HEADER    LYASE/HYDROLASE                         16-JUN-14   4UPF              
TITLE     ASSEMBLY PRINCIPLES OF THE UNIQUE CAGE FORMED BY THE ATPASE RAVA      
TITLE    2 HEXAMER AND THE LYSINE DECARBOXYLASE LDCI DECAMER                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSINE DECARBOXYLASE, INDUCIBLE;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LDC, INDUCIBLE LYSINE DECARBOXYLASE;                        
COMPND   5 EC: 4.1.1.18;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ATPASE RAVA;                                               
COMPND   9 CHAIN: D;                                                            
COMPND  10 FRAGMENT: LARA DOMAIN RESIDUES 329-440;                              
COMPND  11 SYNONYM: REGULATORY ATPASE VARIANT A;                                
COMPND  12 EC: 3.6.3.1;                                                         
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655;      
SOURCE   3 ORGANISM_TAXID: 511145;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VARIANT: CF1693 SOURCE 7;                          
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET22B;                                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655;      
SOURCE  11 ORGANISM_TAXID: 511145;                                              
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  15 EXPRESSION_SYSTEM_VARIANT: GOLD PLYSS;                               
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 EXPRESSION_SYSTEM_VECTOR: P11                                        
KEYWDS    LYASE-HYDROLASE COMPLEX, LYSINE DECARBOXYLASE, AAA+ ATPASE, ACID      
KEYWDS   2 STRESS RESPONSE                                                      
EXPDTA    ELECTRON MICROSCOPY                                                   
MDLTYP    CA ATOMS ONLY, CHAIN A, D                                             
AUTHOR    H.MALET,K.LIU,M.EL BAKKOURI,S.W.S.CHAN,G.EFFANTIN,M.BACIA,W.A.HOURY,  
AUTHOR   2 I.GUTSCHE                                                            
REVDAT   3   30-AUG-17 4UPF    1       REMARK                                   
REVDAT   2   10-SEP-14 4UPF    1       JRNL                                     
REVDAT   1   20-AUG-14 4UPF    0                                                
JRNL        AUTH   H.MALET,K.LIU,M.EL BAKKOURI,S.W.S.CHAN,G.EFFANTIN,M.BACIA,   
JRNL        AUTH 2 W.A.HOURY,I.GUTSCHE                                          
JRNL        TITL   ASSEMBLY PRINCIPLES OF A UNIQUE CAGE FORMED BY HEXAMERIC AND 
JRNL        TITL 2 DECAMERIC E. COLI PROTEINS.                                  
JRNL        REF    ELIFE                         V.   3 03653 2014              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   25097238                                                     
JRNL        DOI    10.7554/ELIFE.03653                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    7.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : CTFFIND, FLEX-EM, SITUS, EMAN, EMAN,      
REMARK   3                            FPM, IMAGIC, SPIDER                       
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 3N75                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FIT                        
REMARK   3   REFINEMENT TARGET            : CROSS-CORRELATION COEFFICIENT       
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : METHOD--FLEXIBLE FOR 3N75, RIGID FOR 3NBX        
REMARK   3  REFINEMENT PROTOCOL--X-RAY                                          
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : 1.464                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 7.500                          
REMARK   3   NUMBER OF PARTICLES               : 23540                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: CROSS-COMMON LINE, PROJECTION MATCHING SUBMISSION     
REMARK   3  BASED ON EXPERIMENTAL DATA FROM EMDB EMD-2681. (DEPOSITION ID:      
REMARK   3  12595).                                                             
REMARK   4                                                                      
REMARK   4 4UPF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.                               
REMARK 100 THE DEPOSITION ID IS D_1290060953.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE CRYO EM              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : COMPLEX BETWEEN A DECAMER OF      
REMARK 245                                    INDUCIBLE LYSINE DECARBOXYLASE    
REMARK 245                                    LDCI AND TEN LARA DOMAINS OF      
REMARK 245                                    THE ATPASE RAVA                   
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.60                              
REMARK 245   SAMPLE SUPPORT DETAILS         : OTHER                             
REMARK 245   SAMPLE VITRIFICATION DETAILS   : VITRIFICATION 1 -- CRYOGEN-       
REMARK 245                                    ETHANE, HUMIDITY- 100,            
REMARK 245                                    TEMPERATURE- 91, INSTRUMENT-      
REMARK 245                                    FEI VITROBOT MARK III, METHOD-    
REMARK 245                                    BLOT FOR 2 SECONDS BEFORE         
REMARK 245                                    PLUNGING                          
REMARK 245   SAMPLE BUFFER                  : 50MM MES PH 6.5, 100MM NACL,      
REMARK 245                                    0.2MM PLP, 1MM DTT, 0.01%         
REMARK 245                                    GLUTARALDEHYDE                    
REMARK 245   PH                             : 6.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 14-SEP-12                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 91.00                          
REMARK 245   MICROSCOPE MODEL                  : FEI TECNAI F30                 
REMARK 245   DETECTOR TYPE                     : GATAN ULTRASCAN 4000 (4K X     
REMARK 245                                       4K)                            
REMARK 245   MINIMUM DEFOCUS (NM)              : 1500.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2700.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : -0.10                          
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : 0.00                           
REMARK 245   NOMINAL CS                        : 2.00                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 20.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 51660                          
REMARK 245   CALIBRATED MAGNIFICATION          : 51660                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : AUTOMATIC DATA ACQUISITION     
REMARK 245  WITH FEI EPU SOFTWARE                                               
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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     LYS A   367                                                      
REMARK 465     GLU A   712                                                      
REMARK 465     SER A   713                                                      
REMARK 465     LYS A   714                                                      
REMARK 465     LYS A   715                                                      
REMARK 465     GLY D   326                                                      
REMARK 465     HIS D   327                                                      
REMARK 465     MET D   328                                                      
REMARK 465     GLN D   329                                                      
REMARK 465     GLN D   330                                                      
REMARK 465     SER D   331                                                      
REMARK 465     ASP D   332                                                      
REMARK 465     LYS D   333                                                      
REMARK 465     THR D   334                                                      
REMARK 465     ALA D   335                                                      
REMARK 465     LEU D   336                                                      
REMARK 465     THR D   337                                                      
REMARK 465     VAL D   338                                                      
REMARK 465     ILE D   339                                                      
REMARK 465     ARG D   340                                                      
REMARK 465     LEU D   341                                                      
REMARK 465     GLY D   342                                                      
REMARK 465     GLY D   343                                                      
REMARK 465     ILE D   344                                                      
REMARK 465     PHE D   345                                                      
REMARK 465     SER D   346                                                      
REMARK 465     ARG D   347                                                      
REMARK 465     ARG D   348                                                      
REMARK 465     GLN D   349                                                      
REMARK 465     GLN D   350                                                      
REMARK 465     TYR D   351                                                      
REMARK 465     GLN D   352                                                      
REMARK 465     LEU D   353                                                      
REMARK 465     PRO D   354                                                      
REMARK 465     VAL D   355                                                      
REMARK 465     ASN D   356                                                      
REMARK 465     VAL D   357                                                      
REMARK 465     THR D   358                                                      
REMARK 465     ALA D   359                                                      
REMARK 465     SER D   360                                                      
