93           O  
ATOM   6311  CB  ASP A 825     182.306 176.948 196.820  1.00303.93           C  
ATOM   6312  CG  ASP A 825     181.364 178.047 196.363  1.00303.93           C  
ATOM   6313  OD1 ASP A 825     181.095 178.139 195.146  1.00303.93           O  
ATOM   6314  OD2 ASP A 825     180.889 178.818 197.223  1.00303.93           O  
ATOM   6315  N   GLY A 826     181.346 173.972 196.038  1.00286.74           N  
ATOM   6316  CA  GLY A 826     180.222 173.080 195.835  1.00286.74           C  
ATOM   6317  C   GLY A 826     178.990 173.468 196.626  1.00286.74           C  
ATOM   6318  O   GLY A 826     177.899 173.591 196.062  1.00286.74           O  
ATOM   6319  N   PHE A 827     179.148 173.667 197.933  1.00278.86           N  
ATOM   6320  CA  PHE A 827     178.032 174.064 198.780  1.00278.86           C  
ATOM   6321  C   PHE A 827     178.573 174.726 200.039  1.00278.86           C  
ATOM   6322  O   PHE A 827     179.719 174.499 200.437  1.00278.86           O  
ATOM   6323  CB  PHE A 827     177.136 172.869 199.127  1.00278.86           C  
ATOM   6324  CG  PHE A 827     177.890 171.658 199.601  1.00278.86           C  
ATOM   6325  CD1 PHE A 827     178.237 170.653 198.713  1.00278.86           C  
ATOM   6326  CD2 PHE A 827     178.247 171.520 200.932  1.00278.86           C  
ATOM   6327  CE1 PHE A 827     178.928 169.536 199.143  1.00278.86           C  
ATOM   6328  CE2 PHE A 827     178.937 170.406 201.368  1.00278.86           C  
ATOM   6329  CZ  PHE A 827     179.278 169.413 200.472  1.00278.86           C  
ATOM   6330  N   GLN A 828     177.723 175.558 200.649  1.00282.55           N  
ATOM   6331  CA  GLN A 828     177.991 176.242 201.922  1.00282.55           C  
ATOM   6332  C   GLN A 828     179.387 176.870 201.938  1.00282.55           C  
ATOM   6333  O   GLN A 828     180.147 176.757 202.902  1.00282.55           O  
ATOM   6334  CB  GLN A 828     177.756 175.320 203.128  1.00282.55           C  
ATOM   6335  CG  GLN A 828     178.652 174.105 203.280  1.00282.55           C  
ATOM   6336  CD  GLN A 828     178.232 173.238 204.448  1.00282.55           C  
ATOM   6337  OE1 GLN A 828     177.245 173.525 205.125  1.00282.55           O  
ATOM   6338  NE2 GLN A 828     178.976 172.168 204.688  1.00282.55           N  
ATOM   6339  N   ASP A 829     179.706 177.553 200.837  1.00288.32           N  
ATOM   6340  CA  ASP A 829     180.985 178.234 200.629  1.00288.32           C  
ATOM   6341  C   ASP A 829     182.185 177.293 200.715  1.00288.32           C  
ATOM   6342  O   ASP A 829     183.284 177.711 201.090  1.00288.32           O  
ATOM   6343  CB  ASP A 829     181.156 179.396 201.614  1.00288.32           C  
ATOM   6344  CG  ASP A 829     180.177 180.525 201.358  1.00288.32           C  
ATOM   6345  OD1 ASP A 829     179.754 180.695 200.195  1.00288.32           O  
ATOM   6346  OD2 ASP A 829     179.828 181.241 202.320  1.00288.32           O  
ATOM   6347  N   ARG A 830     182.005 176.018 200.373  1.00272.16           N  
ATOM   6348  CA  ARG A 830     183.123 175.085 200.341  1.00272.16           C  
ATOM   6349  C   ARG A 830     182.881 174.078 199.222  1.00272.16           C  
ATOM   6350  O   ARG A 830     181.838 174.092 198.562  1.00272.16           O  
ATOM   6351  CB  ARG A 830     183.330 174.393 201.693  1.00272.16           C  
ATOM   6352  CG  ARG A 830     182.258 173.396 202.087  1.00272.16           C  
ATOM   6353  CD  ARG A 830     182.604 172.767 203.426  1.00272.16           C  
ATOM   6354  NE  ARG A 830     181.698 171.683 203.790  1.00272.16           N  
ATOM   6355  CZ  ARG A 830     181.833 170.934 204.880  1.00272.16           C  
ATOM   6356  NH1 ARG A 830     182.839 171.153 205.715  1.00272.16           N  
ATOM   6357  NH2 ARG A 830     180.962 169.968 205.137  1.00272.16           N  
ATOM   6358  N   SER A 831     183.860 173.200 199.009  1.00267.01           N  
ATOM   6359  CA  SER A 831     183.804 172.246 197.908  1.00267.01           C  
ATOM   6360  C   SER A 831     183.383 170.845 198.329  1.00267.01           C  
ATOM   6361  O   SER A 831     182.706 170.159 197.557  1.00267.01           O  
ATOM   6362  CB  SER A 831     185.165 172.166 197.208  1.00267.01           C  
ATOM   6363  OG  SER A 831     186.153 171.632 198.073  1.00267.01           O  
ATOM   6364  N   LEU A 832     183.762 170.404 199.521  1.00256.52           N  
ATOM   6365  CA  LEU A 832     183.614 169.017 199.931  1.00256.52           C  
ATOM   6366  C   LEU A 832     183.219 168.951 201.396  1.00256.52           C  
ATOM   6367  O   LEU A 832     183.479 169.886 202.161  1.00256.52           O  
ATOM   6368  CB  LEU A 832     184.907 168.219 199.709  1.00256.52           C  
ATOM   6369  CG  LEU A 832     185.328 167.953 198.263  1.00256.52           C  
ATOM   6370  CD1 LEU A 832     186.682 167.264 198.224  1.00256.52           C  
ATOM   6371  CD2 LEU A 832     184.279 167.124 197.538  1.00256.52           C  
ATOM   6372  N   PRO A 833     182.588 167.851 201.820  1.00250.42           N  
ATOM   6373  CA  PRO A 833     182.386 167.614 203.257  1.00250.42           C  
ATOM   6374  C   PRO A 833     183.656 167.229 203.997  1.00250.42           C  
ATOM   6375  O   PRO A 833     183.613 167.055 205.220  1.00250.42           O  
ATOM   6376  CB  PRO A 833     181.375 166.456 203.281  1.00250.42           C  
ATOM   6377  CG  PRO A 833     180.712 166.494 201.942  1.00250.42           C  
ATOM   6378  CD  PRO A 833     181.782 166.936 200.993  1.00250.42           C  
ATOM   6379  N   HIS A 834     184.779 167.091 203.295  1.00236.54           N  
ATOM   6380  CA  HIS A 834     186.068 166.776 203.894  1.00236.54           C  
ATOM   6381  C   HIS A 834     186.848 168.015 204.314  1.00236.54           C  
ATOM   6382  O   HIS A 834     187.888 167.880 204.969  1.00236.54           O  
ATOM   6383  CB  HIS A 834     186.919 165.959 202.914  1.00236.54           C  
ATOM   6384  CG  HIS A 834     186.312 164.645 202.534  1.00236.54           C  
ATOM   6385  ND1 HIS A 834     186.839 163.841 201.547  1.00236.54           N  
ATOM   6386  CD2 HIS A 834     185.222 163.994 203.006  1.00236.54           C  
ATOM   6387  CE1 HIS A 834     186.102 162.751 201.428  1.00236.54           C  
ATOM   6388  NE2 HIS A 834     185.114 162.820 202.302  1.00236.54           N  
ATOM   6389  N   PHE A 835     186.376 169.207 203.957  1.00245.21           N  
ATOM   6390  CA  PHE A 835     187.111 170.448 204.120  1.00245.21           C  
ATOM   6391  C   PHE A 835     186.321 171.418 204.992  1.00245.21           C  
ATOM   6392  O   PHE A 835     185.087 171.422 204.959  1.00245.21           O  
ATOM   6393  CB  PHE A 835     187.390 171.085 202.754  1.00245.21           C  
ATOM   6394  CG  PHE A 835     188.426 170.353 201.949  1.00245.21           C  
ATOM   6395  CD1 PHE A 835     189.383 169.572 202.577  1.00245.21           C  
ATOM   6396  CD2 PHE A 835     188.425 170.420 200.566  1.00245.21           C  
ATOM   6397  CE1 PHE A 835     190.333 168.890 201.841  1.00245.21           C  
ATOM   6398  CE2 PHE A 835     189.372 169.737 199.825  1.00245.21           C  
ATOM   6399  CZ  PHE A 835     190.327 168.972 200.463  1.00245.21           C  
ATOM   6400  N   PRO A 836     187.000 172.244 205.785  1.00243.84           N  
ATOM   6401  CA  PRO A 836     186.290 173.103 206.740  1.00243.84           C  
ATOM   6402  C   PRO A 836     185.524 174.222 206.048  1.00243.84           C  
ATOM   6403  O   PRO A 836     185.636 174.459 204.844  1.00243.84           O  
ATOM   6404  CB  PRO A 836     187.414 173.657 207.621  1.00243.84           C  
ATOM   6405  CG  PRO A 836     188.631 173.585 206.761  1.00243.84           C  
ATOM   6406  CD  PRO A 836     188.463 172.356 205.920  1.00243.84           C  
ATOM   6407  N   LYS A 837     184.726 174.917 206.855  1.00254.18           N  
ATOM   6408  CA  LYS A 837     183.857 175.974 206.355  1.00254.18           C  
ATOM   6409  C   LYS A 837     184.655 177.177 205.866  1.00254.18           C  
ATOM   6410  O   LYS A 837     185.697 177.522 206.430  1.00254.18           O  
ATOM   6411  CB  LYS A 837     182.874 176.410 207.442  1.00254.18           C  
ATOM   6412  CG  LYS A 837     181.584 175.599 207.489  1.00254.18           C  
ATOM   6413  CD  LYS A 837     181.796 174.219 208.095  1.00254.18           C  
ATOM   6414  CE  LYS A 837     182.159 174.308 209.569  1.00254.18           C  
ATOM   6415  NZ  LYS A 837     182.321 172.960 210.181  1.00254.18           N  
ATOM   6416  N   ASN A 838     184.181 177.760 204.759  1.00267.07           N  
ATOM   6417  CA  ASN A 838     184.702 178.944 204.072  1.00267.07           C  
ATOM   6418  C   ASN A 838     186.219 179.101 204.135  1.00267.07           C  
ATOM   6419  O   ASN A 838     186.724 180.199 204.393  1.00267.07           O  
ATOM   6420  CB  ASN A 838     183.994 180.221 204.573  1.00267.07           C  
ATOM   6421  CG  ASN A 838     184.242 180.536 206.048  1.00267.07           C  
ATOM   6422  OD1 ASN A 838     185.128 179.985 206.693  1.00267.07           O  
ATOM   6423  ND2 ASN A 838     183.438 181.447 206.584  1.00267.07           N  
ATOM   6424  N   SER A 839     186.955 178.023 203.881  1.00264.74           N  
ATOM   6425  CA  SER A 839     188.413 178.029 203.978  1.00264.74           C  
ATOM   6426  C   SER A 839     188.960 178.173 202.562  1.00264.74           C  
ATOM   6427  O   SER A 839     188.960 177.217 201.783  1.00264.74           O  
ATOM   6428  CB  SER A 839     188.920 176.762 204.658  1.00264.74           C  
ATOM   6429  OG  SER A 839     188.450 176.684 205.993  1.00264.74           O  
ATOM   6430  N   LYS A 840     189.426 179.376 202.231  1.00273.79           N  
ATOM   6431  CA  LYS A 840     189.774 179.714 200.850  1.00273.79           C  
ATOM   6432  C   LYS A 840     191.266 179.492 200.590  1.00273.79           C  
ATOM   6433  O   LYS A 840     192.001 180.390 200.182  1.00273.79           O  
ATOM   6434  CB  LYS A 840     189.363 181.150 200.545  1.00273.79           C  
ATOM   6435  CG  LYS A 840     187.859 181.369 200.534  1.00273.79           C  
ATOM   6436  CD  LYS A 840     187.507 182.836 200.355  1.00273.79           C  
ATOM   6437  CE  LYS A 840     187.800 183.305 198.939  1.00273.79           C  
ATOM   6438  NZ  LYS A 840     187.345 184.704 198.710  1.00273.79           N  
ATOM   6439  N   THR A 841     191.709 178.258 200.831  1.00266.54           N  
ATOM   6440  CA  THR A 841     193.088 177.920 200.523  1.00266.54           C  
ATOM   6441  C   THR A 841     193.151 176.953 199.344  1.00266.54           C  
ATOM   6442  O   THR A 841     192.254 176.122 199.164  1.00266.54           O  
ATOM   6443  CB  THR A 841     193.801 177.296 201.731  1.00266.54           C  
ATOM   6444  OG1 THR A 841     195.142 176.941 201.368  1.00266.54           O  
ATOM   6445  CG2 THR A 841     193.061 176.060 202.222  1.00266.54           C  
ATOM   6446  N   PRO A 842     194.186 177.043 198.515  1.00268.40           N  
ATOM   6447  CA  PRO A 842     194.522 175.926 197.628  1.00268.40           C  
ATOM   6448  C   PRO A 842     195.189 174.780 198.371  1.00268.40           C  
ATOM   6449  O   PRO A 842     195.903 174.981 199.356  1.00268.40           O  
ATOM   6450  CB  PRO A 842     195.488 176.556 196.616  1.00268.40           C  
ATOM   6451  CG  PRO A 842     196.079 177.720 197.335  1.00268.40           C  
ATOM   6452  CD  PRO A 842     195.003 178.238 198.243  1.00268.40           C  
ATOM   6453  N   GLN A 843     194.982 173.576 197.831  1.00254.78           N  
ATOM   6454  CA  GLN A 843     194.907 172.243 198.453  1.00254.78           C  
ATOM   6455  C   GLN A 843     193.527 171.986 199.048  1.00254.78           C  
ATOM   6456  O   GLN A 843     193.274 170.867 199.514  1.00254.78           O  
ATOM   6457  CB  GLN A 843     195.966 171.976 199.541  1.00254.78           C  
ATOM   6458  CG  GLN A 843     195.649 172.515 200.938  1.00254.78           C  
ATOM   6459  CD  GLN A 843     195.042 171.466 201.852  1.00254.78           C  
ATOM   6460  OE1 GLN A 843     195.329 170.276 201.726  1.00254.78           O  
ATOM   6461  NE2 GLN A 843     194.196 171.905 202.776  1.00254.78           N  
ATOM   6462  N   SER A 844     192.622 172.960 199.033  1.00254.16           N  
ATOM   6463  CA  SER A 844     191.241 172.737 199.434  1.00254.16           C  
ATOM   6464  C   SER A 844     190.217 173.103 198.372  1.00254.16           C  
ATOM   6465  O   SER A 844     189.146 172.495 198.339  1.00254.16           O  
ATOM   6466  CB  SER A 844     190.925 173.523 200.716  1.00254.16           C  
ATOM   6467  OG  SER A 844     189.569 173.365 201.095  1.00254.16           O  
ATOM   6468  N   LYS A 845     190.506 174.076 197.509  1.00257.82           N  
ATOM   6469  CA  LYS A 845     189.626 174.392 196.390  1.00257.82           C  
ATOM   6470  C   LYS A 845     190.045 173.692 195.101  1.00257.82           C  
ATOM   6471  O   LYS A 845     189.301 172.857 194.579  1.00257.82           O  
ATOM   6472  CB  LYS A 845     189.560 175.910 196.177  1.00257.82           C  
ATOM   6473  CG  LYS A 845     188.703 176.636 197.201  1.00257.82           C  
ATOM   6474  CD  LYS A 845     188.545 178.104 196.845  1.00257.82           C  
ATOM   6475  CE  LYS A 845     187.638 178.820 197.831  1.00257.82           C  
ATOM   6476  NZ  LYS A 845     187.470 180.255 197.473  1.00257.82           N  
ATOM   6477  N   GLY A 846     191.226 174.012 194.578  1.00258.09           N  
ATOM   6478  CA  GLY A 846     191.597 173.500 193.274  1.00258.09           C  
ATOM   6479  C   GLY A 846     192.895 172.724 193.180  1.00258.09           C  
ATOM   6480  O   GLY A 846     193.009 171.818 192.349  1.00258.09           O  
ATOM   6481  N   PHE A 847     193.881 173.051 194.011  1.00244.65           N  
ATOM   6482  CA  PHE A 847     195.252 172.644 193.738  1.00244.65           C  
ATOM   6483  C   PHE A 847     195.534 171.256 194.298  1.00244.65           C  
ATOM   6484  O   PHE A 847     195.082 170.903 195.390  1.00244.65           O  
ATOM   6485  CB  PHE A 847     196.239 173.651 194.330  1.00244.65           C  
ATOM   6486  CG  PHE A 847     197.675 173.362 193.990  1.00244.65           C  
ATOM   6487  CD1 PHE A 847     198.145 173.541 192.699  1.00244.65           C  
ATOM   6488  CD2 PHE A 847     198.554 172.913 194.962  1.00244.65           C  
ATOM   6489  CE1 PHE A 847     199.465 173.278 192.383  1.00244.65           C  
ATOM   6490  CE2 PHE A 847     199.876 172.648 194.652  1.00244.65           C  
ATOM   6491  CZ  PHE A 847     200.331 172.831 193.361  1.00244.65           C  
ATOM   6492  N   VAL A 848     196.297 170.477 193.535  1.00225.34           N  
ATOM   6493  CA  VAL A 848     196.727 169.136 193.914  1.00225.34           C  
ATOM   6494  C   VAL A 848     198.236 169.062 193.726  1.00225.34           C  
ATOM   6495  O   VAL A 848     198.741 169.332 192.630  1.00225.34           O  
ATOM   6496  CB  VAL A 848     196.008 168.048 193.097  1.00225.34           C  
ATOM   6497  CG1 VAL A 848     195.853 168.479 191.650  1.00225.34           C  
ATOM   6498  CG2 VAL A 848     196.758 166.731 193.183  1.00225.34           C  
ATOM   6499  N   ARG A 849     198.958 168.716 194.793  1.00218.42           N  
ATOM   6500  CA  ARG A 849     200.390 168.974 194.847  1.00218.42           C  
ATOM   6501  C   ARG A 849     201.250 167.763 194.510  1.00218.42           C  
ATOM   6502  O   ARG A 849     202.427 167.937 194.178  1.00218.42           O  
ATOM   6503  CB  ARG A 849     200.784 169.485 196.239  1.00218.42           C  
ATOM   6504  CG  ARG A 849     200.535 168.484 197.358  1.00218.42           C  
ATOM   6505  CD  ARG A 849     200.985 169.030 198.704  1.00218.42           C  
ATOM   6506  NE  ARG A 849     202.434 169.197 198.764  1.00218.42           N  
ATOM   6507  CZ  ARG A 849     203.284 168.228 199.090  1.00218.42           C  
ATOM   6508  NH1 ARG A 849     202.830 167.020 199.393  1.00218.42           N  
ATOM   6509  NH2 ARG A 849     204.589 168.468 199.116  1.00218.42           N  
ATOM   6510  N   ASN A 850     200.707 166.554 194.586  1.00195.69           N  
ATOM   6511  CA  ASN A 850     201.499 165.346 194.413  1.00195.69           C  
ATOM   6512  C   ASN A 850     201.416 164.841 192.975  1.00195.69           C  
ATOM   6513  O   ASN A 850     200.471 165.134 192.238  1.00195.69           O  
ATOM   6514  CB  ASN A 850     201.043 164.258 195.388  1.00195.69           C  
ATOM   6515  CG  ASN A 850     199.542 164.052 195.373  1.00195.69           C  
ATOM   6516  OD1 ASN A 850     198.825 164.668 194.585  1.00195.69           O  
ATOM   6517  ND2 ASN A 850     199.057 163.179 196.249  1.00195.69           N  
ATOM   6518  N   SER A 851     202.427 164.069 192.585  1.00182.24           N  
ATOM   6519  CA  SER A 851     202.587 163.645 191.203  1.00182.24           C  
ATOM   6520  C   SER A 851     201.765 162.389 190.918  1.00182.24           C  
ATOM   6521  O   SER A 851     201.235 161.738 191.822  1.00182.24           O  
ATOM   6522  CB  SER A 851     204.063 163.397 190.888  1.00182.24           C  
ATOM   6523  OG  SER A 851     204.229 162.902 189.571  1.00182.24           O  
ATOM   6524  N   PHE A 852     201.664 162.051 189.629  1.00168.00           N  
ATOM   6525  CA  PHE A 852     201.009 160.806 189.240  1.00168.00           C  
ATOM   6526  C   PHE A 852     201.804 159.581 189.677  1.00168.00           C  
ATOM   6527  O   PHE A 852     201.219 158.518 189.909  1.00168.00           O  
ATOM   6528  CB  PHE A 852     200.787 160.781 187.727  1.00168.00           C  
ATOM   6529  CG  PHE A 852     199.636 161.630 187.266  1.00168.00           C  
ATOM   6530  CD1 PHE A 852     198.656 162.036 188.156  1.00168.00           C  
ATOM   6531  CD2 PHE A 852     199.534 162.021 185.940  1.00168.00           C  
ATOM   6532  CE1 PHE A 852     197.595 162.814 187.733  1.00168.00           C  
ATOM   6533  CE2 PHE A 852     198.476 162.801 185.512  1.00168.00           C  
ATOM   6534  CZ  PHE A 852     197.506 163.198 186.410  1.00168.00           C  
ATOM   6535  N   PHE A 853     203.129 159.705 189.791  1.00165.71           N  
ATOM   6536  CA  PHE A 853     203.931 158.600 190.309  1.00165.71           C  
ATOM   6537  C   PHE A 853     203.696 158.399 191.800  1.00165.71           C  
ATOM   6538  O   PHE A 853     203.652 157.261 192.283  1.00165.71           O  
ATOM   6539  CB  PHE A 853     205.413 158.850 190.027  1.00165.71           C  
ATOM   6540  CG  PHE A 853     206.321 157.778 190.558  1.00165.71           C  
ATOM   6541  CD1 PHE A 853     206.402 156.544 189.932  1.00165.71           C  
ATOM   6542  CD2 PHE A 853     207.089 158.001 191.689  1.00165.71           C  
ATOM   6543  CE1 PHE A 853     207.238 155.556 190.421  1.00165.71           C  
ATOM   6544  CE2 PHE A 853     207.925 157.018 192.183  1.00165.71           C  
ATOM   6545  CZ  PHE A 853     208.000 155.794 191.549  1.00165.71           C  
ATOM   6546  N   SER A 854     203.543 159.496 192.543  1.00171.98           N  
ATOM   6547  CA  SER A 854     203.316 159.411 193.982  1.00171.98           C  
ATOM   6548  C   SER A 854     201.942 158.828 194.288  1.00171.98           C  
ATOM   6549  O   SER A 854     201.813 157.903 195.098  1.00171.98           O  
ATOM   6550  CB  SER A 854     203.474 160.792 194.620  1.00171.98           C  
ATOM   6551  OG  SER A 854     202.526 161.704 194.095  1.00171.98           O  
ATOM   6552  N   GLY A 855     200.906 159.358 193.650  1.00175.36           N  
ATOM   6553  CA  GLY A 855     199.541 158.934 193.885  1.00175.36           C  
ATOM   6554  C   GLY A 855     198.636 160.112 194.185  1.00175.36           C  
ATOM   6555  O   GLY A 855     199.071 161.248 194.356  1.00175.36           O  
ATOM   6556  N   LEU A 856     197.343 159.807 194.245  1.00177.37           N  
ATOM   6557  CA  LEU A 856     196.310 160.800 194.500  1.00177.37           C  
ATOM   6558  C   LEU A 856     195.475 160.402 195.707  1.00177.37           C  
ATOM   6559  O   LEU A 856     195.100 159.235 195.861  1.00177.37           O  
ATOM   6560  CB  LEU A 856     195.399 160.980 193.278  1.00177.37           C  
ATOM   6561  CG  LEU A 856     195.808 162.024 192.235  1.00177.37           C  
ATOM   6562  CD1 LEU A 856     197.034 161.576 191.453  1.00177.37           C  
ATOM   6563  CD2 LEU A 856     194.648 162.318 191.293  1.00177.37           C  
ATOM   6564  N   SER A 857     195.189 161.385 196.560  1.00188.14           N  
ATOM   6565  CA  SER A 857     194.347 161.191 197.726  1.00188.14           C  
ATOM   6566  C   SER A 857     192.872 161.224 197.325  1.00188.14           C  
ATOM   6567  O   SER A 857     192.510 161.825 196.310  1.00188.14           O  
ATOM   6568  CB  SER A 857     194.637 162.263 198.772  1.00188.14           C  
ATOM   6569  OG  SER A 857     194.070 163.505 198.404  1.00188.14           O  
ATOM   6570  N   PRO A 858     192.008 160.574 198.101  1.00189.17           N  
ATOM   6571  CA  PRO A 858     190.571 160.534 197.772  1.00189.17           C  
ATOM   6572  C   PRO A 858     189.916 161.905 197.688  1.00189.17           C  
ATOM   6573  O   PRO A 858     188.944 162.063 196.933  1.00189.17           O  
ATOM   6574  CB  PRO A 858     189.977 159.707 198.922  1.00189.17           C  
ATOM   6575  CG  PRO A 858     191.098 158.830 199.355  1.00189.17           C  
ATOM   6576  CD  PRO A 858     192.346 159.651 199.201  1.00189.17           C  
ATOM   6577  N   PRO A 859     190.385 162.935 198.427  1.00198.16           N  
ATOM   6578  CA  PRO A 859     189.884 164.285 198.121  1.00198.16           C  
ATOM   6579  C   PRO A 859     190.351 164.840 196.782  1.00198.16           C  
ATOM   6580  O   PRO A 859     189.533 165.349 196.009  1.00198.16           O  
ATOM   6581  CB  PRO A 859     190.403 165.132 199.295  1.00198.16           C  
ATOM   6582  CG  PRO A 859     191.508 164.342 199.885  1.00198.16           C  
ATOM   6583  CD  PRO A 859     191.069 162.922 199.732  1.00198.16           C  
ATOM   6584  N   GLU A 860     191.649 164.755 196.488  1.00199.99           N  
ATOM   6585  CA  GLU A 860     192.173 165.350 195.263  1.00199.99           C  
ATOM   6586  C   GLU A 860     191.882 164.517 194.021  1.00199.99           C  
ATOM   6587  O   GLU A 860     192.054 165.020 192.905  1.00199.99           O  
ATOM   6588  CB  GLU A 860     193.681 165.581 195.390  1.00199.99           C  
ATOM   6589  CG  GLU A 860     194.505 164.314 195.424  1.00199.99           C  
ATOM   6590  CD  GLU A 860     195.891 164.540 195.993  1.00199.99           C  
ATOM   6591  OE1 GLU A 860     196.230 165.703 196.297  1.00199.99           O  
ATOM   6592  OE2 GLU A 860     196.640 163.552 196.143  1.00199.99           O  
ATOM   6593  N   PHE A 861     191.450 163.265 194.185  1.00184.68           N  
ATOM   6594  CA  PHE A 861     191.037 162.459 193.040  1.00184.68           C  
ATOM   6595  C   PHE A 861     189.802 163.030 192.357  1.00184.68           C  
ATOM   6596  O   PHE A 861     189.653 162.898 191.136  1.00184.68           O  
ATOM   6597  CB  PHE A 861     190.783 161.018 193.482  1.00184.68           C  
ATOM   6598  CG  PHE A 861     190.315 160.116 192.376  1.00184.68           C  
ATOM   6599  CD1 PHE A 861     191.205 159.644 191.426  1.00184.68           C  
ATOM   6600  CD2 PHE A 861     188.985 159.738 192.288  1.00184.68           C  
ATOM   6601  CE1 PHE A 861     190.779 158.814 190.407  1.00184.68           C  
ATOM   6602  CE2 PHE A 861     188.552 158.908 191.271  1.00184.68           C  
ATOM   6603  CZ  PHE A 861     189.450 158.446 190.330  1.00184.68           C  
ATOM   6604  N   LEU A 862     188.910 163.668 193.117  1.00200.62           N  
ATOM   6605  CA  LEU A 862     187.703 164.228 192.520  1.00200.62           C  
ATOM   6606  C   LEU A 862     188.000 165.492 191.724  1.00200.62           C  
ATOM   6607  O   LEU A 862     187.341 165.751 190.710  1.00200.62           O  
ATOM   6608  CB  LEU A 862     186.663 164.506 193.607  1.00200.62           C  
ATOM   6609  CG  LEU A 862     185.233 164.847 193.178  1.00200.62           C  
ATOM   6610  CD1 LEU A 862     184.242 164.279 194.178  1.00200.62           C  
ATOM   6611  CD2 LEU A 862     185.036 166.351 193.044  1.00200.62           C  
ATOM   6612  N   PHE A 863     188.979 166.289 192.158  1.00224.06           N  
ATOM   6613  CA  PHE A 863     189.237 167.560 191.489  1.00224.06           C  
ATOM   6614  C   PHE A 863     189.905 167.357 190.136  1.00224.06           C  
ATOM   6615  O   PHE A 863     189.756 168.197 189.241  1.00224.06           O  
ATOM   6616  CB  PHE A 863     190.100 168.456 192.377  1.00224.06           C  
ATOM   6617  CG  PHE A 863     189.435 168.855 193.663  1.00224.06           C  
ATOM   6618  CD1 PHE A 863     188.402 169.777 193.667  1.00224.06           C  
ATOM   6619  CD2 PHE A 863     189.844 168.309 194.868  1.00224.06           C  
ATOM   6620  CE1 PHE A 863     187.788 170.146 194.849  1.00224.06           C  
ATOM   6621  CE2 PHE A 863     189.235 168.675 196.053  1.00224.06           C  
ATOM   6622  CZ  PHE A 863     188.206 169.595 196.043  1.00224.06           C  
ATOM   6623  N   HIS A 864     190.642 166.257 189.966  1.00212.42           N  
ATOM   6624  CA  HIS A 864     191.104 165.870 188.638  1.00212.42           C  
ATOM   6625  C   HIS A 864     189.960 165.353 187.776  1.00212.42           C  
ATOM   6626  O   HIS A 864     189.985 165.510 186.551  1.00212.42           O  
ATOM   6627  CB  HIS A 864     192.203 164.813 188.753  1.00212.42           C  
ATOM   6628  CG  HIS A 864     192.907 164.527 187.463  1.00212.42           C  
ATOM   6629  ND1 HIS A 864     193.636 163.376 187.255  1.00212.42           N  
ATOM   6630  CD2 HIS A 864     192.998 165.243 186.318  1.00212.42           C  
ATOM   6631  CE1 HIS A 864     194.143 163.393 186.035  1.00212.42           C  
ATOM   6632  NE2 HIS A 864     193.771 164.515 185.445  1.00212.42           N  
ATOM   6633  N   ALA A 865     188.951 164.741 188.396  1.00208.42           N  
ATOM   6634  CA  ALA A 865     187.821 164.154 187.691  1.00208.42           C  
ATOM   6635  C   ALA A 865     186.712 165.160 187.403  1.00208.42           C  
ATOM   6636  O   ALA A 865     185.565 164.753 187.180  1.00208.42           O  
ATOM   6637  CB  ALA A 865     187.263 162.971 188.485  1.00208.42           C  
ATOM   6638  N   ILE A 866     187.019 166.453 187.399  1.00216.40           N  
ATOM   6639  CA  ILE A 866     186.119 167.477 186.883  1.00216.40           C  
ATOM   6640  C   ILE A 866     186.629 168.055 185.568  1.00216.40           C  
ATOM   6641  O   ILE A 866     185.876 168.181 184.601  1.00216.40           O  
ATOM   6642  CB  ILE A 866     185.900 168.596 187.925  1.00216.40           C  
ATOM   6643  CG1 ILE A 866     185.506 168.006 189.279  1.00216.40           C  
ATOM   6644  CG2 ILE A 866     184.832 169.563 187.445  1.00216.40           C  
ATOM   6645  CD1 ILE A 866     184.235 167.205 189.244  1.00216.40           C  
ATOM   6646  N   SER A 867     187.914 168.414 185.515  1.00229.80           N  
ATOM   6647  CA  SER A 867     188.511 168.851 184.257  1.00229.80           C  
ATOM   6648  C   SER A 867     188.572 167.724 183.233  1.00229.80           C  
ATOM   6649  O   SER A 867     188.501 167.983 182.026  1.00229.80           O  
ATOM   6650  CB  SER A 867     189.909 169.415 184.509  1.00229.80           C  
ATOM   6651  OG  SER A 867     190.526 169.808 183.295  1.00229.80           O  
ATOM   6652  N   GLY A 868     188.705 166.476 183.688  1.00229.30           N  
ATOM   6653  CA  GLY A 868     188.611 165.350 182.775  1.00229.30           C  
