HEADER    TRANSPORT PROTEIN                       27-AUG-14   4UY0              
TITLE     CONSERVED MECHANISMS OF MICROTUBULE-STIMULATED ADP RELEASE, ATP       
TITLE    2 BINDING, AND FORCE GENERATION IN TRANSPORT KINESINS                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUBULIN ALPHA-1B CHAIN;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA-TUBULIN UBIQUITOUS, TUBULIN K-ALPHA-1;                
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TUBULIN BETA-2B CHAIN;                                     
COMPND   7 CHAIN: B;                                                            
COMPND   8 FRAGMENT: RESIDUES 2-427;                                            
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: KINESIN HEAVY CHAIN ISOFORM 5A;                            
COMPND  11 CHAIN: C;                                                            
COMPND  12 FRAGMENT: MOTOR DOMAIN, UNP RESIDUES 1-340;                          
COMPND  13 SYNONYM: KINESIN HEAVY CHAIN NEURON-SPECIFIC 1, NEURONAL KINESIN     
COMPND  14 HEAVY CHAIN, NKHC;                                                   
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   7 ORGANISM_COMMON: CATTLE;                                             
SOURCE   8 ORGANISM_TAXID: 9913;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET151-D-TOPO                             
KEYWDS    TRANSPORT PROTEIN                                                     
EXPDTA    ELECTRON MICROSCOPY                                                   
MDLTYP    CA ATOMS ONLY, CHAIN A, B, C                                          
AUTHOR    J.ATHERTON,I.FARABELLA,I.M.YU,S.S.ROSENFELD,A.HOUDUSSE,M.TOPF,        
AUTHOR   2 C.MOORES                                                             
REVDAT   3   30-AUG-17 4UY0    1       REMARK                                   
REVDAT   2   22-OCT-14 4UY0    1       JRNL                                     
REVDAT   1   24-SEP-14 4UY0    0                                                
JRNL        AUTH   J.ATHERTON,I.FARABELLA,I.YU,S.S.ROSENFELD,A.HOUDUSSE,M.TOPF, 
JRNL        AUTH 2 C.A.MOORES                                                   
JRNL        TITL   CONSERVED MECHANISMS OF MICROTUBULE-STIMULATED ADP RELEASE,  
JRNL        TITL 2 ATP BINDING, AND FORCE GENERATION IN TRANSPORT KINESINS.     
JRNL        REF    ELIFE                         V.   3  3680 2014              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   25209998                                                     
JRNL        DOI    10.7554/ELIFE.03680                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    7.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : FLEX-EM, UCSF CHIMERA, FREALIGN, SPIDER   
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 4HNA                                
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 REFINEMENT PROTOCOL--X-RAY      
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)  : 7.700                          
REMARK   3   NUMBER OF PARTICLES               : 65572                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD   
REMARK   3  -2771. (DEPOSITION ID: 12604).                                      
REMARK   4                                                                      
REMARK   4 4UY0 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_1290061623.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE                      
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : HELICAL ARRAY                     
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : 3-PROTOFILAMENT MICROTUBULE       
REMARK 245                                    -BOUND HUMAN KINESIN-1 MOTOR      
REMARK 245                                    DOMAIN WITH AMPPNP                
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 6.80                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 10-DEC-12                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 90.00                          
REMARK 245   MICROSCOPE MODEL                  : FEI POLARA 300                 
REMARK 245   DETECTOR TYPE                     : GATAN ULTRASCAN 4000 (4K X     
REMARK 245                                       4K)                            
REMARK 245   MINIMUM DEFOCUS (NM)              : 400.00                         
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3500.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.30                           
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             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : 100000                         
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     0                                                      
REMARK 465     GLN A    33A                                                     
REMARK 465     MET A    33B                                                     
REMARK 465     PRO A    33C                                                     
REMARK 465     SER A    33D                                                     
REMARK 465     ASP A    33E                                                     
REMARK 465     LYS A    33F                                                     
REMARK 465     THR A    33G                                                     
REMARK 465     ILE A    33H                                                     
REMARK 465     GLY A    33I                                                     
REMARK 465     GLY A    33J                                                     
REMARK 465     GLY A    33K                                                     
REMARK 465     ASP A    33L                                                     
REMARK 465     ASP A    33M                                                     
REMARK 465     SER A    33N                                                     
REMARK 465     PHE A    33O                                                     
REMARK 465     ASN A    33P                                                     
REMARK 465     THR A    33Q                                                     
REMARK 465     PHE A    33R                                                     
REMARK 465     PHE A    33S                                                     
REMARK 465     SER A    33T                                                     
REMARK 465     GLU A    33U                                                     
REMARK 465     THR A    33V                                                     
REMARK 465     GLY A    33W                                                     
REMARK 465     ALA A    33X                                                     
REMARK 465     GLY A    33Y                                                     
REMARK 465     LYS A    33Z                                                     
REMARK 465     VAL A   413                                                      
REMARK 465     GLU A   414                                                      
REMARK 465     GLY A   415                                                      
REMARK 465     GLU A   416                                                      
REMARK 465     GLY A   417                                                      
REMARK 465     GLU A   418                                                      
REMARK 465     GLU A   419                                                      
REMARK 465     GLU A   420                                                      
REMARK 465     GLY A   421                                                      
REMARK 465     GLU A   422                                                      
REMARK 465     GLU A   423                                                      
REMARK 465     TYR A   424                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     THR C     4                                                      
REMARK 465     ASN C     5                                                      
REMARK 465     ALA C   339                                                      
REMARK 465     GLU C   340                                                      
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     ANP C 1343                                                       
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                             ALF C1341  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP C1339   O3B                                                    
REMARK 620 2 ALF C1341   F1   94.8                                              
REMARK 620 3 ALF C1341   F2   92.0 172.0                                        
REMARK 620 4 ALF C1341   F3   98.3  87.1  87.7                                  
REMARK 620 5 ALF C1341   F4   92.8  92.4  91.5 168.9                            
REMARK 620 N                    1     2     3     4                             
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 1413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 1415                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 1427                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 B 1428                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 1339                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1340                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF C 1341                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP C 1343                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UXO   RELATED DB: PDB                                   
REMARK 900 CONSERVED MECHANISMS OF MICROTUBULE-STIMULATED ADP RELEASE , ATP     
REMARK 900 BINDING, AND FORCE GENERATION IN TRANSPORT KINESINS                  
REMARK 900 RELATED ID: 4UXP   RELATED DB: PDB                                   
REMARK 900 CONSERVED MECHANISMS OF MICROTUBULE-STIMULATED ADP RELEASE , ATP     
REMARK 900 BINDING, AND FORCE GENERATION IN TRANSPORT KINESINS                  
REMARK 900 RELATED ID: 4UXR   RELATED DB: PDB                                   
REMARK 900 CONSERVED MECHANISMS OF MICROTUBULE-STIMULATED ADP RELEASE , ATP     
REMARK 900 BINDING, AND FORCE GENERATION IN TRANSPORT KINESINS                  
REMARK 900 RELATED ID: 4UXS   RELATED DB: PDB                                   
REMARK 900 CONSERVED MECHANISMS OF MICROTUBULE-STIMULATED ADP RELEASE , ATP     
REMARK 900 BINDING, AND FORCE GENERATION IN TRANSPORT KINESINS                  
REMARK 900 RELATED ID: 4UXT   RELATED DB: PDB                                   
REMARK 900 CONSERVED MECHANISMS OF MICROTUBULE-STIMULATED ADP RELEASE , ATP     
REMARK 900 BINDING, AND FORCE GENERATION IN TRANSPORT KINESINS                  
REMARK 900 RELATED ID: 4UXY   RELATED DB: PDB                                   
REMARK 900 CONSERVED MECHANISMS OF MICROTUBULE-STIMULATED ADP RELEASE , ATP     
REMARK 900 BINDING, AND FORCE GENERATION IN TRANSPORT KINESINS                  
REMARK 900 RELATED ID: EMD-2771   RELATED DB: EMDB                              
DBREF  4UY0 A    0   424  UNP    P81947   TBA1B_BOVIN      1    451             
DBREF  4UY0 B    1   426  UNP    Q6B856   TBB2B_BOVIN      2    427             
DBREF  4UY0 C    1   340  UNP    Q12840   KIF5A_HUMAN      1    340             
SEQADV 4UY0 SER A  109  UNP  P81947    LEU   136 CONFLICT                       
SEQADV 4UY0 GLY A  205  UNP  P81947    SER   232 CONFLICT                       
SEQADV 4UY0 GLY A  238  UNP  P81947    ILE   265 CONFLICT                       
SEQADV 4UY0 THR A  313  UNP  P81947    SER   340 CONFLICT                       
SEQADV 4UY0 GLU A  331  UNP  P81947    GLN   358 CONFLICT                       
SEQADV 4UY0 ALA B   54  UNP  Q6B856    THR    55 CONFLICT                       
SEQADV 4UY0 VAL B  169  UNP  Q6B856    MET   170 CONFLICT                       
SEQADV 4UY0 ALA B  295  UNP  Q6B856    SER   296 CONFLICT                       
SEQADV 4UY0 VAL B  315  UNP  Q6B856    ILE   316 CONFLICT                       