REMARK 465     PRO D   435                                                      
REMARK 465     GLY D   436                                                      
REMARK 465     SER D   437                                                      
REMARK 465     SER D   438                                                      
REMARK 465     ALA D   439                                                      
REMARK 465     GLU D   440                                                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UPB   RELATED DB: PDB                                   
REMARK 900 ELECTRON CRYO-MICROSCOPY OF THE COMPLEX FORMED BETWEEN THE           
REMARK 900 HEXAMERIC ATPASE RAVA AND THE DECAMERIC INDUCIBLE DECARBOXYLASE LDCI 
REMARK 900 RELATED ID: EMD-2681   RELATED DB: EMDB                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE LARA DOMAIN (FROM GLN329 TO GLU440) WAS PCR AMPLIFIED            
REMARK 999 FROM THE P11-RAVA PLASMID. THE PCR PRODUCT WAS DIGESTED              
REMARK 999 WITH NDEI AND BAMHI (NEB) AND LIGATED INTO AN EMPTY P11              
REMARK 999 VECTOR TO PRODUCE P11-LARA. THE RESULTING CONSTRUCT HAS AN           
REMARK 999 N-TERMINAL HIS6-TAG FOLLOWED BY A TOBACCO ETCH VIRUS (TEV)           
REMARK 999 CUT SITE THAT LEAVES THE THREE RESIDUES GHM AT THE                   
REMARK 999 TERMINUS OF THE CONSTRUCT AFTER TEV CLEAVAGE.                        
DBREF  4UPF A    1   715  UNP    P0A9H3   LDCI_ECOLI       1    715             
DBREF  4UPF D  329   440  UNP    P31473   RAVA_ECOLI     329    440             
SEQADV 4UPF GLY D  326  UNP  P31473              EXPRESSION TAG                 
SEQADV 4UPF HIS D  327  UNP  P31473              EXPRESSION TAG                 
SEQADV 4UPF MET D  328  UNP  P31473              EXPRESSION TAG                 
SEQRES   1 A  715  MET ASN VAL ILE ALA ILE LEU ASN HIS MET GLY VAL TYR          
SEQRES   2 A  715  PHE LYS GLU GLU PRO ILE ARG GLU LEU HIS ARG ALA LEU          
SEQRES   3 A  715  GLU ARG LEU ASN PHE GLN ILE VAL TYR PRO ASN ASP ARG          
SEQRES   4 A  715  ASP ASP LEU LEU LYS LEU ILE GLU ASN ASN ALA ARG LEU          
SEQRES   5 A  715  CYS GLY VAL ILE PHE ASP TRP ASP LYS TYR ASN LEU GLU          
SEQRES   6 A  715  LEU CYS GLU GLU ILE SER LYS MET ASN GLU ASN LEU PRO          
SEQRES   7 A  715  LEU TYR ALA PHE ALA ASN THR TYR SER THR LEU ASP VAL          
SEQRES   8 A  715  SER LEU ASN ASP LEU ARG LEU GLN ILE SER PHE PHE GLU          
SEQRES   9 A  715  TYR ALA LEU GLY ALA ALA GLU ASP ILE ALA ASN LYS ILE          
SEQRES  10 A  715  LYS GLN THR THR ASP GLU TYR ILE ASN THR ILE LEU PRO          
SEQRES  11 A  715  PRO LEU THR LYS ALA LEU PHE LYS TYR VAL ARG GLU GLY          
SEQRES  12 A  715  LYS TYR THR PHE CYS THR PRO GLY HIS MET GLY GLY THR          
SEQRES  13 A  715  ALA PHE GLN LYS SER PRO VAL GLY SER LEU PHE TYR ASP          
SEQRES  14 A  715  PHE PHE GLY PRO ASN THR MET LYS SER ASP ILE SER ILE          
SEQRES  15 A  715  SER VAL SER GLU LEU GLY SER LEU LEU ASP HIS SER GLY          
SEQRES  16 A  715  PRO HIS LYS GLU ALA GLU GLN TYR ILE ALA ARG VAL PHE          
SEQRES  17 A  715  ASN ALA ASP ARG SER TYR MET VAL THR ASN GLY THR SER          
SEQRES  18 A  715  THR ALA ASN LYS ILE VAL GLY MET TYR SER ALA PRO ALA          
SEQRES  19 A  715  GLY SER THR ILE LEU ILE ASP ARG ASN CYS HIS LYS SER          
SEQRES  20 A  715  LEU THR HIS LEU MET MET MET SER ASP VAL THR PRO ILE          
SEQRES  21 A  715  TYR PHE ARG PRO THR ARG ASN ALA TYR GLY ILE LEU GLY          
SEQRES  22 A  715  GLY ILE PRO GLN SER GLU PHE GLN HIS ALA THR ILE ALA          
SEQRES  23 A  715  LYS ARG VAL LYS GLU THR PRO ASN ALA THR TRP PRO VAL          
SEQRES  24 A  715  HIS ALA VAL ILE THR ASN SER THR TYR ASP GLY LEU LEU          
SEQRES  25 A  715  TYR ASN THR ASP PHE ILE LYS LYS THR LEU ASP VAL LYS          
SEQRES  26 A  715  SER ILE HIS PHE ASP SER ALA TRP VAL PRO TYR THR ASN          
SEQRES  27 A  715  PHE SER PRO ILE TYR GLU GLY LYS CYS GLY MET SER GLY          
SEQRES  28 A  715  GLY ARG VAL GLU GLY LYS VAL ILE TYR GLU THR GLN SER          
SEQRES  29 A  715  THR HIS LYS LEU LEU ALA ALA PHE SER GLN ALA SER MET          
SEQRES  30 A  715  ILE HIS VAL LYS GLY ASP VAL ASN GLU GLU THR PHE ASN          
SEQRES  31 A  715  GLU ALA TYR MET MET HIS THR THR THR SER PRO HIS TYR          
SEQRES  32 A  715  GLY ILE VAL ALA SER THR GLU THR ALA ALA ALA MET MET          
SEQRES  33 A  715  LYS GLY ASN ALA GLY LYS ARG LEU ILE ASN GLY SER ILE          
SEQRES  34 A  715  GLU ARG ALA ILE LYS PHE ARG LYS GLU ILE LYS ARG LEU          
SEQRES  35 A  715  ARG THR GLU SER ASP GLY TRP PHE PHE ASP VAL TRP GLN          
SEQRES  36 A  715  PRO ASP HIS ILE ASP THR THR GLU CYS TRP PRO LEU ARG          
SEQRES  37 A  715  SER ASP SER THR TRP HIS GLY PHE LYS ASN ILE ASP ASN          
SEQRES  38 A  715  GLU HIS MET TYR LEU ASP PRO ILE LYS VAL THR LEU LEU          
SEQRES  39 A  715  THR PRO GLY MET GLU LYS ASP GLY THR MET SER ASP PHE          
SEQRES  40 A  715  GLY ILE PRO ALA SER ILE VAL ALA LYS TYR LEU ASP GLU          
SEQRES  41 A  715  HIS GLY ILE VAL VAL GLU LYS THR GLY PRO TYR ASN LEU          
SEQRES  42 A  715  LEU PHE LEU PHE SER ILE GLY ILE ASP LYS THR LYS ALA          
SEQRES  43 A  715  LEU SER LEU LEU ARG ALA LEU THR ASP PHE LYS ARG ALA          
SEQRES  44 A  715  PHE ASP LEU ASN LEU ARG VAL LYS ASN MET LEU PRO SER          
SEQRES  45 A  715  LEU TYR ARG GLU ASP PRO GLU PHE TYR GLU ASN MET ARG          
SEQRES  46 A  715  ILE GLN GLU LEU ALA GLN ASN ILE HIS LYS LEU ILE VAL          
SEQRES  47 A  715  HIS HIS ASN LEU PRO ASP LEU MET TYR ARG ALA PHE GLU          
SEQRES  48 A  715  VAL LEU PRO THR MET VAL MET THR PRO TYR ALA ALA PHE          
SEQRES  49 A  715  GLN LYS GLU LEU HIS GLY MET THR GLU GLU VAL TYR LEU          
SEQRES  50 A  715  ASP GLU MET VAL GLY ARG ILE ASN ALA ASN MET ILE LEU          
SEQRES  51 A  715  PRO TYR PRO PRO GLY VAL PRO LEU VAL MET PRO GLY GLU          
SEQRES  52 A  715  MET ILE THR GLU GLU SER ARG PRO VAL LEU GLU PHE LEU          
SEQRES  53 A  715  GLN MET LEU CYS GLU ILE GLY ALA HIS TYR PRO GLY PHE          
SEQRES  54 A  715  GLU THR ASP ILE HIS GLY ALA TYR ARG GLN ALA ASP GLY          
SEQRES  55 A  715  ARG TYR THR VAL LYS VAL LEU LYS GLU GLU SER LYS LYS          
SEQRES   1 D  115  GLY HIS MET GLN GLN SER ASP LYS THR ALA LEU THR VAL          
SEQRES   2 D  115  ILE ARG LEU GLY GLY ILE PHE SER ARG ARG GLN GLN TYR          
SEQRES   3 D  115  GLN LEU PRO VAL ASN VAL THR ALA SER THR LEU THR LEU          
SEQRES   4 D  115  LEU LEU GLN LYS PRO LEU LYS LEU HIS ASP MET GLU VAL          
SEQRES   5 D  115  VAL HIS ILE SER PHE GLU ARG SER ALA LEU GLU GLN TRP          
SEQRES   6 D  115  LEU SER LYS GLY GLY GLU ILE ARG GLY LYS LEU ASN GLY          
SEQRES   7 D  115  ILE GLY PHE ALA GLN LYS LEU ASN LEU GLU VAL ASP SER          
SEQRES   8 D  115  ALA GLN HIS LEU VAL VAL ARG ASP VAL SER LEU GLN GLY          
SEQRES   9 D  115  SER THR LEU ALA LEU PRO GLY SER SER ALA GLU                  
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  MET A   1     -26.407 -20.109 -13.243  1.00 28.91           C  
ATOM      2  CA  ASN A   2     -24.485 -16.796 -12.978  1.00 24.81           C  
ATOM      3  CA  VAL A   3     -22.801 -15.910 -16.254  1.00 19.93           C  
ATOM      4  CA  ILE A   4     -24.096 -12.777 -18.061  1.00 18.55           C  
ATOM      5  CA  ALA A   5     -22.792 -11.894 -21.497  1.00 17.43           C  
ATOM      6  CA  ILE A   6     -22.397  -8.279 -22.584  1.00 18.15           C  
ATOM      7  CA  LEU A   7     -22.026  -7.816 -26.313  1.00 21.30           C  
ATOM      8  CA  ASN A   8     -20.106  -4.356 -27.220  1.00 23.53           C  
ATOM      9  CA  HIS A   9     -17.849  -1.250 -28.447  1.00 23.78           C  
ATOM     10  CA  MET A  10     -20.511   1.379 -29.334  1.00 21.98           C  
ATOM     11  CA  GLY A  11     -18.349   4.477 -29.874  1.00 20.34           C  
ATOM     12  CA  VAL A  12     -20.452   6.660 -27.534  1.00 19.53           C  
ATOM     13  CA  TYR A  13     -19.930   7.373 -23.877  1.00 17.09           C  
ATOM     14  CA  PHE A  14     -23.689   7.849 -23.269  1.00 16.44           C  
ATOM     15  CA  LYS A  15     -24.075   4.086 -23.953  1.00 15.55           C  
ATOM     16  CA  GLU A  16     -20.690   2.765 -22.842  1.00 16.46           C  
ATOM     17  CA  GLU A  17     -20.599   4.337 -19.405  1.00 16.40           C  
ATOM     18  CA  PRO A  18     -23.969   3.022 -18.227  1.00 15.64           C  
ATOM     19  CA  ILE A  19     -22.874  -0.453 -19.382  1.00 17.09           C  
ATOM     20  CA  ARG A  20     -19.668  -0.078 -17.328  1.00 18.05           C  
ATOM     21  CA  GLU A  21     -21.827   0.870 -14.332  1.00 16.13           C  
ATOM     22  CA  LEU A  22     -24.012  -2.190 -14.974  1.00 15.94           C  
ATOM     23  CA  HIS A  23     -20.960  -4.538 -15.110  1.00 16.93           C  
ATOM     24  CA  ARG A  24     -20.050  -3.313 -11.609  1.00 18.20           C  
ATOM     25  CA  ALA A  25     -23.613  -3.545 -10.273  1.00 17.75           C  
ATOM     26  CA  LEU A  26     -23.923  -7.109 -11.591  1.00 18.60           C  
ATOM     27  CA  GLU A  27     -20.546  -8.159 -10.143  1.00 20.98           C  
ATOM     28  CA  ARG A  28     -21.828  -6.900  -6.753  1.00 23.53           C  
ATOM     29  CA  LEU A  29     -24.707  -9.386  -7.122  1.00 23.20           C  
ATOM     30  CA  ASN A  30     -22.166 -12.157  -7.795  1.00 24.37           C  
ATOM     31  CA  PHE A  31     -22.600 -12.573 -11.547  1.00 19.49           C  
ATOM     32  CA  GLN A  32     -19.572 -13.347 -13.786  1.00 18.93           C  
ATOM     33  CA  ILE A  33     -19.482 -11.040 -16.801  1.00 17.78           C  
ATOM     34  CA  VAL A  34     -18.240 -12.152 -20.201  1.00 17.24           C  
ATOM     35  CA  TYR A  35     -17.569 -10.066 -23.333  1.00 18.07           C  
ATOM     36  CA  PRO A  36     -18.007 -11.871 -26.682  1.00 18.63           C  
ATOM     37  CA  ASN A  37     -16.254 -10.142 -29.582  1.00 22.25           C  
ATOM     38  CA  ASP A  38     -19.140 -10.496 -31.961  1.00 24.32           C  