ATOM   6654  C   GLY A 868     187.232 165.150 182.180  1.00229.30           C  
ATOM   6655  O   GLY A 868     187.103 164.605 181.079  1.00229.30           O  
ATOM   6656  N   ARG A 869     186.186 165.580 182.887  1.00231.88           N  
ATOM   6657  CA  ARG A 869     184.862 165.637 182.275  1.00231.88           C  
ATOM   6658  C   ARG A 869     184.774 166.763 181.252  1.00231.88           C  
ATOM   6659  O   ARG A 869     184.142 166.606 180.200  1.00231.88           O  
ATOM   6660  CB  ARG A 869     183.795 165.807 183.357  1.00231.88           C  
ATOM   6661  CG  ARG A 869     182.375 165.926 182.826  1.00231.88           C  
ATOM   6662  CD  ARG A 869     181.989 164.712 181.996  1.00231.88           C  
ATOM   6663  NE  ARG A 869     182.201 163.464 182.723  1.00231.88           N  
ATOM   6664  CZ  ARG A 869     181.323 162.932 183.567  1.00231.88           C  
ATOM   6665  NH1 ARG A 869     180.166 163.540 183.794  1.00231.88           N  
ATOM   6666  NH2 ARG A 869     181.601 161.793 184.186  1.00231.88           N  
ATOM   6667  N   GLU A 870     185.400 167.906 181.545  1.00234.66           N  
ATOM   6668  CA  GLU A 870     185.367 169.036 180.621  1.00234.66           C  
ATOM   6669  C   GLU A 870     186.080 168.724 179.311  1.00234.66           C  
ATOM   6670  O   GLU A 870     185.731 169.288 178.268  1.00234.66           O  
ATOM   6671  CB  GLU A 870     185.986 170.266 181.288  1.00234.66           C  
ATOM   6672  CG  GLU A 870     185.708 171.584 180.579  1.00234.66           C  
ATOM   6673  CD  GLU A 870     186.731 171.902 179.505  1.00234.66           C  
ATOM   6674  OE1 GLU A 870     187.899 171.489 179.655  1.00234.66           O  
ATOM   6675  OE2 GLU A 870     186.365 172.567 178.513  1.00234.66           O  
ATOM   6676  N   GLY A 871     187.068 167.826 179.336  1.00238.86           N  
ATOM   6677  CA  GLY A 871     187.755 167.447 178.113  1.00238.86           C  
ATOM   6678  C   GLY A 871     186.909 166.663 177.132  1.00238.86           C  
ATOM   6679  O   GLY A 871     187.276 166.567 175.956  1.00238.86           O  
ATOM   6680  N   LEU A 872     185.787 166.101 177.581  1.00238.59           N  
ATOM   6681  CA  LEU A 872     184.876 165.399 176.687  1.00238.59           C  
ATOM   6682  C   LEU A 872     183.630 166.201 176.340  1.00238.59           C  
ATOM   6683  O   LEU A 872     183.031 165.958 175.287  1.00238.59           O  
ATOM   6684  CB  LEU A 872     184.450 164.057 177.301  1.00238.59           C  
ATOM   6685  CG  LEU A 872     185.407 162.869 177.160  1.00238.59           C  
ATOM   6686  CD1 LEU A 872     186.623 163.014 178.065  1.00238.59           C  
ATOM   6687  CD2 LEU A 872     184.680 161.562 177.441  1.00238.59           C  
ATOM   6688  N   VAL A 873     183.228 167.144 177.195  1.00237.51           N  
ATOM   6689  CA  VAL A 873     182.037 167.940 176.915  1.00237.51           C  
ATOM   6690  C   VAL A 873     182.298 168.930 175.786  1.00237.51           C  
ATOM   6691  O   VAL A 873     181.465 169.100 174.887  1.00237.51           O  
ATOM   6692  CB  VAL A 873     181.569 168.654 178.196  1.00237.51           C  
ATOM   6693  CG1 VAL A 873     180.481 169.669 177.878  1.00237.51           C  
ATOM   6694  CG2 VAL A 873     181.087 167.640 179.223  1.00237.51           C  
ATOM   6695  N   ASP A 874     183.457 169.593 175.808  1.00238.56           N  
ATOM   6696  CA  ASP A 874     183.688 170.726 174.918  1.00238.56           C  
ATOM   6697  C   ASP A 874     183.769 170.328 173.449  1.00238.56           C  
ATOM   6698  O   ASP A 874     183.634 171.198 172.581  1.00238.56           O  
ATOM   6699  CB  ASP A 874     184.970 171.457 175.324  1.00238.56           C  
ATOM   6700  CG  ASP A 874     186.167 170.530 175.418  1.00238.56           C  
ATOM   6701  OD1 ASP A 874     185.990 169.304 175.256  1.00238.56           O  
ATOM   6702  OD2 ASP A 874     187.288 171.029 175.653  1.00238.56           O  
ATOM   6703  N   THR A 875     183.985 169.046 173.146  1.00229.48           N  
ATOM   6704  CA  THR A 875     183.928 168.612 171.754  1.00229.48           C  
ATOM   6705  C   THR A 875     182.502 168.608 171.216  1.00229.48           C  
ATOM   6706  O   THR A 875     182.300 168.734 170.003  1.00229.48           O  
ATOM   6707  CB  THR A 875     184.547 167.222 171.608  1.00229.48           C  
ATOM   6708  OG1 THR A 875     183.799 166.279 172.386  1.00229.48           O  
ATOM   6709  CG2 THR A 875     185.993 167.231 172.085  1.00229.48           C  
ATOM   6710  N   ALA A 876     181.508 168.469 172.092  1.00228.54           N  
ATOM   6711  CA  ALA A 876     180.122 168.356 171.656  1.00228.54           C  
ATOM   6712  C   ALA A 876     179.502 169.688 171.255  1.00228.54           C  
ATOM   6713  O   ALA A 876     178.423 169.690 170.653  1.00228.54           O  
ATOM   6714  CB  ALA A 876     179.276 167.712 172.757  1.00228.54           C  
ATOM   6715  N   VAL A 877     180.146 170.811 171.567  1.00218.98           N  
ATOM   6716  CA  VAL A 877     179.556 172.121 171.318  1.00218.98           C  
ATOM   6717  C   VAL A 877     180.202 172.790 170.110  1.00218.98           C  
ATOM   6718  O   VAL A 877     179.574 173.614 169.436  1.00218.98           O  
ATOM   6719  CB  VAL A 877     179.660 173.015 172.571  1.00218.98           C  
ATOM   6720  CG1 VAL A 877     181.109 173.387 172.857  1.00218.98           C  
ATOM   6721  CG2 VAL A 877     178.792 174.259 172.423  1.00218.98           C  
ATOM   6722  N   LYS A 878     181.452 172.435 169.813  1.00210.74           N  
ATOM   6723  CA  LYS A 878     182.162 173.042 168.693  1.00210.74           C  
ATOM   6724  C   LYS A 878     182.107 172.216 167.415  1.00210.74           C  
ATOM   6725  O   LYS A 878     181.996 172.787 166.325  1.00210.74           O  
ATOM   6726  CB  LYS A 878     183.627 173.287 169.073  1.00210.74           C  
ATOM   6727  CG  LYS A 878     184.423 174.060 168.034  1.00210.74           C  
ATOM   6728  CD  LYS A 878     185.878 174.204 168.449  1.00210.74           C  
ATOM   6729  CE  LYS A 878     186.045 175.266 169.524  1.00210.74           C  
ATOM   6730  NZ  LYS A 878     187.478 175.515 169.841  1.00210.74           N  
ATOM   6731  N   THR A 879     182.181 170.886 167.513  1.00208.29           N  
ATOM   6732  CA  THR A 879     182.187 170.067 166.305  1.00208.29           C  
ATOM   6733  C   THR A 879     180.858 170.140 165.562  1.00208.29           C  
ATOM   6734  O   THR A 879     180.821 169.949 164.341  1.00208.29           O  
ATOM   6735  CB  THR A 879     182.518 168.615 166.651  1.00208.29           C  
ATOM   6736  OG1 THR A 879     181.590 168.130 167.630  1.00208.29           O  
ATOM   6737  CG2 THR A 879     183.934 168.507 167.198  1.00208.29           C  
ATOM   6738  N   ALA A 880     179.763 170.412 166.274  1.00196.43           N  
ATOM   6739  CA  ALA A 880     178.468 170.578 165.625  1.00196.43           C  
ATOM   6740  C   ALA A 880     178.340 171.930 164.933  1.00196.43           C  
ATOM   6741  O   ALA A 880     177.774 172.018 163.838  1.00196.43           O  
ATOM   6742  CB  ALA A 880     177.344 170.396 166.646  1.00196.43           C  
ATOM   6743  N   GLU A 881     178.857 172.992 165.554  1.00180.32           N  
ATOM   6744  CA  GLU A 881     178.711 174.331 164.992  1.00180.32           C  
ATOM   6745  C   GLU A 881     179.726 174.616 163.890  1.00180.32           C  
ATOM   6746  O   GLU A 881     179.394 175.278 162.901  1.00180.32           O  
ATOM   6747  CB  GLU A 881     178.828 175.378 166.102  1.00180.32           C  
ATOM   6748  CG  GLU A 881     178.536 176.799 165.648  1.00180.32           C  
ATOM   6749  CD  GLU A 881     178.605 177.800 166.784  1.00180.32           C  
ATOM   6750  OE1 GLU A 881     178.900 177.388 167.925  1.00180.32           O  
ATOM   6751  OE2 GLU A 881     178.365 179.001 166.536  1.00180.32           O  
ATOM   6752  N   THR A 882     180.961 174.130 164.036  1.00179.71           N  
ATOM   6753  CA  THR A 882     182.013 174.493 163.089  1.00179.71           C  
ATOM   6754  C   THR A 882     181.747 173.905 161.708  1.00179.71           C  
ATOM   6755  O   THR A 882     181.859 174.603 160.693  1.00179.71           O  
ATOM   6756  CB  THR A 882     183.374 174.035 163.616  1.00179.71           C  
ATOM   6757  OG1 THR A 882     183.636 174.663 164.877  1.00179.71           O  
ATOM   6758  CG2 THR A 882     184.477 174.404 162.635  1.00179.71           C  
ATOM   6759  N   GLY A 883     181.393 172.620 161.648  1.00167.43           N  
ATOM   6760  CA  GLY A 883     180.937 172.041 160.395  1.00167.43           C  
ATOM   6761  C   GLY A 883     179.665 172.669 159.861  1.00167.43           C  
ATOM   6762  O   GLY A 883     179.447 172.704 158.647  1.00167.43           O  
ATOM   6763  N   TYR A 884     178.810 173.171 160.753  1.00162.30           N  
ATOM   6764  CA  TYR A 884     177.662 173.971 160.338  1.00162.30           C  
ATOM   6765  C   TYR A 884     178.055 175.391 159.941  1.00162.30           C  
ATOM   6766  O   TYR A 884     177.502 175.942 158.982  1.00162.30           O  
ATOM   6767  CB  TYR A 884     176.620 174.006 161.457  1.00162.30           C  
ATOM   6768  CG  TYR A 884     175.432 174.892 161.162  1.00162.30           C  
ATOM   6769  CD1 TYR A 884     174.500 174.537 160.195  1.00162.30           C  
ATOM   6770  CD2 TYR A 884     175.240 176.081 161.852  1.00162.30           C  
ATOM   6771  CE1 TYR A 884     173.412 175.345 159.921  1.00162.30           C  
ATOM   6772  CE2 TYR A 884     174.155 176.894 161.586  1.00162.30           C  
ATOM   6773  CZ  TYR A 884     173.245 176.521 160.620  1.00162.30           C  
ATOM   6774  OH  TYR A 884     172.162 177.327 160.354  1.00162.30           O  
ATOM   6775  N   MET A 885     179.001 176.001 160.659  1.00154.70           N  
ATOM   6776  CA  MET A 885     179.444 177.344 160.295  1.00154.70           C  
ATOM   6777  C   MET A 885     180.262 177.339 159.009  1.00154.70           C  
ATOM   6778  O   MET A 885     180.146 178.260 158.193  1.00154.70           O  
ATOM   6779  CB  MET A 885     180.247 177.959 161.443  1.00154.70           C  
ATOM   6780  CG  MET A 885     180.738 179.375 161.183  1.00154.70           C  
ATOM   6781  SD  MET A 885     182.429 179.430 160.560  1.00154.70           S  
ATOM   6782  CE  MET A 885     183.350 179.052 162.049  1.00154.70           C  
ATOM   6783  N   SER A 886     181.088 176.315 158.804  1.00136.17           N  
ATOM   6784  CA  SER A 886     181.840 176.207 157.559  1.00136.17           C  
ATOM   6785  C   SER A 886     180.994 175.706 156.395  1.00136.17           C  
ATOM   6786  O   SER A 886     181.495 175.653 155.267  1.00136.17           O  
ATOM   6787  CB  SER A 886     183.046 175.283 157.752  1.00136.17           C  
ATOM   6788  OG  SER A 886     183.775 175.136 156.546  1.00136.17           O  
ATOM   6789  N   ARG A 887     179.735 175.340 156.637  1.00132.52           N  
ATOM   6790  CA  ARG A 887     178.775 175.124 155.562  1.00132.52           C  
ATOM   6791  C   ARG A 887     177.954 176.369 155.255  1.00132.52           C  
ATOM   6792  O   ARG A 887     177.550 176.567 154.103  1.00132.52           O  
ATOM   6793  CB  ARG A 887     177.852 173.951 155.917  1.00132.52           C  
ATOM   6794  CG  ARG A 887     177.038 173.384 154.754  1.00132.52           C  
ATOM   6795  CD  ARG A 887     175.676 174.050 154.612  1.00132.52           C  
ATOM   6796  NE  ARG A 887     174.926 174.033 155.865  1.00132.52           N  
ATOM   6797  CZ  ARG A 887     174.160 173.022 156.262  1.00132.52           C  
ATOM   6798  NH1 ARG A 887     173.513 173.091 157.417  1.00132.52           N  
ATOM   6799  NH2 ARG A 887     174.040 171.941 155.503  1.00132.52           N  
ATOM   6800  N   ARG A 888     177.705 177.212 156.260  1.00133.00           N  
ATOM   6801  CA  ARG A 888     176.865 178.392 156.071  1.00133.00           C  
ATOM   6802  C   ARG A 888     177.477 179.355 155.059  1.00133.00           C  
ATOM   6803  O   ARG A 888     176.850 179.700 154.051  1.00133.00           O  
ATOM   6804  CB  ARG A 888     176.640 179.092 157.412  1.00133.00           C  
ATOM   6805  CG  ARG A 888     175.921 180.426 157.298  1.00133.00           C  
ATOM   6806  CD  ARG A 888     175.723 181.072 158.660  1.00133.00           C  
ATOM   6807  NE  ARG A 888     174.676 180.413 159.435  1.00133.00           N  
ATOM   6808  CZ  ARG A 888     174.381 180.711 160.696  1.00133.00           C  
ATOM   6809  NH1 ARG A 888     175.057 181.659 161.331  1.00133.00           N  
ATOM   6810  NH2 ARG A 888     173.412 180.060 161.324  1.00133.00           N  
ATOM   6811  N   LEU A 889     178.708 179.803 155.313  1.00123.93           N  
ATOM   6812  CA  LEU A 889     179.354 180.737 154.398  1.00123.93           C  
ATOM   6813  C   LEU A 889     179.819 180.062 153.114  1.00123.93           C  
ATOM   6814  O   LEU A 889     180.059 180.754 152.119  1.00123.93           O  
ATOM   6815  CB  LEU A 889     180.529 181.426 155.098  1.00123.93           C  
ATOM   6816  CG  LEU A 889     181.681 180.567 155.630  1.00123.93           C  
ATOM   6817  CD1 LEU A 889     182.805 180.444 154.611  1.00123.93           C  
ATOM   6818  CD2 LEU A 889     182.205 181.130 156.943  1.00123.93           C  
ATOM   6819  N   MET A 890     179.958 178.735 153.117  1.00121.70           N  
ATOM   6820  CA  MET A 890     180.266 178.019 151.883  1.00121.70           C  
ATOM   6821  C   MET A 890     179.150 178.190 150.858  1.00121.70           C  
ATOM   6822  O   MET A 890     179.410 178.278 149.652  1.00121.70           O  
ATOM   6823  CB  MET A 890     180.497 176.538 152.189  1.00121.70           C  
ATOM   6824  CG  MET A 890     180.779 175.665 150.976  1.00121.70           C  
ATOM   6825  SD  MET A 890     182.246 176.178 150.063  1.00121.70           S  
ATOM   6826  CE  MET A 890     181.892 175.503 148.443  1.00121.70           C  
ATOM   6827  N   LYS A 891     177.900 178.242 151.324  1.00127.57           N  
ATOM   6828  CA  LYS A 891     176.761 178.382 150.421  1.00127.57           C  
ATOM   6829  C   LYS A 891     176.746 179.742 149.731  1.00127.57           C  
ATOM   6830  O   LYS A 891     176.439 179.834 148.537  1.00127.57           O  
ATOM   6831  CB  LYS A 891     175.458 178.158 151.188  1.00127.57           C  
ATOM   6832  CG  LYS A 891     174.214 178.170 150.315  1.00127.57           C  
ATOM   6833  CD  LYS A 891     174.191 176.979 149.371  1.00127.57           C  
ATOM   6834  CE  LYS A 891     174.030 175.674 150.134  1.00127.57           C  
ATOM   6835  NZ  LYS A 891     172.687 175.565 150.767  1.00127.57           N  
ATOM   6836  N   SER A 892     177.075 180.807 150.460  1.00122.53           N  
ATOM   6837  CA  SER A 892     177.023 182.159 149.916  1.00122.53           C  
ATOM   6838  C   SER A 892     178.212 182.501 149.027  1.00122.53           C  
ATOM   6839  O   SER A 892     178.235 183.593 148.449  1.00122.53           O  
ATOM   6840  CB  SER A 892     176.928 183.179 151.053  1.00122.53           C  
ATOM   6841  OG  SER A 892     176.964 184.504 150.553  1.00122.53           O  
ATOM   6842  N   LEU A 893     179.193 181.606 148.899  1.00108.44           N  
ATOM   6843  CA  LEU A 893     180.502 181.991 148.387  1.00108.44           C  
ATOM   6844  C   LEU A 893     181.065 180.913 147.465  1.00108.44           C  
ATOM   6845  O   LEU A 893     182.238 180.991 147.080  1.00108.44           O  
ATOM   6846  CB  LEU A 893     181.448 182.275 149.571  1.00108.44           C  
ATOM   6847  CG  LEU A 893     182.668 183.200 149.490  1.00108.44           C  
ATOM   6848  CD1 LEU A 893     182.867 183.864 150.840  1.00108.44           C  
ATOM   6849  CD2 LEU A 893     183.932 182.459 149.119  1.00108.44           C  
ATOM   6850  N   GLU A 894     180.250 179.930 147.077  1.00122.55           N  
ATOM   6851  CA  GLU A 894     180.742 178.709 146.448  1.00122.55           C  
ATOM   6852  C   GLU A 894     181.170 178.907 145.000  1.00122.55           C  
ATOM   6853  O   GLU A 894     181.912 178.072 144.471  1.00122.55           O  
ATOM   6854  CB  GLU A 894     179.670 177.621 146.515  1.00122.55           C  
ATOM   6855  CG  GLU A 894     178.410 177.947 145.732  1.00122.55           C  
ATOM   6856  CD  GLU A 894     177.297 176.951 145.979  1.00122.55           C  
ATOM   6857  OE1 GLU A 894     177.476 176.055 146.831  1.00122.55           O  
ATOM   6858  OE2 GLU A 894     176.241 177.064 145.322  1.00122.55           O  
ATOM   6859  N   ASP A 895     180.731 179.980 144.345  1.00115.62           N  
ATOM   6860  CA  ASP A 895     180.970 180.176 142.915  1.00115.62           C  
ATOM   6861  C   ASP A 895     181.676 181.507 142.676  1.00115.62           C  
ATOM   6862  O   ASP A 895     181.046 182.524 142.377  1.00115.62           O  
ATOM   6863  CB  ASP A 895     179.638 180.092 142.141  1.00115.62           C  
ATOM   6864  CG  ASP A 895     178.530 180.896 142.797  1.00115.62           C  
ATOM   6865  OD1 ASP A 895     178.761 181.445 143.895  1.00115.62           O  
ATOM   6866  OD2 ASP A 895     177.429 180.981 142.213  1.00115.62           O  
ATOM   6867  N   LEU A 896     183.001 181.489 142.807  1.00103.53           N  
ATOM   6868  CA  LEU A 896     183.850 182.622 142.444  1.00103.53           C  
ATOM   6869  C   LEU A 896     185.104 182.056 141.795  1.00103.53           C  
ATOM   6870  O   LEU A 896     185.937 181.452 142.479  1.00103.53           O  
ATOM   6871  CB  LEU A 896     184.203 183.475 143.663  1.00103.53           C  
ATOM   6872  CG  LEU A 896     183.077 184.245 144.356  1.00103.53           C  
ATOM   6873  CD1 LEU A 896     183.591 184.912 145.622  1.00103.53           C  
ATOM   6874  CD2 LEU A 896     182.475 185.275 143.416  1.00103.53           C  
ATOM   6875  N   SER A 897     185.243 182.244 140.485  1.00110.95           N  
ATOM   6876  CA  SER A 897     186.353 181.678 139.735  1.00110.95           C  
ATOM   6877  C   SER A 897     187.114 182.776 139.007  1.00110.95           C  
ATOM   6878  O   SER A 897     186.559 183.828 138.675  1.00110.95           O  
ATOM   6879  CB  SER A 897     185.866 180.631 138.726  1.00110.95           C  
ATOM   6880  OG  SER A 897     185.119 181.236 137.684  1.00110.95           O  
ATOM   6881  N   CYS A 898     188.395 182.518 138.761  1.00107.24           N  
ATOM   6882  CA  CYS A 898     189.270 183.470 138.090  1.00107.24           C  
ATOM   6883  C   CYS A 898     189.173 183.281 136.581  1.00107.24           C  
ATOM   6884  O   CYS A 898     189.389 182.175 136.073  1.00107.24           O  
ATOM   6885  CB  CYS A 898     190.711 183.298 138.567  1.00107.24           C  
ATOM   6886  SG  CYS A 898     190.932 183.615 140.330  1.00107.24           S  
ATOM   6887  N   GLN A 899     188.851 184.357 135.869  1.00103.54           N  
ATOM   6888  CA  GLN A 899     188.836 184.328 134.416  1.00103.54           C  
ATOM   6889  C   GLN A 899     190.239 184.584 133.869  1.00103.54           C  
ATOM   6890  O   GLN A 899     191.172 184.922 134.602  1.00103.54           O  
ATOM   6891  CB  GLN A 899     187.845 185.354 133.869  1.00103.54           C  
ATOM   6892  CG  GLN A 899     186.417 185.141 134.339  1.00103.54           C  
ATOM   6893  CD  GLN A 899     185.850 183.810 133.887  1.00103.54           C  
ATOM   6894  OE1 GLN A 899     186.064 183.384 132.752  1.00103.54           O  
ATOM   6895  NE2 GLN A 899     185.124 183.143 134.777  1.00103.54           N  
ATOM   6896  N   TYR A 900     190.385 184.416 132.553  1.00 93.13           N  
ATOM   6897  CA  TYR A 900     191.709 184.470 131.944  1.00 93.13           C  
ATOM   6898  C   TYR A 900     192.269 185.883 131.856  1.00 93.13           C  
ATOM   6899  O   TYR A 900     193.410 186.049 131.409  1.00 93.13           O  
ATOM   6900  CB  TYR A 900     191.668 183.840 130.549  1.00 93.13           C  
ATOM   6901  CG  TYR A 900     191.476 182.341 130.563  1.00 93.13           C  
ATOM   6902  CD1 TYR A 900     192.559 181.485 130.721  1.00 93.13           C  
ATOM   6903  CD2 TYR A 900     190.214 181.780 130.420  1.00 93.13           C  
ATOM   6904  CE1 TYR A 900     192.391 180.113 130.733  1.00 93.13           C  
ATOM   6905  CE2 TYR A 900     190.035 180.409 130.432  1.00 93.13           C  
ATOM   6906  CZ  TYR A 900     191.127 179.581 130.589  1.00 93.13           C  
ATOM   6907  OH  TYR A 900     190.954 178.216 130.604  1.00 93.13           O  
ATOM   6908  N   ASP A 901     191.507 186.897 132.265  1.00 99.46           N  
ATOM   6909  CA  ASP A 901     191.997 188.264 132.363  1.00 99.46           C  
ATOM   6910  C   ASP A 901     192.602 188.565 133.731  1.00 99.46           C  
ATOM   6911  O   ASP A 901     192.784 189.739 134.075  1.00 99.46           O  
ATOM   6912  CB  ASP A 901     190.873 189.254 132.046  1.00 99.46           C  
ATOM   6913  CG  ASP A 901     189.631 189.015 132.882  1.00 99.46           C  
ATOM   6914  OD1 ASP A 901     189.612 188.034 133.654  1.00 99.46           O  
ATOM   6915  OD2 ASP A 901     188.675 189.810 132.769  1.00 99.46           O  
ATOM   6916  N   ASN A 902     192.913 187.526 134.508  1.00100.70           N  
ATOM   6917  CA  ASN A 902     193.347 187.656 135.900  1.00100.70           C  
ATOM   6918  C   ASN A 902     192.348 188.466 136.723  1.00100.70           C  
ATOM   6919  O   ASN A 902     192.719 189.301 137.551  1.00100.70           O  
ATOM   6920  CB  ASN A 902     194.748 188.268 135.985  1.00100.70           C  
ATOM   6921  CG  ASN A 902     195.830 187.310 135.526  1.00100.70           C  
ATOM   6922  OD1 ASN A 902     195.809 186.125 135.862  1.00100.70           O  
ATOM   6923  ND2 ASN A 902     196.782 187.819 134.754  1.00100.70           N  
ATOM   6924  N   THR A 903     191.061 188.212 136.492  1.00 98.74           N  
ATOM   6925  CA  THR A 903     189.981 188.916 137.172  1.00 98.74           C  
ATOM   6926  C   THR A 903     188.980 187.889 137.677  1.00 98.74           C  
ATOM   6927  O   THR A 903     188.378 187.164 136.879  1.00 98.74           O  
ATOM   6928  CB  THR A 903     189.295 189.925 136.245  1.00 98.74           C  
ATOM   6929  OG1 THR A 903     190.247 190.907 135.816  1.00 98.74           O  
ATOM   6930  CG2 THR A 903     188.150 190.617 136.966  1.00 98.74           C  
ATOM   6931  N   VAL A 904     188.803 187.827 138.993  1.00 98.42           N  
ATOM   6932  CA  VAL A 904     187.817 186.931 139.584  1.00 98.42           C  
ATOM   6933  C   VAL A 904     186.442 187.583 139.514  1.00 98.42           C  
ATOM   6934  O   VAL A 904     186.296 188.795 139.718  1.00 98.42           O  
ATOM   6935  CB  VAL A 904     188.208 186.569 141.030  1.00 98.42           C  
ATOM   6936  CG1 VAL A 904     188.245 187.807 141.913  1.00 98.42           C  
ATOM   6937  CG2 VAL A 904     187.257 185.524 141.600  1.00 98.42           C  
ATOM   6938  N   ARG A 905     185.428 186.781 139.196  1.00104.71           N  
ATOM   6939  CA  ARG A 905     184.071 187.285 139.056  1.00104.71           C  
ATOM   6940  C   ARG A 905     183.087 186.158 139.332  1.00104.71           C  
ATOM   6941  O   ARG A 905     183.427 184.975 139.252  1.00104.71           O  
ATOM   6942  CB  ARG A 905     183.836 187.890 137.666  1.00104.71           C  
ATOM   6943  CG  ARG A 905     183.981 186.908 136.520  1.00104.71           C  
ATOM   6944  CD  ARG A 905     183.853 187.624 135.188  1.00104.71           C  
ATOM   6945  NE  ARG A 905     184.997 188.492 134.923  1.00104.71           N  
ATOM   6946  CZ  ARG A 905     185.053 189.372 133.929  1.00104.71           C  
ATOM   6947  NH1 ARG A 905     184.019 189.521 133.112  1.00104.71           N  
ATOM   6948  NH2 ARG A 905     186.137 190.119 133.762  1.00104.71           N  
ATOM   6949  N   THR A 906     181.857 186.545 139.661  1.00112.28           N  
ATOM   6950  CA  THR A 906     180.843 185.590 140.080  1.00112.28           C  
ATOM   6951  C   THR A 906     180.320 184.802 138.878  1.00112.28           C  
ATOM   6952  O   THR A 906     180.733 185.002 137.732  1.00112.28           O  
ATOM   6953  CB  THR A 906     179.702 186.307 140.798  1.00112.28           C  
ATOM   6954  OG1 THR A 906     178.769 185.341 141.300  1.00112.28           O  
ATOM   6955  CG2 THR A 906     178.983 187.251 139.846  1.00112.28           C  
ATOM   6956  N   SER A 907     179.393 183.884 139.160  1.00118.26           N  
ATOM   6957  CA  SER A 907     178.809 183.055 138.110  1.00118.26           C  
ATOM   6958  C   SER A 907     177.976 183.871 137.130  1.00118.26           C  
ATOM   6959  O   SER A 907     177.868 183.500 135.956  1.00118.26           O  
ATOM   6960  CB  SER A 907     177.958 181.946 138.731  1.00118.26           C  
ATOM   6961  OG  SER A 907     176.813 182.480 139.372  1.00118.26           O  
ATOM   6962  N   ALA A 908     177.383 184.976 137.582  1.00120.23           N  
ATOM   6963  CA  ALA A 908     176.622 185.859 136.710  1.00120.23           C  
ATOM   6964  C   ALA A 908     177.485 186.936 136.061  1.00120.23           C  
ATOM   6965  O   ALA A 908     176.965 187.999 135.701  1.00120.23           O  
ATOM   6966  CB  ALA A 908     175.473 186.506 137.487  1.00120.23           C  
ATOM   6967  N   ASN A 909     178.788 186.685 135.917  1.00113.64           N  
ATOM   6968  CA  ASN A 909     179.691 187.534 135.140  1.00113.64           C  
ATOM   6969  C   ASN A 909     179.798 188.940 135.726  1.00113.64           C  
ATOM   6970  O   ASN A 909     179.952 189.920 134.994  1.00113.64           O  
ATOM   6971  CB  ASN A 909     179.258 187.596 133.670  1.00113.64           C  
ATOM   6972  CG  ASN A 909     180.389 187.989 132.738  1.00113.64           C  
ATOM   6973  OD1 ASN A 909     181.493 188.301 133.180  1.00113.64           O  
ATOM   6974  ND2 ASN A 909     180.115 187.975 131.439  1.00113.64           N  
ATOM   6975  N   GLY A 910     179.716 189.054 137.046  1.00111.32           N  
ATOM   6976  CA  GLY A 910     179.801 190.338 137.728  1.00111.32           C  
ATOM   6977  C   GLY A 910     181.076 190.446 138.546  1.00111.32           C  
ATOM   6978  O   GLY A 910     181.469 189.496 139.228  1.00111.32           O  
ATOM   6979  N   ILE A 911     181.716 191.613 138.470  1.00107.95           N  
ATOM   6980  CA  ILE A 911     183.024 191.801 139.084  1.00107.95           C  
ATOM   6981  C   ILE A 911     182.863 191.861 140.597  1.00107.95           C  
ATOM   6982  O   ILE A 911     181.963 192.537 141.112  1.00107.95           O  
ATOM   6983  CB  ILE A 911     183.696 193.072 138.542  1.00107.95           C  
ATOM   6984  CG1 ILE A 911     183.799 193.011 137.017  1.00107.95           C  
ATOM   6985  CG2 ILE A 911     185.073 193.259 139.163  1.00107.95           C  
ATOM   6986  CD1 ILE A 911     184.637 191.861 136.506  1.00107.95           C  
ATOM   6987  N   VAL A 912     183.720 191.142 141.319  1.00105.99           N  
ATOM   6988  CA  VAL A 912     183.810 191.256 142.774  1.00105.99           C  
ATOM   6989  C   VAL A 912     185.058 192.031 143.189  1.00105.99           C  
ATOM   6990  O   VAL A 912     184.966 193.050 143.875  1.00105.99           O  
ATOM   6991  CB  VAL A 912     183.765 189.865 143.445  1.00105.99           C  
ATOM   6992  CG1 VAL A 912     183.918 189.999 144.953  1.00105.99           C  
ATOM   6993  CG2 VAL A 912     182.470 189.148 143.095  1.00105.99           C  
ATOM   6994  N   GLN A 913     186.235 191.562 142.780  1.00103.54           N  
ATOM   6995  CA  GLN A 913     187.460 192.342 142.871  1.00103.54           C  