SEQRES   1 A  451  MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY          
SEQRES   2 A  451  VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU          
SEQRES   3 A  451  GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP          
SEQRES   4 A  451  LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE          
SEQRES   5 A  451  PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA          
SEQRES   6 A  451  VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL          
SEQRES   7 A  451  ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN          
SEQRES   8 A  451  LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA          
SEQRES   9 A  451  ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU          
SEQRES  10 A  451  VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR          
SEQRES  11 A  451  GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY          
SEQRES  12 A  451  GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG          
SEQRES  13 A  451  LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE          
SEQRES  14 A  451  SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL          
SEQRES  15 A  451  GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU          
SEQRES  16 A  451  GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA          
SEQRES  17 A  451  ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG          
SEQRES  18 A  451  PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE          
SEQRES  19 A  451  VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA          
SEQRES  20 A  451  LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL          
SEQRES  21 A  451  PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA          
SEQRES  22 A  451  PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU          
SEQRES  23 A  451  SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA          
SEQRES  24 A  451  ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR          
SEQRES  25 A  451  MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO          
SEQRES  26 A  451  LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS          
SEQRES  27 A  451  ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE          
SEQRES  28 A  451  LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO          
SEQRES  29 A  451  GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET          
SEQRES  30 A  451  LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG          
SEQRES  31 A  451  LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA          
SEQRES  32 A  451  PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY          
SEQRES  33 A  451  GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU          
SEQRES  34 A  451  LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY          
SEQRES  35 A  451  GLU GLY GLU GLU GLU GLY GLU GLU TYR                          
SEQRES   1 B  426  ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY ASN          
SEQRES   2 B  426  GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP GLU          
SEQRES   3 B  426  HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP SER          
SEQRES   4 B  426  ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN GLU          
SEQRES   5 B  426  ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU VAL          
SEQRES   6 B  426  ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER GLY          
SEQRES   7 B  426  PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL PHE          
SEQRES   8 B  426  GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY HIS          
SEQRES   9 B  426  TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU ASP          
SEQRES  10 B  426  VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU GLN          
SEQRES  11 B  426  GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR GLY          
SEQRES  12 B  426  SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG GLU          
SEQRES  13 B  426  GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL VAL          
SEQRES  14 B  426  PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO TYR          
SEQRES  15 B  426  ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN THR          
SEQRES  16 B  426  ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR ASP          
SEQRES  17 B  426  ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR TYR          
SEQRES  18 B  426  GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER GLY          
SEQRES  19 B  426  VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN ALA          
SEQRES  20 B  426  ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE PRO          
SEQRES  21 B  426  ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU THR          
SEQRES  22 B  426  SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL PRO          
SEQRES  23 B  426  GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET MET          
SEQRES  24 B  426  ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR VAL          
SEQRES  25 B  426  ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU VAL          
SEQRES  26 B  426  ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER SER          
SEQRES  27 B  426  TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR ALA          
SEQRES  28 B  426  VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER ALA          
SEQRES  29 B  426  THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU PHE          
SEQRES  30 B  426  LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG ARG          
SEQRES  31 B  426  LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET ASP          
SEQRES  32 B  426  GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN ASP          
SEQRES  33 B  426  LEU VAL SER GLU TYR GLN GLN TYR GLN ASP                      
SEQRES   1 C  340  MET ALA GLU THR ASN ASN GLU CYS SER ILE LYS VAL LEU          
SEQRES   2 C  340  CYS ARG PHE ARG PRO LEU ASN GLN ALA GLU ILE LEU ARG          
SEQRES   3 C  340  GLY ASP LYS PHE ILE PRO ILE PHE GLN GLY ASP ASP SER          
SEQRES   4 C  340  VAL VAL ILE GLY GLY LYS PRO TYR VAL PHE ASP ARG VAL          
SEQRES   5 C  340  PHE PRO PRO ASN THR THR GLN GLU GLN VAL TYR HIS ALA          
SEQRES   6 C  340  CYS ALA MET GLN ILE VAL LYS ASP VAL LEU ALA GLY TYR          
SEQRES   7 C  340  ASN GLY THR ILE PHE ALA TYR GLY GLN THR SER SER GLY          
SEQRES   8 C  340  LYS THR HIS THR MET GLU GLY LYS LEU HIS ASP PRO GLN          
SEQRES   9 C  340  LEU MET GLY ILE ILE PRO ARG ILE ALA ARG ASP ILE PHE          
SEQRES  10 C  340  ASN HIS ILE TYR SER MET ASP GLU ASN LEU GLU PHE HIS          
SEQRES  11 C  340  ILE LYS VAL SER TYR PHE GLU ILE TYR LEU ASP LYS ILE          
SEQRES  12 C  340  ARG ASP LEU LEU ASP VAL THR LYS THR ASN LEU SER VAL          
SEQRES  13 C  340  HIS GLU ASP LYS ASN ARG VAL PRO PHE VAL LYS GLY CYS          
SEQRES  14 C  340  THR GLU ARG PHE VAL SER SER PRO GLU GLU ILE LEU ASP          
SEQRES  15 C  340  VAL ILE ASP GLU GLY LYS SER ASN ARG HIS VAL ALA VAL          
SEQRES  16 C  340  THR ASN MET ASN GLU HIS SER SER ARG SER HIS SER ILE          
SEQRES  17 C  340  PHE LEU ILE ASN ILE LYS GLN GLU ASN MET GLU THR GLU          
SEQRES  18 C  340  GLN LYS LEU SER GLY LYS LEU TYR LEU VAL ASP LEU ALA          
SEQRES  19 C  340  GLY SER GLU LYS VAL SER LYS THR GLY ALA GLU GLY ALA          
SEQRES  20 C  340  VAL LEU ASP GLU ALA LYS ASN ILE ASN LYS SER LEU SER          
SEQRES  21 C  340  ALA LEU GLY ASN VAL ILE SER ALA LEU ALA GLU GLY THR          
SEQRES  22 C  340  LYS SER TYR VAL PRO TYR ARG ASP SER LYS MET THR ARG          
SEQRES  23 C  340  ILE LEU GLN ASP SER LEU GLY GLY ASN CYS ARG THR THR          
SEQRES  24 C  340  MET PHE ILE CYS CYS SER PRO SER SER TYR ASN ASP ALA          
SEQRES  25 C  340  GLU THR LYS SER THR LEU MET PHE GLY GLN ARG ALA LYS          
SEQRES  26 C  340  THR ILE LYS ASN THR ALA SER VAL ASN LEU GLU LEU THR          
SEQRES  27 C  340  ALA GLU                                                      
HET     ZN  A1413       1                                                       
HET     MG  A1414       1                                                       
HET    GTP  A1415      32                                                       
HET    GDP  B1427      28                                                       
HET    TA1  B1428      62                                                       
HET    ADP  C1339      27                                                       
HET     MG  C1340       1                                                       
HET    ALF  C1341       5                                                       
HET    ANP  C1343       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     TA1 TAXOL                                                            
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     ALF TETRAFLUOROALUMINATE ION                                         
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   6  GTP    C10 H16 N5 O14 P3                                            
FORMUL   7  GDP    C10 H15 N5 O11 P2                                            
FORMUL   8  TA1    C47 H51 N O14                                                
FORMUL   9  ADP    C10 H15 N5 O10 P2                                            
FORMUL  11  ALF    AL F4 1-                                                     
FORMUL  12  ANP    C10 H17 N6 O12 P3                                            
LINK        MG    MG A1414                 O1G GTP A1415     1555   1555  2.45  
LINK         O3B ADP C1339                AL   ALF C1341     1555   1555  1.96  
LINK         O2B ADP C1339                MG    MG C1340     1555   1555  2.09  
SITE     1 AC1  1 HIS A 256                                                     
SITE     1 AC2  1 GTP A1415                                                     
SITE     1 AC3  9 GLY A   9  GLN A  10  ALA A  11  ALA A  72                    
SITE     2 AC3  9 ASN A  74  GLY A 116  GLY A 117  THR A 118                    
SITE     3 AC3  9  MG A1414                                                     
SITE     1 AC4  4 GLY B   9  CYS B  11  THR B 142  GLY B 143                    
SITE     1 AC5  5 VAL B  22  LEU B 272  ARG B 275  PRO B 357                    
SITE     2 AC5  5 ARG B 358                                                     
SITE     1 AC6  7 ARG C  17  SER C  89  GLY C  91  THR C  93                    
SITE     2 AC6  7  MG C1340  ALF C1341  ANP C1343                               
SITE     1 AC7  2 ADP C1339  ALF C1341                                          
SITE     1 AC8  5 SER C 202  ALA C 234  GLY C 235  ADP C1339                    
SITE     2 AC8  5  MG C1340                                                     
SITE     1 AC9  2 GLY C  91  ADP C1339                                          
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  ARG A   1     194.034 324.806 212.224  1.00 90.72           C  
ATOM      2  CA  GLU A   2     194.843 324.396 215.922  1.00 76.37           C  
ATOM      3  CA  CYS A   3     192.786 323.189 218.873  1.00 53.93           C  
ATOM      4  CA  ILE A   4     193.353 324.589 222.359  1.00 42.08           C  
ATOM      5  CA  SER A   5     192.771 322.325 225.351  1.00 26.32           C  
ATOM      6  CA  ILE A   6     191.509 323.014 228.845  1.00 20.58           C  
ATOM      7  CA  HIS A   7     192.270 320.282 231.344  1.00 24.92           C  
ATOM      8  CA  VAL A   8     189.833 320.804 234.206  1.00 24.49           C  
ATOM      9  CA  GLY A   9     189.731 319.003 237.550  1.00 29.78           C  
ATOM     10  CA  GLN A  10     192.558 317.124 239.243  1.00 23.82           C  
ATOM     11  CA  ALA A  11     191.774 314.139 237.060  1.00 17.32           C  
ATOM     12  CA  GLY A  12     191.470 316.091 233.821  1.00 14.25           C  
ATOM     13  CA  VAL A  13     194.852 317.410 234.869  1.00 16.05           C  