ATOM     39  CA  ARG A  39     -22.338 -12.328 -32.697  1.00 25.07           C  
ATOM     40  CA  ASP A  40     -20.707 -15.662 -33.576  1.00 24.31           C  
ATOM     41  CA  ASP A  41     -18.514 -15.545 -30.413  1.00 19.37           C  
ATOM     42  CA  LEU A  42     -21.653 -14.995 -28.294  1.00 19.73           C  
ATOM     43  CA  LEU A  43     -23.448 -17.950 -29.909  1.00 21.27           C  
ATOM     44  CA  LYS A  44     -20.428 -20.164 -29.144  1.00 21.56           C  
ATOM     45  CA  LEU A  45     -20.425 -18.998 -25.526  1.00 20.77           C  
ATOM     46  CA  ILE A  46     -24.125 -19.910 -25.230  1.00 23.36           C  
ATOM     47  CA  GLU A  47     -23.551 -23.226 -27.006  1.00 28.41           C  
ATOM     48  CA  ASN A  48     -20.621 -24.151 -24.703  1.00 26.80           C  
ATOM     49  CA  ASN A  49     -21.855 -22.748 -21.395  1.00 22.58           C  
ATOM     50  CA  ALA A  50     -25.242 -23.855 -19.999  1.00 21.68           C  
ATOM     51  CA  ARG A  51     -24.670 -21.491 -17.054  1.00 21.33           C  
ATOM     52  CA  LEU A  52     -24.753 -18.415 -19.252  1.00 21.57           C  
ATOM     53  CA  CYS A  53     -28.149 -17.116 -18.129  1.00 21.90           C  
ATOM     54  CA  GLY A  54     -28.573 -13.643 -19.774  1.00 19.19           C  
ATOM     55  CA  VAL A  55     -27.388 -11.487 -22.691  1.00 17.91           C  
ATOM     56  CA  ILE A  56     -27.079  -7.702 -22.628  1.00 17.78           C  
ATOM     57  CA  PHE A  57     -26.926  -5.925 -26.008  1.00 16.87           C  
ATOM     58  CA  ASP A  58     -27.833  -2.838 -28.030  1.00 17.78           C  
ATOM     59  CA  TRP A  59     -31.224  -3.643 -29.564  1.00 19.98           C  
ATOM     60  CA  ASP A  60     -30.789  -1.854 -32.923  1.00 21.07           C  
ATOM     61  CA  LYS A  61     -27.223  -3.116 -33.494  1.00 20.83           C  
ATOM     62  CA  TYR A  62     -27.931  -6.796 -32.883  1.00 20.78           C  
ATOM     63  CA  ASN A  63     -31.602  -7.838 -32.670  1.00 23.02           C  
ATOM     64  CA  LEU A  64     -31.851  -8.972 -36.342  1.00 26.37           C  
ATOM     65  CA  GLU A  65     -28.529 -10.832 -35.941  1.00 29.35           C  
ATOM     66  CA  LEU A  66     -29.277 -12.530 -32.558  1.00 25.86           C  
ATOM     67  CA  CYS A  67     -32.921 -13.137 -31.758  1.00 24.06           C  
ATOM     68  CA  GLU A  68     -33.642 -15.941 -34.199  1.00 26.90           C  
ATOM     69  CA  GLU A  69     -30.339 -17.763 -33.510  1.00 26.19           C  
ATOM     70  CA  ILE A  70     -30.854 -17.583 -29.745  1.00 25.32           C  
ATOM     71  CA  SER A  71     -34.489 -18.785 -29.977  1.00 27.30           C  
ATOM     72  CA  LYS A  72     -33.172 -21.915 -31.815  1.00 29.46           C  
ATOM     73  CA  MET A  73     -30.768 -22.631 -28.911  1.00 29.42           C  
ATOM     74  CA  ASN A  74     -32.793 -21.694 -25.863  1.00 25.88           C  
ATOM     75  CA  GLU A  75     -36.267 -20.258 -25.953  1.00 26.56           C  
ATOM     76  CA  ASN A  76     -36.185 -19.020 -22.427  1.00 22.99           C  
ATOM     77  CA  LEU A  77     -32.804 -17.367 -22.235  1.00 19.17           C  
ATOM     78  CA  PRO A  78     -33.193 -13.863 -20.769  1.00 18.27           C  
ATOM     79  CA  LEU A  79     -32.400 -11.018 -23.146  1.00 19.76           C  
ATOM     80  CA  TYR A  80     -31.691  -7.521 -21.854  1.00 19.20           C  
ATOM     81  CA  ALA A  81     -32.131  -5.211 -24.814  1.00 18.16           C  
ATOM     82  CA  PHE A  82     -30.992  -1.603 -24.657  1.00 18.90           C  
ATOM     83  CA  ALA A  83     -33.261   0.581 -26.769  1.00 20.42           C  
ATOM     84  CA  ASN A  84     -32.697   3.793 -28.742  1.00 22.69           C  
ATOM     85  CA  THR A  85     -35.376   6.495 -29.276  1.00 23.76           C  
ATOM     86  CA  TYR A  86     -36.435   4.998 -32.621  1.00 25.59           C  
ATOM     87  CA  SER A  87     -36.020   1.305 -31.749  1.00 22.62           C  
ATOM     88  CA  THR A  88     -38.857  -0.888 -33.036  1.00 23.01           C  
ATOM     89  CA  LEU A  89     -39.928  -4.518 -33.553  1.00 23.13           C  
ATOM     90  CA  ASP A  90     -39.337  -6.117 -36.937  1.00 25.93           C  
ATOM     91  CA  VAL A  91     -42.087  -8.406 -38.281  1.00 26.47           C  
ATOM     92  CA  SER A  92     -39.544 -11.287 -38.468  1.00 26.64           C  
ATOM     93  CA  LEU A  93     -39.612 -11.419 -34.645  1.00 25.22           C  
ATOM     94  CA  ASN A  94     -43.376 -12.079 -34.439  1.00 26.82           C  
ATOM     95  CA  ASP A  95     -43.238 -15.836 -34.165  1.00 29.16           C  
ATOM     96  CA  LEU A  96     -39.994 -16.286 -32.178  1.00 25.83           C  
ATOM     97  CA  ARG A  97     -40.105 -17.452 -28.584  1.00 26.44           C  
ATOM     98  CA  LEU A  98     -38.050 -14.799 -26.794  1.00 23.26           C  
ATOM     99  CA  GLN A  99     -37.715 -13.573 -23.256  1.00 22.57           C  
ATOM    100  CA  ILE A 100     -36.912  -9.841 -23.629  1.00 21.66           C  
ATOM    101  CA  SER A 101     -36.617  -6.967 -21.170  1.00 21.54           C  
ATOM    102  CA  PHE A 102     -36.062  -3.499 -22.619  1.00 19.13           C  
ATOM    103  CA  PHE A 103     -33.806  -0.968 -20.879  1.00 19.58           C  
ATOM    104  CA  GLU A 104     -32.597   2.605 -21.477  1.00 20.12           C  
ATOM    105  CA  TYR A 105     -29.015   3.925 -21.351  1.00 18.14           C  
ATOM    106  CA  ALA A 106     -28.875   6.129 -18.249  1.00 20.50           C  
ATOM    107  CA  LEU A 107     -26.270   7.018 -15.642  1.00 19.58           C  
ATOM    108  CA  GLY A 108     -27.149   5.804 -12.184  1.00 21.54           C  
ATOM    109  CA  ALA A 109     -29.745   3.227 -13.352  1.00 19.77           C  
ATOM    110  CA  ALA A 110     -27.293   0.263 -12.990  1.00 19.83           C  
ATOM    111  CA  GLU A 111     -28.332  -0.762  -9.472  1.00 22.11           C  
ATOM    112  CA  ASP A 112     -31.988  -0.943 -10.509  1.00 21.57           C  
ATOM    113  CA  ILE A 113     -31.241  -2.743 -13.793  1.00 17.62           C  
ATOM    114  CA  ALA A 114     -28.988  -5.260 -11.941  1.00 18.04           C  
ATOM    115  CA  ASN A 115     -31.828  -5.983  -9.505  1.00 20.22           C  
ATOM    116  CA  LYS A 116     -34.262  -6.596 -12.379  1.00 19.72           C  
ATOM    117  CA  ILE A 117     -31.729  -8.914 -14.022  1.00 18.69           C  
ATOM    118  CA  LYS A 118     -31.388 -10.857 -10.725  1.00 20.93           C  
ATOM    119  CA  GLN A 119     -35.210 -11.160 -10.588  1.00 23.13           C  
ATOM    120  CA  THR A 120     -35.458 -12.269 -14.228  1.00 20.15           C  
ATOM    121  CA  THR A 121     -32.661 -14.833 -13.638  1.00 20.29           C  
ATOM    122  CA  ASP A 122     -34.628 -16.317 -10.719  1.00 21.58           C  
ATOM    123  CA  GLU A 123     -37.724 -16.366 -12.985  1.00 22.72           C  
ATOM    124  CA  TYR A 124     -35.697 -18.210 -15.635  1.00 20.92           C  
ATOM    125  CA  ILE A 125     -34.453 -20.755 -13.061  1.00 21.85           C  
ATOM    126  CA  ASN A 126     -38.048 -21.194 -11.885  1.00 25.91           C  
ATOM    127  CA  THR A 127     -39.299 -21.786 -15.452  1.00 25.57           C  
ATOM    128  CA  ILE A 128     -36.777 -24.482 -16.308  1.00 22.83           C  
ATOM    129  CA  LEU A 129     -36.799 -26.571 -13.073  1.00 22.30           C  
ATOM    130  CA  PRO A 130     -39.317 -29.507 -12.466  1.00 21.63           C  
ATOM    131  CA  PRO A 131     -41.903 -29.134  -9.659  1.00 21.74           C  
ATOM    132  CA  LEU A 132     -41.010 -31.530  -6.804  1.00 21.62           C  
ATOM    133  CA  THR A 133     -37.233 -30.927  -7.077  1.00 21.17           C  
ATOM    134  CA  LYS A 134     -37.891 -27.175  -7.093  1.00 23.01           C  
ATOM    135  CA  ALA A 135     -40.065 -27.479  -3.940  1.00 22.38           C  
ATOM    136  CA  LEU A 136     -37.446 -29.652  -2.235  1.00 22.75           C  
ATOM    137  CA  PHE A 137     -34.607 -27.143  -2.923  1.00 23.76           C  
ATOM    138  CA  LYS A 138     -36.806 -24.286  -1.741  1.00 25.45           C  
ATOM    139  CA  TYR A 139     -37.663 -26.165   1.454  1.00 25.24           C  
ATOM    140  CA  VAL A 140     -33.948 -26.736   2.149  1.00 27.69           C  
ATOM    141  CA  ARG A 141     -33.301 -22.977   1.695  1.00 33.90           C  
ATOM    142  CA  GLU A 142     -36.322 -21.684   3.682  1.00 39.72           C  
ATOM    143  CA  GLY A 143     -38.051 -24.361   5.891  1.00 45.19           C  
ATOM    144  CA  LYS A 144     -37.921 -24.520   9.797  1.00 48.98           C  
ATOM    145  CA  TYR A 145     -39.698 -27.690  10.959  1.00 46.76           C  
ATOM    146  CA  THR A 146     -38.621 -29.128  14.336  1.00 42.43           C  
ATOM    147  CA  PHE A 147     -39.733 -32.325  16.206  1.00 41.44           C  
ATOM    148  CA  CYS A 148     -39.567 -34.206  12.975  1.00 44.00           C  
ATOM    149  CA  THR A 149     -38.400 -37.467  11.520  1.00 38.74           C  
ATOM    150  CA  PRO A 150     -35.812 -38.378  10.079  1.00 34.37           C  
ATOM    151  CA  GLY A 151     -34.404 -38.304  13.609  1.00 32.21           C  
ATOM    152  CA  HIS A 152     -31.233 -36.675  12.350  1.00 29.71           C  
ATOM    153  CA  MET A 153     -33.167 -33.430  11.703  1.00 31.42           C  
ATOM    154  CA  GLY A 154     -31.403 -32.004   8.675  1.00 29.11           C  
ATOM    155  CA  GLY A 155     -28.087 -33.524   9.799  1.00 28.82           C  
ATOM    156  CA  THR A 156     -28.246 -31.967  13.298  1.00 31.78           C  
ATOM    157  CA  ALA A 157     -27.886 -35.279  15.147  1.00 29.89           C  
ATOM    158  CA  PHE A 158     -24.695 -36.097  13.213  1.00 28.20           C  
ATOM    159  CA  GLN A 159     -22.931 -32.894  14.451  1.00 30.33           C  
ATOM    160  CA  LYS A 160     -23.054 -33.939  18.094  1.00 29.42           C  
ATOM    161  CA  SER A 161     -20.883 -37.000  17.381  1.00 24.23           C  
ATOM    162  CA  PRO A 162     -17.216 -37.095  16.331  1.00 22.28           C  
ATOM    163  CA  VAL A 163     -17.821 -39.806  13.725  1.00 21.08           C  