ATOM   6996  C   GLN A 913     188.288 192.107 141.616  1.00103.54           C  
ATOM   6997  O   GLN A 913     188.199 191.049 140.987  1.00103.54           O  
ATOM   6998  CB  GLN A 913     188.271 191.995 144.129  1.00103.54           C  
ATOM   6999  CG  GLN A 913     188.754 190.558 144.198  1.00103.54           C  
ATOM   7000  CD  GLN A 913     189.624 190.297 145.412  1.00103.54           C  
ATOM   7001  OE1 GLN A 913     190.001 191.223 146.131  1.00103.54           O  
ATOM   7002  NE2 GLN A 913     189.945 189.030 145.648  1.00103.54           N  
ATOM   7003  N   PHE A 914     189.094 193.106 141.252  1.00 99.82           N  
ATOM   7004  CA  PHE A 914     189.794 193.046 139.974  1.00 99.82           C  
ATOM   7005  C   PHE A 914     190.968 192.076 140.022  1.00 99.82           C  
ATOM   7006  O   PHE A 914     191.161 191.286 139.091  1.00 99.82           O  
ATOM   7007  CB  PHE A 914     190.268 194.442 139.569  1.00 99.82           C  
ATOM   7008  CG  PHE A 914     189.149 195.394 139.257  1.00 99.82           C  
ATOM   7009  CD1 PHE A 914     188.544 195.389 138.011  1.00 99.82           C  
ATOM   7010  CD2 PHE A 914     188.699 196.291 140.211  1.00 99.82           C  
ATOM   7011  CE1 PHE A 914     187.513 196.263 137.721  1.00 99.82           C  
ATOM   7012  CE2 PHE A 914     187.668 197.167 139.928  1.00 99.82           C  
ATOM   7013  CZ  PHE A 914     187.075 197.153 138.681  1.00 99.82           C  
ATOM   7014  N   THR A 915     191.760 192.121 141.090  1.00104.61           N  
ATOM   7015  CA  THR A 915     192.814 191.149 141.338  1.00104.61           C  
ATOM   7016  C   THR A 915     192.615 190.513 142.707  1.00104.61           C  
ATOM   7017  O   THR A 915     192.113 191.151 143.637  1.00104.61           O  
ATOM   7018  CB  THR A 915     194.205 191.794 141.266  1.00104.61           C  
ATOM   7019  OG1 THR A 915     194.322 192.798 142.283  1.00104.61           O  
ATOM   7020  CG2 THR A 915     194.432 192.430 139.902  1.00104.61           C  
ATOM   7021  N   TYR A 916     193.009 189.246 142.826  1.00102.19           N  
ATOM   7022  CA  TYR A 916     192.930 188.552 144.108  1.00102.19           C  
ATOM   7023  C   TYR A 916     193.982 189.121 145.050  1.00102.19           C  
ATOM   7024  O   TYR A 916     195.185 188.933 144.840  1.00102.19           O  
ATOM   7025  CB  TYR A 916     193.119 187.051 143.920  1.00102.19           C  
ATOM   7026  CG  TYR A 916     193.187 186.290 145.225  1.00102.19           C  
ATOM   7027  CD1 TYR A 916     192.076 186.194 146.053  1.00102.19           C  
ATOM   7028  CD2 TYR A 916     194.361 185.670 145.630  1.00102.19           C  
ATOM   7029  CE1 TYR A 916     192.133 185.506 147.250  1.00102.19           C  
ATOM   7030  CE2 TYR A 916     194.427 184.975 146.824  1.00102.19           C  
ATOM   7031  CZ  TYR A 916     193.311 184.897 147.630  1.00102.19           C  
ATOM   7032  OH  TYR A 916     193.371 184.203 148.816  1.00102.19           O  
ATOM   7033  N   GLY A 917     193.533 189.815 146.093  1.00102.90           N  
ATOM   7034  CA  GLY A 917     194.448 190.585 146.909  1.00102.90           C  
ATOM   7035  C   GLY A 917     194.969 191.793 146.149  1.00102.90           C  
ATOM   7036  O   GLY A 917     194.308 192.337 145.259  1.00102.90           O  
ATOM   7037  N   GLY A 918     196.181 192.222 146.509  1.00115.84           N  
ATOM   7038  CA  GLY A 918     196.762 193.379 145.853  1.00115.84           C  
ATOM   7039  C   GLY A 918     197.390 193.097 144.506  1.00115.84           C  
ATOM   7040  O   GLY A 918     197.573 194.028 143.716  1.00115.84           O  
ATOM   7041  N   ASP A 919     197.723 191.837 144.223  1.00118.19           N  
ATOM   7042  CA  ASP A 919     198.532 191.506 143.055  1.00118.19           C  
ATOM   7043  C   ASP A 919     198.010 190.342 142.225  1.00118.19           C  
ATOM   7044  O   ASP A 919     198.413 190.221 141.061  1.00118.19           O  
ATOM   7045  CB  ASP A 919     199.978 191.201 143.475  1.00118.19           C  
ATOM   7046  CG  ASP A 919     200.058 190.160 144.571  1.00118.19           C  
ATOM   7047  OD1 ASP A 919     198.995 189.768 145.099  1.00118.19           O  
ATOM   7048  OD2 ASP A 919     201.183 189.735 144.908  1.00118.19           O  
ATOM   7049  N   GLY A 920     197.140 189.489 142.762  1.00109.28           N  
ATOM   7050  CA  GLY A 920     196.675 188.340 142.010  1.00109.28           C  
ATOM   7051  C   GLY A 920     197.716 187.251 141.841  1.00109.28           C  
ATOM   7052  O   GLY A 920     198.197 187.022 140.727  1.00109.28           O  
ATOM   7053  N   LEU A 921     198.076 186.571 142.928  1.00107.01           N  
ATOM   7054  CA  LEU A 921     198.973 185.427 142.859  1.00107.01           C  
ATOM   7055  C   LEU A 921     198.420 184.285 143.702  1.00107.01           C  
ATOM   7056  O   LEU A 921     197.583 184.483 144.585  1.00107.01           O  
ATOM   7057  CB  LEU A 921     200.393 185.787 143.328  1.00107.01           C  
ATOM   7058  CG  LEU A 921     200.711 185.676 144.821  1.00107.01           C  
ATOM   7059  CD1 LEU A 921     202.216 185.729 145.044  1.00107.01           C  
ATOM   7060  CD2 LEU A 921     200.010 186.758 145.624  1.00107.01           C  
ATOM   7061  N   ASP A 922     198.902 183.083 143.410  1.00115.05           N  
ATOM   7062  CA  ASP A 922     198.429 181.881 144.092  1.00115.05           C  
ATOM   7063  C   ASP A 922     198.862 181.907 145.552  1.00115.05           C  
ATOM   7064  O   ASP A 922     200.067 181.972 145.830  1.00115.05           O  
ATOM   7065  CB  ASP A 922     198.979 180.641 143.389  1.00115.05           C  
ATOM   7066  CG  ASP A 922     198.313 179.356 143.850  1.00115.05           C  
ATOM   7067  OD1 ASP A 922     197.388 179.422 144.685  1.00115.05           O  
ATOM   7068  OD2 ASP A 922     198.718 178.275 143.373  1.00115.05           O  
ATOM   7069  N   PRO A 923     197.932 181.860 146.511  1.00109.95           N  
ATOM   7070  CA  PRO A 923     198.335 181.903 147.926  1.00109.95           C  
ATOM   7071  C   PRO A 923     199.000 180.630 148.421  1.00109.95           C  
ATOM   7072  O   PRO A 923     199.748 180.691 149.405  1.00109.95           O  
ATOM   7073  CB  PRO A 923     197.011 182.157 148.659  1.00109.95           C  
ATOM   7074  CG  PRO A 923     195.967 181.623 147.735  1.00109.95           C  
ATOM   7075  CD  PRO A 923     196.469 181.923 146.352  1.00109.95           C  
ATOM   7076  N   LEU A 924     198.760 179.483 147.783  1.00110.97           N  
ATOM   7077  CA  LEU A 924     199.395 178.248 148.230  1.00110.97           C  
ATOM   7078  C   LEU A 924     200.828 178.126 147.726  1.00110.97           C  
ATOM   7079  O   LEU A 924     201.665 177.513 148.397  1.00110.97           O  
ATOM   7080  CB  LEU A 924     198.564 177.038 147.791  1.00110.97           C  
ATOM   7081  CG  LEU A 924     198.402 176.732 146.298  1.00110.97           C  
ATOM   7082  CD1 LEU A 924     199.469 175.762 145.799  1.00110.97           C  
ATOM   7083  CD2 LEU A 924     197.009 176.191 146.011  1.00110.97           C  
ATOM   7084  N   GLU A 925     201.127 178.696 146.562  1.00117.46           N  
ATOM   7085  CA  GLU A 925     202.451 178.572 145.952  1.00117.46           C  
ATOM   7086  C   GLU A 925     203.319 179.770 146.346  1.00117.46           C  
ATOM   7087  O   GLU A 925     203.782 180.552 145.516  1.00117.46           O  
ATOM   7088  CB  GLU A 925     202.320 178.444 144.438  1.00117.46           C  
ATOM   7089  CG  GLU A 925     203.586 178.004 143.717  1.00117.46           C  
ATOM   7090  CD  GLU A 925     203.957 176.564 144.015  1.00117.46           C  
ATOM   7091  OE1 GLU A 925     203.054 175.776 144.367  1.00117.46           O  
ATOM   7092  OE2 GLU A 925     205.150 176.218 143.891  1.00117.46           O  
ATOM   7093  N   MET A 926     203.525 179.910 147.655  1.00119.19           N  
ATOM   7094  CA  MET A 926     204.309 181.008 148.199  1.00119.19           C  
ATOM   7095  C   MET A 926     205.215 180.505 149.313  1.00119.19           C  
ATOM   7096  O   MET A 926     204.920 179.509 149.977  1.00119.19           O  
ATOM   7097  CB  MET A 926     203.411 182.133 148.731  1.00119.19           C  
ATOM   7098  CG  MET A 926     202.630 182.865 147.655  1.00119.19           C  
ATOM   7099  SD  MET A 926     201.643 184.215 148.322  1.00119.19           S  
ATOM   7100  CE  MET A 926     202.936 185.384 148.732  1.00119.19           C  
ATOM   7101  N   GLU A 927     206.326 181.210 149.505  1.00120.47           N  
ATOM   7102  CA  GLU A 927     207.313 180.897 150.523  1.00120.47           C  
ATOM   7103  C   GLU A 927     207.100 181.791 151.746  1.00120.47           C  
ATOM   7104  O   GLU A 927     206.061 182.441 151.897  1.00120.47           O  
ATOM   7105  CB  GLU A 927     208.723 181.034 149.946  1.00120.47           C  
ATOM   7106  CG  GLU A 927     209.145 179.869 149.060  1.00120.47           C  
ATOM   7107  CD  GLU A 927     208.561 179.944 147.662  1.00120.47           C  
ATOM   7108  OE1 GLU A 927     207.928 180.966 147.331  1.00120.47           O  
ATOM   7109  OE2 GLU A 927     208.734 178.978 146.892  1.00120.47           O  
ATOM   7110  N   GLY A 928     208.093 181.821 152.634  1.00131.22           N  
ATOM   7111  CA  GLY A 928     207.878 182.337 153.969  1.00131.22           C  
ATOM   7112  C   GLY A 928     207.657 183.837 154.007  1.00131.22           C  
ATOM   7113  O   GLY A 928     207.984 184.579 153.079  1.00131.22           O  
ATOM   7114  N   ASN A 929     207.075 184.275 155.127  1.00141.82           N  
ATOM   7115  CA  ASN A 929     206.752 185.679 155.395  1.00141.82           C  
ATOM   7116  C   ASN A 929     205.827 186.262 154.331  1.00141.82           C  
ATOM   7117  O   ASN A 929     205.843 187.468 154.072  1.00141.82           O  
ATOM   7118  CB  ASN A 929     208.022 186.527 155.521  1.00141.82           C  
ATOM   7119  CG  ASN A 929     207.832 187.736 156.418  1.00141.82           C  
ATOM   7120  OD1 ASN A 929     208.797 188.402 156.792  1.00141.82           O  
ATOM   7121  ND2 ASN A 929     206.584 188.023 156.771  1.00141.82           N  
ATOM   7122  N   ALA A 930     205.010 185.401 153.725  1.00131.88           N  
ATOM   7123  CA  ALA A 930     204.089 185.774 152.651  1.00131.88           C  
ATOM   7124  C   ALA A 930     204.806 186.484 151.504  1.00131.88           C  
ATOM   7125  O   ALA A 930     204.277 187.419 150.899  1.00131.88           O  
ATOM   7126  CB  ALA A 930     202.940 186.630 153.188  1.00131.88           C  
ATOM   7127  N   GLN A 931     206.024 186.039 151.193  1.00127.15           N  
ATOM   7128  CA  GLN A 931     206.663 186.450 149.954  1.00127.15           C  
ATOM   7129  C   GLN A 931     207.130 185.228 149.175  1.00127.15           C  
ATOM   7130  O   GLN A 931     207.648 184.275 149.769  1.00127.15           O  
ATOM   7131  CB  GLN A 931     207.860 187.380 150.215  1.00127.15           C  
ATOM   7132  CG  GLN A 931     207.504 188.844 150.448  1.00127.15           C  
ATOM   7133  CD  GLN A 931     206.856 189.090 151.794  1.00127.15           C  
ATOM   7134  OE1 GLN A 931     205.755 189.633 151.876  1.00127.15           O  
ATOM   7135  NE2 GLN A 931     207.540 188.693 152.860  1.00127.15           N  
ATOM   7136  N   PRO A 932     206.958 185.220 147.845  1.00114.71           N  
ATOM   7137  CA  PRO A 932     207.321 184.052 147.033  1.00114.71           C  
ATOM   7138  C   PRO A 932     208.789 184.053 146.612  1.00114.71           C  
ATOM   7139  O   PRO A 932     209.125 183.787 145.452  1.00114.71           O  
ATOM   7140  CB  PRO A 932     206.388 184.180 145.825  1.00114.71           C  
ATOM   7141  CG  PRO A 932     206.202 185.650 145.677  1.00114.71           C  
ATOM   7142  CD  PRO A 932     206.194 186.214 147.073  1.00114.71           C  
ATOM   7143  N   VAL A 933     209.683 184.349 147.555  1.00120.75           N  
ATOM   7144  CA  VAL A 933     211.102 184.454 147.230  1.00120.75           C  
ATOM   7145  C   VAL A 933     211.969 183.604 148.151  1.00120.75           C  
ATOM   7146  O   VAL A 933     212.683 182.706 147.688  1.00120.75           O  
ATOM   7147  CB  VAL A 933     211.556 185.925 147.252  1.00120.75           C  
ATOM   7148  CG1 VAL A 933     211.246 186.580 145.925  1.00120.75           C  
ATOM   7149  CG2 VAL A 933     210.856 186.673 148.370  1.00120.75           C  
ATOM   7150  N   ASN A 934     211.908 183.874 149.455  1.00122.06           N  
ATOM   7151  CA  ASN A 934     212.882 183.368 150.421  1.00122.06           C  
ATOM   7152  C   ASN A 934     214.308 183.696 149.965  1.00122.06           C  
ATOM   7153  O   ASN A 934     215.088 182.830 149.569  1.00122.06           O  
ATOM   7154  CB  ASN A 934     212.694 181.863 150.647  1.00122.06           C  
ATOM   7155  CG  ASN A 934     213.443 181.357 151.866  1.00122.06           C  
ATOM   7156  OD1 ASN A 934     214.068 182.130 152.592  1.00122.06           O  
ATOM   7157  ND2 ASN A 934     213.379 180.052 152.099  1.00122.06           N  
ATOM   7158  N   PHE A 935     214.613 184.999 150.020  1.00120.89           N  
ATOM   7159  CA  PHE A 935     215.859 185.511 149.454  1.00120.89           C  
ATOM   7160  C   PHE A 935     217.092 184.858 150.068  1.00120.89           C  
ATOM   7161  O   PHE A 935     218.099 184.674 149.376  1.00120.89           O  
ATOM   7162  CB  PHE A 935     215.951 187.028 149.635  1.00120.89           C  
ATOM   7163  CG  PHE A 935     214.990 187.810 148.784  1.00120.89           C  
ATOM   7164  CD1 PHE A 935     215.141 187.859 147.407  1.00120.89           C  
ATOM   7165  CD2 PHE A 935     213.963 188.533 149.366  1.00120.89           C  
ATOM   7166  CE1 PHE A 935     214.265 188.590 146.625  1.00120.89           C  
ATOM   7167  CE2 PHE A 935     213.088 189.269 148.591  1.00120.89           C  
ATOM   7168  CZ  PHE A 935     213.237 189.296 147.219  1.00120.89           C  
ATOM   7169  N   ASN A 936     217.040 184.506 151.354  1.00117.07           N  
ATOM   7170  CA  ASN A 936     218.231 183.982 152.017  1.00117.07           C  
ATOM   7171  C   ASN A 936     218.562 182.577 151.528  1.00117.07           C  
ATOM   7172  O   ASN A 936     219.720 182.274 151.217  1.00117.07           O  
ATOM   7173  CB  ASN A 936     218.033 183.992 153.533  1.00117.07           C  
ATOM   7174  CG  ASN A 936     217.905 185.394 154.097  1.00117.07           C  
ATOM   7175  OD1 ASN A 936     218.598 186.315 153.664  1.00117.07           O  
ATOM   7176  ND2 ASN A 936     217.015 185.562 155.068  1.00117.07           N  
ATOM   7177  N   ARG A 937     217.556 181.703 151.453  1.00116.82           N  
ATOM   7178  CA  ARG A 937     217.793 180.351 150.961  1.00116.82           C  
ATOM   7179  C   ARG A 937     218.097 180.350 149.467  1.00116.82           C  
ATOM   7180  O   ARG A 937     218.973 179.609 149.006  1.00116.82           O  
ATOM   7181  CB  ARG A 937     216.589 179.463 151.277  1.00116.82           C  
ATOM   7182  CG  ARG A 937     216.752 178.012 150.859  1.00116.82           C  
ATOM   7183  CD  ARG A 937     215.490 177.216 151.146  1.00116.82           C  
ATOM   7184  NE  ARG A 937     214.346 177.699 150.380  1.00116.82           N  
ATOM   7185  CZ  ARG A 937     214.097 177.367 149.118  1.00116.82           C  
ATOM   7186  NH1 ARG A 937     214.919 176.553 148.468  1.00116.82           N  
ATOM   7187  NH2 ARG A 937     213.030 177.855 148.503  1.00116.82           N  
ATOM   7188  N   SER A 938     217.382 181.174 148.695  1.00115.82           N  
ATOM   7189  CA  SER A 938     217.602 181.229 147.253  1.00115.82           C  
ATOM   7190  C   SER A 938     218.971 181.801 146.902  1.00115.82           C  
ATOM   7191  O   SER A 938     219.515 181.487 145.837  1.00115.82           O  
ATOM   7192  CB  SER A 938     216.501 182.053 146.585  1.00115.82           C  
ATOM   7193  OG  SER A 938     216.565 183.411 146.982  1.00115.82           O  
ATOM   7194  N   TRP A 939     219.542 182.634 147.774  1.00120.47           N  
ATOM   7195  CA  TRP A 939     220.920 183.078 147.583  1.00120.47           C  
ATOM   7196  C   TRP A 939     221.898 181.915 147.701  1.00120.47           C  
ATOM   7197  O   TRP A 939     222.757 181.722 146.833  1.00120.47           O  
ATOM   7198  CB  TRP A 939     221.266 184.177 148.589  1.00120.47           C  
ATOM   7199  CG  TRP A 939     222.654 184.723 148.425  1.00120.47           C  
ATOM   7200  CD1 TRP A 939     223.766 184.357 149.127  1.00120.47           C  
ATOM   7201  CD2 TRP A 939     223.078 185.736 147.503  1.00120.47           C  
ATOM   7202  NE1 TRP A 939     224.855 185.076 148.698  1.00120.47           N  
ATOM   7203  CE2 TRP A 939     224.459 185.930 147.702  1.00120.47           C  
ATOM   7204  CE3 TRP A 939     222.424 186.497 146.529  1.00120.47           C  
ATOM   7205  CZ2 TRP A 939     225.198 186.852 146.964  1.00120.47           C  
ATOM   7206  CZ3 TRP A 939     223.159 187.412 145.797  1.00120.47           C  
ATOM   7207  CH2 TRP A 939     224.531 187.582 146.018  1.00120.47           C  
ATOM   7208  N   ASP A 940     221.784 181.128 148.773  1.00121.44           N  
ATOM   7209  CA  ASP A 940     222.734 180.043 148.993  1.00121.44           C  
ATOM   7210  C   ASP A 940     222.522 178.898 148.012  1.00121.44           C  
ATOM   7211  O   ASP A 940     223.484 178.211 147.649  1.00121.44           O  
ATOM   7212  CB  ASP A 940     222.628 179.538 150.432  1.00121.44           C  
ATOM   7213  CG  ASP A 940     223.000 180.599 151.449  1.00121.44           C  
ATOM   7214  OD1 ASP A 940     223.797 181.497 151.107  1.00121.44           O  
ATOM   7215  OD2 ASP A 940     222.496 180.534 152.590  1.00121.44           O  
ATOM   7216  N   HIS A 941     221.280 178.671 147.577  1.00117.20           N  
ATOM   7217  CA  HIS A 941     221.035 177.675 146.538  1.00117.20           C  
ATOM   7218  C   HIS A 941     221.680 178.083 145.219  1.00117.20           C  
ATOM   7219  O   HIS A 941     222.217 177.236 144.494  1.00117.20           O  
ATOM   7220  CB  HIS A 941     219.531 177.464 146.359  1.00117.20           C  
ATOM   7221  CG  HIS A 941     219.179 176.577 145.206  1.00117.20           C  
ATOM   7222  ND1 HIS A 941     219.392 175.215 145.222  1.00117.20           N  
ATOM   7223  CD2 HIS A 941     218.627 176.856 144.001  1.00117.20           C  
ATOM   7224  CE1 HIS A 941     218.987 174.694 144.078  1.00117.20           C  
ATOM   7225  NE2 HIS A 941     218.519 175.669 143.319  1.00117.20           N  
ATOM   7226  N   ALA A 942     221.636 179.376 144.888  1.00117.40           N  
ATOM   7227  CA  ALA A 942     222.369 179.867 143.726  1.00117.40           C  
ATOM   7228  C   ALA A 942     223.874 179.866 143.963  1.00117.40           C  
ATOM   7229  O   ALA A 942     224.648 179.667 143.019  1.00117.40           O  
ATOM   7230  CB  ALA A 942     221.891 181.270 143.356  1.00117.40           C  
ATOM   7231  N   TYR A 943     224.305 180.084 145.207  1.00118.75           N  
ATOM   7232  CA  TYR A 943     225.732 180.207 145.491  1.00118.75           C  
ATOM   7233  C   TYR A 943     226.444 178.866 145.355  1.00118.75           C  
ATOM   7234  O   TYR A 943     227.552 178.797 144.811  1.00118.75           O  
ATOM   7235  CB  TYR A 943     225.943 180.789 146.888  1.00118.75           C  
ATOM   7236  CG  TYR A 943     227.398 180.952 147.268  1.00118.75           C  
ATOM   7237  CD1 TYR A 943     228.167 181.972 146.721  1.00118.75           C  
ATOM   7238  CD2 TYR A 943     228.001 180.090 148.173  1.00118.75           C  
ATOM   7239  CE1 TYR A 943     229.498 182.125 147.064  1.00118.75           C  
ATOM   7240  CE2 TYR A 943     229.331 180.236 148.523  1.00118.75           C  
ATOM   7241  CZ  TYR A 943     230.074 181.255 147.965  1.00118.75           C  
ATOM   7242  OH  TYR A 943     231.397 181.405 148.311  1.00118.75           O  
ATOM   7243  N   ASN A 944     225.823 177.791 145.842  1.00118.72           N  
ATOM   7244  CA  ASN A 944     226.495 176.498 145.908  1.00118.72           C  
ATOM   7245  C   ASN A 944     226.543 175.807 144.551  1.00118.72           C  
ATOM   7246  O   ASN A 944     227.465 175.025 144.294  1.00118.72           O  
ATOM   7247  CB  ASN A 944     225.801 175.599 146.933  1.00118.72           C  
ATOM   7248  CG  ASN A 944     226.737 174.569 147.539  1.00118.72           C  
ATOM   7249  OD1 ASN A 944     226.401 173.917 148.527  1.00118.72           O  
ATOM   7250  ND2 ASN A 944     227.920 174.423 146.953  1.00118.72           N  
ATOM   7251  N   ILE A 945     225.572 176.076 143.678  1.00117.43           N  
ATOM   7252  CA  ILE A 945     225.476 175.331 142.428  1.00117.43           C  
ATOM   7253  C   ILE A 945     226.530 175.804 141.429  1.00117.43           C  
ATOM   7254  O   ILE A 945     226.937 175.042 140.544  1.00117.43           O  
ATOM   7255  CB  ILE A 945     224.053 175.438 141.851  1.00117.43           C  
ATOM   7256  CG1 ILE A 945     223.838 174.398 140.748  1.00117.43           C  
ATOM   7257  CG2 ILE A 945     223.779 176.844 141.334  1.00117.43           C  
ATOM   7258  CD1 ILE A 945     223.929 172.968 141.233  1.00117.43           C  
ATOM   7259  N   THR A 946     226.992 177.050 141.550  1.00130.20           N  
ATOM   7260  CA  THR A 946     227.991 177.614 140.649  1.00130.20           C  
ATOM   7261  C   THR A 946     229.223 178.098 141.408  1.00130.20           C  
ATOM   7262  O   THR A 946     229.950 178.970 140.922  1.00130.20           O  
ATOM   7263  CB  THR A 946     227.389 178.751 139.820  1.00130.20           C  
ATOM   7264  OG1 THR A 946     228.380 179.272 138.924  1.00130.20           O  
ATOM   7265  CG2 THR A 946     226.885 179.863 140.723  1.00130.20           C  
ATOM   7266  N   PHE A 947     229.470 177.537 142.589  1.00135.46           N  
ATOM   7267  CA  PHE A 947     230.651 177.869 143.376  1.00135.46           C  
ATOM   7268  C   PHE A 947     231.900 177.283 142.728  1.00135.46           C  
ATOM   7269  O   PHE A 947     231.993 176.067 142.531  1.00135.46           O  
ATOM   7270  CB  PHE A 947     230.496 177.352 144.804  1.00135.46           C  
ATOM   7271  CG  PHE A 947     231.709 177.571 145.660  1.00135.46           C  
ATOM   7272  CD1 PHE A 947     232.024 178.834 146.130  1.00135.46           C  
ATOM   7273  CD2 PHE A 947     232.537 176.511 145.991  1.00135.46           C  
ATOM   7274  CE1 PHE A 947     233.142 179.036 146.916  1.00135.46           C  
ATOM   7275  CE2 PHE A 947     233.655 176.706 146.777  1.00135.46           C  
ATOM   7276  CZ  PHE A 947     233.958 177.970 147.238  1.00135.46           C  
ATOM   7277  N   ASN A 948     232.858 178.146 142.397  1.00156.00           N  
ATOM   7278  CA  ASN A 948     234.155 177.695 141.903  1.00156.00           C  
ATOM   7279  C   ASN A 948     235.201 178.747 142.235  1.00156.00           C  
ATOM   7280  O   ASN A 948     235.072 179.906 141.829  1.00156.00           O  
ATOM   7281  CB  ASN A 948     234.110 177.436 140.395  1.00156.00           C  
ATOM   7282  CG  ASN A 948     235.320 176.668 139.899  1.00156.00           C  
ATOM   7283  OD1 ASN A 948     236.200 176.301 140.677  1.00156.00           O  
ATOM   7284  ND2 ASN A 948     235.370 176.422 138.594  1.00156.00           N  
ATOM   7285  N   ASN A 949     236.234 178.334 142.974  1.00161.35           N  
ATOM   7286  CA  ASN A 949     237.383 179.191 143.242  1.00161.35           C  
ATOM   7287  C   ASN A 949     238.264 179.387 142.016  1.00161.35           C  
ATOM   7288  O   ASN A 949     239.101 180.296 142.009  1.00161.35           O  
ATOM   7289  CB  ASN A 949     238.211 178.614 144.393  1.00161.35           C  
ATOM   7290  CG  ASN A 949     238.586 177.160 144.171  1.00161.35           C  
ATOM   7291  OD1 ASN A 949     238.247 176.566 143.148  1.00161.35           O  
ATOM   7292  ND2 ASN A 949     239.292 176.579 145.135  1.00161.35           N  
ATOM   7293  N   GLN A 950     238.096 178.560 140.984  1.00168.99           N  
ATOM   7294  CA  GLN A 950     238.875 178.695 139.760  1.00168.99           C  
ATOM   7295  C   GLN A 950     238.412 179.856 138.891  1.00168.99           C  
ATOM   7296  O   GLN A 950     239.186 180.329 138.052  1.00168.99           O  
ATOM   7297  CB  GLN A 950     238.818 177.395 138.954  1.00168.99           C  
ATOM   7298  CG  GLN A 950     239.355 176.182 139.696  1.00168.99           C  
ATOM   7299  CD  GLN A 950     240.822 176.320 140.052  1.00168.99           C  
ATOM   7300  OE1 GLN A 950     241.625 176.798 139.251  1.00168.99           O  
ATOM   7301  NE2 GLN A 950     241.180 175.900 141.260  1.00168.99           N  
ATOM   7302  N   ASP A 951     237.180 180.324 139.068  1.00165.42           N  
ATOM   7303  CA  ASP A 951     236.709 181.486 138.336  1.00165.42           C  
ATOM   7304  C   ASP A 951     237.323 182.764 138.907  1.00165.42           C  
ATOM   7305  O   ASP A 951     238.001 182.759 139.939  1.00165.42           O  
ATOM   7306  CB  ASP A 951     235.183 181.561 138.374  1.00165.42           C  
ATOM   7307  CG  ASP A 951     234.525 180.437 137.598  1.00165.42           C  
ATOM   7308  OD1 ASP A 951     235.146 179.932 136.639  1.00165.42           O  
ATOM   7309  OD2 ASP A 951     233.387 180.059 137.946  1.00165.42           O  
ATOM   7310  N   LYS A 952     237.073 183.876 138.216  1.00160.42           N  
ATOM   7311  CA  LYS A 952     237.722 185.139 138.555  1.00160.42           C  
ATOM   7312  C   LYS A 952     237.007 185.851 139.698  1.00160.42           C  
ATOM   7313  O   LYS A 952     237.584 186.065 140.769  1.00160.42           O  
ATOM   7314  CB  LYS A 952     237.788 186.040 137.318  1.00160.42           C  
ATOM   7315  CG  LYS A 952     238.486 187.370 137.556  1.00160.42           C  
ATOM   7316  CD  LYS A 952     239.970 187.175 137.825  1.00160.42           C  
ATOM   7317  CE  LYS A 952     240.681 188.509 137.988  1.00160.42           C  
ATOM   7318  NZ  LYS A 952     240.251 189.221 139.222  1.00160.42           N  
ATOM   7319  N   GLY A 953     235.753 186.223 139.488  1.00150.99           N  
ATOM   7320  CA  GLY A 953     235.027 187.072 140.409  1.00150.99           C  
ATOM   7321  C   GLY A 953     234.776 188.453 139.827  1.00150.99           C  
ATOM   7322  O   GLY A 953     235.320 188.842 138.792  1.00150.99           O  
ATOM   7323  N   LEU A 954     233.928 189.201 140.528  1.00150.77           N  
ATOM   7324  CA  LEU A 954     233.511 190.525 140.093  1.00150.77           C  
ATOM   7325  C   LEU A 954     233.713 191.543 141.207  1.00150.77           C  
ATOM   7326  O   LEU A 954     233.993 191.204 142.360  1.00150.77           O  
ATOM   7327  CB  LEU A 954     232.045 190.532 139.639  1.00150.77           C  
ATOM   7328  CG  LEU A 954     231.709 189.743 138.373  1.00150.77           C  
ATOM   7329  CD1 LEU A 954     230.224 189.844 138.072  1.00150.77           C  
ATOM   7330  CD2 LEU A 954     232.535 190.236 137.195  1.00150.77           C  
ATOM   7331  N   LEU A 955     233.564 192.805 140.831  1.00162.13           N  
ATOM   7332  CA  LEU A 955     233.702 194.011 141.628  1.00162.13           C  
ATOM   7333  C   LEU A 955     232.333 194.484 142.096  1.00162.13           C  
ATOM   7334  O   LEU A 955     231.307 194.109 141.521  1.00162.13           O  
ATOM   7335  CB  LEU A 955     234.401 195.111 140.818  1.00162.13           C  
ATOM   7336  CG  LEU A 955     235.932 195.022 140.791  1.00162.13           C  
ATOM   7337  CD1 LEU A 955     236.415 193.943 139.828  1.00162.13           C  
ATOM   7338  CD2 LEU A 955     236.563 196.365 140.454  1.00162.13           C  