ATOM     14  CA  GLN A  14     196.429 314.009 235.649  1.00 19.43           C  
ATOM     15  CA  ILE A  15     195.117 312.696 232.353  1.00 18.31           C  
ATOM     16  CA  GLY A  16     196.323 316.002 230.980  1.00 26.23           C  
ATOM     17  CA  ASN A  17     199.865 315.579 232.219  1.00 29.97           C  
ATOM     18  CA  ALA A  18     199.682 312.133 230.585  1.00 37.71           C  
ATOM     19  CA  CYS A  19     198.243 313.030 227.191  1.00 43.89           C  
ATOM     20  CA  TRP A  20     200.615 315.936 227.339  1.00 51.95           C  
ATOM     21  CA  GLU A  21     203.472 313.561 227.968  1.00 59.11           C  
ATOM     22  CA  LEU A  22     202.804 311.170 225.120  1.00 62.00           C  
ATOM     23  CA  TYR A  23     202.895 314.280 222.955  1.00 70.43           C  
ATOM     24  CA  CYS A  24     206.437 315.608 223.160  1.00 67.24           C  
ATOM     25  CA  LEU A  25     207.432 311.950 223.351  1.00 73.69           C  
ATOM     26  CA  GLU A  26     206.397 311.451 219.720  1.00 74.74           C  
ATOM     27  CA  HIS A  27     207.460 314.915 218.575  1.00 77.34           C  
ATOM     28  CA  GLY A  28     211.062 314.903 219.791  1.00 86.18           C  
ATOM     29  CA  ILE A  29     210.567 317.816 222.166  1.00 87.45           C  
ATOM     30  CA  GLN A  30     212.192 316.851 225.499  1.00 86.37           C  
ATOM     31  CA  PRO A  31     211.451 318.472 228.942  1.00 89.63           C  
ATOM     32  CA  ASP A  32     212.519 321.918 227.852  1.00 96.86           C  
ATOM     33  CA  GLY A  33     211.993 322.518 224.126  1.00 94.83           C  
ATOM     34  CA  HIS A  34     208.672 324.677 222.618  1.00 99.59           C  
ATOM     35  CA  VAL A  35     205.463 325.899 224.276  1.00 96.92           C  
ATOM     36  CA  PRO A  36     202.238 323.933 224.933  1.00 88.64           C  
ATOM     37  CA  ARG A  37     198.869 325.177 223.754  1.00 69.26           C  
ATOM     38  CA  ALA A  38     196.518 324.564 226.653  1.00 49.94           C  
ATOM     39  CA  VAL A  39     195.631 325.433 230.214  1.00 45.70           C  
ATOM     40  CA  PHE A  40     195.139 323.804 233.613  1.00 38.52           C  
ATOM     41  CA  VAL A  41     192.272 324.547 236.017  1.00 35.38           C  
ATOM     42  CA  ASP A  42     191.651 323.328 239.576  1.00 31.66           C  
ATOM     43  CA  LEU A  43     190.318 324.656 242.874  1.00 30.66           C  
ATOM     44  CA  GLU A  44     192.783 322.502 244.821  1.00 43.59           C  
ATOM     45  CA  PRO A  45     196.312 323.854 244.452  1.00 46.27           C  
ATOM     46  CA  THR A  46     198.253 320.740 245.451  1.00 48.55           C  
ATOM     47  CA  VAL A  47     197.274 318.959 242.192  1.00 58.12           C  
ATOM     48  CA  ILE A  48     198.185 321.565 239.551  1.00 63.45           C  
ATOM     49  CA  ASP A  49     201.212 321.960 241.765  1.00 69.97           C  
ATOM     50  CA  GLU A  50     202.120 318.413 240.689  1.00 70.62           C  
ATOM     51  CA  VAL A  51     202.545 319.868 237.233  1.00 70.09           C  
ATOM     52  CA  ARG A  52     204.509 322.647 238.895  1.00 74.67           C  
ATOM     53  CA  THR A  53     206.716 320.262 240.910  1.00 80.03           C  
ATOM     54  CA  GLY A  54     206.900 317.020 238.944  1.00 79.49           C  
ATOM     55  CA  THR A  55     207.864 316.139 235.384  1.00 76.49           C  
ATOM     56  CA  TYR A  56     207.071 318.493 232.494  1.00 71.97           C  
ATOM     57  CA  ARG A  57     207.644 321.259 235.006  1.00 84.74           C  
ATOM     58  CA  GLN A  58     209.143 323.983 232.786  1.00 84.53           C  
ATOM     59  CA  LEU A  59     207.276 323.050 229.611  1.00 77.11           C  
ATOM     60  CA  PHE A  60     204.423 325.249 230.827  1.00 75.47           C  
ATOM     61  CA  HIS A  61     203.850 328.901 231.542  1.00 78.06           C  
ATOM     62  CA  PRO A  62     202.741 329.666 235.082  1.00 83.61           C  
ATOM     63  CA  GLU A  63     200.108 331.552 233.111  1.00 78.49           C  
ATOM     64  CA  GLN A  64     198.380 328.473 231.637  1.00 69.51           C  
ATOM     65  CA  LEU A  65     198.237 326.951 235.115  1.00 68.73           C  
ATOM     66  CA  ILE A  66     195.183 328.313 236.942  1.00 68.32           C  
ATOM     67  CA  THR A  67     194.550 327.473 240.601  1.00 68.88           C  
ATOM     68  CA  GLY A  68     192.171 328.573 243.332  1.00 66.50           C  
ATOM     69  CA  LYS A  69     194.038 327.918 246.605  1.00 67.02           C  
ATOM     70  CA  GLU A  70     190.560 327.799 248.074  1.00 62.40           C  
ATOM     71  CA  ASP A  71     188.542 324.622 248.174  1.00 52.52           C  
ATOM     72  CA  ALA A  72     187.722 321.958 245.603  1.00 34.76           C  
ATOM     73  CA  ALA A  73     184.588 320.349 247.100  1.00 26.25           C  
ATOM     74  CA  ASN A  74     183.293 317.208 245.523  1.00 25.16           C  
ATOM     75  CA  ASN A  75     180.126 319.015 244.704  1.00 15.90           C  
ATOM     76  CA  TYR A  76     178.960 320.502 241.436  1.00  6.91           C  
ATOM     77  CA  ALA A  77     177.157 323.547 242.859  1.00  6.65           C  
ATOM     78  CA  ARG A  78     180.120 324.896 244.782  1.00 10.39           C  
ATOM     79  CA  GLY A  79     182.446 324.316 241.872  1.00 17.30           C  
ATOM     80  CA  HIS A  80     180.085 325.726 239.266  1.00 20.11           C  
ATOM     81  CA  TYR A  81     178.318 328.511 241.166  1.00 19.97           C  
ATOM     82  CA  THR A  82     179.763 329.730 244.491  1.00 14.79           C  
ATOM     83  CA  ILE A  83     183.493 329.077 244.349  1.00 22.39           C  
ATOM     84  CA  GLY A  84     184.287 327.969 240.807  1.00 31.58           C  
ATOM     85  CA  LYS A  85     182.796 331.288 239.676  1.00 37.27           C  
ATOM     86  CA  GLU A  86     185.545 333.492 241.083  1.00 41.42           C  
ATOM     87  CA  ILE A  87     188.168 331.811 238.893  1.00 32.89           C  
ATOM     88  CA  ILE A  88     186.289 331.454 235.596  1.00 24.51           C  
ATOM     89  CA  ASP A  89     186.969 335.012 234.381  1.00 26.78           C  
ATOM     90  CA  LEU A  90     190.680 334.493 234.847  1.00 23.76           C  
ATOM     91  CA  VAL A  91     190.335 331.022 233.337  1.00 24.82           C  
ATOM     92  CA  LEU A  92     188.585 332.367 230.258  1.00 27.75           C  
ATOM     93  CA  ASP A  93     191.156 335.123 229.933  1.00 39.11           C  
ATOM     94  CA  ARG A  94     193.758 332.501 229.057  1.00 44.01           C  
ATOM     95  CA  ILE A  95     191.526 330.684 226.583  1.00 48.00           C  
ATOM     96  CA  ARG A  96     191.030 334.126 225.031  1.00 54.11           C  
ATOM     97  CA  LYS A  97     194.680 335.127 225.405  1.00 44.21           C  
ATOM     98  CA  LEU A  98     195.868 331.745 224.091  1.00 49.40           C  
ATOM     99  CA  ALA A  99     193.055 331.738 221.520  1.00 56.85           C  
ATOM    100  CA  ASP A 100     194.230 335.040 220.085  1.00 68.82           C  
ATOM    101  CA  GLN A 101     197.960 334.397 219.783  1.00 79.45           C  
ATOM    102  CA  CYS A 102     197.307 331.538 217.309  1.00 86.84           C  
ATOM    103  CA  THR A 103     196.290 331.512 213.610  1.00 77.26           C  
ATOM    104  CA  GLY A 104     192.740 330.528 212.657  1.00 66.48           C  
ATOM    105  CA  LEU A 105     192.050 327.842 215.285  1.00 49.07           C  
ATOM    106  CA  GLN A 106     189.429 325.084 215.187  1.00 35.99           C  
ATOM    107  CA  GLY A 107     188.407 324.600 218.804  1.00 25.53           C  
ATOM    108  CA  PHE A 108     189.216 323.580 222.379  1.00 22.95           C  
ATOM    109  CA  SER A 109     189.793 319.983 223.390  1.00 11.40           C  
ATOM    110  CA  VAL A 110     188.420 320.101 226.958  1.00  6.65           C  
ATOM    111  CA  PHE A 111     189.547 317.501 229.541  1.00 13.94           C  
ATOM    112  CA  HIS A 112     187.296 316.920 232.555  1.00 22.19           C  
ATOM    113  CA  SER A 113     186.147 314.178 234.917  1.00 26.99           C  
ATOM    114  CA  PHE A 114     182.356 314.241 234.909  1.00 35.87           C  
ATOM    115  CA  GLY A 115     181.861 313.253 238.543  1.00 38.67           C  
ATOM    116  CA  GLY A 116     184.011 315.729 240.420  1.00 35.73           C  
ATOM    117  CA  GLY A 117     183.711 319.181 241.911  1.00 33.40           C  
ATOM    118  CA  THR A 118     186.143 321.212 239.834  1.00 20.53           C  
ATOM    119  CA  GLY A 119     185.611 318.869 236.929  1.00 15.71           C  
ATOM    120  CA  SER A 120     181.838 318.720 236.707  1.00 14.46           C  
ATOM    121  CA  GLY A 121     180.748 322.100 237.998  1.00 19.79           C  
ATOM    122  CA  PHE A 122     183.421 324.525 236.862  1.00 23.20           C  
ATOM    123  CA  THR A 123     183.738 323.282 233.288  1.00 22.10           C  
ATOM    124  CA  SER A 124     179.995 323.308 233.131  1.00 19.40           C  
ATOM    125  CA  LEU A 125     180.266 327.072 233.063  1.00 16.83           C  
ATOM    126  CA  LEU A 126     183.626 327.135 231.270  1.00 19.01           C  
ATOM    127  CA  MET A 127     182.249 325.300 228.260  1.00 24.75           C  
ATOM    128  CA  GLU A 128     179.196 327.386 229.003  1.00 28.50           C  
ATOM    129  CA  ARG A 129     181.029 330.684 228.597  1.00 30.73           C  
ATOM    130  CA  LEU A 130     182.772 329.270 225.464  1.00 30.23           C  
ATOM    131  CA  SER A 131     179.697 328.287 223.481  1.00 31.63           C  
ATOM    132  CA  VAL A 132     178.852 331.983 223.587  1.00 41.27           C  
ATOM    133  CA  ASP A 133     182.268 333.542 223.109  1.00 40.24           C  
ATOM    134  CA  TYR A 134     183.163 331.263 220.202  1.00 39.78           C  
ATOM    135  CA  GLY A 135     179.957 329.590 219.085  1.00 39.54           C  
ATOM    136  CA  LYS A 136     181.749 329.544 215.741  1.00 34.48           C  
ATOM    137  CA  LYS A 137     184.107 326.661 216.570  1.00 32.52           C  
ATOM    138  CA  SER A 138     184.451 323.100 217.796  1.00 22.09           C  
ATOM    139  CA  LYS A 139     183.803 322.093 221.378  1.00 18.88           C  
ATOM    140  CA  LEU A 140     184.916 318.516 221.740  1.00 13.86           C  
ATOM    141  CA  GLU A 141     185.046 317.658 225.404  1.00 15.54           C  
ATOM    142  CA  PHE A 142     186.946 314.562 226.372  1.00 18.38           C  
ATOM    143  CA  SER A 143     185.286 313.145 229.495  1.00 18.69           C  
ATOM    144  CA  ILE A 144     185.963 310.312 231.966  1.00 17.69           C  
ATOM    145  CA  TYR A 145     182.429 309.502 232.984  1.00 28.93           C  
ATOM    146  CA  PRO A 146     181.508 307.561 236.246  1.00 37.41           C  
ATOM    147  CA  ALA A 147     182.668 303.961 236.661  1.00 43.64           C  
ATOM    148  CA  PRO A 148     179.542 301.762 236.306  1.00 51.14           C  
ATOM    149  CA  GLN A 149     179.981 300.164 239.760  1.00 57.23           C  
ATOM    150  CA  VAL A 150     183.356 301.363 240.923  1.00 52.37           C  
ATOM    151  CA  SER A 151     182.606 305.033 241.465  1.00 51.22           C  
ATOM    152  CA  THR A 152     184.523 307.015 244.040  1.00 38.52           C  
ATOM    153  CA  ALA A 153     182.732 310.111 245.321  1.00 20.70           C  
ATOM    154  CA  VAL A 154     179.595 309.308 247.248  1.00  2.00           C  
ATOM    155  CA  VAL A 155     177.653 311.856 245.267  1.00  3.41           C  
ATOM    156  CA  GLU A 156     179.235 311.296 241.806  1.00 11.10           C  
ATOM    157  CA  PRO A 157     175.841 311.162 240.007  1.00  6.05           C  
ATOM    158  CA  TYR A 158     174.751 314.496 241.423  1.00  3.97           C  
ATOM    159  CA  ASN A 159     177.926 315.878 239.891  1.00  2.00           C  
ATOM    160  CA  SER A 160     177.502 314.038 236.585  1.00  6.16           C  
ATOM    161  CA  ILE A 161     173.854 314.516 235.881  1.00  8.44           C  
ATOM    162  CA  LEU A 162     174.717 318.170 236.380  1.00 10.17           C  