ATOM    164  CA  GLY A 164     -21.220 -38.290  12.808  1.00 21.07           C  
ATOM    165  CA  SER A 165     -19.516 -34.939  12.133  1.00 21.12           C  
ATOM    166  CA  LEU A 166     -17.280 -36.644   9.583  1.00 20.39           C  
ATOM    167  CA  PHE A 167     -20.306 -38.225   7.854  1.00 20.03           C  
ATOM    168  CA  TYR A 168     -22.139 -34.836   7.860  1.00 21.50           C  
ATOM    169  CA  ASP A 169     -19.101 -32.993   6.539  1.00 22.77           C  
ATOM    170  CA  PHE A 170     -18.576 -35.537   3.779  1.00 20.94           C  
ATOM    171  CA  PHE A 171     -22.150 -35.390   2.380  1.00 22.27           C  
ATOM    172  CA  GLY A 172     -22.674 -31.689   3.231  1.00 23.54           C  
ATOM    173  CA  PRO A 173     -25.584 -29.513   4.456  1.00 23.69           C  
ATOM    174  CA  ASN A 174     -27.841 -29.709   1.368  1.00 22.74           C  
ATOM    175  CA  THR A 175     -27.742 -33.530   1.204  1.00 22.20           C  
ATOM    176  CA  MET A 176     -28.471 -33.789   4.931  1.00 23.55           C  
ATOM    177  CA  LYS A 177     -31.243 -31.159   4.960  1.00 23.68           C  
ATOM    178  CA  SER A 178     -33.024 -32.594   1.910  1.00 23.39           C  
ATOM    179  CA  ASP A 179     -33.534 -35.898   3.728  1.00 24.59           C  
ATOM    180  CA  ILE A 180     -37.081 -35.204   4.906  1.00 26.87           C  
ATOM    181  CA  SER A 181     -40.436 -36.920   5.612  1.00 28.57           C  
ATOM    182  CA  ILE A 182     -44.142 -36.223   4.943  1.00 31.34           C  
ATOM    183  CA  SER A 183     -44.046 -33.856   7.960  1.00 33.62           C  
ATOM    184  CA  VAL A 184     -42.967 -31.332   5.281  1.00 33.63           C  
ATOM    185  CA  SER A 185     -46.532 -31.012   4.152  1.00 34.80           C  
ATOM    186  CA  GLU A 186     -45.847 -28.684   1.329  1.00 33.56           C  
ATOM    187  CA  LEU A 187     -44.049 -31.420  -0.635  1.00 30.92           C  
ATOM    188  CA  GLY A 188     -47.135 -33.654  -0.540  1.00 29.27           C  
ATOM    189  CA  SER A 189     -46.690 -37.416  -0.321  1.00 26.46           C  
ATOM    190  CA  LEU A 190     -45.312 -40.144  -2.545  1.00 25.91           C  
ATOM    191  CA  LEU A 191     -47.715 -42.790  -1.208  1.00 29.77           C  
ATOM    192  CA  ASP A 192     -50.790 -40.523  -1.515  1.00 31.42           C  
ATOM    193  CA  HIS A 193     -49.542 -39.247  -4.877  1.00 29.87           C  
ATOM    194  CA  SER A 194     -50.387 -35.748  -3.667  1.00 29.29           C  
ATOM    195  CA  GLY A 195     -49.098 -32.153  -4.161  1.00 26.67           C  
ATOM    196  CA  PRO A 196     -45.722 -31.801  -5.905  1.00 24.98           C  
ATOM    197  CA  HIS A 197     -45.488 -35.636  -6.003  1.00 25.08           C  
ATOM    198  CA  LYS A 198     -48.603 -35.685  -8.202  1.00 26.81           C  
ATOM    199  CA  GLU A 199     -47.069 -32.955 -10.292  1.00 26.05           C  
ATOM    200  CA  ALA A 200     -43.827 -34.963 -10.568  1.00 24.54           C  
ATOM    201  CA  GLU A 201     -45.704 -38.072 -11.737  1.00 26.04           C  
ATOM    202  CA  GLN A 202     -47.624 -36.125 -14.400  1.00 25.83           C  
ATOM    203  CA  TYR A 203     -44.435 -34.380 -15.467  1.00 25.30           C  
ATOM    204  CA  ILE A 204     -42.624 -37.743 -15.843  1.00 24.18           C  
ATOM    205  CA  ALA A 205     -45.530 -39.373 -17.667  1.00 25.11           C  
ATOM    206  CA  ARG A 206     -45.525 -36.574 -20.244  1.00 26.49           C  
ATOM    207  CA  VAL A 207     -41.750 -36.727 -20.829  1.00 24.88           C  
ATOM    208  CA  PHE A 208     -41.712 -40.548 -21.030  1.00 26.53           C  
ATOM    209  CA  ASN A 209     -44.866 -40.970 -23.222  1.00 28.51           C  
ATOM    210  CA  ALA A 210     -46.933 -42.810 -20.594  1.00 28.85           C  
ATOM    211  CA  ASP A 211     -50.603 -42.426 -19.581  1.00 29.96           C  
ATOM    212  CA  ARG A 212     -49.475 -42.773 -15.956  1.00 30.04           C  
ATOM    213  CA  SER A 213     -46.009 -43.063 -14.289  1.00 26.74           C  
ATOM    214  CA  TYR A 214     -44.984 -44.226 -10.806  1.00 26.15           C  
ATOM    215  CA  MET A 215     -41.728 -43.367  -8.998  1.00 25.93           C  
ATOM    216  CA  VAL A 216     -40.176 -46.420  -7.328  1.00 24.49           C  
ATOM    217  CA  THR A 217     -37.418 -46.022  -4.720  1.00 23.23           C  
ATOM    218  CA  ASN A 218     -36.342 -49.648  -4.489  1.00 24.23           C  
ATOM    219  CA  GLY A 219     -35.122 -50.229  -8.052  1.00 24.70           C  
ATOM    220  CA  THR A 220     -36.643 -52.009 -11.036  1.00 27.37           C  
ATOM    221  CA  SER A 221     -36.273 -55.190  -8.881  1.00 28.03           C  
ATOM    222  CA  THR A 222     -39.259 -53.734  -7.004  1.00 27.07           C  
ATOM    223  CA  ALA A 223     -40.990 -52.085  -9.974  1.00 26.14           C  
ATOM    224  CA  ASN A 224     -41.145 -55.550 -11.657  1.00 27.78           C  
ATOM    225  CA  LYS A 225     -42.905 -57.012  -8.589  1.00 28.49           C  
ATOM    226  CA  ILE A 226     -45.427 -54.189  -8.283  1.00 28.50           C  
ATOM    227  CA  VAL A 227     -46.468 -54.727 -11.895  1.00 29.14           C  
ATOM    228  CA  GLY A 228     -46.381 -58.533 -11.438  1.00 33.94           C  
ATOM    229  CA  MET A 229     -48.424 -58.708  -8.226  1.00 35.78           C  
ATOM    230  CA  TYR A 230     -51.157 -56.473  -9.623  1.00 32.66           C  
ATOM    231  CA  SER A 231     -51.240 -58.411 -12.907  1.00 33.28           C  
ATOM    232  CA  ALA A 232     -51.045 -62.089 -11.875  1.00 35.63           C  
ATOM    233  CA  PRO A 233     -53.414 -63.294  -9.116  1.00 36.22           C  
ATOM    234  CA  ALA A 234     -52.841 -66.659  -7.358  1.00 38.07           C  
ATOM    235  CA  GLY A 235     -53.692 -69.632  -9.548  1.00 38.54           C  
ATOM    236  CA  SER A 236     -53.046 -67.710 -12.745  1.00 36.96           C  
ATOM    237  CA  THR A 237     -50.612 -68.526 -15.527  1.00 35.67           C  
ATOM    238  CA  ILE A 238     -48.064 -65.954 -16.867  1.00 35.19           C  
ATOM    239  CA  LEU A 239     -45.874 -65.903 -19.962  1.00 33.73           C  
ATOM    240  CA  ILE A 240     -42.312 -65.039 -18.992  1.00 33.99           C  
ATOM    241  CA  ASP A 241     -39.149 -64.415 -20.961  1.00 32.87           C  
ATOM    242  CA  ARG A 242     -36.705 -67.210 -20.113  1.00 33.04           C  
ATOM    243  CA  ASN A 243     -34.114 -64.446 -20.390  1.00 33.80           C  
ATOM    244  CA  CYS A 244     -35.414 -62.802 -17.228  1.00 33.72           C  
ATOM    245  CA  HIS A 245     -33.876 -60.766 -14.393  1.00 31.00           C  
ATOM    246  CA  LYS A 246     -33.586 -62.476 -11.023  1.00 31.20           C  
ATOM    247  CA  SER A 247     -36.290 -60.130  -9.656  1.00 27.69           C  
ATOM    248  CA  LEU A 248     -38.832 -61.872 -11.957  1.00 30.29           C  
ATOM    249  CA  THR A 249     -37.752 -65.253 -10.532  1.00 33.16           C  
ATOM    250  CA  HIS A 250     -38.296 -63.676  -7.094  1.00 34.12           C  
ATOM    251  CA  LEU A 251     -41.795 -62.645  -8.234  1.00 34.38           C  
ATOM    252  CA  MET A 252     -42.603 -66.280  -9.240  1.00 37.35           C  
ATOM    253  CA  MET A 253     -41.226 -67.483  -5.899  1.00 39.35           C  
ATOM    254  CA  MET A 254     -43.486 -65.015  -4.089  1.00 40.63           C  
ATOM    255  CA  SER A 255     -46.678 -65.363  -6.163  1.00 39.34           C  
ATOM    256  CA  ASP A 256     -48.657 -68.587  -6.529  1.00 36.77           C  
ATOM    257  CA  VAL A 257     -48.521 -68.514 -10.328  1.00 35.40           C  
ATOM    258  CA  THR A 258     -47.626 -70.971 -13.077  1.00 35.13           C  
ATOM    259  CA  PRO A 259     -45.042 -69.917 -15.633  1.00 35.58           C  
ATOM    260  CA  ILE A 260     -44.843 -70.757 -19.310  1.00 35.75           C  
ATOM    261  CA  TYR A 261     -41.575 -69.479 -20.863  1.00 34.39           C  
ATOM    262  CA  PHE A 262     -41.017 -67.490 -23.980  1.00 34.81           C  
ATOM    263  CA  ARG A 263     -37.885 -69.111 -25.512  1.00 37.12           C  
ATOM    264  CA  PRO A 264     -35.183 -66.720 -26.695  1.00 37.18           C  
ATOM    265  CA  THR A 265     -32.685 -67.684 -29.396  1.00 37.77           C  
ATOM    266  CA  ARG A 266     -28.847 -67.348 -29.051  1.00 36.63           C  
ATOM    267  CA  ASN A 267     -25.732 -67.384 -31.214  1.00 33.93           C  
ATOM    268  CA  ALA A 268     -22.383 -69.252 -31.076  1.00 33.69           C  
ATOM    269  CA  TYR A 269     -20.797 -66.409 -29.029  1.00 34.02           C  
ATOM    270  CA  GLY A 270     -23.432 -67.066 -26.362  1.00 34.14           C  
ATOM    271  CA  ILE A 271     -25.173 -63.749 -27.015  1.00 33.43           C  
ATOM    272  CA  LEU A 272     -28.943 -64.014 -26.484  1.00 34.65           C  
ATOM    273  CA  GLY A 273     -31.243 -63.316 -29.357  1.00 32.99           C  
ATOM    274  CA  GLY A 274     -34.890 -62.437 -29.486  1.00 32.57           C  
ATOM    275  CA  ILE A 275     -37.848 -64.636 -28.688  1.00 32.66           C  
ATOM    276  CA  PRO A 276     -38.985 -65.675 -32.219  1.00 32.87           C  
ATOM    277  CA  GLN A 277     -42.267 -64.323 -33.682  1.00 35.04           C  
ATOM    278  CA  SER A 278     -43.771 -67.853 -33.387  1.00 38.03           C  
ATOM    279  CA  GLU A 279     -43.656 -67.671 -29.558  1.00 37.33           C  
ATOM    280  CA  PHE A 280     -46.223 -64.831 -29.525  1.00 36.85           C  
ATOM    281  CA  GLN A 281     -48.813 -66.571 -31.712  1.00 38.95           C  
ATOM    282  CA  HIS A 282     -52.091 -67.847 -30.339  1.00 40.06           C  
ATOM    283  CA  ALA A 283     -51.604 -71.456 -31.512  1.00 41.16           C  
ATOM    284  CA  THR A 284     -48.177 -71.767 -29.874  1.00 40.29           C  
ATOM    285  CA  ILE A 285     -49.412 -70.468 -26.528  1.00 39.21           C  
ATOM    286  CA  ALA A 286     -52.589 -72.602 -26.614  1.00 41.12           C  
ATOM    287  CA  LYS A 287     -50.499 -75.755 -27.131  1.00 43.62           C  
ATOM    288  CA  ARG A 288     -48.233 -74.919 -24.142  1.00 43.50           C  