ATOM   7339  N   PRO A 956     232.271 195.303 143.150  1.00171.75           N  
ATOM   7340  CA  PRO A 956     230.953 195.714 143.663  1.00171.75           C  
ATOM   7341  C   PRO A 956     230.134 196.545 142.689  1.00171.75           C  
ATOM   7342  O   PRO A 956     228.901 196.444 142.709  1.00171.75           O  
ATOM   7343  CB  PRO A 956     231.309 196.521 144.919  1.00171.75           C  
ATOM   7344  CG  PRO A 956     232.607 195.948 145.368  1.00171.75           C  
ATOM   7345  CD  PRO A 956     233.351 195.622 144.100  1.00171.75           C  
ATOM   7346  N   TYR A 957     230.756 197.365 141.841  1.00192.91           N  
ATOM   7347  CA  TYR A 957     229.963 198.070 140.841  1.00192.91           C  
ATOM   7348  C   TYR A 957     229.665 197.193 139.632  1.00192.91           C  
ATOM   7349  O   TYR A 957     228.701 197.462 138.907  1.00192.91           O  
ATOM   7350  CB  TYR A 957     230.660 199.360 140.395  1.00192.91           C  
ATOM   7351  CG  TYR A 957     231.949 199.162 139.630  1.00192.91           C  
ATOM   7352  CD1 TYR A 957     233.163 199.056 140.291  1.00192.91           C  
ATOM   7353  CD2 TYR A 957     231.952 199.100 138.241  1.00192.91           C  
ATOM   7354  CE1 TYR A 957     234.342 198.883 139.595  1.00192.91           C  
ATOM   7355  CE2 TYR A 957     233.127 198.925 137.536  1.00192.91           C  
ATOM   7356  CZ  TYR A 957     234.319 198.817 138.218  1.00192.91           C  
ATOM   7357  OH  TYR A 957     235.493 198.644 137.521  1.00192.91           O  
ATOM   7358  N   ALA A 958     230.476 196.156 139.404  1.00171.61           N  
ATOM   7359  CA  ALA A 958     230.315 195.313 138.224  1.00171.61           C  
ATOM   7360  C   ALA A 958     229.056 194.461 138.304  1.00171.61           C  
ATOM   7361  O   ALA A 958     228.432 194.180 137.274  1.00171.61           O  
ATOM   7362  CB  ALA A 958     231.546 194.426 138.040  1.00171.61           C  
ATOM   7363  N   ILE A 959     228.669 194.039 139.511  1.00163.47           N  
ATOM   7364  CA  ILE A 959     227.502 193.176 139.655  1.00163.47           C  
ATOM   7365  C   ILE A 959     226.215 193.962 139.450  1.00163.47           C  
ATOM   7366  O   ILE A 959     225.210 193.407 138.988  1.00163.47           O  
ATOM   7367  CB  ILE A 959     227.527 192.462 141.021  1.00163.47           C  
ATOM   7368  CG1 ILE A 959     227.769 193.459 142.158  1.00163.47           C  
ATOM   7369  CG2 ILE A 959     228.589 191.372 141.034  1.00163.47           C  
ATOM   7370  CD1 ILE A 959     226.506 193.934 142.846  1.00163.47           C  
ATOM   7371  N   MET A 960     226.211 195.253 139.789  1.00155.69           N  
ATOM   7372  CA  MET A 960     224.987 196.037 139.659  1.00155.69           C  
ATOM   7373  C   MET A 960     224.641 196.274 138.194  1.00155.69           C  
ATOM   7374  O   MET A 960     223.462 196.287 137.823  1.00155.69           O  
ATOM   7375  CB  MET A 960     225.131 197.367 140.399  1.00155.69           C  
ATOM   7376  CG  MET A 960     225.211 197.234 141.910  1.00155.69           C  
ATOM   7377  SD  MET A 960     223.745 196.460 142.618  1.00155.69           S  
ATOM   7378  CE  MET A 960     222.504 197.704 142.273  1.00155.69           C  
ATOM   7379  N   GLU A 961     225.655 196.463 137.346  1.00163.20           N  
ATOM   7380  CA  GLU A 961     225.412 196.557 135.912  1.00163.20           C  
ATOM   7381  C   GLU A 961     225.146 195.192 135.292  1.00163.20           C  
ATOM   7382  O   GLU A 961     224.432 195.100 134.287  1.00163.20           O  
ATOM   7383  CB  GLU A 961     226.601 197.225 135.218  1.00163.20           C  
ATOM   7384  CG  GLU A 961     226.810 198.679 135.609  1.00163.20           C  
ATOM   7385  CD  GLU A 961     225.674 199.574 135.155  1.00163.20           C  
ATOM   7386  OE1 GLU A 961     225.127 199.332 134.059  1.00163.20           O  
ATOM   7387  OE2 GLU A 961     225.328 200.518 135.895  1.00163.20           O  
ATOM   7388  N   THR A 962     225.707 194.128 135.872  1.00157.79           N  
ATOM   7389  CA  THR A 962     225.304 192.775 135.501  1.00157.79           C  
ATOM   7390  C   THR A 962     223.871 192.481 135.927  1.00157.79           C  
ATOM   7391  O   THR A 962     223.156 191.748 135.234  1.00157.79           O  
ATOM   7392  CB  THR A 962     226.263 191.755 136.118  1.00157.79           C  
ATOM   7393  OG1 THR A 962     227.612 192.103 135.783  1.00157.79           O  
ATOM   7394  CG2 THR A 962     225.969 190.355 135.599  1.00157.79           C  
ATOM   7395  N   ALA A 963     223.431 193.051 137.050  1.00153.00           N  
ATOM   7396  CA  ALA A 963     222.035 192.926 137.455  1.00153.00           C  
ATOM   7397  C   ALA A 963     221.121 193.709 136.520  1.00153.00           C  
ATOM   7398  O   ALA A 963     220.193 193.149 135.925  1.00153.00           O  
ATOM   7399  CB  ALA A 963     221.866 193.397 138.900  1.00153.00           C  
ATOM   7400  N   ASN A 964     221.384 195.008 136.361  1.00148.20           N  
ATOM   7401  CA  ASN A 964     220.512 195.877 135.580  1.00148.20           C  
ATOM   7402  C   ASN A 964     220.523 195.544 134.095  1.00148.20           C  
ATOM   7403  O   ASN A 964     219.686 196.072 133.354  1.00148.20           O  
ATOM   7404  CB  ASN A 964     220.912 197.340 135.784  1.00148.20           C  
ATOM   7405  CG  ASN A 964     220.592 197.843 137.177  1.00148.20           C  
ATOM   7406  OD1 ASN A 964     219.522 197.567 137.720  1.00148.20           O  
ATOM   7407  ND2 ASN A 964     221.522 198.587 137.766  1.00148.20           N  
ATOM   7408  N   GLU A 965     221.446 194.693 133.645  1.00155.10           N  
ATOM   7409  CA  GLU A 965     221.329 194.103 132.317  1.00155.10           C  
ATOM   7410  C   GLU A 965     220.060 193.269 132.174  1.00155.10           C  
ATOM   7411  O   GLU A 965     219.477 193.215 131.084  1.00155.10           O  
ATOM   7412  CB  GLU A 965     222.562 193.250 132.015  1.00155.10           C  
ATOM   7413  CG  GLU A 965     222.568 192.624 130.629  1.00155.10           C  
ATOM   7414  CD  GLU A 965     223.803 191.784 130.374  1.00155.10           C  
ATOM   7415  OE1 GLU A 965     224.667 191.705 131.273  1.00155.10           O  
ATOM   7416  OE2 GLU A 965     223.911 191.201 129.274  1.00155.10           O  
ATOM   7417  N   ILE A 966     219.607 192.624 133.250  1.00145.02           N  
ATOM   7418  CA  ILE A 966     218.510 191.667 133.133  1.00145.02           C  
ATOM   7419  C   ILE A 966     217.192 192.297 133.567  1.00145.02           C  
ATOM   7420  O   ILE A 966     216.245 192.372 132.777  1.00145.02           O  
ATOM   7421  CB  ILE A 966     218.800 190.395 133.950  1.00145.02           C  
ATOM   7422  CG1 ILE A 966     220.113 189.755 133.494  1.00145.02           C  
ATOM   7423  CG2 ILE A 966     217.649 189.409 133.825  1.00145.02           C  
ATOM   7424  CD1 ILE A 966     220.133 189.379 132.029  1.00145.02           C  
ATOM   7425  N   LEU A 967     217.112 192.752 134.820  1.00147.45           N  
ATOM   7426  CA  LEU A 967     215.851 193.291 135.317  1.00147.45           C  
ATOM   7427  C   LEU A 967     215.577 194.699 134.807  1.00147.45           C  
ATOM   7428  O   LEU A 967     214.485 195.227 135.046  1.00147.45           O  
ATOM   7429  CB  LEU A 967     215.811 193.278 136.850  1.00147.45           C  
ATOM   7430  CG  LEU A 967     216.383 194.453 137.648  1.00147.45           C  
ATOM   7431  CD1 LEU A 967     215.896 194.390 139.087  1.00147.45           C  
ATOM   7432  CD2 LEU A 967     217.893 194.459 137.613  1.00147.45           C  
ATOM   7433  N   GLY A 968     216.538 195.313 134.122  1.00144.36           N  
ATOM   7434  CA  GLY A 968     216.320 196.542 133.398  1.00144.36           C  
ATOM   7435  C   GLY A 968     215.213 196.450 132.368  1.00144.36           C  
ATOM   7436  O   GLY A 968     214.148 197.057 132.518  1.00144.36           O  
ATOM   7437  N   PRO A 969     215.434 195.667 131.307  1.00143.83           N  
ATOM   7438  CA  PRO A 969     214.419 195.559 130.244  1.00143.83           C  
ATOM   7439  C   PRO A 969     213.098 194.964 130.702  1.00143.83           C  
ATOM   7440  O   PRO A 969     212.108 195.072 129.966  1.00143.83           O  
ATOM   7441  CB  PRO A 969     215.097 194.658 129.203  1.00143.83           C  
ATOM   7442  CG  PRO A 969     216.556 194.868 129.426  1.00143.83           C  
ATOM   7443  CD  PRO A 969     216.710 195.047 130.912  1.00143.83           C  
ATOM   7444  N   LEU A 970     213.045 194.341 131.880  1.00143.85           N  
ATOM   7445  CA  LEU A 970     211.756 193.974 132.456  1.00143.85           C  
ATOM   7446  C   LEU A 970     210.937 195.207 132.815  1.00143.85           C  
ATOM   7447  O   LEU A 970     209.704 195.181 132.724  1.00143.85           O  
ATOM   7448  CB  LEU A 970     211.961 193.097 133.692  1.00143.85           C  
ATOM   7449  CG  LEU A 970     212.002 191.575 133.514  1.00143.85           C  
ATOM   7450  CD1 LEU A 970     210.666 191.056 133.007  1.00143.85           C  
ATOM   7451  CD2 LEU A 970     213.134 191.150 132.588  1.00143.85           C  
ATOM   7452  N   GLU A 971     211.602 196.291 133.222  1.00144.98           N  
ATOM   7453  CA  GLU A 971     210.902 197.473 133.715  1.00144.98           C  
ATOM   7454  C   GLU A 971     210.309 198.310 132.586  1.00144.98           C  
ATOM   7455  O   GLU A 971     209.224 198.880 132.745  1.00144.98           O  
ATOM   7456  CB  GLU A 971     211.840 198.322 134.572  1.00144.98           C  
ATOM   7457  CG  GLU A 971     212.274 197.647 135.861  1.00144.98           C  
ATOM   7458  CD  GLU A 971     213.315 198.446 136.617  1.00144.98           C  
ATOM   7459  OE1 GLU A 971     213.815 199.449 136.065  1.00144.98           O  
ATOM   7460  OE2 GLU A 971     213.630 198.072 137.766  1.00144.98           O  
ATOM   7461  N   GLU A 972     210.994 198.403 131.444  1.00151.33           N  
ATOM   7462  CA  GLU A 972     210.464 199.204 130.347  1.00151.33           C  
ATOM   7463  C   GLU A 972     209.391 198.489 129.538  1.00151.33           C  
ATOM   7464  O   GLU A 972     208.762 199.125 128.685  1.00151.33           O  
ATOM   7465  CB  GLU A 972     211.588 199.653 129.406  1.00151.33           C  
ATOM   7466  CG  GLU A 972     212.558 200.655 130.016  1.00151.33           C  
ATOM   7467  CD  GLU A 972     213.753 199.991 130.663  1.00151.33           C  
ATOM   7468  OE1 GLU A 972     213.929 198.773 130.463  1.00151.33           O  
ATOM   7469  OE2 GLU A 972     214.514 200.683 131.370  1.00151.33           O  
ATOM   7470  N   ARG A 973     209.159 197.195 129.773  1.00146.82           N  
ATOM   7471  CA  ARG A 973     207.980 196.566 129.191  1.00146.82           C  
ATOM   7472  C   ARG A 973     206.709 197.008 129.903  1.00146.82           C  
ATOM   7473  O   ARG A 973     205.625 196.956 129.310  1.00146.82           O  
ATOM   7474  CB  ARG A 973     208.112 195.042 129.233  1.00146.82           C  
ATOM   7475  CG  ARG A 973     207.142 194.313 128.315  1.00146.82           C  
ATOM   7476  CD  ARG A 973     207.381 192.813 128.326  1.00146.82           C  
ATOM   7477  NE  ARG A 973     207.025 192.207 129.605  1.00146.82           N  
ATOM   7478  CZ  ARG A 973     207.902 191.651 130.433  1.00146.82           C  
ATOM   7479  NH1 ARG A 973     209.189 191.629 130.117  1.00146.82           N  
ATOM   7480  NH2 ARG A 973     207.494 191.121 131.579  1.00146.82           N  
ATOM   7481  N   LEU A 974     206.824 197.446 131.154  1.00146.49           N  
ATOM   7482  CA  LEU A 974     205.728 198.096 131.855  1.00146.49           C  
ATOM   7483  C   LEU A 974     205.659 199.555 131.422  1.00146.49           C  
ATOM   7484  O   LEU A 974     206.680 200.250 131.396  1.00146.49           O  
ATOM   7485  CB  LEU A 974     205.921 197.991 133.367  1.00146.49           C  
ATOM   7486  CG  LEU A 974     206.142 196.577 133.911  1.00146.49           C  
ATOM   7487  CD1 LEU A 974     206.323 196.600 135.423  1.00146.49           C  
ATOM   7488  CD2 LEU A 974     205.005 195.647 133.510  1.00146.49           C  
ATOM   7489  N   VAL A 975     204.460 200.023 131.081  1.00155.93           N  
ATOM   7490  CA  VAL A 975     204.328 201.243 130.293  1.00155.93           C  
ATOM   7491  C   VAL A 975     203.909 202.401 131.189  1.00155.93           C  
ATOM   7492  O   VAL A 975     204.313 203.547 130.959  1.00155.93           O  
ATOM   7493  CB  VAL A 975     203.337 201.049 129.129  1.00155.93           C  
ATOM   7494  CG1 VAL A 975     203.882 200.032 128.139  1.00155.93           C  
ATOM   7495  CG2 VAL A 975     201.977 200.603 129.647  1.00155.93           C  
ATOM   7496  N   ARG A 976     203.107 202.114 132.213  1.00169.41           N  
ATOM   7497  CA  ARG A 976     202.557 203.133 133.108  1.00169.41           C  
ATOM   7498  C   ARG A 976     201.811 204.212 132.315  1.00169.41           C  
ATOM   7499  O   ARG A 976     202.241 205.359 132.191  1.00169.41           O  
ATOM   7500  CB  ARG A 976     203.658 203.737 133.989  1.00169.41           C  
ATOM   7501  CG  ARG A 976     203.153 204.721 135.039  1.00169.41           C  
ATOM   7502  CD  ARG A 976     202.221 204.051 136.034  1.00169.41           C  
ATOM   7503  NE  ARG A 976     201.701 204.998 137.017  1.00169.41           N  
ATOM   7504  CZ  ARG A 976     202.282 205.262 138.182  1.00169.41           C  
ATOM   7505  NH1 ARG A 976     203.405 204.644 138.521  1.00169.41           N  
ATOM   7506  NH2 ARG A 976     201.737 206.140 139.014  1.00169.41           N  
ATOM   7507  N   TYR A 977     200.679 203.795 131.753  1.00177.67           N  
ATOM   7508  CA  TYR A 977     199.765 204.757 131.160  1.00177.67           C  
ATOM   7509  C   TYR A 977     199.123 205.610 132.251  1.00177.67           C  
ATOM   7510  O   TYR A 977     199.161 205.281 133.440  1.00177.67           O  
ATOM   7511  CB  TYR A 977     198.681 204.044 130.350  1.00177.67           C  
ATOM   7512  CG  TYR A 977     199.167 203.420 129.059  1.00177.67           C  
ATOM   7513  CD1 TYR A 977     200.413 203.736 128.533  1.00177.67           C  
ATOM   7514  CD2 TYR A 977     198.374 202.516 128.365  1.00177.67           C  
ATOM   7515  CE1 TYR A 977     200.856 203.165 127.354  1.00177.67           C  
ATOM   7516  CE2 TYR A 977     198.808 201.941 127.185  1.00177.67           C  
ATOM   7517  CZ  TYR A 977     200.049 202.270 126.684  1.00177.67           C  
ATOM   7518  OH  TYR A 977     200.486 201.700 125.510  1.00177.67           O  
ATOM   7519  N   ASP A 978     198.525 206.722 131.834  1.00189.35           N  
ATOM   7520  CA  ASP A 978     197.789 207.570 132.758  1.00189.35           C  
ATOM   7521  C   ASP A 978     196.337 207.098 132.834  1.00189.35           C  
ATOM   7522  O   ASP A 978     195.988 206.010 132.369  1.00189.35           O  
ATOM   7523  CB  ASP A 978     197.906 209.038 132.348  1.00189.35           C  
ATOM   7524  CG  ASP A 978     197.307 209.324 130.981  1.00189.35           C  
ATOM   7525  OD1 ASP A 978     196.882 208.375 130.290  1.00189.35           O  
ATOM   7526  OD2 ASP A 978     197.260 210.511 130.597  1.00189.35           O  
ATOM   7527  N   ASN A 979     195.471 207.919 133.428  1.00185.36           N  
ATOM   7528  CA  ASN A 979     194.063 207.561 133.541  1.00185.36           C  
ATOM   7529  C   ASN A 979     193.311 207.678 132.223  1.00185.36           C  
ATOM   7530  O   ASN A 979     192.199 207.149 132.120  1.00185.36           O  
ATOM   7531  CB  ASN A 979     193.382 208.435 134.597  1.00185.36           C  
ATOM   7532  CG  ASN A 979     193.833 208.106 136.006  1.00185.36           C  
ATOM   7533  OD1 ASN A 979     194.055 206.943 136.344  1.00185.36           O  
ATOM   7534  ND2 ASN A 979     193.969 209.131 136.839  1.00185.36           N  
ATOM   7535  N   SER A 980     193.880 208.348 131.214  1.00191.92           N  
ATOM   7536  CA  SER A 980     193.201 208.571 129.935  1.00191.92           C  
ATOM   7537  C   SER A 980     194.132 208.190 128.782  1.00191.92           C  
ATOM   7538  O   SER A 980     194.819 209.041 128.213  1.00191.92           O  
ATOM   7539  CB  SER A 980     192.732 210.023 129.824  1.00191.92           C  
ATOM   7540  OG  SER A 980     191.784 210.332 130.831  1.00191.92           O  
ATOM   7541  N   GLY A 981     194.148 206.903 128.438  1.00195.74           N  
ATOM   7542  CA  GLY A 981     194.712 206.463 127.175  1.00195.74           C  
ATOM   7543  C   GLY A 981     196.221 206.514 127.054  1.00195.74           C  
ATOM   7544  O   GLY A 981     196.881 205.475 126.966  1.00195.74           O  
ATOM   7545  N   CYS A 982     196.778 207.725 127.051  1.00196.70           N  
ATOM   7546  CA  CYS A 982     198.182 207.936 126.717  1.00196.70           C  
ATOM   7547  C   CYS A 982     199.104 207.619 127.888  1.00196.70           C  
ATOM   7548  O   CYS A 982     198.703 206.944 128.841  1.00196.70           O  
ATOM   7549  CB  CYS A 982     198.406 209.377 126.248  1.00196.70           C  
ATOM   7550  SG  CYS A 982     198.085 210.635 127.504  1.00196.70           S  
ATOM   7551  N   LEU A 983     200.344 208.089 127.813  1.00187.57           N  
ATOM   7552  CA  LEU A 983     201.302 207.931 128.895  1.00187.57           C  
ATOM   7553  C   LEU A 983     201.217 209.109 129.863  1.00187.57           C  
ATOM   7554  O   LEU A 983     200.575 210.127 129.597  1.00187.57           O  
ATOM   7555  CB  LEU A 983     202.724 207.803 128.343  1.00187.57           C  
ATOM   7556  CG  LEU A 983     203.195 206.430 127.855  1.00187.57           C  
ATOM   7557  CD1 LEU A 983     202.595 206.094 126.498  1.00187.57           C  
ATOM   7558  CD2 LEU A 983     204.715 206.372 127.803  1.00187.57           C  
ATOM   7559  N   VAL A 984     201.880 208.954 131.004  1.00187.48           N  
ATOM   7560  CA  VAL A 984     202.041 210.025 131.978  1.00187.48           C  
ATOM   7561  C   VAL A 984     203.477 210.525 131.908  1.00187.48           C  
ATOM   7562  O   VAL A 984     204.391 209.800 131.498  1.00187.48           O  
ATOM   7563  CB  VAL A 984     201.673 209.555 133.403  1.00187.48           C  
ATOM   7564  CG1 VAL A 984     202.736 208.613 133.953  1.00187.48           C  
ATOM   7565  CG2 VAL A 984     201.449 210.743 134.332  1.00187.48           C  
ATOM   7566  N   LYS A 985     203.671 211.782 132.300  1.00202.02           N  
ATOM   7567  CA  LYS A 985     205.002 212.370 132.294  1.00202.02           C  
ATOM   7568  C   LYS A 985     205.884 211.721 133.355  1.00202.02           C  
ATOM   7569  O   LYS A 985     205.425 211.383 134.449  1.00202.02           O  
ATOM   7570  CB  LYS A 985     204.912 213.879 132.529  1.00202.02           C  
ATOM   7571  CG  LYS A 985     206.236 214.616 132.401  1.00202.02           C  
ATOM   7572  CD  LYS A 985     206.036 216.124 132.441  1.00202.02           C  
ATOM   7573  CE  LYS A 985     206.056 216.650 133.868  1.00202.02           C  
ATOM   7574  NZ  LYS A 985     204.708 216.609 134.498  1.00202.02           N  
ATOM   7575  N   ARG A 986     207.164 211.549 133.014  1.00205.52           N  
ATOM   7576  CA  ARG A 986     208.100 210.833 133.875  1.00205.52           C  
ATOM   7577  C   ARG A 986     208.324 211.526 135.213  1.00205.52           C  
ATOM   7578  O   ARG A 986     208.767 210.875 136.166  1.00205.52           O  
ATOM   7579  CB  ARG A 986     209.441 210.658 133.158  1.00205.52           C  
ATOM   7580  CG  ARG A 986     209.361 209.950 131.809  1.00205.52           C  
ATOM   7581  CD  ARG A 986     209.271 208.433 131.958  1.00205.52           C  
ATOM   7582  NE  ARG A 986     207.938 207.975 132.343  1.00205.52           N  
ATOM   7583  CZ  ARG A 986     206.914 207.862 131.503  1.00205.52           C  
ATOM   7584  NH1 ARG A 986     207.065 208.171 130.222  1.00205.52           N  
ATOM   7585  NH2 ARG A 986     205.738 207.436 131.943  1.00205.52           N  
ATOM   7586  N   GLU A 987     208.034 212.820 135.313  1.00205.49           N  
ATOM   7587  CA  GLU A 987     208.083 213.502 136.598  1.00205.49           C  
ATOM   7588  C   GLU A 987     206.799 213.277 137.386  1.00205.49           C  
ATOM   7589  O   GLU A 987     205.700 213.256 136.823  1.00205.49           O  
ATOM   7590  CB  GLU A 987     208.311 215.000 136.396  1.00205.49           C  
ATOM   7591  CG  GLU A 987     209.675 215.352 135.825  1.00205.49           C  
ATOM   7592  CD  GLU A 987     210.804 215.072 136.796  1.00205.49           C  
ATOM   7593  OE1 GLU A 987     210.590 215.221 138.018  1.00205.49           O  
ATOM   7594  OE2 GLU A 987     211.906 214.704 136.339  1.00205.49           O  
ATOM   7595  N   ASP A 988     206.953 213.107 138.700  1.00197.80           N  
ATOM   7596  CA  ASP A 988     205.840 212.981 139.641  1.00197.80           C  
ATOM   7597  C   ASP A 988     204.943 211.794 139.279  1.00197.80           C  
ATOM   7598  O   ASP A 988     203.760 211.941 138.962  1.00197.80           O  
ATOM   7599  CB  ASP A 988     205.041 214.287 139.714  1.00197.80           C  
ATOM   7600  CG  ASP A 988     204.081 214.320 140.887  1.00197.80           C  
ATOM   7601  OD1 ASP A 988     204.552 214.418 142.039  1.00197.80           O  
ATOM   7602  OD2 ASP A 988     202.856 214.256 140.656  1.00197.80           O  
ATOM   7603  N   LEU A 989     205.535 210.600 139.330  1.00189.92           N  
ATOM   7604  CA  LEU A 989     204.799 209.385 138.996  1.00189.92           C  
ATOM   7605  C   LEU A 989     203.930 208.926 140.163  1.00189.92           C  
ATOM   7606  O   LEU A 989     202.702 208.854 140.051  1.00189.92           O  
ATOM   7607  CB  LEU A 989     205.774 208.277 138.588  1.00189.92           C  
ATOM   7608  CG  LEU A 989     206.628 208.520 137.342  1.00189.92           C  
ATOM   7609  CD1 LEU A 989     207.669 207.421 137.188  1.00189.92           C  
ATOM   7610  CD2 LEU A 989     205.753 208.607 136.105  1.00189.92           C  
ATOM   7611  N   ASN A 990     204.562 208.613 141.295  1.00185.73           N  
ATOM   7612  CA  ASN A 990     203.867 208.160 142.500  1.00185.73           C  
ATOM   7613  C   ASN A 990     203.165 209.345 143.160  1.00185.73           C  
ATOM   7614  O   ASN A 990     203.681 209.991 144.076  1.00185.73           O  
ATOM   7615  CB  ASN A 990     204.844 207.483 143.456  1.00185.73           C  
ATOM   7616  CG  ASN A 990     206.131 208.267 143.630  1.00185.73           C  
ATOM   7617  OD1 ASN A 990     206.288 209.356 143.079  1.00185.73           O  
ATOM   7618  ND2 ASN A 990     207.061 207.713 144.399  1.00185.73           N  
ATOM   7619  N   LYS A 991     201.952 209.635 142.682  1.00184.16           N  
ATOM   7620  CA  LYS A 991     201.204 210.793 143.160  1.00184.16           C  
ATOM   7621  C   LYS A 991     199.809 210.412 143.643  1.00184.16           C  
ATOM   7622  O   LYS A 991     198.956 211.292 143.807  1.00184.16           O  
ATOM   7623  CB  LYS A 991     201.108 211.863 142.069  1.00184.16           C  
ATOM   7624  CG  LYS A 991     200.313 211.434 140.845  1.00184.16           C  
ATOM   7625  CD  LYS A 991     200.329 212.508 139.771  1.00184.16           C  
ATOM   7626  CE  LYS A 991     199.565 213.745 140.214  1.00184.16           C  
ATOM   7627  NZ  LYS A 991     199.541 214.792 139.156  1.00184.16           N  
ATOM   7628  N   ALA A 992     199.562 209.119 143.870  1.00183.88           N  
ATOM   7629  CA  ALA A 992     198.282 208.623 144.380  1.00183.88           C  
ATOM   7630  C   ALA A 992     197.114 209.002 143.473  1.00183.88           C  
ATOM   7631  O   ALA A 992     195.997 209.223 143.946  1.00183.88           O  
ATOM   7632  CB  ALA A 992     198.026 209.107 145.811  1.00183.88           C  
ATOM   7633  N   GLU A 993     197.354 209.083 142.164  1.00179.60           N  
ATOM   7634  CA  GLU A 993     196.272 209.374 141.232  1.00179.60           C  
ATOM   7635  C   GLU A 993     196.319 208.457 140.016  1.00179.60           C  
ATOM   7636  O   GLU A 993     195.289 208.214 139.378  1.00179.60           O  
ATOM   7637  CB  GLU A 993     196.334 210.840 140.793  1.00179.60           C  
ATOM   7638  CG  GLU A 993     195.119 211.315 140.011  1.00179.60           C  
ATOM   7639  CD  GLU A 993     195.214 212.774 139.613  1.00179.60           C  
ATOM   7640  OE1 GLU A 993     196.234 213.416 139.941  1.00179.60           O  
ATOM   7641  OE2 GLU A 993     194.269 213.280 138.972  1.00179.60           O  
ATOM   7642  N   TYR A 994     197.500 207.934 139.690  1.00171.26           N  
ATOM   7643  CA  TYR A 994     197.691 207.152 138.474  1.00171.26           C  
ATOM   7644  C   TYR A 994     198.179 205.740 138.782  1.00171.26           C  
ATOM   7645  O   TYR A 994     198.957 205.165 138.019  1.00171.26           O  
ATOM   7646  CB  TYR A 994     198.661 207.858 137.526  1.00171.26           C  
ATOM   7647  CG  TYR A 994     198.151 209.182 137.004  1.00171.26           C  
ATOM   7648  CD1 TYR A 994     197.270 209.237 135.932  1.00171.26           C  
ATOM   7649  CD2 TYR A 994     198.552 210.379 137.583  1.00171.26           C  
ATOM   7650  CE1 TYR A 994     196.804 210.446 135.450  1.00171.26           C  
ATOM   7651  CE2 TYR A 994     198.090 211.593 137.109  1.00171.26           C  
ATOM   7652  CZ  TYR A 994     197.217 211.620 136.043  1.00171.26           C  
ATOM   7653  OH  TYR A 994     196.753 212.827 135.570  1.00171.26           O  
ATOM   7654  N   VAL A 995     197.731 205.170 139.898  1.00155.58           N  
ATOM   7655  CA  VAL A 995     198.038 203.778 140.214  1.00155.58           C  
ATOM   7656  C   VAL A 995     197.227 202.888 139.276  1.00155.58           C  
ATOM   7657  O   VAL A 995     196.001 202.806 139.391  1.00155.58           O  
ATOM   7658  CB  VAL A 995     197.743 203.455 141.683  1.00155.58           C  
ATOM   7659  CG1 VAL A 995     198.030 201.989 141.973  1.00155.58           C  
ATOM   7660  CG2 VAL A 995     198.561 204.355 142.597  1.00155.58           C  
ATOM   7661  N   ASP A 996     197.905 202.222 138.346  1.00159.82           N  
ATOM   7662  CA  ASP A 996     197.233 201.427 137.332  1.00159.82           C  
ATOM   7663  C   ASP A 996     196.957 200.023 137.871  1.00159.82           C  
ATOM   7664  O   ASP A 996     197.044 199.764 139.075  1.00159.82           O  
ATOM   7665  CB  ASP A 996     198.066 201.398 136.052  1.00159.82           C  
ATOM   7666  CG  ASP A 996     199.519 201.055 136.310  1.00159.82           C  
ATOM   7667  OD1 ASP A 996     199.915 200.994 137.493  1.00159.82           O  
ATOM   7668  OD2 ASP A 996     200.267 200.848 135.331  1.00159.82           O  
ATOM   7669  N   GLN A 997     196.616 199.097 136.972  1.00154.50           N  
ATOM   7670  CA  GLN A 997     196.132 197.777 137.363  1.00154.50           C  
ATOM   7671  C   GLN A 997     197.206 196.915 138.015  1.00154.50           C  
ATOM   7672  O   GLN A 997     196.873 195.872 138.587  1.00154.50           O  
ATOM   7673  CB  GLN A 997     195.557 197.049 136.147  1.00154.50           C  
ATOM   7674  CG  GLN A 997     196.589 196.683 135.093  1.00154.50           C  
ATOM   7675  CD  GLN A 997     195.969 196.028 133.874  1.00154.50           C  
ATOM   7676  OE1 GLN A 997     194.759 195.809 133.820  1.00154.50           O  
ATOM   7677  NE2 GLN A 997     196.799 195.711 132.887  1.00154.50           N  
ATOM   7678  N   TYR A 998     198.473 197.318 137.945  1.00147.27           N  
ATOM   7679  CA  TYR A 998     199.559 196.613 138.613  1.00147.27           C  
ATOM   7680  C   TYR A 998     200.489 197.620 139.272  1.00147.27           C  
ATOM   7681  O   TYR A 998     200.888 198.606 138.645  1.00147.27           O  