ATOM    163  CA  THR A 163     177.751 318.411 234.156  1.00  9.50           C  
ATOM    164  CA  THR A 164     175.844 316.670 231.394  1.00 18.93           C  
ATOM    165  CA  HIS A 165     172.789 318.945 231.367  1.00 23.95           C  
ATOM    166  CA  THR A 166     174.774 322.149 231.562  1.00 22.18           C  
ATOM    167  CA  THR A 167     177.352 321.139 228.964  1.00 30.97           C  
ATOM    168  CA  LEU A 168     174.900 319.336 226.653  1.00 33.77           C  
ATOM    169  CA  GLU A 169     173.708 322.536 225.062  1.00 39.79           C  
ATOM    170  CA  HIS A 170     177.307 323.694 224.612  1.00 34.63           C  
ATOM    171  CA  SER A 171     179.573 320.892 223.373  1.00 22.91           C  
ATOM    172  CA  ASP A 172     180.164 319.776 219.814  1.00 25.46           C  
ATOM    173  CA  CYS A 173     181.239 316.191 220.410  1.00 26.43           C  
ATOM    174  CA  ALA A 174     181.882 314.692 223.817  1.00 28.15           C  
ATOM    175  CA  PHE A 175     184.346 311.810 223.853  1.00 30.53           C  
ATOM    176  CA  MET A 176     183.930 309.324 226.643  1.00 30.61           C  
ATOM    177  CA  VAL A 177     186.405 307.013 228.335  1.00 20.65           C  
ATOM    178  CA  ASP A 178     185.133 304.889 231.226  1.00 29.43           C  
ATOM    179  CA  ASN A 179     187.612 304.610 234.083  1.00 22.56           C  
ATOM    180  CA  GLU A 180     186.523 301.081 235.124  1.00 20.12           C  
ATOM    181  CA  ALA A 181     186.024 299.598 231.665  1.00 11.03           C  
ATOM    182  CA  ILE A 182     189.652 300.630 231.078  1.00 10.08           C  
ATOM    183  CA  TYR A 183     190.798 298.570 234.043  1.00 22.92           C  
ATOM    184  CA  ASP A 184     189.361 295.505 232.408  1.00 23.58           C  
ATOM    185  CA  ILE A 185     191.624 296.251 229.500  1.00 23.63           C  
ATOM    186  CA  CYS A 186     194.506 296.407 231.994  1.00 28.44           C  
ATOM    187  CA  ARG A 187     193.495 293.094 233.490  1.00 40.94           C  
ATOM    188  CA  ARG A 188     192.308 291.235 230.373  1.00 38.84           C  
ATOM    189  CA  ASN A 189     194.318 292.841 227.584  1.00 31.32           C  
ATOM    190  CA  LEU A 190     197.674 293.568 229.131  1.00 40.55           C  
ATOM    191  CA  ASP A 191     197.554 291.665 232.397  1.00 57.49           C  
ATOM    192  CA  ILE A 192     198.320 293.713 235.523  1.00 59.12           C  
ATOM    193  CA  GLU A 193     196.403 293.999 238.786  1.00 67.12           C  
ATOM    194  CA  ARG A 194     198.753 296.884 239.554  1.00 69.11           C  
ATOM    195  CA  PRO A 195     197.240 299.617 237.363  1.00 53.30           C  
ATOM    196  CA  THR A 196     198.161 303.013 238.757  1.00 43.24           C  
ATOM    197  CA  TYR A 197     196.043 305.966 237.708  1.00 35.46           C  
ATOM    198  CA  THR A 198     199.237 306.894 235.921  1.00 40.10           C  
ATOM    199  CA  ASN A 199     198.400 304.061 233.535  1.00 30.22           C  
ATOM    200  CA  LEU A 200     194.802 304.677 232.598  1.00 16.19           C  
ATOM    201  CA  ASN A 201     196.183 308.087 231.824  1.00 22.59           C  
ATOM    202  CA  ARG A 202     198.841 306.609 229.514  1.00 16.14           C  
ATOM    203  CA  LEU A 203     196.030 304.857 227.776  1.00  6.87           C  
ATOM    204  CA  ILE A 204     193.636 307.705 227.170  1.00 10.37           C  
ATOM    205  CA  GLY A 205     196.947 309.468 226.753  1.00 21.17           C  
ATOM    206  CA  GLN A 206     197.144 307.191 223.722  1.00 25.16           C  
ATOM    207  CA  ILE A 207     193.623 307.162 222.311  1.00 17.99           C  
ATOM    208  CA  VAL A 208     193.749 310.947 222.576  1.00 12.48           C  
ATOM    209  CA  SER A 209     197.028 311.134 220.704  1.00 22.42           C  
ATOM    210  CA  SER A 210     195.177 309.466 217.867  1.00 23.30           C  
ATOM    211  CA  ILE A 211     192.526 312.152 217.908  1.00 23.29           C  
ATOM    212  CA  THR A 212     194.371 315.487 217.785  1.00 44.11           C  
ATOM    213  CA  ALA A 213     198.123 314.940 217.657  1.00 49.53           C  
ATOM    214  CA  SER A 214     198.461 312.646 214.627  1.00 59.69           C  
ATOM    215  CA  LEU A 215     195.252 313.663 212.896  1.00 65.02           C  
ATOM    216  CA  ARG A 216     196.057 317.370 212.842  1.00 68.97           C  
ATOM    217  CA  PHE A 217     199.219 315.803 211.406  1.00 81.08           C  
ATOM    218  CA  ASP A 218     199.438 315.183 207.613  1.00 74.39           C  
ATOM    219  CA  GLY A 219     198.488 311.786 206.255  1.00 59.02           C  
ATOM    220  CA  ALA A 220     196.912 309.757 203.456  1.00 50.29           C  
ATOM    221  CA  LEU A 221     193.367 310.534 204.633  1.00 38.92           C  
ATOM    222  CA  ASN A 222     193.406 313.559 206.971  1.00 32.91           C  
ATOM    223  CA  VAL A 223     190.489 314.250 209.294  1.00 30.37           C  
ATOM    224  CA  ASP A 224     189.952 317.750 210.708  1.00 25.27           C  
ATOM    225  CA  LEU A 225     188.332 318.321 214.122  1.00 17.06           C  
ATOM    226  CA  THR A 226     185.245 319.717 212.503  1.00 21.53           C  
ATOM    227  CA  GLU A 227     185.249 316.500 210.445  1.00 22.00           C  
ATOM    228  CA  PHE A 228     184.445 314.633 213.627  1.00 22.53           C  
ATOM    229  CA  GLN A 229     181.371 316.365 214.898  1.00 20.73           C  
ATOM    230  CA  THR A 230     180.166 316.385 211.275  1.00  9.52           C  
ATOM    231  CA  ASN A 231     180.793 312.727 210.496  1.00  6.03           C  
ATOM    232  CA  LEU A 232     180.173 311.834 214.167  1.00  6.83           C  
ATOM    233  CA  VAL A 233     177.085 313.574 215.539  1.00  9.49           C  
ATOM    234  CA  PRO A 234     173.730 312.910 213.934  1.00  7.37           C  
ATOM    235  CA  TYR A 235     172.021 315.305 216.300  1.00 16.29           C  
ATOM    236  CA  PRO A 236     172.677 318.578 218.201  1.00 16.05           C  
ATOM    237  CA  ARG A 237     172.767 316.854 221.569  1.00 22.39           C  
ATOM    238  CA  GLY A 238     176.518 317.243 222.238  1.00 23.25           C  
ATOM    239  CA  HIS A 239     176.489 313.545 221.465  1.00 11.08           C  
ATOM    240  CA  PHE A 240     178.992 311.392 223.155  1.00  8.40           C  
ATOM    241  CA  PRO A 241     180.897 308.824 221.150  1.00 17.01           C  
ATOM    242  CA  LEU A 242     183.182 306.212 222.829  1.00 12.30           C  
ATOM    243  CA  ALA A 243     186.957 305.884 222.464  1.00 11.58           C  
ATOM    244  CA  THR A 244     188.529 302.553 221.542  1.00 13.25           C  
ATOM    245  CA  TYR A 245     192.048 301.519 220.685  1.00 18.93           C  
ATOM    246  CA  ALA A 246     193.202 298.422 218.836  1.00 29.84           C  
ATOM    247  CA  PRO A 247     196.741 297.186 219.498  1.00 34.85           C  
ATOM    248  CA  VAL A 248     196.371 297.187 223.255  1.00 39.09           C  
ATOM    249  CA  ILE A 249     198.796 294.322 223.527  1.00 46.85           C  
ATOM    250  CA  SER A 250     201.315 293.912 226.373  1.00 55.16           C  
ATOM    251  CA  ALA A 251     204.964 294.842 225.786  1.00 66.26           C  
ATOM    252  CA  GLU A 252     206.282 291.837 227.647  1.00 78.70           C  
ATOM    253  CA  LYS A 253     203.893 288.951 227.783  1.00 82.76           C  
ATOM    254  CA  ALA A 254     202.501 287.840 224.472  1.00 79.12           C  
ATOM    255  CA  TYR A 255     203.940 288.814 221.138  1.00 80.90           C  
ATOM    256  CA  HIS A 256     202.066 288.446 217.964  1.00 75.09           C  
ATOM    257  CA  GLU A 257     202.454 292.245 217.489  1.00 59.49           C  
ATOM    258  CA  GLN A 258     202.473 291.843 213.661  1.00 39.32           C  
ATOM    259  CA  LEU A 259     198.724 291.829 213.573  1.00 34.04           C  
ATOM    260  CA  SER A 260     197.814 293.108 210.095  1.00 31.22           C  
ATOM    261  CA  VAL A 261     194.960 295.563 209.770  1.00 29.39           C  
ATOM    262  CA  ALA A 262     192.446 292.821 209.112  1.00 32.21           C  
ATOM    263  CA  GLU A 263     192.997 291.961 212.788  1.00 36.32           C  
ATOM    264  CA  ILE A 264     193.374 295.229 214.690  1.00 29.52           C  
ATOM    265  CA  THR A 265     190.090 296.477 213.206  1.00 17.98           C  
ATOM    266  CA  ASN A 266     188.116 293.488 214.279  1.00 34.10           C  
ATOM    267  CA  ALA A 267     189.627 294.006 217.726  1.00 30.79           C  
ATOM    268  CA  CYS A 268     187.803 297.284 218.037  1.00 13.70           C  
ATOM    269  CA  PHE A 269     184.252 296.011 217.919  1.00 21.47           C  
ATOM    270  CA  GLU A 270     184.665 293.228 220.448  1.00 31.40           C  
ATOM    271  CA  PRO A 271     183.242 294.922 223.552  1.00 27.43           C  
ATOM    272  CA  ALA A 272     186.204 293.958 225.733  1.00 26.57           C  
ATOM    273  CA  ASN A 273     188.403 296.704 224.399  1.00 27.39           C  
ATOM    274  CA  GLN A 274     186.590 299.971 224.394  1.00 35.05           C  
ATOM    275  CA  MET A 275     187.442 302.127 227.362  1.00 37.27           C  
ATOM    276  CA  VAL A 276     183.748 302.183 228.310  1.00 36.82           C  
ATOM    277  CA  LYS A 277     181.431 299.853 230.232  1.00 51.41           C  
ATOM    278  CA  CYS A 278     178.824 300.311 227.532  1.00 60.84           C  
ATOM    279  CA  ASP A 279     179.236 296.860 225.991  1.00 66.94           C  
ATOM    280  CA  PRO A 280     177.230 296.955 222.706  1.00 67.26           C  
ATOM    281  CA  ARG A 281     174.464 295.242 224.668  1.00 79.29           C  
ATOM    282  CA  HIS A 282     172.130 296.412 221.893  1.00 80.11           C  
ATOM    283  CA  GLY A 283     173.347 299.880 221.069  1.00 55.66           C  
ATOM    284  CA  LYS A 284     173.443 300.144 217.307  1.00 30.92           C  
ATOM    285  CA  TYR A 285     176.415 302.105 216.086  1.00 21.10           C  
ATOM    286  CA  MET A 286     175.351 305.142 214.077  1.00  9.30           C  
ATOM    287  CA  ALA A 287     178.731 306.462 213.008  1.00 10.29           C  
ATOM    288  CA  CYS A 288     182.314 305.412 213.607  1.00 12.21           C  
ATOM    289  CA  CYS A 289     185.492 307.330 212.853  1.00 15.81           C  
ATOM    290  CA  LEU A 290     188.151 304.737 212.309  1.00  8.50           C  
ATOM    291  CA  LEU A 291     191.371 306.623 212.818  1.00 15.06           C  
ATOM    292  CA  TYR A 292     194.282 304.479 211.704  1.00 21.99           C  
ATOM    293  CA  ARG A 293     197.933 305.351 212.024  1.00 31.61           C  
ATOM    294  CA  GLY A 294     201.094 303.653 210.826  1.00 40.46           C  
ATOM    295  CA  ASP A 295     201.577 301.383 207.811  1.00 51.76           C  
ATOM    296  CA  VAL A 296     198.090 300.876 206.375  1.00 45.09           C  
ATOM    297  CA  VAL A 297     196.996 300.243 202.768  1.00 43.42           C  
ATOM    298  CA  PRO A 298     193.709 302.009 201.998  1.00 48.35           C  
ATOM    299  CA  LYS A 299     192.436 298.836 200.333  1.00 35.28           C  
ATOM    300  CA  ASP A 300     193.287 296.874 203.446  1.00 25.97           C  
ATOM    301  CA  VAL A 301     190.891 299.232 205.180  1.00 23.06           C  
ATOM    302  CA  ASN A 302     188.408 299.601 202.343  1.00 29.42           C  
ATOM    303  CA  ALA A 303     188.020 295.841 202.776  1.00 22.83           C  
ATOM    304  CA  ALA A 304     188.590 295.160 206.450  1.00 23.95           C  
ATOM    305  CA  ILE A 305     185.699 297.554 206.947  1.00 18.32           C  
ATOM    306  CA  ALA A 306     183.723 295.982 204.105  1.00 16.38           C  
ATOM    307  CA  THR A 307     183.996 292.614 205.828  1.00 20.68           C  
ATOM    308  CA  ILE A 308     182.630 294.295 208.949  1.00 22.91           C  
ATOM    309  CA  LYS A 309     179.782 296.127 207.207  1.00 41.56           C  
ATOM    310  CA  THR A 310     178.530 292.625 206.465  1.00 64.14           C  