ATOM    289  CA  VAL A 289     -51.270 -74.138 -21.988  1.00 44.75           C  
ATOM    290  CA  LYS A 290     -52.621 -77.611 -22.927  1.00 48.26           C  
ATOM    291  CA  GLU A 291     -49.302 -79.313 -22.024  1.00 49.68           C  
ATOM    292  CA  THR A 292     -48.681 -77.397 -18.785  1.00 49.61           C  
ATOM    293  CA  PRO A 293     -50.242 -78.747 -15.582  1.00 50.47           C  
ATOM    294  CA  ASN A 294     -52.699 -76.301 -13.961  1.00 49.17           C  
ATOM    295  CA  ALA A 295     -52.077 -73.735 -16.693  1.00 44.64           C  
ATOM    296  CA  THR A 296     -54.886 -71.576 -17.996  1.00 41.39           C  
ATOM    297  CA  TRP A 297     -54.749 -68.857 -20.651  1.00 38.54           C  
ATOM    298  CA  PRO A 298     -51.982 -66.374 -19.601  1.00 36.15           C  
ATOM    299  CA  VAL A 299     -53.265 -63.239 -17.883  1.00 34.74           C  
ATOM    300  CA  HIS A 300     -49.841 -61.459 -17.997  1.00 32.60           C  
ATOM    301  CA  ALA A 301     -46.697 -61.591 -20.192  1.00 30.84           C  
ATOM    302  CA  VAL A 302     -43.183 -60.252 -19.370  1.00 30.85           C  
ATOM    303  CA  ILE A 303     -40.576 -59.622 -22.083  1.00 28.74           C  
ATOM    304  CA  THR A 304     -37.034 -58.291 -21.495  1.00 28.24           C  
ATOM    305  CA  ASN A 305     -36.619 -55.474 -23.963  1.00 27.03           C  
ATOM    306  CA  SER A 306     -33.876 -54.806 -24.959  1.00 26.34           C  
ATOM    307  CA  THR A 307     -31.611 -57.738 -24.238  1.00 27.79           C  
ATOM    308  CA  TYR A 308     -28.398 -56.844 -22.349  1.00 29.92           C  
ATOM    309  CA  ASP A 309     -26.398 -56.710 -25.618  1.00 30.03           C  
ATOM    310  CA  GLY A 310     -28.877 -54.267 -27.156  1.00 28.76           C  
ATOM    311  CA  LEU A 311     -31.355 -56.270 -29.227  1.00 27.89           C  
ATOM    312  CA  LEU A 312     -34.697 -54.551 -29.256  1.00 27.77           C  
ATOM    313  CA  TYR A 313     -37.974 -56.146 -30.388  1.00 30.12           C  
ATOM    314  CA  ASN A 314     -40.455 -54.910 -32.940  1.00 31.78           C  
ATOM    315  CA  THR A 315     -42.966 -54.086 -30.182  1.00 31.74           C  
ATOM    316  CA  ASP A 316     -45.651 -53.146 -32.742  1.00 35.47           C  
ATOM    317  CA  PHE A 317     -45.685 -56.790 -33.808  1.00 36.38           C  
ATOM    318  CA  ILE A 318     -45.810 -58.007 -30.200  1.00 35.82           C  
ATOM    319  CA  LYS A 319     -48.710 -55.746 -29.206  1.00 38.10           C  
ATOM    320  CA  LYS A 320     -50.672 -56.763 -32.330  1.00 40.40           C  
ATOM    321  CA  THR A 321     -49.882 -60.494 -32.035  1.00 37.85           C  
ATOM    322  CA  LEU A 322     -49.719 -61.425 -28.378  1.00 37.08           C  
ATOM    323  CA  ASP A 323     -53.285 -62.204 -27.234  1.00 37.34           C  
ATOM    324  CA  VAL A 324     -52.632 -61.318 -23.581  1.00 34.08           C  
ATOM    325  CA  LYS A 325     -54.448 -58.482 -21.827  1.00 33.30           C  
ATOM    326  CA  SER A 326     -51.357 -57.295 -19.900  1.00 32.42           C  
ATOM    327  CA  ILE A 327     -47.912 -57.010 -21.432  1.00 30.09           C  
ATOM    328  CA  HIS A 328     -44.884 -55.897 -19.344  1.00 29.57           C  
ATOM    329  CA  PHE A 329     -41.634 -54.907 -21.060  1.00 28.83           C  
ATOM    330  CA  ASP A 330     -38.785 -55.091 -18.495  1.00 27.49           C  
ATOM    331  CA  SER A 331     -37.021 -52.113 -20.045  1.00 26.68           C  
ATOM    332  CA  ALA A 332     -34.330 -51.622 -17.350  1.00 27.63           C  
ATOM    333  CA  TRP A 333     -31.586 -51.233 -20.000  1.00 29.03           C  
ATOM    334  CA  VAL A 334     -33.416 -48.803 -22.290  1.00 27.26           C  
ATOM    335  CA  PRO A 335     -34.908 -45.912 -20.224  1.00 26.08           C  
ATOM    336  CA  TYR A 336     -34.075 -43.444 -23.039  1.00 25.66           C  
ATOM    337  CA  THR A 337     -36.155 -44.895 -25.910  1.00 25.72           C  
ATOM    338  CA  ASN A 338     -38.698 -42.074 -25.914  1.00 26.46           C  
ATOM    339  CA  PHE A 339     -35.982 -39.481 -26.715  1.00 26.36           C  
ATOM    340  CA  SER A 340     -34.861 -40.480 -30.196  1.00 28.46           C  
ATOM    341  CA  PRO A 341     -37.055 -41.414 -33.178  1.00 30.23           C  
ATOM    342  CA  ILE A 342     -34.727 -44.403 -33.846  1.00 28.96           C  
ATOM    343  CA  TYR A 343     -36.471 -46.314 -31.058  1.00 27.63           C  
ATOM    344  CA  GLU A 344     -40.062 -45.843 -32.370  1.00 29.79           C  
ATOM    345  CA  GLY A 345     -41.845 -49.203 -32.696  1.00 29.88           C  
ATOM    346  CA  LYS A 346     -39.166 -50.808 -30.482  1.00 28.75           C  
ATOM    347  CA  CYS A 347     -40.214 -49.940 -26.940  1.00 29.63           C  
ATOM    348  CA  GLY A 348     -43.221 -50.559 -24.667  1.00 29.88           C  
ATOM    349  CA  MET A 349     -44.521 -46.985 -24.690  1.00 30.59           C  
ATOM    350  CA  SER A 350     -44.152 -46.425 -28.457  1.00 33.25           C  
ATOM    351  CA  GLY A 351     -47.384 -45.388 -30.221  1.00 38.18           C  
ATOM    352  CA  GLY A 352     -50.799 -45.143 -28.588  1.00 40.97           C  
ATOM    353  CA  ARG A 353     -53.116 -47.349 -26.596  1.00 38.53           C  
ATOM    354  CA  VAL A 354     -53.719 -50.949 -27.563  1.00 29.51           C  
ATOM    355  CA  GLU A 355     -57.449 -51.733 -27.347  1.00 39.33           C  
ATOM    356  CA  GLY A 356     -58.126 -54.289 -24.624  1.00 37.73           C  
ATOM    357  CA  LYS A 357     -54.552 -54.419 -23.286  1.00 34.08           C  
ATOM    358  CA  VAL A 358     -52.460 -52.603 -20.668  1.00 30.80           C  
ATOM    359  CA  ILE A 359     -48.757 -52.157 -21.557  1.00 29.54           C  
ATOM    360  CA  TYR A 360     -45.977 -51.486 -19.012  1.00 27.67           C  
ATOM    361  CA  GLU A 361     -42.360 -50.435 -19.113  1.00 26.26           C  
ATOM    362  CA  THR A 362     -40.258 -50.757 -15.989  1.00 25.20           C  
ATOM    363  CA  GLN A 363     -37.076 -48.682 -16.208  1.00 25.56           C  
ATOM    364  CA  SER A 364     -33.918 -48.391 -14.117  1.00 27.39           C  
ATOM    365  CA  THR A 365     -33.494 -44.624 -14.241  1.00 25.43           C  
ATOM    366  CA  HIS A 366     -30.133 -44.943 -12.430  1.00 25.47           C  
ATOM    367  CA  LEU A 368     -28.675 -45.510 -18.241  1.00 27.13           C  
ATOM    368  CA  LEU A 369     -30.097 -42.111 -17.359  1.00 26.30           C  
ATOM    369  CA  ALA A 370     -28.899 -39.787 -14.576  1.00 23.79           C  
ATOM    370  CA  ALA A 371     -30.485 -40.644 -11.226  1.00 21.97           C  
ATOM    371  CA  PHE A 372     -29.492 -41.975  -7.804  1.00 21.19           C  
ATOM    372  CA  SER A 373     -29.239 -45.754  -7.250  1.00 22.32           C  
ATOM    373  CA  GLN A 374     -32.635 -47.319  -6.481  1.00 23.05           C  
ATOM    374  CA  ALA A 375     -34.499 -44.800  -8.736  1.00 22.96           C  
ATOM    375  CA  SER A 376     -36.933 -46.651 -11.029  1.00 23.80           C  
ATOM    376  CA  MET A 377     -40.090 -45.836 -13.027  1.00 23.82           C  
ATOM    377  CA  ILE A 378     -43.251 -47.763 -13.945  1.00 24.75           C  
ATOM    378  CA  HIS A 379     -44.838 -46.451 -17.101  1.00 25.09           C  
ATOM    379  CA  VAL A 380     -48.429 -47.474 -17.915  1.00 27.80           C  
ATOM    380  CA  LYS A 381     -50.149 -47.321 -21.265  1.00 30.38           C  
ATOM    381  CA  GLY A 382     -53.835 -48.277 -20.923  1.00 33.61           C  
ATOM    382  CA  ASP A 383     -56.240 -48.523 -18.061  1.00 37.69           C  
ATOM    383  CA  VAL A 384     -55.227 -49.921 -14.750  1.00 36.72           C  
ATOM    384  CA  ASN A 385     -57.395 -50.065 -11.704  1.00 38.48           C  
ATOM    385  CA  GLU A 386     -55.968 -47.156  -9.927  1.00 39.84           C  
ATOM    386  CA  GLU A 387     -56.814 -48.056  -6.286  1.00 37.12           C  
ATOM    387  CA  THR A 388     -55.867 -51.732  -6.633  1.00 33.18           C  
ATOM    388  CA  PHE A 389     -52.677 -50.772  -8.494  1.00 31.96           C  
ATOM    389  CA  ASN A 390     -51.844 -48.381  -5.604  1.00 32.20           C  
ATOM    390  CA  GLU A 391     -52.268 -51.216  -3.068  1.00 32.02           C  
ATOM    391  CA  ALA A 392     -49.714 -53.244  -5.090  1.00 29.31           C  
ATOM    392  CA  TYR A 393     -47.422 -50.164  -5.231  1.00 28.57           C  
ATOM    393  CA  MET A 394     -47.756 -49.522  -1.516  1.00 29.98           C  
ATOM    394  CA  MET A 395     -47.074 -53.166  -0.593  1.00 30.77           C  
ATOM    395  CA  HIS A 396     -43.536 -52.793  -1.912  1.00 30.00           C  
ATOM    396  CA  THR A 397     -42.916 -49.065  -1.198  1.00 28.65           C  
ATOM    397  CA  THR A 398     -41.472 -48.125   2.134  1.00 26.60           C  
ATOM    398  CA  THR A 399     -43.168 -45.849   4.606  1.00 27.68           C  
ATOM    399  CA  SER A 400     -40.618 -43.122   4.501  1.00 26.41           C  
ATOM    400  CA  PRO A 401     -39.308 -42.315   1.060  1.00 25.15           C  
ATOM    401  CA  HIS A 402     -35.802 -41.027   0.455  1.00 22.86           C  
ATOM    402  CA  TYR A 403     -36.641 -37.679  -1.133  1.00 20.92           C  
ATOM    403  CA  GLY A 404     -33.242 -37.432  -2.876  1.00 20.80           C  
ATOM    404  CA  ILE A 405     -33.891 -40.638  -4.829  1.00 21.03           C  
ATOM    405  CA  VAL A 406     -37.446 -39.401  -5.672  1.00 21.18           C  
ATOM    406  CA  ALA A 407     -36.161 -35.934  -6.756  1.00 21.18           C  
ATOM    407  CA  SER A 408     -33.507 -37.556  -8.954  1.00 21.29           C  
ATOM    408  CA  THR A 409     -36.207 -39.586 -10.705  1.00 21.94           C  
ATOM    409  CA  GLU A 410     -38.121 -36.404 -11.539  1.00 22.42           C  
ATOM    410  CA  THR A 411     -34.892 -34.559 -12.463  1.00 21.48           C  
ATOM    411  CA  ALA A 412     -33.970 -37.354 -14.866  1.00 21.21           C  
ATOM    412  CA  ALA A 413     -37.184 -36.464 -16.721  1.00 21.43           C  
ATOM    413  CA  ALA A 414     -36.410 -32.732 -16.577  1.00 22.43           C  