ATOM   7682  CB  TYR A 998     200.335 195.724 137.629  1.00147.27           C  
ATOM   7683  CG  TYR A 998     200.941 196.464 136.456  1.00147.27           C  
ATOM   7684  CD1 TYR A 998     200.209 196.681 135.295  1.00147.27           C  
ATOM   7685  CD2 TYR A 998     202.248 196.931 136.502  1.00147.27           C  
ATOM   7686  CE1 TYR A 998     200.757 197.353 134.220  1.00147.27           C  
ATOM   7687  CE2 TYR A 998     202.804 197.605 135.433  1.00147.27           C  
ATOM   7688  CZ  TYR A 998     202.055 197.812 134.294  1.00147.27           C  
ATOM   7689  OH  TYR A 998     202.606 198.480 133.225  1.00147.27           O  
ATOM   7690  N   ASP A 999     200.816 197.377 140.540  1.00145.62           N  
ATOM   7691  CA  ASP A 999     201.878 198.120 141.214  1.00145.62           C  
ATOM   7692  C   ASP A 999     202.809 197.252 142.049  1.00145.62           C  
ATOM   7693  O   ASP A 999     203.962 197.647 142.252  1.00145.62           O  
ATOM   7694  CB  ASP A 999     201.278 199.212 142.111  1.00145.62           C  
ATOM   7695  CG  ASP A 999     202.321 200.186 142.622  1.00145.62           C  
ATOM   7696  OD1 ASP A 999     202.785 201.031 141.827  1.00145.62           O  
ATOM   7697  OD2 ASP A 999     202.676 200.107 143.817  1.00145.62           O  
ATOM   7698  N   ALA A1000     202.369 196.092 142.539  1.00139.06           N  
ATOM   7699  CA  ALA A1000     203.262 195.200 143.268  1.00139.06           C  
ATOM   7700  C   ALA A1000     204.242 194.486 142.346  1.00139.06           C  
ATOM   7701  O   ALA A1000     205.308 194.063 142.805  1.00139.06           O  
ATOM   7702  CB  ALA A1000     202.452 194.175 144.062  1.00139.06           C  
ATOM   7703  N   GLU A1001     203.904 194.344 141.063  1.00136.25           N  
ATOM   7704  CA  GLU A1001     204.819 193.717 140.113  1.00136.25           C  
ATOM   7705  C   GLU A1001     206.054 194.580 139.879  1.00136.25           C  
ATOM   7706  O   GLU A1001     207.184 194.078 139.896  1.00136.25           O  
ATOM   7707  CB  GLU A1001     204.095 193.441 138.795  1.00136.25           C  
ATOM   7708  CG  GLU A1001     204.960 192.771 137.739  1.00136.25           C  
ATOM   7709  CD  GLU A1001     204.195 192.466 136.467  1.00136.25           C  
ATOM   7710  OE1 GLU A1001     202.994 192.802 136.399  1.00136.25           O  
ATOM   7711  OE2 GLU A1001     204.794 191.890 135.534  1.00136.25           O  
ATOM   7712  N   ARG A1002     205.861 195.883 139.659  1.00142.94           N  
ATOM   7713  CA  ARG A1002     207.007 196.779 139.549  1.00142.94           C  
ATOM   7714  C   ARG A1002     207.671 197.013 140.900  1.00142.94           C  
ATOM   7715  O   ARG A1002     208.878 197.273 140.957  1.00142.94           O  
ATOM   7716  CB  ARG A1002     206.587 198.109 138.920  1.00142.94           C  
ATOM   7717  CG  ARG A1002     205.578 198.907 139.727  1.00142.94           C  
ATOM   7718  CD  ARG A1002     205.272 200.229 139.046  1.00142.94           C  
ATOM   7719  NE  ARG A1002     204.560 200.044 137.785  1.00142.94           N  
ATOM   7720  CZ  ARG A1002     204.317 201.020 136.916  1.00142.94           C  
ATOM   7721  NH1 ARG A1002     204.738 202.252 137.168  1.00142.94           N  
ATOM   7722  NH2 ARG A1002     203.661 200.764 135.793  1.00142.94           N  
ATOM   7723  N   ASP A1003     206.908 196.926 141.992  1.00134.47           N  
ATOM   7724  CA  ASP A1003     207.508 197.039 143.317  1.00134.47           C  
ATOM   7725  C   ASP A1003     208.344 195.812 143.652  1.00134.47           C  
ATOM   7726  O   ASP A1003     209.346 195.920 144.369  1.00134.47           O  
ATOM   7727  CB  ASP A1003     206.422 197.248 144.372  1.00134.47           C  
ATOM   7728  CG  ASP A1003     206.992 197.499 145.754  1.00134.47           C  
ATOM   7729  OD1 ASP A1003     207.495 198.616 145.998  1.00134.47           O  
ATOM   7730  OD2 ASP A1003     206.938 196.580 146.598  1.00134.47           O  
ATOM   7731  N   PHE A1004     207.948 194.641 143.146  1.00130.33           N  
ATOM   7732  CA  PHE A1004     208.752 193.437 143.323  1.00130.33           C  
ATOM   7733  C   PHE A1004     210.090 193.538 142.602  1.00130.33           C  
ATOM   7734  O   PHE A1004     211.086 192.973 143.068  1.00130.33           O  
ATOM   7735  CB  PHE A1004     207.976 192.216 142.830  1.00130.33           C  
ATOM   7736  CG  PHE A1004     208.747 190.933 142.920  1.00130.33           C  
ATOM   7737  CD1 PHE A1004     208.973 190.331 144.145  1.00130.33           C  
ATOM   7738  CD2 PHE A1004     209.248 190.329 141.779  1.00130.33           C  
ATOM   7739  CE1 PHE A1004     209.682 189.152 144.231  1.00130.33           C  
ATOM   7740  CE2 PHE A1004     209.960 189.148 141.858  1.00130.33           C  
ATOM   7741  CZ  PHE A1004     210.177 188.559 143.087  1.00130.33           C  
ATOM   7742  N   TYR A1005     210.136 194.248 141.473  1.00134.31           N  
ATOM   7743  CA  TYR A1005     211.404 194.447 140.780  1.00134.31           C  
ATOM   7744  C   TYR A1005     212.316 195.405 141.536  1.00134.31           C  
ATOM   7745  O   TYR A1005     213.541 195.244 141.504  1.00134.31           O  
ATOM   7746  CB  TYR A1005     211.151 194.962 139.363  1.00134.31           C  
ATOM   7747  CG  TYR A1005     210.575 193.921 138.429  1.00134.31           C  
ATOM   7748  CD1 TYR A1005     210.768 192.566 138.665  1.00134.31           C  
ATOM   7749  CD2 TYR A1005     209.832 194.293 137.316  1.00134.31           C  
ATOM   7750  CE1 TYR A1005     210.244 191.611 137.815  1.00134.31           C  
ATOM   7751  CE2 TYR A1005     209.301 193.345 136.462  1.00134.31           C  
ATOM   7752  CZ  TYR A1005     209.512 192.006 136.716  1.00134.31           C  
ATOM   7753  OH  TYR A1005     208.983 191.057 135.870  1.00134.31           O  
ATOM   7754  N   HIS A1006     211.745 196.402 142.215  1.00134.91           N  
ATOM   7755  CA  HIS A1006     212.516 197.158 143.197  1.00134.91           C  
ATOM   7756  C   HIS A1006     212.918 196.280 144.375  1.00134.91           C  
ATOM   7757  O   HIS A1006     214.053 196.361 144.859  1.00134.91           O  
ATOM   7758  CB  HIS A1006     211.716 198.367 143.680  1.00134.91           C  
ATOM   7759  CG  HIS A1006     211.526 199.423 142.637  1.00134.91           C  
ATOM   7760  ND1 HIS A1006     212.545 200.257 142.228  1.00134.91           N  
ATOM   7761  CD2 HIS A1006     210.435 199.785 141.921  1.00134.91           C  
ATOM   7762  CE1 HIS A1006     212.090 201.085 141.305  1.00134.91           C  
ATOM   7763  NE2 HIS A1006     210.813 200.820 141.100  1.00134.91           N  
ATOM   7764  N   SER A1007     212.001 195.431 144.847  1.00133.25           N  
ATOM   7765  CA  SER A1007     212.260 194.644 146.048  1.00133.25           C  
ATOM   7766  C   SER A1007     213.420 193.677 145.851  1.00133.25           C  
ATOM   7767  O   SER A1007     214.108 193.329 146.818  1.00133.25           O  
ATOM   7768  CB  SER A1007     210.999 193.882 146.458  1.00133.25           C  
ATOM   7769  OG  SER A1007     209.928 194.772 146.718  1.00133.25           O  
ATOM   7770  N   LEU A1008     213.655 193.233 144.615  1.00134.60           N  
ATOM   7771  CA  LEU A1008     214.870 192.486 144.317  1.00134.60           C  
ATOM   7772  C   LEU A1008     216.063 193.401 144.061  1.00134.60           C  
ATOM   7773  O   LEU A1008     217.203 193.010 144.336  1.00134.60           O  
ATOM   7774  CB  LEU A1008     214.635 191.570 143.113  1.00134.60           C  
ATOM   7775  CG  LEU A1008     215.633 190.440 142.838  1.00134.60           C  
ATOM   7776  CD1 LEU A1008     214.914 189.248 142.232  1.00134.60           C  
ATOM   7777  CD2 LEU A1008     216.752 190.898 141.914  1.00134.60           C  
ATOM   7778  N   ARG A1009     215.831 194.612 143.548  1.00142.14           N  
ATOM   7779  CA  ARG A1009     216.945 195.505 143.242  1.00142.14           C  
ATOM   7780  C   ARG A1009     217.599 196.032 144.514  1.00142.14           C  
ATOM   7781  O   ARG A1009     218.810 195.882 144.712  1.00142.14           O  
ATOM   7782  CB  ARG A1009     216.476 196.661 142.357  1.00142.14           C  
ATOM   7783  CG  ARG A1009     217.580 197.660 142.046  1.00142.14           C  
ATOM   7784  CD  ARG A1009     217.137 198.713 141.046  1.00142.14           C  
ATOM   7785  NE  ARG A1009     216.967 198.154 139.709  1.00142.14           N  
ATOM   7786  CZ  ARG A1009     216.445 198.816 138.682  1.00142.14           C  
ATOM   7787  NH1 ARG A1009     216.038 200.069 138.836  1.00142.14           N  
ATOM   7788  NH2 ARG A1009     216.331 198.227 137.500  1.00142.14           N  
ATOM   7789  N   GLU A1010     216.813 196.654 145.394  1.00144.06           N  
ATOM   7790  CA  GLU A1010     217.354 197.192 146.635  1.00144.06           C  
ATOM   7791  C   GLU A1010     217.553 196.129 147.711  1.00144.06           C  
ATOM   7792  O   GLU A1010     217.729 196.480 148.885  1.00144.06           O  
ATOM   7793  CB  GLU A1010     216.458 198.315 147.166  1.00144.06           C  
ATOM   7794  CG  GLU A1010     216.601 199.635 146.417  1.00144.06           C  
ATOM   7795  CD  GLU A1010     215.584 199.802 145.306  1.00144.06           C  
ATOM   7796  OE1 GLU A1010     214.620 199.012 145.255  1.00144.06           O  
ATOM   7797  OE2 GLU A1010     215.749 200.726 144.482  1.00144.06           O  
ATOM   7798  N   TYR A1011     217.529 194.848 147.346  1.00132.94           N  
ATOM   7799  CA  TYR A1011     218.087 193.801 148.193  1.00132.94           C  
ATOM   7800  C   TYR A1011     219.551 193.538 147.858  1.00132.94           C  
ATOM   7801  O   TYR A1011     220.407 193.535 148.749  1.00132.94           O  
ATOM   7802  CB  TYR A1011     217.267 192.515 148.048  1.00132.94           C  
ATOM   7803  CG  TYR A1011     217.853 191.327 148.776  1.00132.94           C  
ATOM   7804  CD1 TYR A1011     217.801 191.241 150.161  1.00132.94           C  
ATOM   7805  CD2 TYR A1011     218.457 190.290 148.077  1.00132.94           C  
ATOM   7806  CE1 TYR A1011     218.336 190.155 150.830  1.00132.94           C  
ATOM   7807  CE2 TYR A1011     218.994 189.201 148.737  1.00132.94           C  
ATOM   7808  CZ  TYR A1011     218.931 189.139 150.112  1.00132.94           C  
ATOM   7809  OH  TYR A1011     219.464 188.056 150.773  1.00132.94           O  
ATOM   7810  N   ILE A1012     219.849 193.315 146.575  1.00134.14           N  
ATOM   7811  CA  ILE A1012     221.137 192.759 146.183  1.00134.14           C  
ATOM   7812  C   ILE A1012     222.255 193.786 146.296  1.00134.14           C  
ATOM   7813  O   ILE A1012     223.435 193.417 146.274  1.00134.14           O  
ATOM   7814  CB  ILE A1012     221.063 192.196 144.752  1.00134.14           C  
ATOM   7815  CG1 ILE A1012     220.643 193.291 143.771  1.00134.14           C  
ATOM   7816  CG2 ILE A1012     220.099 191.022 144.691  1.00134.14           C  
ATOM   7817  CD1 ILE A1012     220.685 192.861 142.324  1.00134.14           C  
ATOM   7818  N   ASN A1013     221.915 195.071 146.418  1.00140.39           N  
ATOM   7819  CA  ASN A1013     222.904 196.075 146.788  1.00140.39           C  
ATOM   7820  C   ASN A1013     223.348 195.949 148.239  1.00140.39           C  
ATOM   7821  O   ASN A1013     224.438 196.418 148.582  1.00140.39           O  
ATOM   7822  CB  ASN A1013     222.353 197.479 146.530  1.00140.39           C  
ATOM   7823  CG  ASN A1013     221.024 197.722 147.220  1.00140.39           C  
ATOM   7824  OD1 ASN A1013     220.508 196.855 147.925  1.00140.39           O  
ATOM   7825  ND2 ASN A1013     220.462 198.908 147.017  1.00140.39           N  
ATOM   7826  N   GLY A1014     222.533 195.331 149.097  1.00142.51           N  
ATOM   7827  CA  GLY A1014     223.013 194.968 150.418  1.00142.51           C  
ATOM   7828  C   GLY A1014     224.137 193.953 150.382  1.00142.51           C  
ATOM   7829  O   GLY A1014     225.035 193.986 151.228  1.00142.51           O  
ATOM   7830  N   LYS A1015     224.109 193.040 149.408  1.00141.46           N  
ATOM   7831  CA  LYS A1015     225.274 192.198 149.159  1.00141.46           C  
ATOM   7832  C   LYS A1015     226.427 192.999 148.569  1.00141.46           C  
ATOM   7833  O   LYS A1015     227.593 192.627 148.746  1.00141.46           O  
ATOM   7834  CB  LYS A1015     224.900 191.043 148.230  1.00141.46           C  
ATOM   7835  CG  LYS A1015     223.870 190.086 148.809  1.00141.46           C  
ATOM   7836  CD  LYS A1015     224.438 189.307 149.984  1.00141.46           C  
ATOM   7837  CE  LYS A1015     223.486 188.208 150.428  1.00141.46           C  
ATOM   7838  NZ  LYS A1015     222.246 188.761 151.039  1.00141.46           N  
ATOM   7839  N   ALA A1016     226.126 194.094 147.868  1.00153.79           N  
ATOM   7840  CA  ALA A1016     227.176 194.913 147.273  1.00153.79           C  
ATOM   7841  C   ALA A1016     227.875 195.773 148.318  1.00153.79           C  
ATOM   7842  O   ALA A1016     229.105 195.900 148.299  1.00153.79           O  
ATOM   7843  CB  ALA A1016     226.597 195.788 146.162  1.00153.79           C  
ATOM   7844  N   THR A1017     227.109 196.373 149.232  1.00156.48           N  
ATOM   7845  CA  THR A1017     227.701 197.259 150.229  1.00156.48           C  
ATOM   7846  C   THR A1017     228.566 196.494 151.222  1.00156.48           C  
ATOM   7847  O   THR A1017     229.533 197.050 151.754  1.00156.48           O  
ATOM   7848  CB  THR A1017     226.609 198.032 150.969  1.00156.48           C  
ATOM   7849  OG1 THR A1017     225.676 197.112 151.550  1.00156.48           O  
ATOM   7850  CG2 THR A1017     225.874 198.963 150.015  1.00156.48           C  
ATOM   7851  N   ALA A1018     228.238 195.227 151.487  1.00160.49           N  
ATOM   7852  CA  ALA A1018     229.053 194.437 152.403  1.00160.49           C  
ATOM   7853  C   ALA A1018     230.421 194.136 151.803  1.00160.49           C  
ATOM   7854  O   ALA A1018     231.433 194.150 152.513  1.00160.49           O  
ATOM   7855  CB  ALA A1018     228.328 193.142 152.769  1.00160.49           C  
ATOM   7856  N   LEU A1019     230.472 193.859 150.497  1.00162.75           N  
ATOM   7857  CA  LEU A1019     231.759 193.693 149.832  1.00162.75           C  
ATOM   7858  C   LEU A1019     232.510 195.014 149.734  1.00162.75           C  
ATOM   7859  O   LEU A1019     233.743 195.034 149.821  1.00162.75           O  
ATOM   7860  CB  LEU A1019     231.557 193.087 148.443  1.00162.75           C  
ATOM   7861  CG  LEU A1019     232.817 192.793 147.625  1.00162.75           C  
ATOM   7862  CD1 LEU A1019     233.696 191.779 148.341  1.00162.75           C  
ATOM   7863  CD2 LEU A1019     232.451 192.301 146.233  1.00162.75           C  
ATOM   7864  N   ALA A1020     231.788 196.124 149.558  1.00166.01           N  
ATOM   7865  CA  ALA A1020     232.435 197.430 149.497  1.00166.01           C  
ATOM   7866  C   ALA A1020     232.965 197.850 150.862  1.00166.01           C  
ATOM   7867  O   ALA A1020     234.042 198.449 150.960  1.00166.01           O  
ATOM   7868  CB  ALA A1020     231.460 198.474 148.954  1.00166.01           C  
ATOM   7869  N   ASN A1021     232.222 197.544 151.929  1.00159.86           N  
ATOM   7870  CA  ASN A1021     232.676 197.876 153.274  1.00159.86           C  
ATOM   7871  C   ASN A1021     233.807 196.972 153.742  1.00159.86           C  
ATOM   7872  O   ASN A1021     234.576 197.370 154.624  1.00159.86           O  
ATOM   7873  CB  ASN A1021     231.508 197.797 154.259  1.00159.86           C  
ATOM   7874  CG  ASN A1021     230.511 198.925 154.072  1.00159.86           C  
ATOM   7875  OD1 ASN A1021     230.892 200.082 153.896  1.00159.86           O  
ATOM   7876  ND2 ASN A1021     229.227 198.591 154.109  1.00159.86           N  
ATOM   7877  N   LEU A1022     233.929 195.771 153.176  1.00166.63           N  
ATOM   7878  CA  LEU A1022     235.009 194.870 153.566  1.00166.63           C  
ATOM   7879  C   LEU A1022     236.335 195.326 152.967  1.00166.63           C  
ATOM   7880  O   LEU A1022     237.311 195.551 153.691  1.00166.63           O  
ATOM   7881  CB  LEU A1022     234.672 193.437 153.137  1.00166.63           C  
ATOM   7882  CG  LEU A1022     235.528 192.272 153.651  1.00166.63           C  
ATOM   7883  CD1 LEU A1022     236.756 192.032 152.778  1.00166.63           C  
ATOM   7884  CD2 LEU A1022     235.934 192.501 155.100  1.00166.63           C  
ATOM   7885  N   ARG A1023     236.385 195.472 151.640  1.00176.49           N  
ATOM   7886  CA  ARG A1023     237.644 195.758 150.962  1.00176.49           C  
ATOM   7887  C   ARG A1023     238.185 197.140 151.303  1.00176.49           C  
ATOM   7888  O   ARG A1023     239.376 197.395 151.094  1.00176.49           O  
ATOM   7889  CB  ARG A1023     237.468 195.629 149.448  1.00176.49           C  
ATOM   7890  CG  ARG A1023     236.508 196.644 148.848  1.00176.49           C  
ATOM   7891  CD  ARG A1023     236.325 196.422 147.355  1.00176.49           C  
ATOM   7892  NE  ARG A1023     237.551 196.690 146.608  1.00176.49           N  
ATOM   7893  CZ  ARG A1023     237.737 196.358 145.335  1.00176.49           C  
ATOM   7894  NH1 ARG A1023     236.773 195.747 144.659  1.00176.49           N  
ATOM   7895  NH2 ARG A1023     238.885 196.640 144.735  1.00176.49           N  
ATOM   7896  N   LYS A1024     237.338 198.033 151.820  1.00168.83           N  
ATOM   7897  CA  LYS A1024     237.811 199.332 152.286  1.00168.83           C  
ATOM   7898  C   LYS A1024     238.731 199.183 153.493  1.00168.83           C  
ATOM   7899  O   LYS A1024     239.863 199.681 153.489  1.00168.83           O  
ATOM   7900  CB  LYS A1024     236.619 200.232 152.617  1.00168.83           C  
ATOM   7901  CG  LYS A1024     236.991 201.663 152.982  1.00168.83           C  
ATOM   7902  CD  LYS A1024     236.947 201.888 154.486  1.00168.83           C  
ATOM   7903  CE  LYS A1024     237.197 203.346 154.833  1.00168.83           C  
ATOM   7904  NZ  LYS A1024     237.174 203.579 156.304  1.00168.83           N  
ATOM   7905  N   SER A1025     238.261 198.499 154.536  1.00164.36           N  
ATOM   7906  CA  SER A1025     239.031 198.368 155.766  1.00164.36           C  
ATOM   7907  C   SER A1025     240.141 197.329 155.672  1.00164.36           C  
ATOM   7908  O   SER A1025     240.970 197.254 156.586  1.00164.36           O  
ATOM   7909  CB  SER A1025     238.101 198.018 156.931  1.00164.36           C  
ATOM   7910  OG  SER A1025     238.829 197.865 158.137  1.00164.36           O  
ATOM   7911  N   ARG A1026     240.183 196.532 154.605  1.00169.84           N  
ATOM   7912  CA  ARG A1026     241.252 195.563 154.405  1.00169.84           C  
ATOM   7913  C   ARG A1026     242.391 196.111 153.549  1.00169.84           C  
ATOM   7914  O   ARG A1026     243.162 195.326 152.985  1.00169.84           O  
ATOM   7915  CB  ARG A1026     240.696 194.282 153.778  1.00169.84           C  
ATOM   7916  CG  ARG A1026     239.631 193.568 154.605  1.00169.84           C  
ATOM   7917  CD  ARG A1026     240.225 192.826 155.798  1.00169.84           C  
ATOM   7918  NE  ARG A1026     240.490 193.703 156.936  1.00169.84           N  
ATOM   7919  CZ  ARG A1026     239.558 194.134 157.780  1.00169.84           C  
ATOM   7920  NH1 ARG A1026     238.294 193.763 157.624  1.00169.84           N  
ATOM   7921  NH2 ARG A1026     239.889 194.931 158.787  1.00169.84           N  
ATOM   7922  N   GLY A1027     242.513 197.435 153.441  1.00189.28           N  
ATOM   7923  CA  GLY A1027     243.633 198.077 152.795  1.00189.28           C  
ATOM   7924  C   GLY A1027     243.367 198.526 151.370  1.00189.28           C  
ATOM   7925  O   GLY A1027     243.959 199.515 150.923  1.00189.28           O  
ATOM   7926  N   MET A1028     242.497 197.825 150.650  1.00199.19           N  
ATOM   7927  CA  MET A1028     242.217 198.163 149.265  1.00199.19           C  
ATOM   7928  C   MET A1028     241.286 199.372 149.183  1.00199.19           C  
ATOM   7929  O   MET A1028     240.645 199.766 150.161  1.00199.19           O  
ATOM   7930  CB  MET A1028     241.604 196.962 148.539  1.00199.19           C  
ATOM   7931  CG  MET A1028     241.707 197.012 147.020  1.00199.19           C  
ATOM   7932  SD  MET A1028     240.987 195.566 146.218  1.00199.19           S  
ATOM   7933  CE  MET A1028     242.189 194.308 146.640  1.00199.19           C  
ATOM   7934  N   LEU A1029     241.224 199.965 147.993  1.00191.49           N  
ATOM   7935  CA  LEU A1029     240.313 201.073 147.737  1.00191.49           C  
ATOM   7936  C   LEU A1029     238.871 200.584 147.795  1.00191.49           C  
ATOM   7937  O   LEU A1029     238.482 199.682 147.046  1.00191.49           O  
ATOM   7938  CB  LEU A1029     240.613 201.704 146.380  1.00191.49           C  
ATOM   7939  CG  LEU A1029     239.781 202.935 146.013  1.00191.49           C  
ATOM   7940  CD1 LEU A1029     240.045 204.072 146.988  1.00191.49           C  
ATOM   7941  CD2 LEU A1029     240.065 203.373 144.584  1.00191.49           C  
ATOM   7942  N   GLY A1030     238.079 201.180 148.682  1.00183.76           N  
ATOM   7943  CA  GLY A1030     236.693 200.786 148.847  1.00183.76           C  
ATOM   7944  C   GLY A1030     235.767 201.446 147.847  1.00183.76           C  
ATOM   7945  O   GLY A1030     235.335 202.586 148.043  1.00183.76           O  
ATOM   7946  N   LEU A1031     235.457 200.733 146.768  1.00185.89           N  
ATOM   7947  CA  LEU A1031     234.773 201.294 145.611  1.00185.89           C  
ATOM   7948  C   LEU A1031     233.395 200.659 145.478  1.00185.89           C  
ATOM   7949  O   LEU A1031     233.259 199.433 145.549  1.00185.89           O  
ATOM   7950  CB  LEU A1031     235.601 201.089 144.338  1.00185.89           C  
ATOM   7951  CG  LEU A1031     236.154 199.692 144.033  1.00185.89           C  
ATOM   7952  CD1 LEU A1031     235.219 198.892 143.138  1.00185.89           C  
ATOM   7953  CD2 LEU A1031     237.539 199.791 143.410  1.00185.89           C  
ATOM   7954  N   LEU A1032     232.375 201.501 145.310  1.00205.65           N  
ATOM   7955  CA  LEU A1032     231.015 201.039 145.059  1.00205.65           C  
ATOM   7956  C   LEU A1032     230.410 201.736 143.846  1.00205.65           C  
ATOM   7957  O   LEU A1032     229.552 201.170 143.161  1.00205.65           O  
ATOM   7958  CB  LEU A1032     230.132 201.256 146.293  1.00205.65           C  
ATOM   7959  CG  LEU A1032     229.612 202.665 146.597  1.00205.65           C  
ATOM   7960  CD1 LEU A1032     228.421 202.596 147.542  1.00205.65           C  
ATOM   7961  CD2 LEU A1032     230.703 203.551 147.181  1.00205.65           C  
ATOM   7962  N   GLU A1033     230.851 202.962 143.574  1.00235.09           N  
ATOM   7963  CA  GLU A1033     230.383 203.697 142.407  1.00235.09           C  
ATOM   7964  C   GLU A1033     231.045 203.165 141.136  1.00235.09           C  
ATOM   7965  O   GLU A1033     232.212 202.764 141.162  1.00235.09           O  
ATOM   7966  CB  GLU A1033     230.671 205.191 142.562  1.00235.09           C  
ATOM   7967  CG  GLU A1033     232.120 205.527 142.886  1.00235.09           C  
ATOM   7968  CD  GLU A1033     232.971 205.715 141.645  1.00235.09           C  
ATOM   7969  OE1 GLU A1033     232.398 205.952 140.561  1.00235.09           O  
ATOM   7970  OE2 GLU A1033     234.212 205.626 141.753  1.00235.09           O  
ATOM   7971  N   PRO A1034     230.321 203.144 140.021  1.00246.66           N  
ATOM   7972  CA  PRO A1034     230.936 202.810 138.733  1.00246.66           C  
ATOM   7973  C   PRO A1034     231.756 203.970 138.201  1.00246.66           C  
ATOM   7974  O   PRO A1034     231.239 205.083 138.018  1.00246.66           O  
ATOM   7975  CB  PRO A1034     229.728 202.520 137.828  1.00246.66           C  
ATOM   7976  CG  PRO A1034     228.606 203.282 138.442  1.00246.66           C  
ATOM   7977  CD  PRO A1034     228.858 203.291 139.923  1.00246.66           C  
ATOM   7978  N   PRO A1035     233.043 203.749 137.944  1.00267.25           N  
ATOM   7979  CA  PRO A1035     233.884 204.819 137.399  1.00267.25           C  
ATOM   7980  C   PRO A1035     233.520 205.156 135.962  1.00267.25           C  
ATOM   7981  O   PRO A1035     233.010 204.324 135.207  1.00267.25           O  
ATOM   7982  CB  PRO A1035     235.300 204.237 137.489  1.00267.25           C  
ATOM   7983  CG  PRO A1035     235.098 202.759 137.461  1.00267.25           C  
ATOM   7984  CD  PRO A1035     233.803 202.510 138.183  1.00267.25           C  
ATOM   7985  N   ALA A1036     233.792 206.405 135.593  1.00320.68           N  
ATOM   7986  CA  ALA A1036     233.363 206.969 134.320  1.00320.68           C  
ATOM   7987  C   ALA A1036     234.280 206.469 133.204  1.00320.68           C  
ATOM   7988  O   ALA A1036     235.098 205.565 133.395  1.00320.68           O  
ATOM   7989  CB  ALA A1036     233.335 208.493 134.401  1.00320.68           C  
ATOM   7990  N   LYS A1037     234.152 207.056 132.015  1.00357.66           N  
ATOM   7991  CA  LYS A1037     234.990 206.683 130.876  1.00357.66           C  
ATOM   7992  C   LYS A1037     236.379 207.270 131.091  1.00357.66           C  
ATOM   7993  O   LYS A1037     236.674 208.404 130.711  1.00357.66           O  
ATOM   7994  CB  LYS A1037     234.373 207.171 129.571  1.00357.66           C  
ATOM   7995  CG  LYS A1037     232.971 206.640 129.283  1.00357.66           C  
ATOM   7996  CD  LYS A1037     232.982 205.158 128.927  1.00357.66           C  
ATOM   7997  CE  LYS A1037     232.521 204.288 130.088  1.00357.66           C  
ATOM   7998  NZ  LYS A1037     232.440 202.853 129.700  1.00357.66           N  
ATOM   7999  N   GLU A1038     237.239 206.472 131.712  1.00367.32           N  
ATOM   8000  CA  GLU A1038     238.593 206.877 132.072  1.00367.32           C  
ATOM   8001  C   GLU A1038     239.516 205.710 131.739  1.00367.32           C  
ATOM   8002  O   GLU A1038     239.190 204.848 130.916  1.00367.32           O  
ATOM   8003  CB  GLU A1038     238.645 207.321 133.543  1.00367.32           C  
ATOM   8004  CG  GLU A1038     238.098 206.304 134.535  1.00367.32           C  
ATOM   8005  CD  GLU A1038     239.160 205.360 135.063  1.00367.32           C  
ATOM   8006  OE1 GLU A1038     240.358 205.697 134.966  1.00367.32           O  
ATOM   8007  OE2 GLU A1038     238.795 204.282 135.578  1.00367.32           O  
ATOM   8008  N   LEU A1039     240.690 205.677 132.370  1.00376.29           N  
ATOM   8009  CA  LEU A1039     241.612 204.564 132.179  1.00376.29           C  
ATOM   8010  C   LEU A1039     240.963 203.280 132.680  1.00376.29           C  
ATOM   8011  O   LEU A1039     240.866 203.052 133.891  1.00376.29           O  
ATOM   8012  CB  LEU A1039     242.937 204.831 132.901  1.00376.29           C  
ATOM   8013  CG  LEU A1039     244.124 203.915 132.588  1.00376.29           C  
ATOM   8014  CD1 LEU A1039     245.426 204.699 132.649  1.00376.29           C  
ATOM   8015  CD2 LEU A1039     244.176 202.730 133.544  1.00376.29           C  
ATOM   8016  N   GLN A1040     240.520 202.436 131.753  1.00373.47           N  
ATOM   8017  CA  GLN A1040     239.718 201.271 132.100  1.00373.47           C  
ATOM   8018  C   GLN A1040     240.598 200.108 132.533  1.00373.47           C  
ATOM   8019  O   GLN A1040     241.652 199.849 131.945  1.00373.47           O  
ATOM   8020  CB  GLN A1040     238.848 200.849 130.915  1.00373.47           C  
ATOM   8021  CG  GLN A1040     237.797 201.873 130.513  1.00373.47           C  
ATOM   8022  CD  GLN A1040     236.745 202.079 131.585  1.00373.47           C  
ATOM   8023  OE1 GLN A1040     236.268 201.122 132.194  1.00373.47           O  