ATOM    311  CA  LYS A 311     178.881 290.918 209.854  1.00 77.19           C  
ATOM    312  CA  ARG A 312     175.353 292.091 210.686  1.00 89.49           C  
ATOM    313  CA  THR A 313     175.752 291.015 214.308  1.00 90.64           C  
ATOM    314  CA  ILE A 314     177.345 294.486 214.391  1.00 81.76           C  
ATOM    315  CA  GLN A 315     174.005 296.027 213.351  1.00 70.01           C  
ATOM    316  CA  PHE A 316     174.333 299.727 212.384  1.00 55.06           C  
ATOM    317  CA  VAL A 317     171.430 302.125 212.587  1.00 59.97           C  
ATOM    318  CA  ASP A 318     168.754 302.050 209.893  1.00 59.27           C  
ATOM    319  CA  TRP A 319     168.708 305.646 208.732  1.00 39.96           C  
ATOM    320  CA  CYS A 320     172.387 305.224 208.201  1.00 28.86           C  
ATOM    321  CA  PRO A 321     173.625 303.529 205.023  1.00 32.22           C  
ATOM    322  CA  THR A 322     177.310 303.969 205.592  1.00 30.77           C  
ATOM    323  CA  GLY A 323     178.716 305.373 208.824  1.00 18.15           C  
ATOM    324  CA  PHE A 324     182.446 304.737 208.579  1.00 14.27           C  
ATOM    325  CA  LYS A 325     184.821 307.688 208.494  1.00 12.21           C  
ATOM    326  CA  VAL A 326     188.182 306.185 207.567  1.00  2.00           C  
ATOM    327  CA  GLY A 327     190.983 308.361 208.907  1.00  8.12           C  
ATOM    328  CA  ILE A 328     194.466 307.330 207.823  1.00 23.70           C  
ATOM    329  CA  ASN A 329     197.626 308.811 209.268  1.00 42.13           C  
ATOM    330  CA  TYR A 330     201.230 307.912 208.480  1.00 64.11           C  
ATOM    331  CA  GLU A 331     203.486 307.935 211.548  1.00 58.76           C  
ATOM    332  CA  PRO A 332     202.814 304.743 213.582  1.00 58.21           C  
ATOM    333  CA  PRO A 333     201.855 305.091 217.298  1.00 62.52           C  
ATOM    334  CA  THR A 334     204.455 305.973 219.925  1.00 62.58           C  
ATOM    335  CA  VAL A 335     204.532 303.979 223.125  1.00 62.67           C  
ATOM    336  CA  VAL A 336     206.079 305.098 226.386  1.00 70.29           C  
ATOM    337  CA  PRO A 337     209.758 303.968 226.433  1.00 77.84           C  
ATOM    338  CA  GLY A 338     209.046 301.433 229.142  1.00 71.52           C  
ATOM    339  CA  GLY A 339     205.509 301.544 230.462  1.00 73.65           C  
ATOM    340  CA  ASP A 340     203.513 298.455 229.509  1.00 77.76           C  
ATOM    341  CA  LEU A 341     202.146 299.266 226.051  1.00 76.32           C  
ATOM    342  CA  ALA A 342     203.220 296.775 223.379  1.00 72.14           C  
ATOM    343  CA  LYS A 343     204.433 299.117 220.607  1.00 74.90           C  
ATOM    344  CA  VAL A 344     203.042 298.004 217.265  1.00 65.43           C  
ATOM    345  CA  GLN A 345     203.492 299.573 213.826  1.00 55.20           C  
ATOM    346  CA  ARG A 346     199.839 300.387 213.312  1.00 39.38           C  
ATOM    347  CA  ALA A 347     196.761 301.004 215.463  1.00 33.17           C  
ATOM    348  CA  VAL A 348     193.044 301.787 215.285  1.00 31.96           C  
ATOM    349  CA  CYS A 349     191.582 304.457 217.559  1.00 21.72           C  
ATOM    350  CA  MET A 350     187.972 304.076 216.587  1.00  7.45           C  
ATOM    351  CA  LEU A 351     185.427 306.221 218.311  1.00 12.52           C  
ATOM    352  CA  SER A 352     181.689 306.218 217.755  1.00 19.82           C  
ATOM    353  CA  ASN A 353     178.164 307.100 218.746  1.00 21.23           C  
ATOM    354  CA  THR A 354     176.356 303.955 219.836  1.00 19.77           C  
ATOM    355  CA  THR A 355     172.738 303.645 220.886  1.00  9.75           C  
ATOM    356  CA  ALA A 356     174.527 301.746 223.607  1.00  4.98           C  
ATOM    357  CA  ILE A 357     175.007 304.642 225.954  1.00  8.75           C  
ATOM    358  CA  ALA A 358     171.204 304.487 226.236  1.00 26.84           C  
ATOM    359  CA  GLU A 359     172.403 302.186 228.978  1.00 36.29           C  
ATOM    360  CA  ALA A 360     175.319 303.996 230.632  1.00 30.31           C  
ATOM    361  CA  TRP A 361     173.190 307.154 230.929  1.00 23.21           C  
ATOM    362  CA  ALA A 362     170.243 305.165 232.223  1.00 19.05           C  
ATOM    363  CA  ARG A 363     172.268 303.381 234.910  1.00 30.76           C  
ATOM    364  CA  LEU A 364     173.761 306.718 235.930  1.00 21.31           C  
ATOM    365  CA  ASP A 365     170.491 308.558 235.987  1.00 26.95           C  
ATOM    366  CA  HIS A 366     168.790 305.947 238.139  1.00 29.62           C  
ATOM    367  CA  LYS A 367     171.648 306.352 240.645  1.00 18.81           C  
ATOM    368  CA  PHE A 368     170.836 310.037 240.964  1.00 13.87           C  
ATOM    369  CA  ASP A 369     167.153 309.513 241.711  1.00 22.36           C  
ATOM    370  CA  LEU A 370     167.767 307.079 244.503  1.00 18.90           C  
ATOM    371  CA  MET A 371     169.653 309.787 246.378  1.00 15.44           C  
ATOM    372  CA  TYR A 372     167.661 312.781 245.254  1.00 26.50           C  
ATOM    373  CA  ALA A 373     164.646 310.739 246.244  1.00 24.37           C  
ATOM    374  CA  LYS A 374     165.921 311.383 249.782  1.00 28.08           C  
ATOM    375  CA  ARG A 375     167.745 314.621 249.130  1.00 21.94           C  
ATOM    376  CA  ALA A 376     170.850 312.872 250.412  1.00  8.20           C  
ATOM    377  CA  PHE A 377     173.707 315.361 250.077  1.00 16.11           C  
ATOM    378  CA  VAL A 378     171.418 318.055 248.776  1.00 14.70           C  
ATOM    379  CA  HIS A 379     172.019 320.520 251.566  1.00 13.33           C  
ATOM    380  CA  TRP A 380     175.568 320.640 250.295  1.00 12.68           C  
ATOM    381  CA  TYR A 381     174.613 322.271 247.054  1.00 24.39           C  
ATOM    382  CA  VAL A 382     171.673 324.391 248.087  1.00 29.93           C  
ATOM    383  CA  GLY A 383     173.916 326.052 250.609  1.00 34.36           C  
ATOM    384  CA  GLU A 384     176.101 326.710 247.610  1.00 28.17           C  
ATOM    385  CA  GLY A 385     173.825 328.716 245.356  1.00 30.26           C  
ATOM    386  CA  MET A 386     171.665 326.091 243.675  1.00 34.63           C  
ATOM    387  CA  GLU A 387     168.063 325.102 244.154  1.00 39.73           C  
ATOM    388  CA  GLU A 388     165.517 322.307 243.975  1.00 54.92           C  
ATOM    389  CA  GLY A 389     165.301 323.694 240.482  1.00 35.87           C  
ATOM    390  CA  GLU A 390     168.709 322.929 239.049  1.00 29.35           C  
ATOM    391  CA  PHE A 391     168.502 319.346 240.278  1.00 35.92           C  
ATOM    392  CA  SER A 392     164.933 318.436 239.358  1.00 40.42           C  
ATOM    393  CA  GLU A 393     165.244 320.484 236.206  1.00 34.69           C  
ATOM    394  CA  ALA A 394     168.509 318.797 235.152  1.00 28.13           C  
ATOM    395  CA  ARG A 395     167.021 315.428 235.858  1.00 25.50           C  
ATOM    396  CA  GLU A 396     164.150 316.129 233.473  1.00 31.02           C  
ATOM    397  CA  ASP A 397     166.973 317.234 231.172  1.00 30.57           C  
ATOM    398  CA  MET A 398     168.711 313.902 230.930  1.00 26.91           C  
ATOM    399  CA  ALA A 399     165.324 312.188 230.909  1.00 35.84           C  
ATOM    400  CA  ALA A 400     164.999 313.418 227.301  1.00 38.28           C  
ATOM    401  CA  LEU A 401     168.497 312.074 226.730  1.00 39.30           C  
ATOM    402  CA  GLU A 402     167.264 308.601 227.621  1.00 50.75           C  
ATOM    403  CA  LYS A 403     164.432 309.096 225.130  1.00 48.67           C  
ATOM    404  CA  ASP A 404     166.699 310.751 222.597  1.00 47.21           C  
ATOM    405  CA  TYR A 405     169.303 307.981 222.537  1.00 37.28           C  
ATOM    406  CA  GLU A 406     166.312 305.645 222.336  1.00 53.57           C  
ATOM    407  CA  GLU A 407     164.422 307.274 219.481  1.00 61.61           C  
ATOM    408  CA  VAL A 408     167.421 307.891 217.212  1.00 65.03           C  
ATOM    409  CA  GLY A 409     167.672 304.119 217.269  1.00 73.86           C  
ATOM    410  CA  VAL A 410     165.820 300.903 218.138  1.00 88.51           C  
ATOM    411  CA  ASP A 411     163.276 302.194 215.590  1.00 92.71           C  
ATOM    412  CA  SER A 412     163.042 302.236 211.786  1.00 87.57           C  
TER     413      SER A 412                                                      
ATOM    414  CA  ARG B   1     194.724 325.495 253.193  1.00 57.69           C  
ATOM    415  CA  GLU B   2     194.820 325.369 257.018  1.00 51.20           C  
ATOM    416  CA  ILE B   3     193.264 324.257 260.338  1.00 35.02           C  
ATOM    417  CA  VAL B   4     193.645 325.154 264.035  1.00 21.82           C  
ATOM    418  CA  HIS B   5     193.564 322.341 266.580  1.00 20.02           C  
ATOM    419  CA  ILE B   6     191.732 322.800 269.878  1.00 26.45           C  
ATOM    420  CA  GLN B   7     192.705 320.912 273.098  1.00 29.82           C  
ATOM    421  CA  ALA B   8     189.583 321.355 275.251  1.00 28.61           C  
ATOM    422  CA  GLY B   9     189.715 319.991 278.786  1.00 25.81           C  
ATOM    423  CA  GLN B  10     192.326 317.614 280.206  1.00 23.23           C  
ATOM    424  CA  CYS B  11     191.586 314.617 278.051  1.00 16.01           C  
ATOM    425  CA  GLY B  12     191.307 316.612 274.876  1.00 26.51           C  
ATOM    426  CA  ASN B  13     194.521 318.084 276.170  1.00 26.78           C  
ATOM    427  CA  GLN B  14     196.326 314.874 277.173  1.00 25.31           C  
ATOM    428  CA  ILE B  15     195.533 313.706 273.643  1.00 25.94           C  
ATOM    429  CA  GLY B  16     196.826 316.966 272.235  1.00 26.06           C  
ATOM    430  CA  ALA B  17     200.214 315.884 273.488  1.00 29.60           C  
ATOM    431  CA  LYS B  18     199.813 312.608 271.625  1.00 37.53           C  
ATOM    432  CA  PHE B  19     198.273 314.078 268.499  1.00 26.95           C  
ATOM    433  CA  TRP B  20     201.148 316.491 268.311  1.00 23.63           C  
ATOM    434  CA  GLU B  21     203.671 313.945 269.491  1.00 32.17           C  
ATOM    435  CA  VAL B  22     202.796 312.018 266.345  1.00 32.98           C  
ATOM    436  CA  ILE B  23     201.943 314.574 263.695  1.00 34.33           C  
ATOM    437  CA  SER B  24     205.246 316.350 264.338  1.00 47.08           C  
ATOM    438  CA  ASP B  25     207.329 313.236 263.591  1.00 58.11           C  
ATOM    439  CA  GLU B  26     205.000 312.840 260.591  1.00 61.30           C  
ATOM    440  CA  HIS B  27     206.366 316.261 259.712  1.00 62.52           C  
ATOM    441  CA  GLY B  28     209.908 316.161 261.123  1.00 75.22           C  
ATOM    442  CA  ILE B  29     209.397 318.859 263.741  1.00 81.60           C  
ATOM    443  CA  ASP B  30     211.529 318.325 266.850  1.00 89.43           C  
ATOM    444  CA  PRO B  31     210.465 319.884 270.190  1.00 90.13           C  
ATOM    445  CA  THR B  32     211.410 323.471 269.334  1.00 92.84           C  
ATOM    446  CA  GLY B  33     213.560 322.355 266.418  1.00 92.58           C  
ATOM    447  CA  SER B  34     212.501 322.728 262.804  1.00 96.36           C  
ATOM    448  CA  TYR B  35     211.981 320.441 259.862  1.00 99.20           C  
ATOM    449  CA  HIS B  36     214.456 317.537 260.059  1.00100.00           C  
ATOM    450  CA  GLY B  37     212.096 315.783 257.663  1.00 99.24           C  
ATOM    451  CA  ASP B  38     213.612 312.628 256.252  1.00 96.42           C  
ATOM    452  CA  SER B  39     212.023 313.861 253.032  1.00 92.02           C  
ATOM    453  CA  ASP B  40     211.109 317.183 251.406  1.00 85.29           C  
ATOM    454  CA  LEU B  41     207.386 316.525 250.968  1.00 82.58           C  
ATOM    455  CA  GLN B  42     206.564 316.668 254.689  1.00 78.10           C  
ATOM    456  CA  LEU B  43     206.976 320.434 254.384  1.00 74.03           C  
ATOM    457  CA  GLU B  44     205.222 321.849 251.327  1.00 73.64           C  
ATOM    458  CA  ARG B  45     201.916 321.509 253.162  1.00 71.38           C  
ATOM    459  CA  ILE B  46     202.794 321.812 256.873  1.00 67.67           C  