ATOM    414  CA  MET A 415     -33.019 -33.500 -18.140  1.00 25.83           C  
ATOM    415  CA  MET A 416     -34.513 -35.511 -21.027  1.00 31.96           C  
ATOM    416  CA  LYS A 417     -37.232 -33.042 -21.766  1.00 39.97           C  
ATOM    417  CA  GLY A 418     -37.704 -31.444 -25.157  1.00 46.32           C  
ATOM    418  CA  ASN A 419     -34.740 -30.343 -27.250  1.00 49.90           C  
ATOM    419  CA  ALA A 420     -31.905 -30.571 -24.787  1.00 48.59           C  
ATOM    420  CA  GLY A 421     -32.907 -34.139 -23.928  1.00 44.96           C  
ATOM    421  CA  LYS A 422     -32.902 -34.967 -27.628  1.00 42.50           C  
ATOM    422  CA  ARG A 423     -29.413 -33.493 -27.872  1.00 39.11           C  
ATOM    423  CA  LEU A 424     -28.161 -35.617 -24.919  1.00 33.41           C  
ATOM    424  CA  ILE A 425     -29.439 -38.888 -26.383  1.00 31.62           C  
ATOM    425  CA  ASN A 426     -28.352 -37.895 -29.903  1.00 30.49           C  
ATOM    426  CA  GLY A 427     -24.884 -37.207 -28.508  1.00 26.76           C  
ATOM    427  CA  SER A 428     -24.600 -40.652 -26.936  1.00 27.51           C  
ATOM    428  CA  ILE A 429     -25.780 -42.314 -30.180  1.00 26.76           C  
ATOM    429  CA  GLU A 430     -23.321 -40.289 -32.285  1.00 26.17           C  
ATOM    430  CA  ARG A 431     -20.439 -41.158 -29.979  1.00 23.77           C  
ATOM    431  CA  ALA A 432     -21.378 -44.872 -29.969  1.00 24.21           C  
ATOM    432  CA  ILE A 433     -21.353 -44.848 -33.791  1.00 25.10           C  
ATOM    433  CA  LYS A 434     -18.080 -42.884 -33.946  1.00 25.24           C  
ATOM    434  CA  PHE A 435     -16.423 -45.489 -31.713  1.00 24.79           C  
ATOM    435  CA  ARG A 436     -17.970 -48.381 -33.721  1.00 25.92           C  
ATOM    436  CA  LYS A 437     -16.484 -46.949 -36.914  1.00 27.77           C  
ATOM    437  CA  GLU A 438     -13.110 -46.355 -35.179  1.00 28.20           C  
ATOM    438  CA  ILE A 439     -12.850 -50.094 -34.309  1.00 28.53           C  
ATOM    439  CA  LYS A 440     -13.644 -51.025 -37.925  1.00 30.38           C  
ATOM    440  CA  ARG A 441     -11.105 -48.462 -39.206  1.00 31.23           C  
ATOM    441  CA  LEU A 442      -8.312 -49.671 -36.893  1.00 32.16           C  
ATOM    442  CA  ARG A 443      -9.172 -53.258 -37.786  1.00 34.54           C  
ATOM    443  CA  THR A 444      -8.258 -52.447 -41.432  1.00 37.51           C  
ATOM    444  CA  GLU A 445      -5.314 -50.179 -40.630  1.00 38.48           C  
ATOM    445  CA  SER A 446      -3.549 -52.257 -37.976  1.00 40.87           C  
ATOM    446  CA  ASP A 447      -0.865 -54.926 -38.581  1.00 43.00           C  
ATOM    447  CA  GLY A 448      -2.350 -58.355 -37.910  1.00 38.16           C  
ATOM    448  CA  TRP A 449      -5.263 -59.253 -35.671  1.00 34.23           C  
ATOM    449  CA  PHE A 450      -7.582 -56.667 -34.117  1.00 32.28           C  
ATOM    450  CA  PHE A 451     -10.865 -56.437 -32.210  1.00 30.92           C  
ATOM    451  CA  ASP A 452     -14.064 -56.470 -34.229  1.00 30.55           C  
ATOM    452  CA  VAL A 453     -17.492 -54.951 -33.554  1.00 30.75           C  
ATOM    453  CA  TRP A 454     -20.581 -57.168 -33.588  1.00 31.73           C  
ATOM    454  CA  GLN A 455     -22.710 -55.169 -36.018  1.00 32.86           C  
ATOM    455  CA  PRO A 456     -23.758 -54.942 -39.687  1.00 37.09           C  
ATOM    456  CA  ASP A 457     -21.036 -54.719 -42.335  1.00 45.47           C  
ATOM    457  CA  HIS A 458     -22.177 -51.176 -43.119  1.00 49.69           C  
ATOM    458  CA  ILE A 459     -23.475 -48.738 -40.542  1.00 47.28           C  
ATOM    459  CA  ASP A 460     -23.637 -45.639 -42.738  1.00 46.62           C  
ATOM    460  CA  THR A 461     -27.037 -44.937 -41.276  1.00 41.21           C  
ATOM    461  CA  THR A 462     -28.171 -43.740 -37.801  1.00 36.47           C  
ATOM    462  CA  GLU A 463     -30.896 -46.146 -36.687  1.00 33.67           C  
ATOM    463  CA  CYS A 464     -31.316 -49.343 -34.713  1.00 31.31           C  
ATOM    464  CA  TRP A 465     -29.966 -51.562 -37.484  1.00 31.56           C  
ATOM    465  CA  PRO A 466     -32.347 -54.399 -38.443  1.00 33.04           C  
ATOM    466  CA  LEU A 467     -31.091 -57.974 -38.100  1.00 34.13           C  
ATOM    467  CA  ARG A 468     -31.792 -59.600 -41.497  1.00 36.89           C  
ATOM    468  CA  SER A 469     -32.129 -63.296 -42.440  1.00 39.54           C  
ATOM    469  CA  ASP A 470     -29.802 -62.591 -45.404  1.00 43.03           C  
ATOM    470  CA  SER A 471     -26.968 -61.282 -43.136  1.00 43.73           C  
ATOM    471  CA  THR A 472     -24.486 -63.382 -41.216  1.00 42.49           C  
ATOM    472  CA  TRP A 473     -23.010 -60.800 -38.814  1.00 36.00           C  
ATOM    473  CA  HIS A 474     -25.480 -61.448 -35.971  1.00 33.92           C  
ATOM    474  CA  GLY A 475     -25.004 -65.262 -35.992  1.00 35.19           C  
ATOM    475  CA  PHE A 476     -28.701 -66.115 -35.484  1.00 38.17           C  
ATOM    476  CA  LYS A 477     -30.103 -68.894 -37.632  1.00 42.97           C  
ATOM    477  CA  ASN A 478     -33.309 -68.340 -39.681  1.00 43.06           C  
ATOM    478  CA  ILE A 479     -34.173 -65.154 -37.892  1.00 39.68           C  
ATOM    479  CA  ASP A 480     -37.545 -63.521 -38.403  1.00 38.92           C  
ATOM    480  CA  ASN A 481     -37.240 -60.306 -40.391  1.00 38.77           C  
ATOM    481  CA  GLU A 482     -38.489 -56.913 -39.157  1.00 37.32           C  
ATOM    482  CA  HIS A 483     -38.385 -58.420 -35.708  1.00 33.80           C  
ATOM    483  CA  MET A 484     -35.001 -57.567 -33.987  1.00 32.38           C  
ATOM    484  CA  TYR A 485     -32.852 -54.421 -34.091  1.00 29.72           C  
ATOM    485  CA  LEU A 486     -29.427 -53.408 -32.716  1.00 27.66           C  
ATOM    486  CA  ASP A 487     -29.299 -50.422 -30.343  1.00 26.49           C  
ATOM    487  CA  PRO A 488     -26.280 -48.295 -31.440  1.00 27.04           C  
ATOM    488  CA  ILE A 489     -25.287 -47.477 -27.854  1.00 27.82           C  
ATOM    489  CA  LYS A 490     -24.713 -51.083 -26.759  1.00 26.00           C  
ATOM    490  CA  VAL A 491     -21.300 -51.814 -28.264  1.00 24.88           C  
ATOM    491  CA  THR A 492     -20.131 -55.433 -28.336  1.00 26.74           C  
ATOM    492  CA  LEU A 493     -16.498 -55.959 -29.207  1.00 27.55           C  
ATOM    493  CA  LEU A 494     -15.350 -59.347 -30.435  1.00 28.26           C  
ATOM    494  CA  THR A 495     -11.968 -60.920 -29.655  1.00 30.50           C  
ATOM    495  CA  PRO A 496     -10.095 -63.279 -31.988  1.00 33.66           C  
ATOM    496  CA  GLY A 497     -10.452 -67.014 -31.834  1.00 37.03           C  
ATOM    497  CA  MET A 498     -14.124 -67.200 -32.727  1.00 42.88           C  
ATOM    498  CA  GLU A 499     -15.156 -68.678 -35.974  1.00 50.39           C  
ATOM    499  CA  LYS A 500     -18.074 -67.890 -38.265  1.00 55.84           C  
ATOM    500  CA  ASP A 501     -19.084 -71.519 -38.011  1.00 56.95           C  
ATOM    501  CA  GLY A 502     -19.261 -71.445 -34.220  1.00 53.96           C  
ATOM    502  CA  THR A 503     -16.217 -73.750 -34.355  1.00 51.25           C  
ATOM    503  CA  MET A 504     -12.910 -72.833 -32.650  1.00 48.10           C  
ATOM    504  CA  SER A 505      -9.951 -70.950 -34.088  1.00 44.77           C  
ATOM    505  CA  ASP A 506      -6.332 -72.033 -33.515  1.00 44.55           C  
ATOM    506  CA  PHE A 507      -5.514 -68.466 -32.352  1.00 40.26           C  
ATOM    507  CA  GLY A 508      -7.702 -67.035 -29.579  1.00 34.56           C  
ATOM    508  CA  ILE A 509      -7.679 -64.330 -26.928  1.00 30.93           C  
ATOM    509  CA  PRO A 510     -10.292 -65.031 -24.233  1.00 30.66           C  
ATOM    510  CA  ALA A 511     -12.268 -61.848 -23.367  1.00 29.11           C  
ATOM    511  CA  SER A 512     -11.532 -62.270 -19.644  1.00 29.59           C  
ATOM    512  CA  ILE A 513      -7.922 -61.281 -20.434  1.00 29.26           C  
ATOM    513  CA  VAL A 514      -8.992 -58.076 -22.228  1.00 27.39           C  
ATOM    514  CA  ALA A 515     -11.291 -57.366 -19.253  1.00 28.07           C  
ATOM    515  CA  LYS A 516      -8.376 -57.677 -16.831  1.00 29.85           C  
ATOM    516  CA  TYR A 517      -6.336 -55.252 -18.944  1.00 28.02           C  
ATOM    517  CA  LEU A 518      -9.225 -52.750 -19.101  1.00 29.45           C  
ATOM    518  CA  ASP A 519      -9.633 -52.934 -15.343  1.00 34.76           C  
ATOM    519  CA  GLU A 520      -5.948 -51.867 -14.975  1.00 36.31           C  
ATOM    520  CA  HIS A 521      -6.951 -48.692 -16.786  1.00 37.20           C  
ATOM    521  CA  GLY A 522     -10.276 -48.258 -15.099  1.00 36.36           C  
ATOM    522  CA  ILE A 523     -12.110 -49.314 -18.129  1.00 32.00           C  
ATOM    523  CA  VAL A 524     -14.762 -51.810 -17.101  1.00 35.37           C  
ATOM    524  CA  VAL A 525     -16.375 -54.230 -19.333  1.00 37.40           C  
ATOM    525  CA  GLU A 526     -19.974 -54.443 -18.161  1.00 38.95           C  
ATOM    526  CA  LYS A 527     -20.539 -57.943 -19.510  1.00 38.90           C  
ATOM    527  CA  THR A 528     -18.143 -60.499 -20.956  1.00 39.42           C  
ATOM    528  CA  GLY A 529     -18.552 -63.870 -22.723  1.00 36.49           C  
ATOM    529  CA  PRO A 530     -15.902 -66.220 -24.140  1.00 32.92           C  
ATOM    530  CA  TYR A 531     -14.989 -63.906 -27.051  1.00 30.29           C  
ATOM    531  CA  ASN A 532     -17.238 -60.837 -26.496  1.00 29.73           C  
ATOM    532  CA  LEU A 533     -17.142 -57.650 -24.403  1.00 27.48           C  
ATOM    533  CA  LEU A 534     -19.978 -55.178 -23.922  1.00 25.79           C  
ATOM    534  CA  PHE A 535     -19.628 -51.375 -23.523  1.00 25.60           C  
ATOM    535  CA  LEU A 536     -22.515 -49.064 -22.689  1.00 26.40           C  
ATOM    536  CA  PHE A 537     -22.163 -45.698 -24.464  1.00 26.64           C  
ATOM    537  CA  SER A 538     -24.530 -43.911 -22.145  1.00 29.05           C  
ATOM    538  CA  ILE A 539     -25.000 -40.220 -21.604  1.00 31.94           C  