ATOM   8024  NE2 GLN A1040     236.375 203.333 131.819  1.00373.47           N  
ATOM   8025  N   GLY A1041     240.154 199.408 133.573  1.00360.90           N  
ATOM   8026  CA  GLY A1041     240.932 198.347 134.179  1.00360.90           C  
ATOM   8027  C   GLY A1041     242.130 198.846 134.957  1.00360.90           C  
ATOM   8028  O   GLY A1041     243.266 198.444 134.686  1.00360.90           O  
ATOM   8029  N   ILE A1042     241.890 199.733 135.926  1.00344.71           N  
ATOM   8030  CA  ILE A1042     242.960 200.154 136.825  1.00344.71           C  
ATOM   8031  C   ILE A1042     243.477 198.973 137.635  1.00344.71           C  
ATOM   8032  O   ILE A1042     244.671 198.905 137.955  1.00344.71           O  
ATOM   8033  CB  ILE A1042     242.479 201.312 137.724  1.00344.71           C  
ATOM   8034  CG1 ILE A1042     241.081 201.030 138.285  1.00344.71           C  
ATOM   8035  CG2 ILE A1042     242.503 202.625 136.955  1.00344.71           C  
ATOM   8036  CD1 ILE A1042     241.071 200.407 139.665  1.00344.71           C  
ATOM   8037  N   ASP A1043     242.596 198.026 137.974  1.00324.23           N  
ATOM   8038  CA  ASP A1043     242.944 196.676 138.407  1.00324.23           C  
ATOM   8039  C   ASP A1043     243.910 196.678 139.587  1.00324.23           C  
ATOM   8040  O   ASP A1043     245.115 196.467 139.401  1.00324.23           O  
ATOM   8041  CB  ASP A1043     243.547 195.888 137.241  1.00324.23           C  
ATOM   8042  CG  ASP A1043     243.691 194.409 137.548  1.00324.23           C  
ATOM   8043  OD1 ASP A1043     242.668 193.692 137.530  1.00324.23           O  
ATOM   8044  OD2 ASP A1043     244.829 193.963 137.803  1.00324.23           O  
ATOM   8045  N   PRO A1044     243.430 196.916 140.811  1.00308.90           N  
ATOM   8046  CA  PRO A1044     244.352 197.165 141.931  1.00308.90           C  
ATOM   8047  C   PRO A1044     245.084 195.912 142.394  1.00308.90           C  
ATOM   8048  O   PRO A1044     245.639 195.885 143.497  1.00308.90           O  
ATOM   8049  CB  PRO A1044     243.425 197.700 143.032  1.00308.90           C  
ATOM   8050  CG  PRO A1044     242.193 198.165 142.313  1.00308.90           C  
ATOM   8051  CD  PRO A1044     242.035 197.207 141.176  1.00308.90           C  
ATOM   8052  N   ASP A1045     245.080 194.867 141.563  1.00310.30           N  
ATOM   8053  CA  ASP A1045     245.904 193.690 141.823  1.00310.30           C  
ATOM   8054  C   ASP A1045     247.376 194.058 141.978  1.00310.30           C  
ATOM   8055  O   ASP A1045     248.038 193.627 142.929  1.00310.30           O  
ATOM   8056  CB  ASP A1045     245.717 192.668 140.700  1.00310.30           C  
ATOM   8057  CG  ASP A1045     246.425 191.357 140.980  1.00310.30           C  
ATOM   8058  OD1 ASP A1045     245.893 190.550 141.770  1.00310.30           O  
ATOM   8059  OD2 ASP A1045     247.512 191.131 140.407  1.00310.30           O  
ATOM   8060  N   GLU A1046     247.911 194.855 141.049  1.00323.22           N  
ATOM   8061  CA  GLU A1046     249.319 195.228 141.131  1.00323.22           C  
ATOM   8062  C   GLU A1046     249.597 196.256 142.221  1.00323.22           C  
ATOM   8063  O   GLU A1046     250.757 196.418 142.614  1.00323.22           O  
ATOM   8064  CB  GLU A1046     249.811 195.754 139.781  1.00323.22           C  
ATOM   8065  CG  GLU A1046     249.150 197.043 139.327  1.00323.22           C  
ATOM   8066  CD  GLU A1046     247.967 196.794 138.415  1.00323.22           C  
ATOM   8067  OE1 GLU A1046     247.545 195.625 138.293  1.00323.22           O  
ATOM   8068  OE2 GLU A1046     247.460 197.767 137.817  1.00323.22           O  
ATOM   8069  N   THR A1047     248.574 196.951 142.719  1.00306.90           N  
ATOM   8070  CA  THR A1047     248.806 197.987 143.721  1.00306.90           C  
ATOM   8071  C   THR A1047     249.061 197.374 145.094  1.00306.90           C  
ATOM   8072  O   THR A1047     250.138 197.547 145.675  1.00306.90           O  
ATOM   8073  CB  THR A1047     247.615 198.947 143.778  1.00306.90           C  
ATOM   8074  OG1 THR A1047     246.441 198.230 144.178  1.00306.90           O  
ATOM   8075  CG2 THR A1047     247.377 199.583 142.417  1.00306.90           C  
ATOM   8076  N   VAL A1048     248.077 196.657 145.626  1.00279.35           N  
ATOM   8077  CA  VAL A1048     248.187 196.027 146.939  1.00279.35           C  
ATOM   8078  C   VAL A1048     248.988 194.737 146.791  1.00279.35           C  
ATOM   8079  O   VAL A1048     249.071 194.189 145.683  1.00279.35           O  
ATOM   8080  CB  VAL A1048     246.800 195.763 147.548  1.00279.35           C  
ATOM   8081  CG1 VAL A1048     246.087 197.077 147.827  1.00279.35           C  
ATOM   8082  CG2 VAL A1048     245.969 194.886 146.625  1.00279.35           C  
ATOM   8083  N   PRO A1049     249.594 194.222 147.858  1.00260.33           N  
ATOM   8084  CA  PRO A1049     250.291 192.934 147.762  1.00260.33           C  
ATOM   8085  C   PRO A1049     249.303 191.784 147.625  1.00260.33           C  
ATOM   8086  O   PRO A1049     248.090 191.937 147.779  1.00260.33           O  
ATOM   8087  CB  PRO A1049     251.074 192.852 149.075  1.00260.33           C  
ATOM   8088  CG  PRO A1049     250.307 193.719 150.017  1.00260.33           C  
ATOM   8089  CD  PRO A1049     249.785 194.850 149.178  1.00260.33           C  
ATOM   8090  N   ASP A1050     249.853 190.604 147.332  1.00248.84           N  
ATOM   8091  CA  ASP A1050     249.026 189.426 147.095  1.00248.84           C  
ATOM   8092  C   ASP A1050     248.408 188.870 148.371  1.00248.84           C  
ATOM   8093  O   ASP A1050     247.562 187.973 148.287  1.00248.84           O  
ATOM   8094  CB  ASP A1050     249.850 188.339 146.401  1.00248.84           C  
ATOM   8095  CG  ASP A1050     251.133 188.015 147.144  1.00248.84           C  
ATOM   8096  OD1 ASP A1050     251.439 188.706 148.139  1.00248.84           O  
ATOM   8097  OD2 ASP A1050     251.836 187.069 146.731  1.00248.84           O  
ATOM   8098  N   ASN A1051     248.806 189.376 149.540  1.00233.89           N  
ATOM   8099  CA  ASN A1051     248.135 188.999 150.780  1.00233.89           C  
ATOM   8100  C   ASN A1051     246.703 189.517 150.820  1.00233.89           C  
ATOM   8101  O   ASN A1051     245.832 188.882 151.425  1.00233.89           O  
ATOM   8102  CB  ASN A1051     248.924 189.521 151.981  1.00233.89           C  
ATOM   8103  CG  ASN A1051     248.542 188.830 153.276  1.00233.89           C  
ATOM   8104  OD1 ASN A1051     247.737 187.899 153.284  1.00233.89           O  
ATOM   8105  ND2 ASN A1051     249.122 189.284 154.381  1.00233.89           N  
ATOM   8106  N   VAL A1052     246.442 190.659 150.183  1.00232.09           N  
ATOM   8107  CA  VAL A1052     245.090 191.208 150.149  1.00232.09           C  
ATOM   8108  C   VAL A1052     244.219 190.451 149.153  1.00232.09           C  
ATOM   8109  O   VAL A1052     243.039 190.195 149.416  1.00232.09           O  
ATOM   8110  CB  VAL A1052     245.142 192.714 149.832  1.00232.09           C  
ATOM   8111  CG1 VAL A1052     243.739 193.298 149.782  1.00232.09           C  
ATOM   8112  CG2 VAL A1052     245.993 193.444 150.860  1.00232.09           C  
ATOM   8113  N   LYS A1053     244.780 190.076 148.000  1.00246.83           N  
ATOM   8114  CA  LYS A1053     244.021 189.277 147.042  1.00246.83           C  
ATOM   8115  C   LYS A1053     243.723 187.885 147.581  1.00246.83           C  
ATOM   8116  O   LYS A1053     242.680 187.306 147.255  1.00246.83           O  
ATOM   8117  CB  LYS A1053     244.771 189.174 145.713  1.00246.83           C  
ATOM   8118  CG  LYS A1053     244.498 190.315 144.745  1.00246.83           C  
ATOM   8119  CD  LYS A1053     245.330 191.541 145.074  1.00246.83           C  
ATOM   8120  CE  LYS A1053     246.805 191.272 144.826  1.00246.83           C  
ATOM   8121  NZ  LYS A1053     247.635 192.492 145.004  1.00246.83           N  
ATOM   8122  N   THR A1054     244.616 187.333 148.402  1.00229.10           N  
ATOM   8123  CA  THR A1054     244.339 186.123 149.162  1.00229.10           C  
ATOM   8124  C   THR A1054     243.694 186.416 150.513  1.00229.10           C  
ATOM   8125  O   THR A1054     243.764 185.578 151.419  1.00229.10           O  
ATOM   8126  CB  THR A1054     245.623 185.315 149.360  1.00229.10           C  
ATOM   8127  OG1 THR A1054     246.584 186.105 150.073  1.00229.10           O  
ATOM   8128  CG2 THR A1054     246.208 184.905 148.016  1.00229.10           C  
ATOM   8129  N   SER A1055     243.079 187.587 150.669  1.00209.26           N  
ATOM   8130  CA  SER A1055     242.200 187.866 151.799  1.00209.26           C  
ATOM   8131  C   SER A1055     240.775 188.174 151.370  1.00209.26           C  
ATOM   8132  O   SER A1055     239.829 187.611 151.933  1.00209.26           O  
ATOM   8133  CB  SER A1055     242.762 189.034 152.626  1.00209.26           C  
ATOM   8134  OG  SER A1055     241.868 189.400 153.662  1.00209.26           O  
ATOM   8135  N   VAL A1056     240.591 189.054 150.385  1.00199.80           N  
ATOM   8136  CA  VAL A1056     239.244 189.435 149.969  1.00199.80           C  
ATOM   8137  C   VAL A1056     238.569 188.291 149.222  1.00199.80           C  
ATOM   8138  O   VAL A1056     237.416 187.940 149.498  1.00199.80           O  
ATOM   8139  CB  VAL A1056     239.288 190.716 149.118  1.00199.80           C  
ATOM   8140  CG1 VAL A1056     237.889 191.100 148.662  1.00199.80           C  
ATOM   8141  CG2 VAL A1056     239.932 191.851 149.900  1.00199.80           C  
ATOM   8142  N   SER A1057     239.279 187.689 148.265  1.00188.74           N  
ATOM   8143  CA  SER A1057     238.716 186.585 147.496  1.00188.74           C  
ATOM   8144  C   SER A1057     238.617 185.294 148.299  1.00188.74           C  
ATOM   8145  O   SER A1057     237.894 184.381 147.888  1.00188.74           O  
ATOM   8146  CB  SER A1057     239.549 186.346 146.236  1.00188.74           C  
ATOM   8147  OG  SER A1057     239.038 185.259 145.484  1.00188.74           O  
ATOM   8148  N   GLN A1058     239.318 185.193 149.428  1.00191.44           N  
ATOM   8149  CA  GLN A1058     239.282 183.972 150.225  1.00191.44           C  
ATOM   8150  C   GLN A1058     238.115 183.936 151.206  1.00191.44           C  
ATOM   8151  O   GLN A1058     237.556 182.862 151.455  1.00191.44           O  
ATOM   8152  CB  GLN A1058     240.603 183.797 150.979  1.00191.44           C  
ATOM   8153  CG  GLN A1058     241.784 183.473 150.079  1.00191.44           C  
ATOM   8154  CD  GLN A1058     241.609 182.164 149.335  1.00191.44           C  
ATOM   8155  OE1 GLN A1058     241.405 182.149 148.121  1.00191.44           O  
ATOM   8156  NE2 GLN A1058     241.689 181.056 150.062  1.00191.44           N  
ATOM   8157  N   LEU A1059     237.730 185.080 151.774  1.00178.95           N  
ATOM   8158  CA  LEU A1059     236.605 185.095 152.705  1.00178.95           C  
ATOM   8159  C   LEU A1059     235.289 184.845 151.979  1.00178.95           C  
ATOM   8160  O   LEU A1059     234.615 183.836 152.219  1.00178.95           O  
ATOM   8161  CB  LEU A1059     236.565 186.420 153.470  1.00178.95           C  
ATOM   8162  CG  LEU A1059     237.273 186.435 154.829  1.00178.95           C  
ATOM   8163  CD1 LEU A1059     238.784 186.359 154.674  1.00178.95           C  
ATOM   8164  CD2 LEU A1059     236.873 187.666 155.630  1.00178.95           C  
ATOM   8165  N   TYR A1060     234.904 185.752 151.083  1.00167.31           N  
ATOM   8166  CA  TYR A1060     233.735 185.525 150.246  1.00167.31           C  
ATOM   8167  C   TYR A1060     233.902 186.268 148.929  1.00167.31           C  
ATOM   8168  O   TYR A1060     234.714 187.188 148.807  1.00167.31           O  
ATOM   8169  CB  TYR A1060     232.441 185.955 150.951  1.00167.31           C  
ATOM   8170  CG  TYR A1060     232.383 187.420 151.327  1.00167.31           C  
ATOM   8171  CD1 TYR A1060     232.875 187.863 152.548  1.00167.31           C  
ATOM   8172  CD2 TYR A1060     231.822 188.357 150.469  1.00167.31           C  
ATOM   8173  CE1 TYR A1060     232.819 189.200 152.899  1.00167.31           C  
ATOM   8174  CE2 TYR A1060     231.762 189.695 150.811  1.00167.31           C  
ATOM   8175  CZ  TYR A1060     232.262 190.110 152.027  1.00167.31           C  
ATOM   8176  OH  TYR A1060     232.204 191.441 152.372  1.00167.31           O  
ATOM   8177  N   ARG A1061     233.111 185.852 147.944  1.00161.74           N  
ATOM   8178  CA  ARG A1061     233.335 186.227 146.555  1.00161.74           C  
ATOM   8179  C   ARG A1061     232.027 186.062 145.798  1.00161.74           C  
ATOM   8180  O   ARG A1061     231.158 185.278 146.189  1.00161.74           O  
ATOM   8181  CB  ARG A1061     234.447 185.390 145.916  1.00161.74           C  
ATOM   8182  CG  ARG A1061     234.207 183.890 145.965  1.00161.74           C  
ATOM   8183  CD  ARG A1061     235.412 183.123 145.445  1.00161.74           C  
ATOM   8184  NE  ARG A1061     235.616 183.327 144.014  1.00161.74           N  
ATOM   8185  CZ  ARG A1061     236.764 183.099 143.384  1.00161.74           C  
ATOM   8186  NH1 ARG A1061     237.821 182.674 144.061  1.00161.74           N  
ATOM   8187  NH2 ARG A1061     236.859 183.311 142.078  1.00161.74           N  
ATOM   8188  N   ILE A1062     231.894 186.812 144.706  1.00145.07           N  
ATOM   8189  CA  ILE A1062     230.686 186.797 143.888  1.00145.07           C  
ATOM   8190  C   ILE A1062     231.113 186.614 142.438  1.00145.07           C  
ATOM   8191  O   ILE A1062     231.703 187.521 141.839  1.00145.07           O  
ATOM   8192  CB  ILE A1062     229.852 188.076 144.053  1.00145.07           C  
ATOM   8193  CG1 ILE A1062     229.325 188.192 145.485  1.00145.07           C  
ATOM   8194  CG2 ILE A1062     228.701 188.093 143.058  1.00145.07           C  
ATOM   8195  CD1 ILE A1062     228.735 189.547 145.809  1.00145.07           C  
ATOM   8196  N   SER A1063     230.818 185.444 141.878  1.00144.47           N  
ATOM   8197  CA  SER A1063     231.114 185.142 140.489  1.00144.47           C  
ATOM   8198  C   SER A1063     230.054 185.749 139.572  1.00144.47           C  
ATOM   8199  O   SER A1063     228.995 186.204 140.012  1.00144.47           O  
ATOM   8200  CB  SER A1063     231.202 183.631 140.276  1.00144.47           C  
ATOM   8201  OG  SER A1063     231.415 183.320 138.910  1.00144.47           O  
ATOM   8202  N   GLU A1064     230.352 185.751 138.272  1.00146.57           N  
ATOM   8203  CA  GLU A1064     229.459 186.392 137.313  1.00146.57           C  
ATOM   8204  C   GLU A1064     228.238 185.523 137.040  1.00146.57           C  
ATOM   8205  O   GLU A1064     227.122 186.037 136.903  1.00146.57           O  
ATOM   8206  CB  GLU A1064     230.208 186.691 136.014  1.00146.57           C  
ATOM   8207  CG  GLU A1064     229.514 187.697 135.107  1.00146.57           C  
ATOM   8208  CD  GLU A1064     228.516 187.047 134.168  1.00146.57           C  
ATOM   8209  OE1 GLU A1064     228.689 185.851 133.850  1.00146.57           O  
ATOM   8210  OE2 GLU A1064     227.560 187.730 133.747  1.00146.57           O  
ATOM   8211  N   LYS A1065     228.435 184.205 136.960  1.00134.07           N  
ATOM   8212  CA  LYS A1065     227.310 183.284 136.855  1.00134.07           C  
ATOM   8213  C   LYS A1065     226.495 183.251 138.143  1.00134.07           C  
ATOM   8214  O   LYS A1065     225.298 182.944 138.109  1.00134.07           O  
ATOM   8215  CB  LYS A1065     227.813 181.886 136.492  1.00134.07           C  
ATOM   8216  CG  LYS A1065     226.716 180.876 136.189  1.00134.07           C  
ATOM   8217  CD  LYS A1065     227.302 179.536 135.775  1.00134.07           C  
ATOM   8218  CE  LYS A1065     226.211 178.516 135.495  1.00134.07           C  
ATOM   8219  NZ  LYS A1065     226.775 177.194 135.108  1.00134.07           N  
ATOM   8220  N   SER A1066     227.119 183.569 139.280  1.00135.24           N  
ATOM   8221  CA  SER A1066     226.466 183.463 140.581  1.00135.24           C  
ATOM   8222  C   SER A1066     225.354 184.484 140.783  1.00135.24           C  
ATOM   8223  O   SER A1066     224.696 184.450 141.830  1.00135.24           O  
ATOM   8224  CB  SER A1066     227.502 183.612 141.698  1.00135.24           C  
ATOM   8225  OG  SER A1066     228.436 182.547 141.679  1.00135.24           O  
ATOM   8226  N   VAL A1067     225.123 185.382 139.827  1.00121.22           N  
ATOM   8227  CA  VAL A1067     223.973 186.267 139.871  1.00121.22           C  
ATOM   8228  C   VAL A1067     222.959 185.950 138.775  1.00121.22           C  
ATOM   8229  O   VAL A1067     221.756 186.146 138.985  1.00121.22           O  
ATOM   8230  CB  VAL A1067     224.422 187.742 139.792  1.00121.22           C  
ATOM   8231  CG1 VAL A1067     223.232 188.687 139.910  1.00121.22           C  
ATOM   8232  CG2 VAL A1067     225.451 188.040 140.872  1.00121.22           C  
ATOM   8233  N   ARG A1068     223.403 185.436 137.626  1.00133.18           N  
ATOM   8234  CA  ARG A1068     222.487 185.156 136.527  1.00133.18           C  
ATOM   8235  C   ARG A1068     221.638 183.920 136.787  1.00133.18           C  
ATOM   8236  O   ARG A1068     220.588 183.760 136.156  1.00133.18           O  
ATOM   8237  CB  ARG A1068     223.267 184.987 135.222  1.00133.18           C  
ATOM   8238  CG  ARG A1068     223.932 186.261 134.726  1.00133.18           C  
ATOM   8239  CD  ARG A1068     224.563 186.058 133.358  1.00133.18           C  
ATOM   8240  NE  ARG A1068     225.288 187.243 132.908  1.00133.18           N  
ATOM   8241  CZ  ARG A1068     224.735 188.249 132.239  1.00133.18           C  
ATOM   8242  NH1 ARG A1068     225.472 189.289 131.875  1.00133.18           N  
ATOM   8243  NH2 ARG A1068     223.444 188.217 131.937  1.00133.18           N  
ATOM   8244  N   LYS A1069     222.068 183.046 137.697  1.00122.59           N  
ATOM   8245  CA  LYS A1069     221.218 181.985 138.222  1.00122.59           C  
ATOM   8246  C   LYS A1069     220.458 182.392 139.475  1.00122.59           C  
ATOM   8247  O   LYS A1069     219.499 181.707 139.849  1.00122.59           O  
ATOM   8248  CB  LYS A1069     222.054 180.736 138.522  1.00122.59           C  
ATOM   8249  CG  LYS A1069     222.756 180.150 137.308  1.00122.59           C  
ATOM   8250  CD  LYS A1069     221.756 179.561 136.326  1.00122.59           C  
ATOM   8251  CE  LYS A1069     221.189 178.246 136.839  1.00122.59           C  
ATOM   8252  NZ  LYS A1069     220.311 177.587 135.833  1.00122.59           N  
ATOM   8253  N   PHE A1070     220.860 183.480 140.134  1.00116.34           N  
ATOM   8254  CA  PHE A1070     220.126 183.950 141.305  1.00116.34           C  
ATOM   8255  C   PHE A1070     218.785 184.551 140.903  1.00116.34           C  
ATOM   8256  O   PHE A1070     217.723 184.044 141.285  1.00116.34           O  
ATOM   8257  CB  PHE A1070     220.963 184.968 142.081  1.00116.34           C  
ATOM   8258  CG  PHE A1070     220.230 185.603 143.228  1.00116.34           C  
ATOM   8259  CD1 PHE A1070     220.002 184.898 144.399  1.00116.34           C  
ATOM   8260  CD2 PHE A1070     219.767 186.905 143.135  1.00116.34           C  
ATOM   8261  CE1 PHE A1070     219.324 185.480 145.454  1.00116.34           C  
ATOM   8262  CE2 PHE A1070     219.090 187.493 144.188  1.00116.34           C  
ATOM   8263  CZ  PHE A1070     218.869 186.779 145.349  1.00116.34           C  
ATOM   8264  N   LEU A1071     218.810 185.635 140.132  1.00112.37           N  
ATOM   8265  CA  LEU A1071     217.581 186.298 139.721  1.00112.37           C  
ATOM   8266  C   LEU A1071     216.929 185.639 138.510  1.00112.37           C  
ATOM   8267  O   LEU A1071     215.954 186.181 137.982  1.00112.37           O  
ATOM   8268  CB  LEU A1071     217.852 187.778 139.433  1.00112.37           C  
ATOM   8269  CG  LEU A1071     219.095 188.141 138.614  1.00112.37           C  
ATOM   8270  CD1 LEU A1071     218.813 188.088 137.118  1.00112.37           C  
ATOM   8271  CD2 LEU A1071     219.616 189.514 139.014  1.00112.37           C  
ATOM   8272  N   GLU A1072     217.439 184.490 138.062  1.00114.25           N  
ATOM   8273  CA  GLU A1072     216.677 183.641 137.153  1.00114.25           C  
ATOM   8274  C   GLU A1072     215.581 182.889 137.898  1.00114.25           C  
ATOM   8275  O   GLU A1072     214.405 182.958 137.526  1.00114.25           O  
ATOM   8276  CB  GLU A1072     217.613 182.664 136.437  1.00114.25           C  
ATOM   8277  CG  GLU A1072     217.018 182.018 135.193  1.00114.25           C  
ATOM   8278  CD  GLU A1072     216.190 180.788 135.507  1.00114.25           C  
ATOM   8279  OE1 GLU A1072     216.471 180.126 136.528  1.00114.25           O  
ATOM   8280  OE2 GLU A1072     215.258 180.482 134.734  1.00114.25           O  
ATOM   8281  N   ILE A1073     215.955 182.164 138.956  1.00110.23           N  
ATOM   8282  CA  ILE A1073     214.978 181.414 139.734  1.00110.23           C  
ATOM   8283  C   ILE A1073     214.136 182.329 140.609  1.00110.23           C  
ATOM   8284  O   ILE A1073     213.026 181.952 141.005  1.00110.23           O  
ATOM   8285  CB  ILE A1073     215.678 180.340 140.589  1.00110.23           C  
ATOM   8286  CG1 ILE A1073     216.670 180.988 141.557  1.00110.23           C  
ATOM   8287  CG2 ILE A1073     216.381 179.325 139.701  1.00110.23           C  
ATOM   8288  CD1 ILE A1073     217.245 180.029 142.576  1.00110.23           C  
ATOM   8289  N   ALA A1074     214.631 183.529 140.926  1.00110.86           N  
ATOM   8290  CA  ALA A1074     213.864 184.448 141.757  1.00110.86           C  
ATOM   8291  C   ALA A1074     212.684 185.058 141.014  1.00110.86           C  
ATOM   8292  O   ALA A1074     211.754 185.554 141.658  1.00110.86           O  
ATOM   8293  CB  ALA A1074     214.772 185.556 142.292  1.00110.86           C  
ATOM   8294  N   LEU A1075     212.695 185.034 139.681  1.00107.50           N  
ATOM   8295  CA  LEU A1075     211.517 185.367 138.893  1.00107.50           C  
ATOM   8296  C   LEU A1075     210.947 184.165 138.156  1.00107.50           C  
ATOM   8297  O   LEU A1075     209.928 184.302 137.470  1.00107.50           O  
ATOM   8298  CB  LEU A1075     211.831 186.496 137.899  1.00107.50           C  
ATOM   8299  CG  LEU A1075     212.852 186.299 136.774  1.00107.50           C  
ATOM   8300  CD1 LEU A1075     212.196 185.769 135.506  1.00107.50           C  
ATOM   8301  CD2 LEU A1075     213.559 187.615 136.489  1.00107.50           C  
ATOM   8302  N   PHE A1076     211.572 182.992 138.276  1.00104.57           N  
ATOM   8303  CA  PHE A1076     210.909 181.758 137.871  1.00104.57           C  
ATOM   8304  C   PHE A1076     209.911 181.301 138.927  1.00104.57           C  
ATOM   8305  O   PHE A1076     208.856 180.751 138.591  1.00104.57           O  
ATOM   8306  CB  PHE A1076     211.945 180.666 137.603  1.00104.57           C  
ATOM   8307  CG  PHE A1076     211.348 179.358 137.167  1.00104.57           C  
ATOM   8308  CD1 PHE A1076     210.836 179.207 135.888  1.00104.57           C  
ATOM   8309  CD2 PHE A1076     211.300 178.279 138.034  1.00104.57           C  
ATOM   8310  CE1 PHE A1076     210.287 178.004 135.483  1.00104.57           C  
ATOM   8311  CE2 PHE A1076     210.752 177.074 137.635  1.00104.57           C  
ATOM   8312  CZ  PHE A1076     210.245 176.937 136.358  1.00104.57           C  
ATOM   8313  N   LYS A1077     210.227 181.520 140.205  1.00102.96           N  
ATOM   8314  CA  LYS A1077     209.272 181.222 141.264  1.00102.96           C  
ATOM   8315  C   LYS A1077     208.206 182.303 141.375  1.00102.96           C  
ATOM   8316  O   LYS A1077     207.055 182.001 141.709  1.00102.96           O  
ATOM   8317  CB  LYS A1077     210.003 181.062 142.597  1.00102.96           C  
ATOM   8318  CG  LYS A1077     210.750 179.748 142.734  1.00102.96           C  
ATOM   8319  CD  LYS A1077     211.386 179.612 144.105  1.00102.96           C  
ATOM   8320  CE  LYS A1077     212.112 178.287 144.238  1.00102.96           C  
ATOM   8321  NZ  LYS A1077     212.782 178.150 145.558  1.00102.96           N  
ATOM   8322  N   TYR A1078     208.570 183.558 141.103  1.00105.53           N  
ATOM   8323  CA  TYR A1078     207.596 184.644 141.155  1.00105.53           C  
ATOM   8324  C   TYR A1078     206.557 184.492 140.053  1.00105.53           C  
ATOM   8325  O   TYR A1078     205.352 184.637 140.293  1.00105.53           O  
ATOM   8326  CB  TYR A1078     208.305 185.994 141.046  1.00105.53           C  
ATOM   8327  CG  TYR A1078     207.358 187.171 140.954  1.00105.53           C  
ATOM   8328  CD1 TYR A1078     206.610 187.573 142.053  1.00105.53           C  
ATOM   8329  CD2 TYR A1078     207.211 187.877 139.768  1.00105.53           C  
ATOM   8330  CE1 TYR A1078     205.742 188.646 141.973  1.00105.53           C  
ATOM   8331  CE2 TYR A1078     206.347 188.952 139.678  1.00105.53           C  
ATOM   8332  CZ  TYR A1078     205.614 189.332 140.783  1.00105.53           C  
ATOM   8333  OH  TYR A1078     204.754 190.402 140.698  1.00105.53           O  
ATOM   8334  N   ARG A1079     207.009 184.198 138.831  1.00102.76           N  
ATOM   8335  CA  ARG A1079     206.086 184.046 137.714  1.00102.76           C  
ATOM   8336  C   ARG A1079     205.239 182.788 137.853  1.00102.76           C  
ATOM   8337  O   ARG A1079     204.077 182.778 137.432  1.00102.76           O  
ATOM   8338  CB  ARG A1079     206.867 184.028 136.399  1.00102.76           C  
ATOM   8339  CG  ARG A1079     206.014 184.100 135.145  1.00102.76           C  
ATOM   8340  CD  ARG A1079     205.792 182.710 134.575  1.00102.76           C  
ATOM   8341  NE  ARG A1079     207.054 182.055 134.242  1.00102.76           N  
ATOM   8342  CZ  ARG A1079     207.200 180.743 134.090  1.00102.76           C  
ATOM   8343  NH1 ARG A1079     206.162 179.933 134.253  1.00102.76           N  
ATOM   8344  NH2 ARG A1079     208.387 180.238 133.785  1.00102.76           N  
ATOM   8345  N   LYS A1080     205.795 181.723 138.436  1.00 98.29           N  
ATOM   8346  CA  LYS A1080     205.001 180.518 138.644  1.00 98.29           C  
ATOM   8347  C   LYS A1080     203.970 180.721 139.745  1.00 98.29           C  
ATOM   8348  O   LYS A1080     202.890 180.120 139.703  1.00 98.29           O  
ATOM   8349  CB  LYS A1080     205.911 179.335 138.978  1.00 98.29           C  
ATOM   8350  CG  LYS A1080     205.199 177.992 139.018  1.00 98.29           C  
ATOM   8351  CD  LYS A1080     206.174 176.857 139.283  1.00 98.29           C  
ATOM   8352  CE  LYS A1080     206.596 176.824 140.743  1.00 98.29           C  
ATOM   8353  NZ  LYS A1080     207.435 175.634 141.054  1.00 98.29           N  
ATOM   8354  N   ALA A1081     204.281 181.567 140.730  1.00 99.93           N  
ATOM   8355  CA  ALA A1081     203.367 181.822 141.835  1.00 99.93           C  
ATOM   8356  C   ALA A1081     202.165 182.660 141.428  1.00 99.93           C  
ATOM   8357  O   ALA A1081     201.262 182.851 142.250  1.00 99.93           O  
ATOM   8358  CB  ALA A1081     204.109 182.513 142.980  1.00 99.93           C  
ATOM   8359  N   ARG A1082     202.126 183.160 140.195  1.00 98.96           N  
ATOM   8360  CA  ARG A1082     200.982 183.938 139.746  1.00 98.96           C  
ATOM   8361  C   ARG A1082     199.748 183.053 139.633  1.00 98.96           C  
ATOM   8362  O   ARG A1082     199.818 181.916 139.157  1.00 98.96           O  
ATOM   8363  CB  ARG A1082     201.280 184.597 138.399  1.00 98.96           C  
ATOM   8364  CG  ARG A1082     200.220 185.589 137.947  1.00 98.96           C  
ATOM   8365  CD  ARG A1082     200.635 186.309 136.673  1.00 98.96           C  
ATOM   8366  NE  ARG A1082     201.820 187.139 136.870  1.00 98.96           N  