ATOM    460  CA  ASN B  47     201.207 325.255 257.138  1.00 63.33           C  
ATOM    461  CA  VAL B  48     197.960 323.393 257.785  1.00 57.47           C  
ATOM    462  CA  TYR B  49     199.181 323.032 261.402  1.00 58.87           C  
ATOM    463  CA  TYR B  50     202.002 325.523 262.021  1.00 66.14           C  
ATOM    464  CA  ASN B  51     203.263 329.097 261.660  1.00 80.80           C  
ATOM    465  CA  GLU B  52     206.434 330.774 260.385  1.00 96.22           C  
ATOM    466  CA  ALA B  53     208.235 333.051 262.864  1.00100.00           C  
ATOM    467  CA  ALA B  54     211.904 332.246 263.407  1.00100.00           C  
ATOM    468  CA  GLY B  55     212.976 329.856 260.649  1.00100.00           C  
ATOM    469  CA  ASN B  56     213.418 326.662 262.638  1.00 97.91           C  
ATOM    470  CA  LYS B  57     210.426 327.229 264.871  1.00 92.73           C  
ATOM    471  CA  TYR B  58     207.205 326.120 263.205  1.00 78.35           C  
ATOM    472  CA  VAL B  59     204.817 326.302 266.152  1.00 62.05           C  
ATOM    473  CA  PRO B  60     201.707 324.137 266.347  1.00 43.28           C  
ATOM    474  CA  ARG B  61     198.642 326.268 265.776  1.00 32.71           C  
ATOM    475  CA  ALA B  62     196.331 324.771 268.380  1.00 25.69           C  
ATOM    476  CA  ILE B  63     194.576 326.003 271.492  1.00 24.20           C  
ATOM    477  CA  LEU B  64     194.945 324.596 275.006  1.00 28.09           C  
ATOM    478  CA  VAL B  65     191.791 325.274 276.982  1.00 30.81           C  
ATOM    479  CA  ASP B  66     191.478 324.026 280.571  1.00 35.04           C  
ATOM    480  CA  LEU B  67     190.355 325.177 284.036  1.00 45.71           C  
ATOM    481  CA  GLU B  68     192.831 322.909 285.844  1.00 58.53           C  
ATOM    482  CA  PRO B  69     196.385 324.217 285.862  1.00 66.30           C  
ATOM    483  CA  GLY B  70     198.199 320.983 286.815  1.00 75.05           C  
ATOM    484  CA  THR B  71     197.094 319.442 283.509  1.00 81.80           C  
ATOM    485  CA  MET B  72     198.458 321.896 280.947  1.00 81.14           C  
ATOM    486  CA  ASP B  73     201.334 322.215 283.430  1.00 82.65           C  
ATOM    487  CA  SER B  74     202.092 318.527 282.835  1.00 78.89           C  
ATOM    488  CA  VAL B  75     201.760 318.807 279.085  1.00 77.54           C  
ATOM    489  CA  ARG B  76     203.895 321.930 279.123  1.00 78.78           C  
ATOM    490  CA  SER B  77     206.456 320.444 281.537  1.00 86.27           C  
ATOM    491  CA  GLY B  78     207.131 317.191 279.697  1.00 94.03           C  
ATOM    492  CA  PRO B  79     208.329 316.181 276.184  1.00 94.10           C  
ATOM    493  CA  PHE B  80     207.082 318.243 273.221  1.00 86.73           C  
ATOM    494  CA  GLY B  81     205.424 320.449 275.819  1.00 88.24           C  
ATOM    495  CA  GLN B  82     207.794 323.321 275.037  1.00 95.55           C  
ATOM    496  CA  ILE B  83     206.772 323.916 271.407  1.00 87.65           C  
ATOM    497  CA  PHE B  84     203.453 325.655 271.996  1.00 78.40           C  
ATOM    498  CA  ARG B  85     203.792 329.433 272.185  1.00 85.18           C  
ATOM    499  CA  PRO B  86     202.630 330.342 275.742  1.00 88.19           C  
ATOM    500  CA  ASP B  87     199.981 332.509 274.125  1.00 82.18           C  
ATOM    501  CA  ASN B  88     198.280 329.188 273.252  1.00 76.34           C  
ATOM    502  CA  PHE B  89     197.697 328.244 276.890  1.00 70.61           C  
ATOM    503  CA  VAL B  90     194.256 329.565 277.806  1.00 72.18           C  
ATOM    504  CA  PHE B  91     194.073 328.331 281.383  1.00 80.56           C  
ATOM    505  CA  GLY B  92     191.428 328.891 284.031  1.00 75.50           C  
ATOM    506  CA  GLN B  93     193.073 328.497 287.436  1.00 73.82           C  
ATOM    507  CA  SER B  94     189.520 328.462 288.822  1.00 69.76           C  
ATOM    508  CA  GLY B  95     188.063 325.257 290.241  1.00 66.97           C  
ATOM    509  CA  ALA B  96     187.835 323.074 287.126  1.00 57.56           C  
ATOM    510  CA  GLY B  97     184.869 321.300 288.737  1.00 39.29           C  
ATOM    511  CA  ASN B  98     183.630 318.198 286.951  1.00 26.36           C  
ATOM    512  CA  ASN B  99     180.414 319.974 286.074  1.00 22.28           C  
ATOM    513  CA  TRP B 100     179.311 320.606 282.489  1.00 16.37           C  
ATOM    514  CA  ALA B 101     177.522 323.582 283.913  1.00  5.22           C  
ATOM    515  CA  LYS B 102     180.625 324.769 285.712  1.00  4.60           C  
ATOM    516  CA  GLY B 103     182.648 324.935 282.521  1.00 12.37           C  
ATOM    517  CA  HIS B 104     179.933 326.121 280.169  1.00 13.18           C  
ATOM    518  CA  TYR B 105     177.939 328.732 282.097  1.00 18.05           C  
ATOM    519  CA  THR B 106     179.748 329.837 285.185  1.00 18.45           C  
ATOM    520  CA  GLU B 107     183.432 329.203 285.178  1.00 31.29           C  
ATOM    521  CA  GLY B 108     184.189 328.575 281.521  1.00 29.91           C  
ATOM    522  CA  ALA B 109     181.997 331.374 280.230  1.00 32.78           C  
ATOM    523  CA  GLU B 110     184.527 333.813 281.629  1.00 38.49           C  
ATOM    524  CA  LEU B 111     187.650 332.224 280.191  1.00 39.83           C  
ATOM    525  CA  VAL B 112     185.908 332.037 276.805  1.00 42.29           C  
ATOM    526  CA  ASP B 113     186.516 335.588 275.576  1.00 44.37           C  
ATOM    527  CA  SER B 114     190.218 335.186 276.407  1.00 40.63           C  
ATOM    528  CA  VAL B 115     190.098 332.104 274.185  1.00 33.60           C  
ATOM    529  CA  LEU B 116     188.101 333.355 271.206  1.00 36.30           C  
ATOM    530  CA  ASP B 117     190.658 336.149 271.269  1.00 42.58           C  
ATOM    531  CA  VAL B 118     193.383 333.707 270.354  1.00 44.32           C  
ATOM    532  CA  VAL B 119     191.237 331.436 268.159  1.00 56.75           C  
ATOM    533  CA  ARG B 120     191.033 334.631 266.055  1.00 68.40           C  
ATOM    534  CA  LYS B 121     194.714 335.447 266.310  1.00 66.99           C  
ATOM    535  CA  GLU B 122     195.339 331.977 264.869  1.00 66.66           C  
ATOM    536  CA  SER B 123     192.541 332.036 262.308  1.00 63.06           C  
ATOM    537  CA  GLU B 124     193.645 335.403 260.947  1.00 70.76           C  
ATOM    538  CA  SER B 125     197.130 333.904 260.785  1.00 73.77           C  
ATOM    539  CA  CYS B 126     197.487 333.688 257.031  1.00 76.00           C  
ATOM    540  CA  ASP B 127     196.432 332.119 253.732  1.00 68.67           C  
ATOM    541  CA  CYS B 128     193.009 330.461 253.821  1.00 61.48           C  
ATOM    542  CA  LEU B 129     191.437 328.686 256.783  1.00 38.17           C  
ATOM    543  CA  GLN B 130     189.735 325.324 256.273  1.00 26.44           C  
ATOM    544  CA  GLY B 131     188.442 324.404 259.746  1.00 14.57           C  
ATOM    545  CA  PHE B 132     189.353 323.566 263.353  1.00 11.67           C  
ATOM    546  CA  GLN B 133     190.181 320.258 265.040  1.00 18.92           C  
ATOM    547  CA  LEU B 134     188.584 319.718 268.440  1.00 22.98           C  
ATOM    548  CA  THR B 135     189.649 317.158 271.030  1.00 14.93           C  
ATOM    549  CA  HIS B 136     187.919 316.544 274.340  1.00  8.47           C  
ATOM    550  CA  SER B 137     185.863 314.158 276.428  1.00 11.41           C  
ATOM    551  CA  LEU B 138     182.127 314.377 276.885  1.00  6.65           C  
ATOM    552  CA  GLY B 139     182.467 313.257 280.476  1.00  6.55           C  
ATOM    553  CA  GLY B 140     183.677 316.285 282.423  1.00  9.94           C  
ATOM    554  CA  GLY B 141     183.677 320.050 282.847  1.00 14.56           C  
ATOM    555  CA  THR B 142     186.489 321.580 280.817  1.00 17.53           C  
ATOM    556  CA  GLY B 143     185.724 319.003 278.178  1.00 16.67           C  
ATOM    557  CA  SER B 144     182.042 318.774 277.394  1.00 22.04           C  
ATOM    558  CA  GLY B 145     180.946 322.106 278.794  1.00 29.36           C  
ATOM    559  CA  MET B 146     183.698 324.605 278.079  1.00 33.89           C  
ATOM    560  CA  GLY B 147     184.840 322.918 274.875  1.00 29.61           C  
ATOM    561  CA  THR B 148     181.289 322.583 273.675  1.00 20.03           C  
ATOM    562  CA  LEU B 149     181.033 326.313 274.177  1.00 23.56           C  
ATOM    563  CA  LEU B 150     184.253 327.065 272.371  1.00 21.87           C  
ATOM    564  CA  ILE B 151     182.651 325.628 269.288  1.00 28.64           C  
ATOM    565  CA  SER B 152     179.215 327.208 269.633  1.00 27.48           C  
ATOM    566  CA  LYS B 153     181.209 330.451 269.440  1.00 24.69           C  
ATOM    567  CA  ILE B 154     183.563 329.294 266.704  1.00 25.92           C  
ATOM    568  CA  ARG B 155     180.527 328.290 264.548  1.00 28.06           C  
ATOM    569  CA  GLU B 156     179.133 331.806 264.860  1.00 32.76           C  
ATOM    570  CA  GLU B 157     182.405 333.379 263.880  1.00 44.52           C  
ATOM    571  CA  TYR B 158     183.052 331.338 260.751  1.00 42.02           C  
ATOM    572  CA  PRO B 159     179.987 329.296 259.719  1.00 41.21           C  
ATOM    573  CA  ASP B 160     182.079 328.724 256.596  1.00 34.05           C  
ATOM    574  CA  ARG B 161     185.174 326.926 257.836  1.00 30.51           C  
ATOM    575  CA  ILE B 162     184.564 323.318 258.934  1.00 27.51           C  
ATOM    576  CA  MET B 163     184.548 321.753 262.403  1.00 28.59           C  
ATOM    577  CA  ASN B 164     185.835 318.259 263.019  1.00 16.68           C  
ATOM    578  CA  THR B 165     185.201 317.048 266.506  1.00  9.00           C  
ATOM    579  CA  PHE B 166     187.069 314.233 268.207  1.00  9.96           C  
ATOM    580  CA  SER B 167     184.926 313.185 271.165  1.00 21.96           C  
ATOM    581  CA  VAL B 168     185.685 310.532 273.733  1.00 12.49           C  
ATOM    582  CA  VAL B 169     182.088 309.459 274.239  1.00 18.70           C  
ATOM    583  CA  PRO B 170     181.541 307.801 277.678  1.00 26.85           C  
ATOM    584  CA  SER B 171     182.663 304.199 277.421  1.00 33.91           C  
ATOM    585  CA  PRO B 172     180.012 301.627 278.377  1.00 38.63           C  
ATOM    586  CA  LYS B 173     181.135 298.792 280.712  1.00 49.10           C  
ATOM    587  CA  VAL B 174     182.685 301.241 283.219  1.00 44.20           C  
ATOM    588  CA  SER B 175     182.378 305.015 283.484  1.00 35.51           C  
ATOM    589  CA  ASP B 176     185.523 306.877 284.488  1.00 27.24           C  
ATOM    590  CA  THR B 177     183.249 309.435 286.134  1.00 22.55           C  
ATOM    591  CA  VAL B 178     179.824 309.465 287.784  1.00  4.27           C  
ATOM    592  CA  VAL B 179     177.691 312.177 286.269  1.00  2.00           C  
ATOM    593  CA  GLU B 180     179.185 311.217 282.913  1.00  6.26           C  
ATOM    594  CA  PRO B 181     175.782 311.046 281.103  1.00  5.92           C  
ATOM    595  CA  TYR B 182     175.123 314.536 282.437  1.00  3.28           C  
ATOM    596  CA  ASN B 183     178.322 316.071 281.114  1.00  2.15           C  
ATOM    597  CA  ALA B 184     177.795 313.949 277.978  1.00 11.48           C  
ATOM    598  CA  THR B 185     174.192 314.301 276.946  1.00 11.42           C  
ATOM    599  CA  LEU B 186     174.777 318.016 277.417  1.00 21.39           C  
ATOM    600  CA  SER B 187     177.778 318.184 275.123  1.00 25.22           C  
ATOM    601  CA  VAL B 188     176.490 315.899 272.332  1.00 36.12           C  
ATOM    602  CA  HIS B 189     173.551 318.294 272.217  1.00 29.68           C  
ATOM    603  CA  GLN B 190     175.961 321.196 271.390  1.00 28.32           C  
ATOM    604  CA  LEU B 191     177.775 318.966 268.889  1.00 26.76           C  
ATOM    605  CA  VAL B 192     174.727 317.858 266.825  1.00 24.52           C  
ATOM    606  CA  GLU B 193     174.319 321.546 266.238  1.00 26.77           C  
ATOM    607  CA  ASN B 194     177.654 323.178 265.547  1.00 20.71           C  
ATOM    608  CA  THR B 195     180.578 320.937 264.462  1.00 23.25           C  