ATOM    539  CA  GLY A 540     -22.275 -40.660 -18.977  1.00 32.45           C  
ATOM    540  CA  ILE A 541     -19.685 -41.650 -21.449  1.00 30.62           C  
ATOM    541  CA  ASP A 542     -18.119 -38.537 -22.961  1.00 27.96           C  
ATOM    542  CA  LYS A 543     -15.498 -38.210 -25.737  1.00 25.24           C  
ATOM    543  CA  THR A 544     -12.701 -38.381 -23.183  1.00 25.90           C  
ATOM    544  CA  LYS A 545     -13.831 -41.797 -21.884  1.00 25.53           C  
ATOM    545  CA  ALA A 546     -14.325 -43.122 -25.430  1.00 24.50           C  
ATOM    546  CA  LEU A 547     -10.836 -42.079 -26.414  1.00 23.62           C  
ATOM    547  CA  SER A 548      -9.405 -43.654 -23.271  1.00 23.78           C  
ATOM    548  CA  LEU A 549     -11.145 -46.964 -24.116  1.00 22.44           C  
ATOM    549  CA  LEU A 550      -9.979 -46.815 -27.747  1.00 23.02           C  
ATOM    550  CA  ARG A 551      -6.383 -46.183 -26.619  1.00 22.30           C  
ATOM    551  CA  ALA A 552      -6.576 -48.923 -24.045  1.00 22.69           C  
ATOM    552  CA  LEU A 553      -7.659 -51.351 -26.775  1.00 24.18           C  
ATOM    553  CA  THR A 554      -4.812 -50.383 -29.106  1.00 25.37           C  
ATOM    554  CA  ASP A 555      -2.434 -50.706 -26.099  1.00 26.98           C  
ATOM    555  CA  PHE A 556      -3.756 -54.199 -25.343  1.00 26.06           C  
ATOM    556  CA  LYS A 557      -2.859 -55.238 -28.903  1.00 27.43           C  
ATOM    557  CA  ARG A 558       0.562 -53.502 -28.721  1.00 27.50           C  
ATOM    558  CA  ALA A 559       1.438 -55.227 -25.400  1.00 27.70           C  
ATOM    559  CA  PHE A 560      -0.032 -58.559 -26.464  1.00 28.88           C  
ATOM    560  CA  ASP A 561       2.087 -58.596 -29.618  1.00 30.74           C  
ATOM    561  CA  LEU A 562       5.277 -57.826 -27.609  1.00 31.44           C  
ATOM    562  CA  ASN A 563       4.280 -60.564 -25.228  1.00 31.40           C  
ATOM    563  CA  LEU A 564       4.760 -58.239 -22.418  1.00 31.29           C  
ATOM    564  CA  ARG A 565       5.128 -60.117 -19.207  1.00 32.01           C  
ATOM    565  CA  VAL A 566       1.945 -60.674 -17.179  1.00 31.60           C  
ATOM    566  CA  LYS A 567       3.831 -58.991 -14.313  1.00 33.25           C  
ATOM    567  CA  ASN A 568       4.148 -55.773 -16.372  1.00 33.57           C  
ATOM    568  CA  MET A 569       0.958 -55.756 -18.433  1.00 31.82           C  
ATOM    569  CA  LEU A 570      -1.440 -57.113 -15.797  1.00 31.62           C  
ATOM    570  CA  PRO A 571       0.038 -56.059 -12.438  1.00 33.70           C  
ATOM    571  CA  SER A 572      -3.194 -56.659 -10.441  1.00 37.10           C  
ATOM    572  CA  LEU A 573      -3.465 -60.199 -11.820  1.00 37.66           C  
ATOM    573  CA  TYR A 574       0.213 -60.731 -10.941  1.00 41.08           C  
ATOM    574  CA  ARG A 575      -0.401 -59.589  -7.333  1.00 45.41           C  
ATOM    575  CA  GLU A 576      -3.017 -62.347  -6.929  1.00 48.16           C  
ATOM    576  CA  ASP A 577      -0.323 -65.013  -7.294  1.00 45.16           C  
ATOM    577  CA  PRO A 578       3.149 -63.525  -7.914  1.00 42.89           C  
ATOM    578  CA  GLU A 579       4.875 -66.920  -7.830  1.00 44.57           C  
ATOM    579  CA  PHE A 580       2.435 -68.413 -10.377  1.00 41.35           C  
ATOM    580  CA  TYR A 581       2.736 -65.388 -12.702  1.00 39.61           C  
ATOM    581  CA  GLU A 582       6.408 -64.435 -12.161  1.00 41.56           C  
ATOM    582  CA  ASN A 583       7.676 -65.582 -15.565  1.00 41.81           C  
ATOM    583  CA  MET A 584       4.531 -65.903 -17.698  1.00 38.86           C  
ATOM    584  CA  ARG A 585       3.973 -63.650 -20.696  1.00 35.61           C  
ATOM    585  CA  ILE A 586       0.637 -62.384 -21.945  1.00 33.14           C  
ATOM    586  CA  GLN A 587       0.540 -64.471 -25.170  1.00 33.94           C  
ATOM    587  CA  GLU A 588       1.136 -67.634 -23.143  1.00 36.92           C  
ATOM    588  CA  LEU A 589      -1.687 -66.814 -20.706  1.00 34.94           C  
ATOM    589  CA  ALA A 590      -3.963 -66.192 -23.669  1.00 34.23           C  
ATOM    590  CA  GLN A 591      -2.922 -69.458 -25.403  1.00 37.72           C  
ATOM    591  CA  ASN A 592      -3.265 -71.614 -22.358  1.00 37.39           C  
ATOM    592  CA  ILE A 593      -6.722 -70.333 -21.358  1.00 35.48           C  
ATOM    593  CA  HIS A 594      -7.920 -70.586 -24.970  1.00 36.45           C  
ATOM    594  CA  LYS A 595      -6.623 -74.170 -25.245  1.00 39.64           C  
ATOM    595  CA  LEU A 596      -8.488 -74.966 -22.032  1.00 41.03           C  
ATOM    596  CA  ILE A 597     -11.686 -73.591 -23.616  1.00 40.78           C  
ATOM    597  CA  VAL A 598     -11.122 -75.598 -26.806  1.00 43.42           C  
ATOM    598  CA  HIS A 599     -10.173 -78.745 -24.864  1.00 46.03           C  
ATOM    599  CA  HIS A 600     -13.145 -78.636 -22.475  1.00 45.87           C  
ATOM    600  CA  ASN A 601     -15.404 -77.990 -25.471  1.00 46.14           C  
ATOM    601  CA  LEU A 602     -16.856 -75.047 -23.501  1.00 43.29           C  
ATOM    602  CA  PRO A 603     -18.955 -73.373 -26.184  1.00 43.03           C  
ATOM    603  CA  ASP A 604     -20.717 -76.556 -27.350  1.00 43.30           C  
ATOM    604  CA  LEU A 605     -21.448 -77.597 -23.773  1.00 40.23           C  
ATOM    605  CA  MET A 606     -22.728 -74.128 -22.906  1.00 38.98           C  
ATOM    606  CA  TYR A 607     -25.117 -74.098 -25.837  1.00 40.82           C  
ATOM    607  CA  ARG A 608     -26.470 -77.596 -25.052  1.00 42.67           C  
ATOM    608  CA  ALA A 609     -26.864 -76.940 -21.296  1.00 42.72           C  
ATOM    609  CA  PHE A 610     -29.400 -74.168 -22.053  1.00 44.71           C  
ATOM    610  CA  GLU A 611     -31.239 -75.826 -24.905  1.00 49.84           C  
ATOM    611  CA  VAL A 612     -32.913 -78.331 -22.540  1.00 51.16           C  
ATOM    612  CA  LEU A 613     -34.857 -77.454 -19.396  1.00 47.75           C  
ATOM    613  CA  PRO A 614     -34.495 -79.046 -15.998  1.00 44.28           C  
ATOM    614  CA  THR A 615     -37.730 -80.769 -14.936  1.00 41.16           C  
ATOM    615  CA  MET A 616     -40.059 -78.728 -12.740  1.00 39.94           C  
ATOM    616  CA  VAL A 617     -40.762 -81.080  -9.858  1.00 39.89           C  
ATOM    617  CA  MET A 618     -42.254 -78.324  -7.705  1.00 38.62           C  
ATOM    618  CA  THR A 619     -42.760 -74.564  -8.169  1.00 35.61           C  
ATOM    619  CA  PRO A 620     -40.157 -72.079  -6.881  1.00 31.73           C  
ATOM    620  CA  TYR A 621     -42.689 -71.123  -4.188  1.00 31.90           C  
ATOM    621  CA  ALA A 622     -43.181 -74.720  -3.043  1.00 33.30           C  
ATOM    622  CA  ALA A 623     -39.394 -75.247  -3.017  1.00 34.29           C  
ATOM    623  CA  PHE A 624     -38.833 -72.148  -0.863  1.00 35.96           C  
ATOM    624  CA  GLN A 625     -41.507 -73.325   1.631  1.00 36.82           C  
ATOM    625  CA  LYS A 626     -39.444 -76.512   2.052  1.00 37.53           C  
ATOM    626  CA  GLU A 627     -36.361 -74.409   2.663  1.00 37.54           C  
ATOM    627  CA  LEU A 628     -38.267 -72.383   5.247  1.00 38.50           C  
ATOM    628  CA  HIS A 629     -38.954 -75.683   7.058  1.00 42.34           C  
ATOM    629  CA  GLY A 630     -35.252 -76.589   7.014  1.00 44.55           C  
ATOM    630  CA  MET A 631     -35.717 -79.369   4.467  1.00 46.91           C  
ATOM    631  CA  THR A 632     -32.442 -78.760   2.642  1.00 46.79           C  
ATOM    632  CA  GLU A 633     -29.019 -80.403   2.594  1.00 48.20           C  
ATOM    633  CA  GLU A 634     -25.821 -80.008   0.531  1.00 50.67           C  
ATOM    634  CA  VAL A 635     -24.662 -82.721  -1.822  1.00 51.49           C  
ATOM    635  CA  TYR A 636     -21.708 -82.676  -4.232  1.00 52.65           C  
ATOM    636  CA  LEU A 637     -22.456 -81.288  -7.694  1.00 52.72           C  
ATOM    637  CA  ASP A 638     -21.678 -84.726  -9.197  1.00 53.93           C  
ATOM    638  CA  GLU A 639     -24.520 -86.269  -7.163  1.00 53.45           C  
ATOM    639  CA  MET A 640     -27.293 -83.867  -8.161  1.00 50.99           C  
ATOM    640  CA  VAL A 641     -29.088 -85.789 -10.947  1.00 47.65           C  
ATOM    641  CA  GLY A 642     -32.553 -86.746  -9.644  1.00 44.36           C  
ATOM    642  CA  ARG A 643     -32.368 -84.177  -6.797  1.00 42.00           C  
ATOM    643  CA  ILE A 644     -34.686 -81.169  -6.300  1.00 39.51           C  
ATOM    644  CA  ASN A 645     -32.651 -77.954  -6.423  1.00 39.00           C  
ATOM    645  CA  ALA A 646     -33.082 -75.539  -3.553  1.00 38.99           C  
ATOM    646  CA  ASN A 647     -31.320 -72.424  -5.073  1.00 40.71           C  
ATOM    647  CA  MET A 648     -31.204 -70.770  -8.470  1.00 40.94           C  
ATOM    648  CA  ILE A 649     -28.056 -71.917 -10.238  1.00 38.91           C  
ATOM    649  CA  LEU A 650     -26.611 -69.031 -12.181  1.00 36.92           C  
ATOM    650  CA  PRO A 651     -23.328 -69.761 -13.922  1.00 35.43           C  
ATOM    651  CA  TYR A 652     -20.906 -67.213 -15.458  1.00 35.34           C  
ATOM    652  CA  PRO A 653     -20.763 -67.685 -18.366  1.00 35.30           C  
ATOM    653  CA  PRO A 654     -23.305 -67.141 -19.830  1.00 35.34           C  
ATOM    654  CA  GLY A 655     -24.810 -65.251 -16.868  1.00 35.25           C  
ATOM    655  CA  VAL A 656     -28.457 -66.398 -17.169  1.00 35.66           C  
ATOM    656  CA  PRO A 657     -30.460 -68.806 -14.910  1.00 35.33           C  
ATOM    657  CA  LEU A 658     -29.656 -72.491 -15.508  1.00 34.80           C  
ATOM    658  CA  VAL A 659     -31.691 -74.252 -12.767  1.00 35.76           C  
ATOM    659  CA  MET A 660     -34.559 -72.768 -10.697  1.00 37.75           C  
ATOM    660  CA  PRO A 661     -35.515 -73.652  -7.152  1.00 37.55           C  
ATOM    661  CA  GLY A 662     -37.836 -76.705  -7.440  1.00 37.17           C  
ATOM    662  CA  GLU A 663     -36.276 -78.039 -10.627  1.00 36.44           C  
ATOM    663  CA  MET A 664     -34.356 -81.300 -11.016  1.00 38.56           C  