ATOM   8367  CZ  ARG A1082     203.010 186.878 136.338  1.00 98.96           C  
ATOM   8368  NH1 ARG A1082     203.179 185.801 135.585  1.00 98.96           N  
ATOM   8369  NH2 ARG A1082     204.033 187.689 136.568  1.00 98.96           N  
ATOM   8370  N   LEU A1083     198.614 183.582 140.085  1.00 97.49           N  
ATOM   8371  CA  LEU A1083     197.404 182.782 140.213  1.00 97.49           C  
ATOM   8372  C   LEU A1083     196.893 182.389 138.832  1.00 97.49           C  
ATOM   8373  O   LEU A1083     196.563 183.255 138.014  1.00 97.49           O  
ATOM   8374  CB  LEU A1083     196.342 183.559 140.986  1.00 97.49           C  
ATOM   8375  CG  LEU A1083     194.978 182.893 141.159  1.00 97.49           C  
ATOM   8376  CD1 LEU A1083     195.120 181.555 141.865  1.00 97.49           C  
ATOM   8377  CD2 LEU A1083     194.057 183.811 141.940  1.00 97.49           C  
ATOM   8378  N   GLU A1084     196.828 181.088 138.573  1.00 92.95           N  
ATOM   8379  CA  GLU A1084     196.329 180.613 137.295  1.00 92.95           C  
ATOM   8380  C   GLU A1084     194.807 180.736 137.245  1.00 92.95           C  
ATOM   8381  O   GLU A1084     194.134 180.634 138.275  1.00 92.95           O  
ATOM   8382  CB  GLU A1084     196.744 179.163 137.064  1.00 92.95           C  
ATOM   8383  CG  GLU A1084     196.198 178.181 138.086  1.00 92.95           C  
ATOM   8384  CD  GLU A1084     196.680 176.763 137.847  1.00 92.95           C  
ATOM   8385  OE1 GLU A1084     197.429 176.545 136.872  1.00 92.95           O  
ATOM   8386  OE2 GLU A1084     196.310 175.867 138.635  1.00 92.95           O  
ATOM   8387  N   PRO A1085     194.240 180.961 136.063  1.00 92.26           N  
ATOM   8388  CA  PRO A1085     192.782 181.058 135.960  1.00 92.26           C  
ATOM   8389  C   PRO A1085     192.130 179.692 136.094  1.00 92.26           C  
ATOM   8390  O   PRO A1085     192.755 178.646 135.902  1.00 92.26           O  
ATOM   8391  CB  PRO A1085     192.561 181.642 134.560  1.00 92.26           C  
ATOM   8392  CG  PRO A1085     193.871 182.284 134.201  1.00 92.26           C  
ATOM   8393  CD  PRO A1085     194.904 181.397 134.824  1.00 92.26           C  
ATOM   8394  N   GLY A1086     190.843 179.717 136.430  1.00 92.26           N  
ATOM   8395  CA  GLY A1086     190.051 178.514 136.546  1.00 92.26           C  
ATOM   8396  C   GLY A1086     189.939 177.973 137.955  1.00 92.26           C  
ATOM   8397  O   GLY A1086     189.075 177.125 138.208  1.00 92.26           O  
ATOM   8398  N   THR A1087     190.783 178.436 138.874  1.00 90.87           N  
ATOM   8399  CA  THR A1087     190.733 177.963 140.250  1.00 90.87           C  
ATOM   8400  C   THR A1087     189.481 178.486 140.942  1.00 90.87           C  
ATOM   8401  O   THR A1087     189.216 179.692 140.941  1.00 90.87           O  
ATOM   8402  CB  THR A1087     191.975 178.419 141.016  1.00 90.87           C  
ATOM   8403  OG1 THR A1087     191.968 179.847 141.131  1.00 90.87           O  
ATOM   8404  CG2 THR A1087     193.239 177.990 140.294  1.00 90.87           C  
ATOM   8405  N   ALA A1088     188.707 177.576 141.535  1.00 86.57           N  
ATOM   8406  CA  ALA A1088     187.535 177.963 142.318  1.00 86.57           C  
ATOM   8407  C   ALA A1088     188.025 178.508 143.656  1.00 86.57           C  
ATOM   8408  O   ALA A1088     188.010 177.836 144.690  1.00 86.57           O  
ATOM   8409  CB  ALA A1088     186.589 176.783 142.498  1.00 86.57           C  
ATOM   8410  N   ILE A1089     188.472 179.767 143.626  1.00 86.63           N  
ATOM   8411  CA  ILE A1089     189.095 180.358 144.803  1.00 86.63           C  
ATOM   8412  C   ILE A1089     188.064 180.693 145.871  1.00 86.63           C  
ATOM   8413  O   ILE A1089     188.422 180.884 147.039  1.00 86.63           O  
ATOM   8414  CB  ILE A1089     189.912 181.600 144.397  1.00 86.63           C  
ATOM   8415  CG1 ILE A1089     190.948 181.939 145.471  1.00 86.63           C  
ATOM   8416  CG2 ILE A1089     188.993 182.786 144.137  1.00 86.63           C  
ATOM   8417  CD1 ILE A1089     192.075 182.810 144.970  1.00 86.63           C  
ATOM   8418  N   GLY A1090     186.784 180.762 145.502  1.00 92.81           N  
ATOM   8419  CA  GLY A1090     185.738 180.858 146.505  1.00 92.81           C  
ATOM   8420  C   GLY A1090     185.604 179.597 147.336  1.00 92.81           C  
ATOM   8421  O   GLY A1090     185.370 179.661 148.547  1.00 92.81           O  
ATOM   8422  N   ALA A1091     185.756 178.434 146.701  1.00 96.26           N  
ATOM   8423  CA  ALA A1091     185.604 177.171 147.416  1.00 96.26           C  
ATOM   8424  C   ALA A1091     186.742 176.947 148.403  1.00 96.26           C  
ATOM   8425  O   ALA A1091     186.508 176.528 149.542  1.00 96.26           O  
ATOM   8426  CB  ALA A1091     185.518 176.013 146.422  1.00 96.26           C  
ATOM   8427  N   ILE A1092     187.982 177.216 147.987  1.00 97.33           N  
ATOM   8428  CA  ILE A1092     189.118 176.941 148.859  1.00 97.33           C  
ATOM   8429  C   ILE A1092     189.215 177.972 149.978  1.00 97.33           C  
ATOM   8430  O   ILE A1092     189.693 177.660 151.075  1.00 97.33           O  
ATOM   8431  CB  ILE A1092     190.415 176.877 148.026  1.00 97.33           C  
ATOM   8432  CG1 ILE A1092     190.691 178.210 147.324  1.00 97.33           C  
ATOM   8433  CG2 ILE A1092     190.320 175.777 146.986  1.00 97.33           C  
ATOM   8434  CD1 ILE A1092     191.676 179.111 148.049  1.00 97.33           C  
ATOM   8435  N   GLY A1093     188.767 179.205 149.731  1.00 98.30           N  
ATOM   8436  CA  GLY A1093     188.752 180.205 150.784  1.00 98.30           C  
ATOM   8437  C   GLY A1093     187.716 179.949 151.860  1.00 98.30           C  
ATOM   8438  O   GLY A1093     187.941 180.270 153.031  1.00 98.30           O  
ATOM   8439  N   ALA A1094     186.570 179.376 151.484  1.00104.71           N  
ATOM   8440  CA  ALA A1094     185.546 179.041 152.469  1.00104.71           C  
ATOM   8441  C   ALA A1094     185.997 177.920 153.399  1.00104.71           C  
ATOM   8442  O   ALA A1094     185.689 177.940 154.596  1.00104.71           O  
ATOM   8443  CB  ALA A1094     184.248 178.658 151.761  1.00104.71           C  
ATOM   8444  N   GLN A1095     186.719 176.934 152.872  1.00101.68           N  
ATOM   8445  CA  GLN A1095     187.195 175.823 153.686  1.00101.68           C  
ATOM   8446  C   GLN A1095     188.525 176.097 154.373  1.00101.68           C  
ATOM   8447  O   GLN A1095     188.853 175.408 155.346  1.00101.68           O  
ATOM   8448  CB  GLN A1095     187.317 174.556 152.833  1.00101.68           C  
ATOM   8449  CG  GLN A1095     185.981 173.987 152.383  1.00101.68           C  
ATOM   8450  CD  GLN A1095     186.132 172.687 151.621  1.00101.68           C  
ATOM   8451  OE1 GLN A1095     187.245 172.221 151.383  1.00101.68           O  
ATOM   8452  NE2 GLN A1095     185.010 172.093 151.234  1.00101.68           N  
ATOM   8453  N   SER A1096     189.298 177.078 153.901  1.00 99.39           N  
ATOM   8454  CA  SER A1096     190.493 177.476 154.638  1.00 99.39           C  
ATOM   8455  C   SER A1096     190.149 178.278 155.887  1.00 99.39           C  
ATOM   8456  O   SER A1096     190.878 178.209 156.883  1.00 99.39           O  
ATOM   8457  CB  SER A1096     191.426 178.281 153.735  1.00 99.39           C  
ATOM   8458  OG  SER A1096     190.842 179.520 153.373  1.00 99.39           O  
ATOM   8459  N   ILE A1097     189.052 179.037 155.860  1.00 92.11           N  
ATOM   8460  CA  ILE A1097     188.636 179.769 157.052  1.00 92.11           C  
ATOM   8461  C   ILE A1097     187.840 178.891 158.011  1.00 92.11           C  
ATOM   8462  O   ILE A1097     187.762 179.205 159.206  1.00 92.11           O  
ATOM   8463  CB  ILE A1097     187.828 181.020 156.663  1.00 92.11           C  
ATOM   8464  CG1 ILE A1097     187.778 182.014 157.827  1.00 92.11           C  
ATOM   8465  CG2 ILE A1097     186.421 180.645 156.221  1.00 92.11           C  
ATOM   8466  CD1 ILE A1097     189.129 182.580 158.205  1.00 92.11           C  
ATOM   8467  N   GLY A1098     187.259 177.795 157.529  1.00106.43           N  
ATOM   8468  CA  GLY A1098     186.541 176.880 158.393  1.00106.43           C  
ATOM   8469  C   GLY A1098     187.389 175.725 158.883  1.00106.43           C  
ATOM   8470  O   GLY A1098     187.532 174.714 158.188  1.00106.43           O  
ATOM   8471  N   GLU A1099     187.952 175.861 160.087  1.00129.19           N  
ATOM   8472  CA  GLU A1099     188.727 174.793 160.703  1.00129.19           C  
ATOM   8473  C   GLU A1099     188.873 175.090 162.184  1.00129.19           C  
ATOM   8474  O   GLU A1099     188.990 176.266 162.555  1.00129.19           O  
ATOM   8475  CB  GLU A1099     190.107 174.649 160.047  1.00129.19           C  
ATOM   8476  CG  GLU A1099     190.935 175.927 160.014  1.00129.19           C  
ATOM   8477  CD  GLU A1099     191.815 176.088 161.239  1.00129.19           C  
ATOM   8478  OE1 GLU A1099     192.092 175.072 161.910  1.00129.19           O  
ATOM   8479  OE2 GLU A1099     192.229 177.230 161.530  1.00129.19           O  
ATOM   8480  N   PRO A1100     188.864 174.071 163.055  1.00145.65           N  
ATOM   8481  CA  PRO A1100     189.029 174.267 164.499  1.00145.65           C  
ATOM   8482  C   PRO A1100     190.444 174.701 164.870  1.00145.65           C  
ATOM   8483  O   PRO A1100     191.238 173.857 165.286  1.00145.65           O  
ATOM   8484  CB  PRO A1100     188.721 172.882 165.079  1.00145.65           C  
ATOM   8485  CG  PRO A1100     187.906 172.199 164.029  1.00145.65           C  
ATOM   8486  CD  PRO A1100     188.470 172.690 162.733  1.00145.65           C  
ATOM   8487  N   MET A1117     187.180 195.480 179.432  1.00233.86           N  
ATOM   8488  CA  MET A1117     187.091 194.393 180.401  1.00233.86           C  
ATOM   8489  C   MET A1117     187.354 193.045 179.740  1.00233.86           C  
ATOM   8490  O   MET A1117     188.438 192.477 179.876  1.00233.86           O  
ATOM   8491  CB  MET A1117     185.719 194.389 181.078  1.00233.86           C  
ATOM   8492  CG  MET A1117     185.577 193.366 182.194  1.00233.86           C  
ATOM   8493  SD  MET A1117     186.650 193.710 183.601  1.00233.86           S  
ATOM   8494  CE  MET A1117     186.815 192.074 184.311  1.00233.86           C  
ATOM   8495  N   ASN A1118     186.355 192.536 179.022  1.00226.85           N  
ATOM   8496  CA  ASN A1118     186.450 191.223 178.402  1.00226.85           C  
ATOM   8497  C   ASN A1118     185.669 191.227 177.096  1.00226.85           C  
ATOM   8498  O   ASN A1118     184.777 192.052 176.883  1.00226.85           O  
ATOM   8499  CB  ASN A1118     185.937 190.119 179.337  1.00226.85           C  
ATOM   8500  CG  ASN A1118     184.548 190.406 179.878  1.00226.85           C  
ATOM   8501  OD1 ASN A1118     183.941 191.429 179.558  1.00226.85           O  
ATOM   8502  ND2 ASN A1118     184.037 189.500 180.703  1.00226.85           N  
ATOM   8503  N   VAL A1119     186.022 190.287 176.219  1.00193.06           N  
ATOM   8504  CA  VAL A1119     185.363 190.146 174.927  1.00193.06           C  
ATOM   8505  C   VAL A1119     185.577 188.718 174.453  1.00193.06           C  
ATOM   8506  O   VAL A1119     186.595 188.092 174.761  1.00193.06           O  
ATOM   8507  CB  VAL A1119     185.898 191.186 173.908  1.00193.06           C  
ATOM   8508  CG1 VAL A1119     187.368 190.934 173.600  1.00193.06           C  
ATOM   8509  CG2 VAL A1119     185.064 191.181 172.633  1.00193.06           C  
ATOM   8510  N   THR A1120     184.606 188.196 173.709  1.00168.48           N  
ATOM   8511  CA  THR A1120     184.776 186.900 173.070  1.00168.48           C  
ATOM   8512  C   THR A1120     185.751 187.002 171.902  1.00168.48           C  
ATOM   8513  O   THR A1120     185.908 188.056 171.281  1.00168.48           O  
ATOM   8514  CB  THR A1120     183.431 186.359 172.583  1.00168.48           C  
ATOM   8515  OG1 THR A1120     183.626 185.092 171.943  1.00168.48           O  
ATOM   8516  CG2 THR A1120     182.787 187.328 171.602  1.00168.48           C  
ATOM   8517  N   LEU A1121     186.424 185.887 171.618  1.00158.86           N  
ATOM   8518  CA  LEU A1121     187.426 185.851 170.563  1.00158.86           C  
ATOM   8519  C   LEU A1121     187.418 184.561 169.755  1.00158.86           C  
ATOM   8520  O   LEU A1121     188.223 184.436 168.827  1.00158.86           O  
ATOM   8521  CB  LEU A1121     188.834 186.070 171.149  1.00158.86           C  
ATOM   8522  CG  LEU A1121     189.452 184.961 172.009  1.00158.86           C  
ATOM   8523  CD1 LEU A1121     190.963 185.114 172.058  1.00158.86           C  
ATOM   8524  CD2 LEU A1121     188.879 184.953 173.420  1.00158.86           C  
ATOM   8525  N   GLY A1122     186.546 183.605 170.068  1.00146.60           N  
ATOM   8526  CA  GLY A1122     186.520 182.349 169.345  1.00146.60           C  
ATOM   8527  C   GLY A1122     185.461 182.202 168.271  1.00146.60           C  
ATOM   8528  O   GLY A1122     185.261 183.096 167.442  1.00146.60           O  
ATOM   8529  N   VAL A1123     184.782 181.050 168.285  1.00139.25           N  
ATOM   8530  CA  VAL A1123     183.635 180.849 167.394  1.00139.25           C  
ATOM   8531  C   VAL A1123     182.543 181.892 167.591  1.00139.25           C  
ATOM   8532  O   VAL A1123     182.015 182.395 166.588  1.00139.25           O  
ATOM   8533  CB  VAL A1123     183.119 179.409 167.516  1.00139.25           C  
ATOM   8534  CG1 VAL A1123     181.888 179.202 166.644  1.00139.25           C  
ATOM   8535  CG2 VAL A1123     184.213 178.420 167.144  1.00139.25           C  
ATOM   8536  N   PRO A1124     182.152 182.278 168.821  1.00143.60           N  
ATOM   8537  CA  PRO A1124     181.172 183.368 168.947  1.00143.60           C  
ATOM   8538  C   PRO A1124     181.768 184.759 168.790  1.00143.60           C  
ATOM   8539  O   PRO A1124     181.144 185.748 169.186  1.00143.60           O  
ATOM   8540  CB  PRO A1124     180.608 183.168 170.359  1.00143.60           C  
ATOM   8541  CG  PRO A1124     181.713 182.525 171.103  1.00143.60           C  
ATOM   8542  CD  PRO A1124     182.384 181.613 170.117  1.00143.60           C  
ATOM   8543  N   ARG A1125     182.969 184.853 168.223  1.00139.79           N  
ATOM   8544  CA  ARG A1125     183.427 186.097 167.616  1.00139.79           C  
ATOM   8545  C   ARG A1125     183.224 186.128 166.108  1.00139.79           C  
ATOM   8546  O   ARG A1125     182.920 187.190 165.555  1.00139.79           O  
ATOM   8547  CB  ARG A1125     184.910 186.329 167.926  1.00139.79           C  
ATOM   8548  CG  ARG A1125     185.463 187.641 167.384  1.00139.79           C  
ATOM   8549  CD  ARG A1125     185.128 188.808 168.301  1.00139.79           C  
ATOM   8550  NE  ARG A1125     183.819 189.390 168.020  1.00139.79           N  
ATOM   8551  CZ  ARG A1125     183.593 190.317 167.096  1.00139.79           C  
ATOM   8552  NH1 ARG A1125     184.592 190.778 166.356  1.00139.79           N  
ATOM   8553  NH2 ARG A1125     182.366 190.786 166.914  1.00139.79           N  
ATOM   8554  N   ILE A1126     183.372 184.985 165.438  1.00128.73           N  
ATOM   8555  CA  ILE A1126     183.213 184.932 163.988  1.00128.73           C  
ATOM   8556  C   ILE A1126     181.741 184.982 163.589  1.00128.73           C  
ATOM   8557  O   ILE A1126     181.403 185.505 162.520  1.00128.73           O  
ATOM   8558  CB  ILE A1126     183.904 183.674 163.432  1.00128.73           C  
ATOM   8559  CG1 ILE A1126     185.362 183.622 163.892  1.00128.73           C  
ATOM   8560  CG2 ILE A1126     183.836 183.644 161.913  1.00128.73           C  
ATOM   8561  CD1 ILE A1126     186.192 184.799 163.428  1.00128.73           C  
ATOM   8562  N   LYS A1127     180.848 184.462 164.434  1.00130.85           N  
ATOM   8563  CA  LYS A1127     179.481 184.191 163.998  1.00130.85           C  
ATOM   8564  C   LYS A1127     178.701 185.480 163.764  1.00130.85           C  
ATOM   8565  O   LYS A1127     177.970 185.598 162.774  1.00130.85           O  
ATOM   8566  CB  LYS A1127     178.768 183.311 165.025  1.00130.85           C  
ATOM   8567  CG  LYS A1127     177.347 182.933 164.638  1.00130.85           C  
ATOM   8568  CD  LYS A1127     176.723 181.998 165.661  1.00130.85           C  
ATOM   8569  CE  LYS A1127     176.369 182.735 166.942  1.00130.85           C  
ATOM   8570  NZ  LYS A1127     175.640 181.859 167.900  1.00130.85           N  
ATOM   8571  N   GLU A1128     178.844 186.458 164.659  1.00136.04           N  
ATOM   8572  CA  GLU A1128     178.099 187.704 164.526  1.00136.04           C  
ATOM   8573  C   GLU A1128     178.695 188.641 163.484  1.00136.04           C  
ATOM   8574  O   GLU A1128     177.999 189.552 163.023  1.00136.04           O  
ATOM   8575  CB  GLU A1128     178.017 188.418 165.878  1.00136.04           C  
ATOM   8576  CG  GLU A1128     179.318 189.064 166.337  1.00136.04           C  
ATOM   8577  CD  GLU A1128     180.269 188.081 166.998  1.00136.04           C  
ATOM   8578  OE1 GLU A1128     180.139 186.862 166.759  1.00136.04           O  
ATOM   8579  OE2 GLU A1128     181.148 188.531 167.762  1.00136.04           O  
ATOM   8580  N   ILE A1129     179.960 188.446 163.105  1.00126.19           N  
ATOM   8581  CA  ILE A1129     180.546 189.259 162.044  1.00126.19           C  
ATOM   8582  C   ILE A1129     179.951 188.880 160.693  1.00126.19           C  
ATOM   8583  O   ILE A1129     179.555 189.748 159.905  1.00126.19           O  
ATOM   8584  CB  ILE A1129     182.079 189.120 162.044  1.00126.19           C  
ATOM   8585  CG1 ILE A1129     182.662 189.633 163.361  1.00126.19           C  
ATOM   8586  CG2 ILE A1129     182.684 189.866 160.864  1.00126.19           C  
ATOM   8587  CD1 ILE A1129     182.376 191.096 163.620  1.00126.19           C  
ATOM   8588  N   ILE A1130     179.876 187.579 160.404  1.00132.53           N  
ATOM   8589  CA  ILE A1130     179.287 187.140 159.144  1.00132.53           C  
ATOM   8590  C   ILE A1130     177.767 187.245 159.147  1.00132.53           C  
ATOM   8591  O   ILE A1130     177.148 187.178 158.078  1.00132.53           O  
ATOM   8592  CB  ILE A1130     179.731 185.704 158.812  1.00132.53           C  
ATOM   8593  CG1 ILE A1130     179.397 184.744 159.959  1.00132.53           C  
ATOM   8594  CG2 ILE A1130     181.220 185.666 158.498  1.00132.53           C  
ATOM   8595  CD1 ILE A1130     178.093 183.987 159.786  1.00132.53           C  
ATOM   8596  N   ASN A1131     177.145 187.402 160.318  1.00135.99           N  
ATOM   8597  CA  ASN A1131     175.708 187.642 160.382  1.00135.99           C  
ATOM   8598  C   ASN A1131     175.346 189.107 160.185  1.00135.99           C  
ATOM   8599  O   ASN A1131     174.205 189.401 159.811  1.00135.99           O  
ATOM   8600  CB  ASN A1131     175.147 187.152 161.718  1.00135.99           C  
ATOM   8601  CG  ASN A1131     175.033 185.642 161.784  1.00135.99           C  
ATOM   8602  OD1 ASN A1131     174.635 184.996 160.815  1.00135.99           O  
ATOM   8603  ND2 ASN A1131     175.380 185.072 162.932  1.00135.99           N  
ATOM   8604  N   ALA A1132     176.285 190.022 160.426  1.00139.00           N  
ATOM   8605  CA  ALA A1132     176.006 191.452 160.539  1.00139.00           C  
ATOM   8606  C   ALA A1132     174.882 191.710 161.544  1.00139.00           C  
ATOM   8607  O   ALA A1132     173.812 192.224 161.213  1.00139.00           O  
ATOM   8608  CB  ALA A1132     175.680 192.060 159.171  1.00139.00           C  
ATOM   8609  N   SER A1133     175.150 191.339 162.793  1.00145.43           N  
ATOM   8610  CA  SER A1133     174.120 191.347 163.821  1.00145.43           C  
ATOM   8611  C   SER A1133     173.979 192.737 164.426  1.00145.43           C  
ATOM   8612  O   SER A1133     174.971 193.431 164.667  1.00145.43           O  
ATOM   8613  CB  SER A1133     174.450 190.331 164.915  1.00145.43           C  
ATOM   8614  OG  SER A1133     175.613 190.709 165.631  1.00145.43           O  
ATOM   8615  N   LYS A1134     172.731 193.141 164.668  1.00141.08           N  
ATOM   8616  CA  LYS A1134     172.476 194.454 165.253  1.00141.08           C  
ATOM   8617  C   LYS A1134     172.884 194.501 166.721  1.00141.08           C  
ATOM   8618  O   LYS A1134     173.438 195.504 167.184  1.00141.08           O  
ATOM   8619  CB  LYS A1134     171.001 194.820 165.095  1.00141.08           C  
ATOM   8620  CG  LYS A1134     170.521 194.854 163.653  1.00141.08           C  
ATOM   8621  CD  LYS A1134     171.151 196.007 162.889  1.00141.08           C  
ATOM   8622  CE  LYS A1134     170.648 196.060 161.456  1.00141.08           C  
ATOM   8623  NZ  LYS A1134     169.211 196.445 161.386  1.00141.08           N  
ATOM   8624  N   VAL A1135     172.621 193.432 167.465  1.00143.25           N  
ATOM   8625  CA  VAL A1135     172.956 193.352 168.882  1.00143.25           C  
ATOM   8626  C   VAL A1135     174.274 192.595 169.004  1.00143.25           C  
ATOM   8627  O   VAL A1135     174.311 191.364 168.921  1.00143.25           O  
ATOM   8628  CB  VAL A1135     171.841 192.682 169.690  1.00143.25           C  
ATOM   8629  CG1 VAL A1135     172.240 192.569 171.155  1.00143.25           C  
ATOM   8630  CG2 VAL A1135     170.541 193.459 169.544  1.00143.25           C  
ATOM   8631  N   ILE A1136     175.363 193.335 169.196  1.00147.51           N  
ATOM   8632  CA  ILE A1136     176.692 192.759 169.357  1.00147.51           C  
ATOM   8633  C   ILE A1136     176.990 192.677 170.848  1.00147.51           C  
ATOM   8634  O   ILE A1136     176.544 193.517 171.640  1.00147.51           O  
ATOM   8635  CB  ILE A1136     177.764 193.576 168.600  1.00147.51           C  
ATOM   8636  CG1 ILE A1136     179.093 192.816 168.557  1.00147.51           C  
ATOM   8637  CG2 ILE A1136     177.937 194.954 169.220  1.00147.51           C  
ATOM   8638  CD1 ILE A1136     180.106 193.412 167.605  1.00147.51           C  
ATOM   8639  N   SER A1137     177.733 191.647 171.244  1.00154.79           N  
ATOM   8640  CA  SER A1137     178.128 191.479 172.636  1.00154.79           C  
ATOM   8641  C   SER A1137     179.416 192.236 172.937  1.00154.79           C  
ATOM   8642  O   SER A1137     180.387 192.156 172.177  1.00154.79           O  
ATOM   8643  CB  SER A1137     178.303 189.996 172.963  1.00154.79           C  
ATOM   8644  OG  SER A1137     178.697 189.814 174.312  1.00154.79           O  
ATOM   8645  N   THR A1138     179.411 192.967 174.054  1.00163.59           N  
ATOM   8646  CA  THR A1138     180.493 193.826 174.527  1.00163.59           C  
ATOM   8647  C   THR A1138     180.987 194.788 173.452  1.00163.59           C  
ATOM   8648  O   THR A1138     182.097 194.613 172.933  1.00163.59           O  
ATOM   8649  CB  THR A1138     181.661 192.980 175.040  1.00163.59           C  
ATOM   8650  OG1 THR A1138     182.266 192.279 173.946  1.00163.59           O  
ATOM   8651  CG2 THR A1138     181.177 191.974 176.073  1.00163.59           C  
ATOM   8652  N   PRO A1139     180.209 195.810 173.087  1.00155.19           N  
ATOM   8653  CA  PRO A1139     180.683 196.759 172.055  1.00155.19           C  
ATOM   8654  C   PRO A1139     181.602 197.832 172.635  1.00155.19           C  
ATOM   8655  O   PRO A1139     181.208 198.957 172.942  1.00155.19           O  
ATOM   8656  CB  PRO A1139     179.377 197.350 171.523  1.00155.19           C  
ATOM   8657  CG  PRO A1139     178.463 197.319 172.703  1.00155.19           C  
ATOM   8658  CD  PRO A1139     178.820 196.087 173.496  1.00155.19           C  
ATOM   8659  N   ILE A1140     182.876 197.491 172.797  1.00152.87           N  
ATOM   8660  CA  ILE A1140     183.860 198.481 173.221  1.00152.87           C  
ATOM   8661  C   ILE A1140     184.338 199.274 172.013  1.00152.87           C  
ATOM   8662  O   ILE A1140     184.499 198.732 170.912  1.00152.87           O  
ATOM   8663  CB  ILE A1140     185.033 197.805 173.955  1.00152.87           C  
ATOM   8664  CG1 ILE A1140     185.780 196.844 173.027  1.00152.87           C  
ATOM   8665  CG2 ILE A1140     184.537 197.076 175.195  1.00152.87           C  
ATOM   8666  CD1 ILE A1140     187.077 196.321 173.606  1.00152.87           C  
ATOM   8667  N   ILE A1141     184.547 200.573 172.210  1.00152.10           N  
ATOM   8668  CA  ILE A1141     185.057 201.451 171.167  1.00152.10           C  
ATOM   8669  C   ILE A1141     186.363 202.063 171.651  1.00152.10           C  
ATOM   8670  O   ILE A1141     186.582 202.230 172.855  1.00152.10           O  
ATOM   8671  CB  ILE A1141     184.035 202.546 170.776  1.00152.10           C  
ATOM   8672  CG1 ILE A1141     183.735 203.473 171.958  1.00152.10           C  
ATOM   8673  CG2 ILE A1141     182.752 201.915 170.257  1.00152.10           C  
ATOM   8674  CD1 ILE A1141     184.487 204.793 171.927  1.00152.10           C  
ATOM   8675  N   ASN A1142     187.238 202.394 170.706  1.00154.63           N  
ATOM   8676  CA  ASN A1142     188.581 202.864 171.018  1.00154.63           C  
ATOM   8677  C   ASN A1142     188.667 204.354 170.723  1.00154.63           C  
ATOM   8678  O   ASN A1142     188.280 204.800 169.638  1.00154.63           O  
ATOM   8679  CB  ASN A1142     189.630 202.097 170.210  1.00154.63           C  
ATOM   8680  CG  ASN A1142     191.037 202.307 170.734  1.00154.63           C  
ATOM   8681  OD1 ASN A1142     191.246 203.006 171.725  1.00154.63           O  
ATOM   8682  ND2 ASN A1142     192.012 201.698 170.069  1.00154.63           N  
ATOM   8683  N   ALA A1143     189.174 205.121 171.687  1.00154.73           N  
ATOM   8684  CA  ALA A1143     189.401 206.547 171.498  1.00154.73           C  
ATOM   8685  C   ALA A1143     190.769 206.925 172.043  1.00154.73           C  
ATOM   8686  O   ALA A1143     191.081 206.626 173.200  1.00154.73           O  
ATOM   8687  CB  ALA A1143     188.312 207.378 172.186  1.00154.73           C  
ATOM   8688  N   VAL A1144     191.580 207.578 171.216  1.00161.42           N  
ATOM   8689  CA  VAL A1144     192.900 208.040 171.626  1.00161.42           C  
ATOM   8690  C   VAL A1144     192.777 209.490 172.071  1.00161.42           C  
ATOM   8691  O   VAL A1144     191.915 210.238 171.593  1.00161.42           O  
ATOM   8692  CB  VAL A1144     193.938 207.875 170.493  1.00161.42           C  
ATOM   8693  CG1 VAL A1144     193.719 208.910 169.400  1.00161.42           C  
ATOM   8694  CG2 VAL A1144     195.356 207.955 171.043  1.00161.42           C  
ATOM   8695  N   LEU A1145     193.631 209.893 173.008  1.00168.90           N  
ATOM   8696  CA  LEU A1145     193.458 211.172 173.679  1.00168.90           C  
ATOM   8697  C   LEU A1145     194.217 212.262 172.923  1.00168.90           C  
ATOM   8698  O   LEU A1145     194.779 212.031 171.849  1.00168.90           O  
ATOM   8699  CB  LEU A1145     193.911 211.071 175.135  1.00168.90           C  
ATOM   8700  CG  LEU A1145     192.876 210.616 176.169  1.00168.90           C  
ATOM   8701  CD1 LEU A1145     191.688 211.563 176.177  1.00168.90           C  
ATOM   8702  CD2 LEU A1145     192.424 209.182 175.929  1.00168.90           C  
ATOM   8703  N   VAL A1146     194.240 213.466 173.483  1.00169.83           N  
ATOM   8704  CA  VAL A1146     195.103 214.542 173.005  1.00169.83           C  
ATOM   8705  C   VAL A1146     196.396 214.612 173.804  1.00169.83           C  
ATOM   8706  O   VAL A1146     197.487 214.659 173.236  1.00169.83           O  
ATOM   8707  CB  VAL A1146     194.347 215.889 173.042  1.00169.83           C  
ATOM   8708  CG1 VAL A1146     195.289 217.038 172.716  1.00169.83           C  
ATOM   8709  CG2 VAL A1146     193.171 215.864 172.078  1.00169.83           C  