ATOM    609  CA  ASP B 196     179.915 319.107 261.154  1.00 13.99           C  
ATOM    610  CA  GLU B 197     182.219 316.068 261.494  1.00 15.97           C  
ATOM    611  CA  THR B 198     182.644 314.177 264.766  1.00  7.39           C  
ATOM    612  CA  TYR B 199     184.917 311.220 265.392  1.00 21.59           C  
ATOM    613  CA  CYS B 200     183.776 309.380 268.561  1.00 27.96           C  
ATOM    614  CA  ILE B 201     186.365 307.271 270.334  1.00 26.43           C  
ATOM    615  CA  ASP B 202     185.803 304.912 273.304  1.00 27.21           C  
ATOM    616  CA  ASN B 203     188.490 304.290 275.892  1.00 14.83           C  
ATOM    617  CA  GLU B 204     187.275 300.662 276.095  1.00 17.09           C  
ATOM    618  CA  ALA B 205     186.779 300.100 272.385  1.00 10.42           C  
ATOM    619  CA  LEU B 206     190.460 301.032 272.320  1.00  3.99           C  
ATOM    620  CA  TYR B 207     191.573 298.811 275.153  1.00  8.93           C  
ATOM    621  CA  ASP B 208     189.980 295.891 273.359  1.00 20.39           C  
ATOM    622  CA  ILE B 209     191.386 296.888 269.990  1.00 32.33           C  
ATOM    623  CA  CYS B 210     194.634 297.557 271.849  1.00 47.56           C  
ATOM    624  CA  PHE B 211     194.848 294.436 274.005  1.00 52.60           C  
ATOM    625  CA  ARG B 212     193.729 291.874 271.424  1.00 49.08           C  
ATOM    626  CA  THR B 213     194.697 293.535 268.121  1.00 38.75           C  
ATOM    627  CA  LEU B 214     198.005 294.495 269.732  1.00 36.97           C  
ATOM    628  CA  LYS B 215     198.841 291.719 272.165  1.00 44.63           C  
ATOM    629  CA  LEU B 216     199.705 294.780 274.299  1.00 44.21           C  
ATOM    630  CA  THR B 217     199.208 293.688 277.935  1.00 48.44           C  
ATOM    631  CA  THR B 218     199.662 297.064 279.690  1.00 49.51           C  
ATOM    632  CA  PRO B 219     197.817 299.601 277.518  1.00 38.42           C  
ATOM    633  CA  THR B 220     198.595 302.821 279.325  1.00 42.25           C  
ATOM    634  CA  TYR B 221     196.553 305.910 278.454  1.00 36.77           C  
ATOM    635  CA  GLY B 222     199.472 307.276 276.476  1.00 39.14           C  
ATOM    636  CA  ASP B 223     198.847 304.331 274.203  1.00 32.15           C  
ATOM    637  CA  LEU B 224     195.112 304.699 273.674  1.00 27.08           C  
ATOM    638  CA  ASN B 225     195.780 308.355 272.993  1.00 24.75           C  
ATOM    639  CA  HIS B 226     198.583 307.369 270.673  1.00 22.57           C  
ATOM    640  CA  LEU B 227     196.324 305.030 268.696  1.00 15.08           C  
ATOM    641  CA  VAL B 228     193.632 307.691 268.380  1.00 15.65           C  
ATOM    642  CA  SER B 229     196.102 310.388 267.329  1.00 16.58           C  
ATOM    643  CA  ALA B 230     197.160 307.883 264.670  1.00 21.00           C  
ATOM    644  CA  THR B 231     193.723 308.089 263.052  1.00 15.77           C  
ATOM    645  CA  MET B 232     193.295 311.873 263.222  1.00 23.03           C  
ATOM    646  CA  SER B 233     196.632 312.096 261.372  1.00 28.79           C  
ATOM    647  CA  GLY B 234     195.409 309.833 258.579  1.00 27.46           C  
ATOM    648  CA  VAL B 235     192.307 311.996 258.274  1.00 29.06           C  
ATOM    649  CA  THR B 236     193.485 315.598 258.084  1.00 40.62           C  
ATOM    650  CA  THR B 237     197.236 316.120 257.676  1.00 50.30           C  
ATOM    651  CA  CYS B 238     197.339 313.078 255.432  1.00 57.67           C  
ATOM    652  CA  LEU B 239     194.963 314.353 252.776  1.00 51.01           C  
ATOM    653  CA  ARG B 240     196.974 317.536 252.796  1.00 52.58           C  
ATOM    654  CA  PHE B 241     199.472 315.404 250.946  1.00 49.65           C  
ATOM    655  CA  PRO B 242     199.466 314.487 247.254  1.00 39.30           C  
ATOM    656  CA  GLY B 243     197.584 311.466 245.950  1.00 31.10           C  
ATOM    657  CA  GLN B 244     196.230 309.853 242.818  1.00 29.54           C  
ATOM    658  CA  LEU B 245     192.851 310.717 244.279  1.00 30.33           C  
ATOM    659  CA  ASN B 246     193.084 313.100 247.192  1.00 37.05           C  
ATOM    660  CA  ALA B 247     190.343 314.623 249.249  1.00 44.64           C  
ATOM    661  CA  ASP B 248     190.267 317.136 252.130  1.00 44.09           C  
ATOM    662  CA  LEU B 249     188.024 317.792 255.128  1.00 34.06           C  
ATOM    663  CA  ARG B 250     185.284 319.007 252.856  1.00 22.35           C  
ATOM    664  CA  LYS B 251     185.353 316.093 250.379  1.00 17.08           C  
ATOM    665  CA  LEU B 252     185.282 314.006 253.549  1.00 19.48           C  
ATOM    666  CA  ALA B 253     182.447 316.142 254.785  1.00 13.32           C  
ATOM    667  CA  VAL B 254     180.644 316.559 251.475  1.00  3.90           C  
ATOM    668  CA  ASN B 255     180.718 312.797 250.869  1.00  6.97           C  
ATOM    669  CA  MET B 256     179.941 311.664 254.350  1.00 20.47           C  
ATOM    670  CA  VAL B 257     177.078 313.704 255.623  1.00 14.83           C  
ATOM    671  CA  PRO B 258     173.821 312.946 253.858  1.00 18.97           C  
ATOM    672  CA  PHE B 259     171.785 314.864 256.403  1.00 21.66           C  
ATOM    673  CA  PRO B 260     172.796 318.113 258.255  1.00 28.77           C  
ATOM    674  CA  ARG B 261     172.645 316.688 261.787  1.00 33.46           C  
ATOM    675  CA  LEU B 262     176.429 316.606 261.435  1.00 20.85           C  
ATOM    676  CA  HIS B 263     176.489 312.934 262.125  1.00 17.05           C  
ATOM    677  CA  PHE B 264     179.245 311.197 263.950  1.00 15.04           C  
ATOM    678  CA  PHE B 265     181.678 308.720 262.532  1.00 14.55           C  
ATOM    679  CA  MET B 266     183.876 305.986 263.896  1.00  5.61           C  
ATOM    680  CA  PRO B 267     187.538 306.003 262.874  1.00  4.00           C  
ATOM    681  CA  GLY B 268     189.577 302.866 262.174  1.00 13.86           C  
ATOM    682  CA  PHE B 269     193.262 302.516 261.341  1.00 21.24           C  
ATOM    683  CA  ALA B 270     194.695 300.000 258.873  1.00 22.98           C  
ATOM    684  CA  PRO B 271     197.869 298.164 259.760  1.00 26.07           C  
ATOM    685  CA  LEU B 272     197.122 297.322 263.337  1.00 31.25           C  
ATOM    686  CA  THR B 273     199.451 294.400 263.951  1.00 46.02           C  
ATOM    687  CA  SER B 274     201.411 293.545 267.124  1.00 66.56           C  
ATOM    688  CA  ARG B 275     205.104 294.483 267.003  1.00 87.05           C  
ATOM    689  CA  GLY B 276     207.590 291.661 266.340  1.00 97.30           C  
ATOM    690  CA  SER B 277     205.768 288.503 265.194  1.00100.00           C  
ATOM    691  CA  GLN B 278     202.542 289.685 263.594  1.00100.00           C  
ATOM    692  CA  GLN B 279     204.712 291.920 261.294  1.00 97.58           C  
ATOM    693  CA  TYR B 280     203.170 289.768 258.638  1.00 97.75           C  
ATOM    694  CA  ARG B 281     203.194 292.483 256.038  1.00100.00           C  
ATOM    695  CA  ALA B 282     199.940 290.992 254.798  1.00 92.86           C  
ATOM    696  CA  LEU B 283     199.191 294.523 253.691  1.00 80.45           C  
ATOM    697  CA  THR B 284     198.849 293.973 249.926  1.00 66.34           C  
ATOM    698  CA  VAL B 285     195.459 295.760 250.361  1.00 44.62           C  
ATOM    699  CA  PRO B 286     192.760 293.138 250.763  1.00 42.51           C  
ATOM    700  CA  GLU B 287     194.395 292.925 254.132  1.00 43.33           C  
ATOM    701  CA  LEU B 288     193.715 296.562 254.944  1.00 31.88           C  
ATOM    702  CA  THR B 289     190.069 296.408 253.923  1.00 21.93           C  
ATOM    703  CA  GLN B 290     189.924 293.121 255.754  1.00 27.22           C  
ATOM    704  CA  GLN B 291     191.067 295.086 258.780  1.00 33.69           C  
ATOM    705  CA  MET B 292     189.198 298.419 258.597  1.00 23.21           C  
ATOM    706  CA  PHE B 293     185.847 296.800 257.824  1.00 26.97           C  
ATOM    707  CA  ASP B 294     185.704 294.232 260.613  1.00 40.24           C  
ATOM    708  CA  ALA B 295     183.713 294.813 263.795  1.00 39.02           C  
ATOM    709  CA  LYS B 296     186.563 294.984 266.265  1.00 32.50           C  
ATOM    710  CA  ASN B 297     188.961 297.656 265.051  1.00 28.60           C  
ATOM    711  CA  MET B 298     186.298 300.351 265.110  1.00 31.57           C  
ATOM    712  CA  MET B 299     187.440 302.858 267.736  1.00 21.60           C  
ATOM    713  CA  ALA B 300     183.741 303.271 268.446  1.00 29.61           C  
ATOM    714  CA  ALA B 301     182.031 301.107 271.049  1.00 39.22           C  
ATOM    715  CA  CYS B 302     179.212 299.930 268.886  1.00 47.77           C  
ATOM    716  CA  ASP B 303     179.704 297.319 266.206  1.00 48.33           C  
ATOM    717  CA  PRO B 304     178.976 298.207 262.552  1.00 40.81           C  
ATOM    718  CA  ARG B 305     177.551 294.740 262.076  1.00 48.63           C  
ATOM    719  CA  HIS B 306     174.693 296.141 264.182  1.00 41.86           C  
ATOM    720  CA  GLY B 307     173.531 298.742 261.678  1.00 23.13           C  
ATOM    721  CA  ARG B 308     173.898 299.859 258.051  1.00 18.23           C  
ATOM    722  CA  TYR B 309     176.332 302.497 256.888  1.00 18.02           C  
ATOM    723  CA  LEU B 310     175.491 305.735 255.119  1.00 12.59           C  
ATOM    724  CA  THR B 311     178.967 306.600 254.070  1.00 20.92           C  
ATOM    725  CA  VAL B 312     182.464 305.301 254.378  1.00 21.66           C  
ATOM    726  CA  ALA B 313     185.780 306.913 253.589  1.00 19.05           C  
ATOM    727  CA  ALA B 314     188.798 304.720 253.256  1.00  6.84           C  
ATOM    728  CA  VAL B 315     191.443 307.374 253.304  1.00  6.33           C  
ATOM    729  CA  PHE B 316     194.438 305.218 252.254  1.00 11.40           C  
ATOM    730  CA  ARG B 317     197.956 306.674 252.251  1.00 33.50           C  
ATOM    731  CA  GLY B 318     200.618 304.483 250.638  1.00 48.28           C  
ATOM    732  CA  ARG B 319     201.367 303.635 246.979  1.00 54.21           C  
ATOM    733  CA  MET B 320     198.694 301.244 245.619  1.00 34.07           C  
ATOM    734  CA  SER B 321     196.688 300.429 242.499  1.00 28.27           C  
ATOM    735  CA  MET B 322     193.671 302.625 241.937  1.00 29.79           C  
ATOM    736  CA  LYS B 323     192.428 299.321 240.624  1.00 26.85           C  
ATOM    737  CA  GLU B 324     193.078 297.027 243.586  1.00 25.85           C  
ATOM    738  CA  VAL B 325     191.662 299.822 245.716  1.00 26.70           C  
ATOM    739  CA  ASP B 326     188.671 300.831 243.686  1.00 44.49           C  
ATOM    740  CA  GLU B 327     188.026 297.127 243.154  1.00 51.41           C  
ATOM    741  CA  GLN B 328     188.244 295.708 246.671  1.00 48.07           C  
ATOM    742  CA  MET B 329     185.870 298.413 247.918  1.00 43.07           C  
ATOM    743  CA  LEU B 330     183.289 296.894 245.608  1.00 47.31           C  
ATOM    744  CA  ASN B 331     183.271 293.245 246.663  1.00 50.87           C  
ATOM    745  CA  VAL B 332     183.191 294.679 250.148  1.00 44.29           C  
ATOM    746  CA  GLN B 333     180.082 296.601 249.116  1.00 55.13           C  
ATOM    747  CA  ASN B 334     178.527 293.423 247.761  1.00 67.16           C  
ATOM    748  CA  LYS B 335     179.544 290.811 250.336  1.00 69.74           C  
ATOM    749  CA  ASN B 336     177.813 293.049 252.858  1.00 69.20           C  
ATOM    750  CA  SER B 337     175.012 294.563 250.775  1.00 69.00           C  
ATOM    751  CA  SER B 338     172.960 293.660 253.833  1.00 63.08           C  
ATOM    752  CA  TYR B 339     174.461 296.418 255.941  1.00 54.97           C  
ATOM    753  CA  PHE B 340     175.535 299.324 253.807  1.00 44.79           C  
ATOM    754  CA  VAL B 341     172.210 301.079 253.118  1.00 41.62           C  
ATOM    755  CA  GLU B 342     170.884 301.071 249.559  1.00 50.05           C  
ATOM    756  CA  TRP B 343     169.676 304.526 248.582  1.00 30.29           C  
ATOM    757  CA  ILE B 344     173.341 305.347 248.018  1.00 29.65           C  