ATOM    664  CA  ILE A 665     -31.658 -82.390 -13.455  1.00 40.38           C  
ATOM    665  CA  THR A 666     -32.627 -85.737 -15.076  1.00 43.60           C  
ATOM    666  CA  GLU A 667     -31.078 -87.829 -17.882  1.00 47.23           C  
ATOM    667  CA  GLU A 668     -33.021 -85.791 -20.403  1.00 48.29           C  
ATOM    668  CA  SER A 669     -31.238 -82.670 -19.002  1.00 45.46           C  
ATOM    669  CA  ARG A 670     -27.777 -84.134 -18.199  1.00 43.84           C  
ATOM    670  CA  PRO A 671     -25.988 -81.465 -20.370  1.00 41.52           C  
ATOM    671  CA  VAL A 672     -26.901 -79.003 -17.578  1.00 40.46           C  
ATOM    672  CA  LEU A 673     -24.771 -80.985 -15.129  1.00 40.76           C  
ATOM    673  CA  GLU A 674     -21.997 -81.591 -17.681  1.00 41.59           C  
ATOM    674  CA  PHE A 675     -21.662 -77.855 -18.393  1.00 40.16           C  
ATOM    675  CA  LEU A 676     -21.501 -77.126 -14.645  1.00 39.39           C  
ATOM    676  CA  GLN A 677     -18.841 -79.824 -13.973  1.00 40.25           C  
ATOM    677  CA  MET A 678     -16.786 -78.498 -16.887  1.00 40.34           C  
ATOM    678  CA  LEU A 679     -16.907 -74.913 -15.497  1.00 40.52           C  
ATOM    679  CA  CYS A 680     -15.671 -76.244 -12.185  1.00 42.10           C  
ATOM    680  CA  GLU A 681     -12.734 -78.034 -13.834  1.00 44.80           C  
ATOM    681  CA  ILE A 682     -11.661 -75.268 -16.267  1.00 43.52           C  
ATOM    682  CA  GLY A 683     -11.696 -72.701 -13.427  1.00 43.24           C  
ATOM    683  CA  ALA A 684      -9.227 -74.583 -11.228  1.00 43.85           C  
ATOM    684  CA  HIS A 685      -6.174 -73.822 -13.413  1.00 44.04           C  
ATOM    685  CA  TYR A 686      -5.484 -70.067 -13.391  1.00 40.88           C  
ATOM    686  CA  PRO A 687      -5.533 -67.758 -10.395  1.00 38.82           C  
ATOM    687  CA  GLY A 688      -7.854 -64.819 -11.211  1.00 36.66           C  
ATOM    688  CA  PHE A 689      -9.905 -66.989 -13.561  1.00 36.40           C  
ATOM    689  CA  GLU A 690     -11.859 -68.907 -10.900  1.00 38.34           C  
ATOM    690  CA  THR A 691     -15.115 -70.782 -11.409  1.00 37.38           C  
ATOM    691  CA  ASP A 692     -18.111 -68.425 -10.948  1.00 37.64           C  
ATOM    692  CA  ILE A 693     -21.383 -70.287 -10.364  1.00 37.94           C  
ATOM    693  CA  HIS A 694     -23.930 -68.748  -8.045  1.00 40.38           C  
ATOM    694  CA  GLY A 695     -25.518 -71.558  -5.982  1.00 43.09           C  
ATOM    695  CA  ALA A 696     -22.388 -73.736  -6.148  1.00 45.87           C  
ATOM    696  CA  TYR A 697     -19.991 -73.757  -3.218  1.00 49.29           C  
ATOM    697  CA  ARG A 698     -16.272 -74.462  -3.527  1.00 51.34           C  
ATOM    698  CA  GLN A 699     -15.136 -76.754  -0.724  1.00 53.91           C  
ATOM    699  CA  ALA A 700     -11.634 -76.594   0.795  1.00 56.36           C  
ATOM    700  CA  ASP A 701     -10.713 -79.682  -1.261  1.00 57.49           C  
ATOM    701  CA  GLY A 702     -11.638 -78.035  -4.599  1.00 55.50           C  
ATOM    702  CA  ARG A 703     -14.936 -79.916  -5.065  1.00 53.19           C  
ATOM    703  CA  TYR A 704     -18.303 -78.085  -5.428  1.00 48.50           C  
ATOM    704  CA  THR A 705     -21.558 -78.590  -3.528  1.00 45.53           C  
ATOM    705  CA  VAL A 706     -25.161 -77.517  -4.198  1.00 42.67           C  
ATOM    706  CA  LYS A 707     -28.128 -77.154  -1.874  1.00 42.16           C  
ATOM    707  CA  VAL A 708     -30.956 -79.643  -2.546  1.00 40.50           C  
ATOM    708  CA  LEU A 709     -34.197 -80.659  -0.909  1.00 42.13           C  
ATOM    709  CA  LYS A 710     -34.022 -83.590   1.578  1.00 46.26           C  
ATOM    710  CA  GLU A 711     -35.319 -86.894   0.275  1.00 50.45           C  
TER     711      GLU A 711                                                      
ATOM    712  CA  THR D 361     -24.210 -98.080  14.769  1.00 84.11           C  
ATOM    713  CA  LEU D 362     -20.810 -97.987  13.048  1.00 85.40           C  
ATOM    714  CA  THR D 363     -17.436 -98.709  14.631  1.00 76.62           C  
ATOM    715  CA  LEU D 364     -14.306 -96.718  13.826  1.00 75.53           C  
ATOM    716  CA  LEU D 365     -10.741 -97.945  14.300  1.00 75.51           C  
ATOM    717  CA  LEU D 366      -7.885 -95.590  15.180  1.00 80.65           C  
ATOM    718  CA  GLN D 367      -4.489 -95.299  13.434  1.00 87.50           C  
ATOM    719  CA  LYS D 368      -2.786 -94.557  16.736  1.00 86.43           C  
ATOM    720  CA  PRO D 369      -4.442 -96.478  19.601  1.00 83.94           C  
ATOM    721  CA  LEU D 370      -4.893 -94.260  22.659  1.00 75.26           C  
ATOM    722  CA  LYS D 371      -5.308 -94.577  26.423  1.00 76.79           C  
ATOM    723  CA  LEU D 372      -8.908 -93.435  27.001  1.00 76.44           C  
ATOM    724  CA  HIS D 373     -10.763 -93.766  30.327  1.00 79.19           C  
ATOM    725  CA  ASP D 374      -7.903 -95.756  31.905  1.00 93.54           C  
ATOM    726  CA  MET D 375      -7.754 -98.352  29.101  1.00 95.66           C  
ATOM    727  CA  GLU D 376      -6.170 -98.651  25.660  1.00 90.47           C  
ATOM    728  CA  VAL D 377      -8.747 -98.473  22.855  1.00 81.44           C  
ATOM    729  CA  VAL D 378      -8.352 -99.674  19.253  1.00 83.74           C  
ATOM    730  CA  HIS D 379     -11.937 -98.960  18.088  1.00 75.02           C  
ATOM    731  CA  ILE D 380     -14.914 -96.777  19.071  1.00 71.54           C  
ATOM    732  CA  SER D 381     -18.506 -97.543  18.097  1.00 71.92           C  
ATOM    733  CA  PHE D 382     -20.925 -94.666  17.520  1.00 73.28           C  
ATOM    734  CA  GLU D 383     -24.671 -94.611  17.150  1.00 82.13           C  
ATOM    735  CA  ARG D 384     -24.747 -93.188  13.599  1.00 87.39           C  
ATOM    736  CA  SER D 385     -27.709 -91.006  14.617  1.00 89.75           C  
ATOM    737  CA  ALA D 386     -25.661 -89.386  17.419  1.00 89.08           C  
ATOM    738  CA  LEU D 387     -22.682 -88.820  15.122  1.00 83.17           C  
ATOM    739  CA  GLU D 388     -24.965 -87.067  12.601  1.00 96.57           C  
ATOM    740  CA  GLN D 389     -26.222 -84.383  14.999  1.00 99.86           C  
ATOM    741  CA  TRP D 390     -22.705 -83.766  16.319  1.00 90.17           C  
ATOM    742  CA  LEU D 391     -21.395 -83.325  12.766  1.00 91.84           C  
ATOM    743  CA  SER D 392     -24.186 -80.796  12.174  1.00103.02           C  
ATOM    744  CA  LYS D 393     -24.932 -79.025  15.479  1.00100.96           C  
ATOM    745  CA  GLY D 394     -21.663 -79.781  17.303  1.00100.13           C  
ATOM    746  CA  GLY D 395     -21.672 -79.907  21.103  1.00 95.98           C  
ATOM    747  CA  GLU D 396     -20.684 -83.099  22.910  1.00 88.78           C  
ATOM    748  CA  ILE D 397     -20.473 -86.640  21.539  1.00 80.20           C  
ATOM    749  CA  ARG D 398     -20.384 -89.988  23.335  1.00 75.67           C  
ATOM    750  CA  GLY D 399     -19.038 -93.310  22.050  1.00 71.18           C  
ATOM    751  CA  LYS D 400     -18.597 -96.794  23.514  1.00 73.29           C  
ATOM    752  CA  LEU D 401     -14.896 -97.617  23.790  1.00 71.62           C  
ATOM    753  CA  ASN D 402     -13.812-100.882  22.141  1.00 65.13           C  
ATOM    754  CA  GLY D 403     -17.494-101.391  21.266  1.00 68.88           C  
ATOM    755  CA  ILE D 404     -18.423-102.280  24.853  1.00 71.99           C  
ATOM    756  CA  GLY D 405     -19.597-100.593  28.060  1.00 77.46           C  
ATOM    757  CA  PHE D 406     -21.283 -97.212  28.420  1.00 82.46           C  
ATOM    758  CA  ALA D 407     -21.292 -94.480  25.772  1.00 79.92           C  
ATOM    759  CA  GLN D 408     -18.439 -92.308  27.082  1.00 73.76           C  
ATOM    760  CA  LYS D 409     -17.958 -88.616  26.262  1.00 73.79           C  
ATOM    761  CA  LEU D 410     -15.089 -88.042  23.825  1.00 78.56           C  
ATOM    762  CA  ASN D 411     -12.596 -85.344  22.904  1.00 78.21           C  
ATOM    763  CA  LEU D 412     -13.475 -85.386  19.204  1.00 80.25           C  
ATOM    764  CA  GLU D 413     -12.839 -82.786  16.494  1.00 81.39           C  
ATOM    765  CA  VAL D 414     -13.256 -82.360  12.737  1.00 86.72           C  
ATOM    766  CA  ASP D 415      -9.811 -82.154  11.114  1.00 88.70           C  
ATOM    767  CA  SER D 416      -8.619 -79.671   8.467  1.00 97.00           C  
ATOM    768  CA  ALA D 417      -8.144 -82.695   6.187  1.00 85.37           C  
ATOM    769  CA  GLN D 418     -11.832 -83.391   7.014  1.00 90.71           C  
ATOM    770  CA  HIS D 419     -11.007 -86.361   9.289  1.00 86.31           C  
ATOM    771  CA  LEU D 420     -12.232 -87.236  12.786  1.00 76.80           C  
ATOM    772  CA  VAL D 421      -9.604 -86.966  15.529  1.00 82.43           C  
ATOM    773  CA  VAL D 422      -9.962 -88.284  19.101  1.00 78.42           C  
ATOM    774  CA  ARG D 423      -7.682 -86.979  21.842  1.00 77.97           C  
ATOM    775  CA  ASP D 424      -6.618 -88.320  25.238  1.00 79.02           C  
ATOM    776  CA  VAL D 425      -5.746 -86.402  28.433  1.00 76.37           C  
ATOM    777  CA  SER D 426      -2.262 -85.727  26.995  1.00 73.44           C  
ATOM    778  CA  LEU D 427      -4.068 -84.165  23.985  1.00 77.62           C  
ATOM    779  CA  GLN D 428      -2.499 -86.918  21.825  1.00 72.41           C  
ATOM    780  CA  GLY D 429      -4.490 -87.154  18.596  1.00 77.15           C  
ATOM    781  CA  SER D 430      -5.646 -90.144  16.567  1.00 73.06           C  
ATOM    782  CA  THR D 431      -7.346 -90.282  13.174  1.00 83.82           C  
ATOM    783  CA  LEU D 432     -10.445 -92.471  12.849  1.00 82.05           C  
ATOM    784  CA  ALA D 433     -10.815 -95.003  10.032  1.00 90.07           C  
ATOM    785  CA  LEU D 434     -13.709 -97.179   8.851  1.00 97.41           C  
TER     786      LEU D 434                                                      
MASTER      176    0    0    0    0    0    0    6  784    2    0   64          
END                                                                             