ATOM   8710  N   ASN A1147     196.287 214.615 175.130  1.00182.41           N  
ATOM   8711  CA  ASN A1147     197.442 214.705 176.007  1.00182.41           C  
ATOM   8712  C   ASN A1147     198.108 213.339 176.157  1.00182.41           C  
ATOM   8713  O   ASN A1147     197.613 212.315 175.678  1.00182.41           O  
ATOM   8714  CB  ASN A1147     197.037 215.259 177.373  1.00182.41           C  
ATOM   8715  CG  ASN A1147     195.905 214.476 178.012  1.00182.41           C  
ATOM   8716  OD1 ASN A1147     195.416 213.495 177.451  1.00182.41           O  
ATOM   8717  ND2 ASN A1147     195.483 214.908 179.195  1.00182.41           N  
ATOM   8718  N   ASP A1148     199.249 213.334 176.835  1.00190.73           N  
ATOM   8719  CA  ASP A1148     199.908 212.098 177.239  1.00190.73           C  
ATOM   8720  C   ASP A1148     199.976 211.920 178.746  1.00190.73           C  
ATOM   8721  O   ASP A1148     199.870 210.791 179.233  1.00190.73           O  
ATOM   8722  CB  ASP A1148     201.328 212.040 176.654  1.00190.73           C  
ATOM   8723  CG  ASP A1148     202.165 213.250 177.029  1.00190.73           C  
ATOM   8724  OD1 ASP A1148     201.613 214.198 177.627  1.00190.73           O  
ATOM   8725  OD2 ASP A1148     203.377 213.250 176.728  1.00190.73           O  
ATOM   8726  N   ASN A1149     200.149 213.000 179.499  1.00192.57           N  
ATOM   8727  CA  ASN A1149     200.138 212.938 180.952  1.00192.57           C  
ATOM   8728  C   ASN A1149     198.742 213.223 181.498  1.00192.57           C  
ATOM   8729  O   ASN A1149     197.866 213.742 180.802  1.00192.57           O  
ATOM   8730  CB  ASN A1149     201.142 213.932 181.539  1.00192.57           C  
ATOM   8731  CG  ASN A1149     202.566 213.646 181.103  1.00192.57           C  
ATOM   8732  OD1 ASN A1149     203.178 214.437 180.386  1.00192.57           O  
ATOM   8733  ND2 ASN A1149     203.100 212.510 181.536  1.00192.57           N  
ATOM   8734  N   ASP A1150     198.545 212.869 182.769  1.00185.03           N  
ATOM   8735  CA  ASP A1150     197.224 212.976 183.382  1.00185.03           C  
ATOM   8736  C   ASP A1150     196.849 214.436 183.611  1.00185.03           C  
ATOM   8737  O   ASP A1150     195.835 214.917 183.092  1.00185.03           O  
ATOM   8738  CB  ASP A1150     197.192 212.193 184.696  1.00185.03           C  
ATOM   8739  CG  ASP A1150     195.783 211.996 185.227  1.00185.03           C  
ATOM   8740  OD1 ASP A1150     194.823 212.445 184.566  1.00185.03           O  
ATOM   8741  OD2 ASP A1150     195.636 211.388 186.308  1.00185.03           O  
ATOM   8742  N   GLU A1151     197.650 215.144 184.415  1.00199.80           N  
ATOM   8743  CA  GLU A1151     197.494 216.577 184.714  1.00199.80           C  
ATOM   8744  C   GLU A1151     196.054 216.949 185.074  1.00199.80           C  
ATOM   8745  O   GLU A1151     195.599 218.063 184.800  1.00199.80           O  
ATOM   8746  CB  GLU A1151     198.029 217.459 183.574  1.00199.80           C  
ATOM   8747  CG  GLU A1151     197.284 217.412 182.247  1.00199.80           C  
ATOM   8748  CD  GLU A1151     197.981 218.208 181.162  1.00199.80           C  
ATOM   8749  OE1 GLU A1151     199.061 218.772 181.438  1.00199.80           O  
ATOM   8750  OE2 GLU A1151     197.451 218.268 180.033  1.00199.80           O  
ATOM   8751  N   ARG A1152     195.334 216.016 185.705  1.00190.06           N  
ATOM   8752  CA  ARG A1152     193.894 216.145 185.955  1.00190.06           C  
ATOM   8753  C   ARG A1152     193.110 216.438 184.678  1.00190.06           C  
ATOM   8754  O   ARG A1152     192.090 217.132 184.703  1.00190.06           O  
ATOM   8755  CB  ARG A1152     193.613 217.213 187.017  1.00190.06           C  
ATOM   8756  CG  ARG A1152     194.207 216.898 188.381  1.00190.06           C  
ATOM   8757  CD  ARG A1152     193.927 218.008 189.381  1.00190.06           C  
ATOM   8758  NE  ARG A1152     192.508 218.103 189.710  1.00190.06           N  
ATOM   8759  CZ  ARG A1152     191.708 219.080 189.297  1.00190.06           C  
ATOM   8760  NH1 ARG A1152     192.182 220.045 188.521  1.00190.06           N  
ATOM   8761  NH2 ARG A1152     190.429 219.085 189.648  1.00190.06           N  
ATOM   8762  N   ALA A1153     193.579 215.910 183.548  1.00178.10           N  
ATOM   8763  CA  ALA A1153     192.928 216.154 182.266  1.00178.10           C  
ATOM   8764  C   ALA A1153     192.781 214.910 181.405  1.00178.10           C  
ATOM   8765  O   ALA A1153     192.115 214.984 180.368  1.00178.10           O  
ATOM   8766  CB  ALA A1153     193.690 217.223 181.470  1.00178.10           C  
ATOM   8767  N   ALA A1154     193.372 213.777 181.787  1.00176.63           N  
ATOM   8768  CA  ALA A1154     193.139 212.520 181.089  1.00176.63           C  
ATOM   8769  C   ALA A1154     191.860 211.826 181.536  1.00176.63           C  
ATOM   8770  O   ALA A1154     191.315 211.017 180.778  1.00176.63           O  
ATOM   8771  CB  ALA A1154     194.330 211.581 181.284  1.00176.63           C  
ATOM   8772  N   ARG A1155     191.370 212.120 182.739  1.00169.42           N  
ATOM   8773  CA  ARG A1155     190.102 211.584 183.215  1.00169.42           C  
ATOM   8774  C   ARG A1155     188.964 212.592 183.137  1.00169.42           C  
ATOM   8775  O   ARG A1155     187.836 212.261 183.514  1.00169.42           O  
ATOM   8776  CB  ARG A1155     190.244 211.083 184.657  1.00169.42           C  
ATOM   8777  CG  ARG A1155     190.529 212.177 185.674  1.00169.42           C  
ATOM   8778  CD  ARG A1155     190.537 211.624 187.092  1.00169.42           C  
ATOM   8779  NE  ARG A1155     191.587 210.630 187.292  1.00169.42           N  
ATOM   8780  CZ  ARG A1155     192.837 210.922 187.638  1.00169.42           C  
ATOM   8781  NH1 ARG A1155     193.199 212.185 187.818  1.00169.42           N  
ATOM   8782  NH2 ARG A1155     193.726 209.952 187.799  1.00169.42           N  
ATOM   8783  N   VAL A1156     189.227 213.810 182.659  1.00165.24           N  
ATOM   8784  CA  VAL A1156     188.177 214.821 182.591  1.00165.24           C  
ATOM   8785  C   VAL A1156     187.281 214.622 181.374  1.00165.24           C  
ATOM   8786  O   VAL A1156     186.136 215.093 181.372  1.00165.24           O  
ATOM   8787  CB  VAL A1156     188.785 216.235 182.594  1.00165.24           C  
ATOM   8788  CG1 VAL A1156     189.353 216.586 181.225  1.00165.24           C  
ATOM   8789  CG2 VAL A1156     187.752 217.263 183.035  1.00165.24           C  
ATOM   8790  N   VAL A1157     187.765 213.927 180.342  1.00167.28           N  
ATOM   8791  CA  VAL A1157     186.897 213.506 179.249  1.00167.28           C  
ATOM   8792  C   VAL A1157     186.106 212.255 179.615  1.00167.28           C  
ATOM   8793  O   VAL A1157     185.038 212.013 179.038  1.00167.28           O  
ATOM   8794  CB  VAL A1157     187.723 213.277 177.971  1.00167.28           C  
ATOM   8795  CG1 VAL A1157     188.653 212.083 178.139  1.00167.28           C  
ATOM   8796  CG2 VAL A1157     186.819 213.108 176.754  1.00167.28           C  
ATOM   8797  N   LYS A1158     186.589 211.467 180.579  1.00167.18           N  
ATOM   8798  CA  LYS A1158     185.818 210.328 181.065  1.00167.18           C  
ATOM   8799  C   LYS A1158     184.573 210.778 181.817  1.00167.18           C  
ATOM   8800  O   LYS A1158     183.550 210.085 181.792  1.00167.18           O  
ATOM   8801  CB  LYS A1158     186.696 209.444 181.955  1.00167.18           C  
ATOM   8802  CG  LYS A1158     186.007 208.191 182.477  1.00167.18           C  
ATOM   8803  CD  LYS A1158     185.650 208.317 183.950  1.00167.18           C  
ATOM   8804  CE  LYS A1158     186.883 208.202 184.830  1.00167.18           C  
ATOM   8805  NZ  LYS A1158     186.538 208.262 186.278  1.00167.18           N  
ATOM   8806  N   GLY A1159     184.634 211.935 182.479  1.00167.52           N  
ATOM   8807  CA  GLY A1159     183.419 212.559 182.972  1.00167.52           C  
ATOM   8808  C   GLY A1159     182.566 213.154 181.872  1.00167.52           C  
ATOM   8809  O   GLY A1159     181.340 213.226 182.003  1.00167.52           O  
ATOM   8810  N   ARG A1160     183.190 213.585 180.775  1.00163.01           N  
ATOM   8811  CA  ARG A1160     182.461 214.174 179.660  1.00163.01           C  
ATOM   8812  C   ARG A1160     181.833 213.133 178.743  1.00163.01           C  
ATOM   8813  O   ARG A1160     180.998 213.495 177.907  1.00163.01           O  
ATOM   8814  CB  ARG A1160     183.379 215.088 178.845  1.00163.01           C  
ATOM   8815  CG  ARG A1160     183.684 216.419 179.516  1.00163.01           C  
ATOM   8816  CD  ARG A1160     184.281 217.414 178.531  1.00163.01           C  
ATOM   8817  NE  ARG A1160     185.591 216.994 178.045  1.00163.01           N  
ATOM   8818  CZ  ARG A1160     186.743 217.345 178.607  1.00163.01           C  
ATOM   8819  NH1 ARG A1160     186.750 218.136 179.671  1.00163.01           N  
ATOM   8820  NH2 ARG A1160     187.890 216.916 178.097  1.00163.01           N  
ATOM   8821  N   VAL A1161     182.206 211.861 178.873  1.00171.16           N  
ATOM   8822  CA  VAL A1161     181.702 210.821 177.986  1.00171.16           C  
ATOM   8823  C   VAL A1161     180.823 209.808 178.714  1.00171.16           C  
ATOM   8824  O   VAL A1161     179.988 209.160 178.064  1.00171.16           O  
ATOM   8825  CB  VAL A1161     182.859 210.104 177.257  1.00171.16           C  
ATOM   8826  CG1 VAL A1161     183.616 209.188 178.210  1.00171.16           C  
ATOM   8827  CG2 VAL A1161     182.351 209.333 176.044  1.00171.16           C  
ATOM   8828  N   GLU A1162     180.964 209.661 180.029  1.00176.69           N  
ATOM   8829  CA  GLU A1162     180.206 208.664 180.768  1.00176.69           C  
ATOM   8830  C   GLU A1162     178.800 209.182 181.054  1.00176.69           C  
ATOM   8831  O   GLU A1162     178.582 210.384 181.230  1.00176.69           O  
ATOM   8832  CB  GLU A1162     180.920 208.308 182.073  1.00176.69           C  
ATOM   8833  CG  GLU A1162     180.447 207.020 182.733  1.00176.69           C  
ATOM   8834  CD  GLU A1162     179.271 207.234 183.665  1.00176.69           C  
ATOM   8835  OE1 GLU A1162     179.151 208.344 184.226  1.00176.69           O  
ATOM   8836  OE2 GLU A1162     178.467 206.294 183.837  1.00176.69           O  
ATOM   8837  N   LYS A1163     177.841 208.258 181.102  1.00177.07           N  
ATOM   8838  CA  LYS A1163     176.474 208.613 181.461  1.00177.07           C  
ATOM   8839  C   LYS A1163     176.382 208.950 182.944  1.00177.07           C  
ATOM   8840  O   LYS A1163     176.157 208.064 183.776  1.00177.07           O  
ATOM   8841  CB  LYS A1163     175.514 207.474 181.111  1.00177.07           C  
ATOM   8842  CG  LYS A1163     174.045 207.812 181.306  1.00177.07           C  
ATOM   8843  CD  LYS A1163     173.161 206.600 181.053  1.00177.07           C  
ATOM   8844  CE  LYS A1163     173.123 206.242 179.576  1.00177.07           C  
ATOM   8845  NZ  LYS A1163     172.180 205.123 179.300  1.00177.07           N  
ATOM   8846  N   THR A1164     176.560 210.226 183.284  1.00179.68           N  
ATOM   8847  CA  THR A1164     176.577 210.655 184.679  1.00179.68           C  
ATOM   8848  C   THR A1164     175.182 210.517 185.277  1.00179.68           C  
ATOM   8849  O   THR A1164     174.256 211.235 184.885  1.00179.68           O  
ATOM   8850  CB  THR A1164     177.074 212.094 184.784  1.00179.68           C  
ATOM   8851  OG1 THR A1164     178.407 212.180 184.265  1.00179.68           O  
ATOM   8852  CG2 THR A1164     177.070 212.554 186.234  1.00179.68           C  
ATOM   8853  N   LEU A1165     175.030 209.597 186.224  1.00178.17           N  
ATOM   8854  CA  LEU A1165     173.757 209.382 186.897  1.00178.17           C  
ATOM   8855  C   LEU A1165     173.657 210.282 188.121  1.00178.17           C  
ATOM   8856  O   LEU A1165     174.614 210.416 188.889  1.00178.17           O  
ATOM   8857  CB  LEU A1165     173.604 207.915 187.301  1.00178.17           C  
ATOM   8858  CG  LEU A1165     172.247 207.485 187.863  1.00178.17           C  
ATOM   8859  CD1 LEU A1165     171.145 207.720 186.843  1.00178.17           C  
ATOM   8860  CD2 LEU A1165     172.288 206.024 188.280  1.00178.17           C  
ATOM   8861  N   LEU A1166     172.488 210.900 188.300  1.00179.89           N  
ATOM   8862  CA  LEU A1166     172.331 211.917 189.333  1.00179.89           C  
ATOM   8863  C   LEU A1166     172.224 211.323 190.731  1.00179.89           C  
ATOM   8864  O   LEU A1166     172.402 212.052 191.713  1.00179.89           O  
ATOM   8865  CB  LEU A1166     171.103 212.784 189.042  1.00179.89           C  
ATOM   8866  CG  LEU A1166     169.751 212.295 189.567  1.00179.89           C  
ATOM   8867  CD1 LEU A1166     168.732 213.424 189.547  1.00179.89           C  
ATOM   8868  CD2 LEU A1166     169.256 211.116 188.749  1.00179.89           C  
ATOM   8869  N   SER A1167     171.933 210.025 190.846  1.00184.69           N  
ATOM   8870  CA  SER A1167     171.840 209.395 192.157  1.00184.69           C  
ATOM   8871  C   SER A1167     173.197 209.285 192.837  1.00184.69           C  
ATOM   8872  O   SER A1167     173.253 209.109 194.059  1.00184.69           O  
ATOM   8873  CB  SER A1167     171.205 208.009 192.034  1.00184.69           C  
ATOM   8874  OG  SER A1167     172.047 207.123 191.320  1.00184.69           O  
ATOM   8875  N   ASP A1168     174.288 209.384 192.075  1.00196.54           N  
ATOM   8876  CA  ASP A1168     175.613 209.539 192.663  1.00196.54           C  
ATOM   8877  C   ASP A1168     175.859 210.953 193.173  1.00196.54           C  
ATOM   8878  O   ASP A1168     176.538 211.128 194.191  1.00196.54           O  
ATOM   8879  CB  ASP A1168     176.687 209.158 191.642  1.00196.54           C  
ATOM   8880  CG  ASP A1168     178.028 208.862 192.287  1.00196.54           C  
ATOM   8881  OD1 ASP A1168     178.108 208.871 193.533  1.00196.54           O  
ATOM   8882  OD2 ASP A1168     179.004 208.621 191.546  1.00196.54           O  
ATOM   8883  N   VAL A1169     175.322 211.969 192.496  1.00190.10           N  
ATOM   8884  CA  VAL A1169     175.561 213.346 192.915  1.00190.10           C  
ATOM   8885  C   VAL A1169     174.491 213.861 193.874  1.00190.10           C  
ATOM   8886  O   VAL A1169     174.741 214.833 194.602  1.00190.10           O  
ATOM   8887  CB  VAL A1169     175.674 214.274 191.690  1.00190.10           C  
ATOM   8888  CG1 VAL A1169     174.300 214.578 191.107  1.00190.10           C  
ATOM   8889  CG2 VAL A1169     176.415 215.558 192.047  1.00190.10           C  
ATOM   8890  N   ALA A1170     173.316 213.238 193.907  1.00191.33           N  
ATOM   8891  CA  ALA A1170     172.331 213.559 194.928  1.00191.33           C  
ATOM   8892  C   ALA A1170     172.697 212.871 196.237  1.00191.33           C  
ATOM   8893  O   ALA A1170     173.380 211.843 196.252  1.00191.33           O  
ATOM   8894  CB  ALA A1170     170.931 213.137 194.483  1.00191.33           C  
ATOM   8895  N   PHE A1171     172.236 213.445 197.343  1.00189.45           N  
ATOM   8896  CA  PHE A1171     172.556 212.899 198.656  1.00189.45           C  
ATOM   8897  C   PHE A1171     171.338 212.580 199.506  1.00189.45           C  
ATOM   8898  O   PHE A1171     171.346 211.581 200.230  1.00189.45           O  
ATOM   8899  CB  PHE A1171     173.459 213.878 199.420  1.00189.45           C  
ATOM   8900  CG  PHE A1171     173.871 213.391 200.779  1.00189.45           C  
ATOM   8901  CD1 PHE A1171     174.795 212.368 200.913  1.00189.45           C  
ATOM   8902  CD2 PHE A1171     173.335 213.957 201.924  1.00189.45           C  
ATOM   8903  CE1 PHE A1171     175.176 211.918 202.162  1.00189.45           C  
ATOM   8904  CE2 PHE A1171     173.712 213.512 203.177  1.00189.45           C  
ATOM   8905  CZ  PHE A1171     174.634 212.490 203.296  1.00189.45           C  
ATOM   8906  N   TYR A1172     170.288 213.396 199.444  1.00180.38           N  
ATOM   8907  CA  TYR A1172     169.163 213.251 200.363  1.00180.38           C  
ATOM   8908  C   TYR A1172     167.919 213.814 199.695  1.00180.38           C  
ATOM   8909  O   TYR A1172     167.905 214.984 199.302  1.00180.38           O  
ATOM   8910  CB  TYR A1172     169.461 213.962 201.687  1.00180.38           C  
ATOM   8911  CG  TYR A1172     168.392 213.823 202.747  1.00180.38           C  
ATOM   8912  CD1 TYR A1172     168.094 212.583 203.298  1.00180.38           C  
ATOM   8913  CD2 TYR A1172     167.717 214.934 203.233  1.00180.38           C  
ATOM   8914  CE1 TYR A1172     167.128 212.448 204.276  1.00180.38           C  
ATOM   8915  CE2 TYR A1172     166.754 214.810 204.217  1.00180.38           C  
ATOM   8916  CZ  TYR A1172     166.462 213.565 204.732  1.00180.38           C  
ATOM   8917  OH  TYR A1172     165.504 213.437 205.712  1.00180.38           O  
ATOM   8918  N   VAL A1173     166.881 212.990 199.566  1.00177.01           N  
ATOM   8919  CA  VAL A1173     165.666 213.357 198.847  1.00177.01           C  
ATOM   8920  C   VAL A1173     164.459 212.980 199.696  1.00177.01           C  
ATOM   8921  O   VAL A1173     164.363 211.848 200.182  1.00177.01           O  
ATOM   8922  CB  VAL A1173     165.601 212.683 197.460  1.00177.01           C  
ATOM   8923  CG1 VAL A1173     165.867 211.186 197.569  1.00177.01           C  
ATOM   8924  CG2 VAL A1173     164.254 212.937 196.803  1.00177.01           C  
ATOM   8925  N   GLN A1174     163.551 213.935 199.889  1.00180.24           N  
ATOM   8926  CA  GLN A1174     162.352 213.705 200.683  1.00180.24           C  
ATOM   8927  C   GLN A1174     161.281 214.695 200.247  1.00180.24           C  
ATOM   8928  O   GLN A1174     161.550 215.651 199.516  1.00180.24           O  
ATOM   8929  CB  GLN A1174     162.638 213.859 202.179  1.00180.24           C  
ATOM   8930  CG  GLN A1174     162.787 215.308 202.623  1.00180.24           C  
ATOM   8931  CD  GLN A1174     164.191 215.844 202.436  1.00180.24           C  
ATOM   8932  OE1 GLN A1174     164.998 215.266 201.708  1.00180.24           O  
ATOM   8933  NE2 GLN A1174     164.491 216.958 203.095  1.00180.24           N  
ATOM   8934  N   ASP A1175     160.058 214.450 200.708  1.00183.90           N  
ATOM   8935  CA  ASP A1175     158.904 215.262 200.349  1.00183.90           C  
ATOM   8936  C   ASP A1175     158.590 216.199 201.508  1.00183.90           C  
ATOM   8937  O   ASP A1175     158.482 215.754 202.656  1.00183.90           O  
ATOM   8938  CB  ASP A1175     157.699 214.374 200.028  1.00183.90           C  
ATOM   8939  CG  ASP A1175     156.598 215.117 199.297  1.00183.90           C  
ATOM   8940  OD1 ASP A1175     156.726 216.343 199.104  1.00183.90           O  
ATOM   8941  OD2 ASP A1175     155.603 214.470 198.910  1.00183.90           O  
ATOM   8942  N   VAL A1176     158.444 217.488 201.212  1.00179.62           N  
ATOM   8943  CA  VAL A1176     158.299 218.520 202.234  1.00179.62           C  
ATOM   8944  C   VAL A1176     156.894 219.100 202.153  1.00179.62           C  
ATOM   8945  O   VAL A1176     156.451 219.523 201.078  1.00179.62           O  
ATOM   8946  CB  VAL A1176     159.358 219.623 202.070  1.00179.62           C  
ATOM   8947  CG1 VAL A1176     159.187 220.691 203.140  1.00179.62           C  
ATOM   8948  CG2 VAL A1176     160.758 219.028 202.119  1.00179.62           C  
ATOM   8949  N   TYR A1177     156.198 219.124 203.288  1.00179.90           N  
ATOM   8950  CA  TYR A1177     154.840 219.643 203.376  1.00179.90           C  
ATOM   8951  C   TYR A1177     154.809 220.802 204.361  1.00179.90           C  
ATOM   8952  O   TYR A1177     155.293 220.669 205.490  1.00179.90           O  
ATOM   8953  CB  TYR A1177     153.863 218.552 203.827  1.00179.90           C  
ATOM   8954  CG  TYR A1177     153.699 217.407 202.852  1.00179.90           C  
ATOM   8955  CD1 TYR A1177     154.010 217.560 201.509  1.00179.90           C  
ATOM   8956  CD2 TYR A1177     153.237 216.169 203.280  1.00179.90           C  
ATOM   8957  CE1 TYR A1177     153.859 216.517 200.617  1.00179.90           C  
ATOM   8958  CE2 TYR A1177     153.086 215.118 202.396  1.00179.90           C  
ATOM   8959  CZ  TYR A1177     153.399 215.298 201.066  1.00179.90           C  
ATOM   8960  OH  TYR A1177     153.252 214.255 200.182  1.00179.90           O  
ATOM   8961  N   LYS A1178     154.243 221.936 203.945  1.00171.68           N  
ATOM   8962  CA  LYS A1178     153.941 222.981 204.917  1.00171.68           C  
ATOM   8963  C   LYS A1178     152.483 222.862 205.340  1.00171.68           C  
ATOM   8964  O   LYS A1178     152.186 222.500 206.483  1.00171.68           O  
ATOM   8965  CB  LYS A1178     154.230 224.366 204.336  1.00171.68           C  
ATOM   8966  CG  LYS A1178     154.010 225.507 205.317  1.00171.68           C  
ATOM   8967  CD  LYS A1178     154.940 225.394 206.514  1.00171.68           C  
ATOM   8968  CE  LYS A1178     156.385 225.645 206.117  1.00171.68           C  
ATOM   8969  NZ  LYS A1178     157.303 225.591 207.289  1.00171.68           N  
ATOM   8970  N   ASP A1179     151.566 223.165 204.418  1.00171.26           N  
ATOM   8971  CA  ASP A1179     150.168 222.764 204.546  1.00171.26           C  
ATOM   8972  C   ASP A1179     149.534 222.361 203.220  1.00171.26           C  
ATOM   8973  O   ASP A1179     148.611 221.540 203.223  1.00171.26           O  
ATOM   8974  CB  ASP A1179     149.345 223.902 205.171  1.00171.26           C  
ATOM   8975  CG  ASP A1179     147.990 223.442 205.684  1.00171.26           C  
ATOM   8976  OD1 ASP A1179     147.710 222.226 205.658  1.00171.26           O  
ATOM   8977  OD2 ASP A1179     147.199 224.307 206.116  1.00171.26           O  
ATOM   8978  N   ASN A1180     150.004 222.891 202.085  1.00162.86           N  
ATOM   8979  CA  ASN A1180     149.265 222.821 200.831  1.00162.86           C  
ATOM   8980  C   ASN A1180     150.207 222.618 199.647  1.00162.86           C  
ATOM   8981  O   ASN A1180     149.856 222.975 198.516  1.00162.86           O  
ATOM   8982  CB  ASN A1180     148.421 224.087 200.628  1.00162.86           C  
ATOM   8983  CG  ASN A1180     147.269 223.878 199.660  1.00162.86           C  
ATOM   8984  OD1 ASN A1180     147.130 222.811 199.064  1.00162.86           O  
ATOM   8985  ND2 ASN A1180     146.438 224.902 199.500  1.00162.86           N  
ATOM   8986  N   LEU A1181     151.390 222.058 199.876  1.00168.16           N  
ATOM   8987  CA  LEU A1181     152.389 221.867 198.835  1.00168.16           C  
ATOM   8988  C   LEU A1181     152.727 220.392 198.686  1.00168.16           C  
ATOM   8989  O   LEU A1181     152.829 219.666 199.678  1.00168.16           O  
ATOM   8990  CB  LEU A1181     153.666 222.662 199.140  1.00168.16           C  
ATOM   8991  CG  LEU A1181     153.719 224.140 198.737  1.00168.16           C  
ATOM   8992  CD1 LEU A1181     153.475 224.297 197.242  1.00168.16           C  
ATOM   8993  CD2 LEU A1181     152.745 224.992 199.543  1.00168.16           C  
ATOM   8994  N   SER A1182     152.892 219.952 197.439  1.00162.40           N  
ATOM   8995  CA  SER A1182     153.292 218.581 197.123  1.00162.40           C  
ATOM   8996  C   SER A1182     154.464 218.684 196.151  1.00162.40           C  
ATOM   8997  O   SER A1182     154.276 218.662 194.931  1.00162.40           O  
ATOM   8998  CB  SER A1182     152.131 217.779 196.540  1.00162.40           C  
ATOM   8999  OG  SER A1182     151.739 218.292 195.279  1.00162.40           O  
ATOM   9000  N   PHE A1183     155.674 218.797 196.696  1.00170.78           N  
ATOM   9001  CA  PHE A1183     156.880 218.945 195.892  1.00170.78           C  
ATOM   9002  C   PHE A1183     157.988 218.095 196.492  1.00170.78           C  
ATOM   9003  O   PHE A1183     158.231 218.150 197.701  1.00170.78           O  
ATOM   9004  CB  PHE A1183     157.317 220.416 195.797  1.00170.78           C  
ATOM   9005  CG  PHE A1183     157.748 221.018 197.107  1.00170.78           C  
ATOM   9006  CD1 PHE A1183     156.815 221.544 197.984  1.00170.78           C  
ATOM   9007  CD2 PHE A1183     159.090 221.083 197.447  1.00170.78           C  
ATOM   9008  CE1 PHE A1183     157.210 222.104 199.185  1.00170.78           C  
ATOM   9009  CE2 PHE A1183     159.491 221.641 198.646  1.00170.78           C  
ATOM   9010  CZ  PHE A1183     158.550 222.153 199.516  1.00170.78           C  
ATOM   9011  N   ILE A1184     158.651 217.309 195.652  1.00169.46           N  
ATOM   9012  CA  ILE A1184     159.835 216.577 196.081  1.00169.46           C  
ATOM   9013  C   ILE A1184     161.007 217.545 196.185  1.00169.46           C  
ATOM   9014  O   ILE A1184     161.071 218.559 195.479  1.00169.46           O  
ATOM   9015  CB  ILE A1184     160.135 215.411 195.117  1.00169.46           C  
ATOM   9016  CG1 ILE A1184     161.087 214.405 195.767  1.00169.46           C  
ATOM   9017  CG2 ILE A1184     160.706 215.924 193.802  1.00169.46           C  
ATOM   9018  CD1 ILE A1184     160.464 213.624 196.903  1.00169.46           C  
ATOM   9019  N   GLN A1185     161.935 217.244 197.088  1.00178.30           N  
ATOM   9020  CA  GLN A1185     163.127 218.055 197.289  1.00178.30           C  
ATOM   9021  C   GLN A1185     164.374 217.225 197.023  1.00178.30           C  
ATOM   9022  O   GLN A1185     164.478 216.079 197.469  1.00178.30           O  
ATOM   9023  CB  GLN A1185     163.166 218.627 198.712  1.00178.30           C  
ATOM   9024  CG  GLN A1185     164.336 219.559 198.990  1.00178.30           C  
ATOM   9025  CD  GLN A1185     165.543 218.831 199.551  1.00178.30           C  
ATOM   9026  OE1 GLN A1185     165.406 217.850 200.282  1.00178.30           O  
ATOM   9027  NE2 GLN A1185     166.734 219.313 199.216  1.00178.30           N  
ATOM   9028  N   VAL A1186     165.318 217.818 196.296  1.00180.05           N  
ATOM   9029  CA  VAL A1186     166.599 217.199 195.980  1.00180.05           C  
ATOM   9030  C   VAL A1186     167.702 218.156 196.409  1.00180.05           C  
ATOM   9031  O   VAL A1186     167.621 219.360 196.143  1.00180.05           O  
ATOM   9032  CB  VAL A1186     166.721 216.859 194.482  1.00180.05           C  
ATOM   9033  CG1 VAL A1186     168.090 216.269 194.175  1.00180.05           C  
ATOM   9034  CG2 VAL A1186     165.618 215.898 194.063  1.00180.05           C  
ATOM   9035  N   ARG A1187     168.726 217.625 197.073  1.00175.78           N  
ATOM   9036  CA  ARG A1187     169.920 218.388 197.404  1.00175.78           C  
ATOM   9037  C   ARG A1187     171.148 217.644 196.900  1.00175.78           C  
ATOM   9038  O   ARG A1187     171.225 216.416 196.994  1.00175.78           O  
ATOM   9039  CB  ARG A1187     170.019 218.643 198.919  1.00175.78           C  
ATOM   9040  CG  ARG A1187     170.017 217.390 199.785  1.00175.78           C  
ATOM   9041  CD  ARG A1187     171.424 216.997 200.206  1.00175.78           C  
ATOM   9042  NE  ARG A1187     172.077 218.059 200.966  1.00175.78           N  
ATOM   9043  CZ  ARG A1187     173.354 218.401 200.830  1.00175.78           C  
ATOM   9044  NH1 ARG A1187     174.122 217.767 199.955  1.00175.78           N  
ATOM   9045  NH2 ARG A1187     173.862 219.380 201.565  1.00175.78           N  
ATOM   9046  N   ILE A1188     172.096 218.397 196.356  1.00174.06           N  
ATOM   9047  CA  ILE A1188     173.291 217.832 195.766  1.00174.06           C  
ATOM   9048  C   ILE A1188     174.457 217.974 196.737  1.00174.06           C  
ATOM   9049  O   ILE A1188     174.386 218.689 197.733  1.00174.06           O  
ATOM   9050  CB  ILE A1188     173.617 218.483 194.400  1.00174.06           C  
ATOM   9051  CG1 ILE A1188     174.011 219.950 194.586  1.00174.06           C  
ATOM   9052  CG2 ILE A1188     172.434 218