ATOM    758  CA  PRO B 345     174.665 303.389 245.059  1.00 35.31           C  
ATOM    759  CA  ASN B 346     178.277 303.908 246.185  1.00 28.59           C  
ATOM    760  CA  ASN B 347     178.430 304.508 249.936  1.00 21.20           C  
ATOM    761  CA  VAL B 348     182.164 304.219 249.957  1.00 15.60           C  
ATOM    762  CA  LYS B 349     184.373 307.234 249.312  1.00  7.97           C  
ATOM    763  CA  THR B 350     187.737 305.920 248.220  1.00  2.00           C  
ATOM    764  CA  ALA B 351     190.525 308.354 248.940  1.00  7.32           C  
ATOM    765  CA  VAL B 352     194.167 307.807 248.106  1.00 17.66           C  
ATOM    766  CA  CYS B 353     197.212 309.677 249.330  1.00 41.06           C  
ATOM    767  CA  ASP B 354     200.728 308.653 248.332  1.00 55.40           C  
ATOM    768  CA  ILE B 355     203.252 308.959 251.136  1.00 59.96           C  
ATOM    769  CA  PRO B 356     202.341 306.573 254.000  1.00 58.14           C  
ATOM    770  CA  PRO B 357     202.794 306.775 257.776  1.00 59.42           C  
ATOM    771  CA  ARG B 358     206.500 307.555 258.100  1.00 68.33           C  
ATOM    772  CA  GLY B 359     207.715 304.078 259.036  1.00 59.28           C  
ATOM    773  CA  LEU B 360     205.023 301.994 257.359  1.00 55.07           C  
ATOM    774  CA  LYS B 361     204.546 300.753 253.782  1.00 49.45           C  
ATOM    775  CA  MET B 362     200.776 301.021 253.488  1.00 44.58           C  
ATOM    776  CA  SER B 363     197.943 302.258 255.721  1.00 40.19           C  
ATOM    777  CA  ALA B 364     194.348 303.496 255.364  1.00 35.52           C  
ATOM    778  CA  THR B 365     192.250 305.522 257.757  1.00 19.99           C  
ATOM    779  CA  PHE B 366     188.593 304.564 257.951  1.00  8.34           C  
ATOM    780  CA  ILE B 367     185.889 307.071 258.699  1.00 12.46           C  
ATOM    781  CA  GLY B 368     182.558 305.343 258.949  1.00 11.41           C  
ATOM    782  CA  ASN B 369     179.175 307.007 259.162  1.00  8.51           C  
ATOM    783  CA  SER B 370     177.197 303.995 260.268  1.00 19.03           C  
ATOM    784  CA  THR B 371     173.711 303.959 261.705  1.00 15.50           C  
ATOM    785  CA  ALA B 372     175.151 301.691 264.338  1.00  7.67           C  
ATOM    786  CA  ILE B 373     176.184 304.635 266.444  1.00  2.00           C  
ATOM    787  CA  GLN B 374     172.518 304.819 267.244  1.00 14.51           C  
ATOM    788  CA  GLU B 375     173.183 302.169 269.870  1.00 14.80           C  
ATOM    789  CA  LEU B 376     175.462 304.511 271.789  1.00 15.58           C  
ATOM    790  CA  PHE B 377     173.571 307.722 272.107  1.00 16.61           C  
ATOM    791  CA  LYS B 378     170.873 305.323 273.230  1.00 16.55           C  
ATOM    792  CA  ARG B 379     173.185 304.139 275.964  1.00 27.51           C  
ATOM    793  CA  ILE B 380     174.137 307.631 277.031  1.00 23.86           C  
ATOM    794  CA  SER B 381     170.552 308.831 276.796  1.00 26.53           C  
ATOM    795  CA  GLU B 382     169.458 305.900 278.946  1.00 34.87           C  
ATOM    796  CA  GLN B 383     171.962 306.557 281.755  1.00 27.14           C  
ATOM    797  CA  PHE B 384     170.642 310.104 281.833  1.00 19.69           C  
ATOM    798  CA  THR B 385     166.965 309.374 282.372  1.00 23.53           C  
ATOM    799  CA  ALA B 386     167.680 306.586 284.903  1.00 21.17           C  
ATOM    800  CA  MET B 387     169.429 309.242 286.974  1.00 16.25           C  
ATOM    801  CA  PHE B 388     167.763 312.358 285.799  1.00 26.94           C  
ATOM    802  CA  ARG B 389     164.493 310.894 286.966  1.00 43.42           C  
ATOM    803  CA  ARG B 390     165.876 311.259 290.503  1.00 35.47           C  
ATOM    804  CA  LYS B 391     167.832 314.461 289.767  1.00 20.61           C  
ATOM    805  CA  ALA B 392     170.857 312.591 291.127  1.00  9.52           C  
ATOM    806  CA  PHE B 393     173.815 314.951 291.171  1.00 15.71           C  
ATOM    807  CA  LEU B 394     171.760 317.742 289.745  1.00 18.28           C  
ATOM    808  CA  HIS B 395     172.330 320.257 292.532  1.00 19.93           C  
ATOM    809  CA  TRP B 396     175.934 320.615 291.315  1.00 24.76           C  
ATOM    810  CA  TYR B 397     174.554 321.889 288.037  1.00 30.69           C  
ATOM    811  CA  THR B 398     171.623 324.067 289.058  1.00 37.85           C  
ATOM    812  CA  GLY B 399     173.573 325.418 292.028  1.00 41.05           C  
ATOM    813  CA  GLU B 400     175.919 326.634 289.319  1.00 37.96           C  
ATOM    814  CA  GLY B 401     173.223 328.572 287.556  1.00 38.22           C  
ATOM    815  CA  MET B 402     171.638 326.004 285.278  1.00 39.38           C  
ATOM    816  CA  ASP B 403     168.075 325.088 284.352  1.00 41.26           C  
ATOM    817  CA  GLU B 404     165.795 322.086 284.922  1.00 45.59           C  
ATOM    818  CA  MET B 405     164.701 322.650 281.337  1.00 45.20           C  
ATOM    819  CA  GLU B 406     168.311 322.666 280.082  1.00 34.38           C  
ATOM    820  CA  PHE B 407     168.831 318.996 280.858  1.00 27.19           C  
ATOM    821  CA  THR B 408     165.416 318.248 279.423  1.00 27.27           C  
ATOM    822  CA  GLU B 409     166.426 320.007 276.250  1.00 38.93           C  
ATOM    823  CA  ALA B 410     169.672 318.166 275.625  1.00 38.51           C  
ATOM    824  CA  GLU B 411     168.405 314.689 276.346  1.00 39.60           C  
ATOM    825  CA  SER B 412     165.440 315.157 274.058  1.00 38.41           C  
ATOM    826  CA  ASN B 413     167.556 316.713 271.311  1.00 30.37           C  
ATOM    827  CA  MET B 414     170.284 314.106 271.504  1.00 30.27           C  
ATOM    828  CA  ASN B 415     167.519 311.573 272.165  1.00 30.82           C  
ATOM    829  CA  ASP B 416     165.726 312.536 268.945  1.00 28.66           C  
ATOM    830  CA  LEU B 417     169.122 312.326 267.280  1.00 23.70           C  
ATOM    831  CA  VAL B 418     168.918 308.577 268.001  1.00 26.78           C  
ATOM    832  CA  SER B 419     165.518 308.425 266.403  1.00 36.87           C  
ATOM    833  CA  GLU B 420     166.511 310.016 263.093  1.00 46.33           C  
ATOM    834  CA  TYR B 421     169.599 307.829 262.655  1.00 37.74           C  
ATOM    835  CA  GLN B 422     167.222 304.844 262.603  1.00 41.57           C  
ATOM    836  CA  GLN B 423     165.245 306.455 259.781  1.00 51.40           C  
ATOM    837  CA  TYR B 424     168.003 305.152 257.505  1.00 56.61           C  
ATOM    838  CA  GLN B 425     168.805 301.827 259.156  1.00 63.11           C  
ATOM    839  CA  ASP B 426     165.343 301.192 257.681  1.00 74.59           C  
TER     840      ASP B 426                                                      
ATOM    841  CA  ASN C   6     137.339 315.795 263.376  1.00 33.28           C  
ATOM    842  CA  GLU C   7     140.545 316.910 261.831  1.00117.13           C  
ATOM    843  CA  CYS C   8     140.401 319.799 259.428  1.00 33.48           C  
ATOM    844  CA  SER C   9     142.492 320.304 256.387  1.00 86.17           C  
ATOM    845  CA  ILE C  10     145.037 322.834 255.496  1.00252.47           C  
ATOM    846  CA  LYS C  11     143.252 325.104 253.148  1.00162.90           C  
ATOM    847  CA  VAL C  12     145.691 326.287 250.615  1.00128.19           C  
ATOM    848  CA  LEU C  13     144.922 329.288 248.518  1.00 82.21           C  
ATOM    849  CA  CYS C  14     146.482 330.425 245.307  1.00 41.76           C  
ATOM    850  CA  ARG C  15     146.521 333.836 243.769  1.00 72.22           C  
ATOM    851  CA  PHE C  16     147.880 335.458 240.675  1.00 56.79           C  
ATOM    852  CA  ARG C  17     148.964 338.911 239.603  1.00214.47           C  
ATOM    853  CA  PRO C  18     149.037 340.576 236.270  1.00 72.05           C  
ATOM    854  CA  LEU C  19     152.214 340.455 234.244  1.00103.90           C  
ATOM    855  CA  ASN C  20     154.966 342.626 235.515  1.00 44.27           C  
ATOM    856  CA  GLN C  21     156.408 344.920 232.909  1.00 40.23           C  
ATOM    857  CA  ALA C  22     159.864 343.403 232.900  1.00 29.38           C  
ATOM    858  CA  GLU C  23     158.044 340.218 232.105  1.00111.04           C  
ATOM    859  CA  ILE C  24     156.217 341.980 229.322  1.00123.86           C  
ATOM    860  CA  LEU C  25     159.428 343.468 227.975  1.00 97.19           C  
ATOM    861  CA  ARG C  26     160.791 340.045 227.124  1.00142.08           C  
ATOM    862  CA  GLY C  27     158.951 337.366 225.261  1.00 36.27           C  
ATOM    863  CA  ASP C  28     157.230 335.769 228.164  1.00 62.67           C  
ATOM    864  CA  LYS C  29     153.758 334.366 227.773  1.00136.02           C  
ATOM    865  CA  PHE C  30     150.879 333.815 230.063  1.00 74.61           C  
ATOM    866  CA  ILE C  31     151.403 330.296 231.285  1.00101.46           C  
ATOM    867  CA  PRO C  32     148.480 329.659 233.671  1.00 81.62           C  
ATOM    868  CA  ILE C  33     145.182 329.288 231.883  1.00116.15           C  
ATOM    869  CA  PHE C  34     142.339 329.928 234.233  1.00 58.81           C  
ATOM    870  CA  GLN C  35     139.384 327.730 233.732  1.00107.93           C  
ATOM    871  CA  GLY C  36     136.913 329.255 236.036  1.00 24.98           C  
ATOM    872  CA  ASP C  37     138.331 330.856 239.127  1.00 55.20           C  
ATOM    873  CA  ASP C  38     139.095 327.700 241.000  1.00 50.25           C  
ATOM    874  CA  SER C  39     141.507 325.923 238.857  1.00109.87           C  
ATOM    875  CA  VAL C  40     144.373 326.946 236.693  1.00 72.16           C  
ATOM    876  CA  VAL C  41     145.694 324.262 234.463  1.00 62.08           C  
ATOM    877  CA  ILE C  42     149.190 323.899 233.234  1.00107.49           C  
ATOM    878  CA  GLY C  43     150.479 322.204 230.144  1.00 12.36           C  
ATOM    879  CA  GLY C  44     147.139 320.465 230.051  1.00 18.01           C  
ATOM    880  CA  LYS C  45     146.917 319.445 233.657  1.00192.53           C  
ATOM    881  CA  PRO C  46     143.926 320.757 235.414  1.00 79.51           C  
ATOM    882  CA  TYR C  47     145.052 321.956 238.809  1.00 88.27           C  
ATOM    883  CA  VAL C  48     142.726 323.224 241.477  1.00 84.14           C  
ATOM    884  CA  PHE C  49     143.180 324.321 245.073  1.00 63.05           C  
ATOM    885  CA  ASP C  50     140.978 325.676 247.814  1.00 92.78           C  
ATOM    886  CA  ARG C  51     140.547 328.776 245.749  1.00116.67           C  
ATOM    887  CA  VAL C  52     142.454 330.337 242.904  1.00 38.15           C  
ATOM    888  CA  PHE C  53     142.259 334.069 242.432  1.00 54.87           C  
ATOM    889  CA  PRO C  54     142.453 335.348 238.872  1.00 85.82           C  
ATOM    890  CA  PRO C  55     145.165 337.854 238.224  1.00 74.85           C  
ATOM    891  CA  ASN C  56     142.502 340.553 238.371  1.00 94.54           C  
ATOM    892  CA  THR C  57     141.795 340.380 242.086  1.00 70.13           C  
ATOM    893  CA  THR C  58     142.844 343.384 244.072  1.00 56.84           C  
ATOM    894  CA  GLN C  59     144.427 342.908 247.374  1.00 53.23           C  
ATOM    895  CA  GLU C  60     140.940 343.386 248.594  1.00122.52           C  
ATOM    896  CA  GLN C  61     139.691 340.434 246.561  1.00163.10           C  
ATOM    897  CA  VAL C  62     142.071 338.279 248.517  1.00 28.49           C  
ATOM    898  CA  TYR C  63     140.704 339.660 251.730  1.00 50.28           C  
ATOM    899  CA  HIS C  64     137.083 339.593 250.624  1.00 49.93           C  
ATOM    900  CA  ALA C  65     137.104 335.952 249.602  1.00 41.80           C  
ATOM    901  CA  CYS C  66     139.418 334.583 252.251  1.00 93.37           C  
ATOM    902  CA  ALA C  67     138.781 336.565 255.355  1.00127.26           C  
ATOM    903  CA  MET C  68     137.464 336.946 257.775  1.00222.84           C  
ATOM    904  CA  GLN C  69     137.784 333.413 259.047  1.00130.70           C  
ATOM    905  CA  ILE C  70     140.790 334.239 261.161  1.00118.16           C  
ATOM    906  CA  VAL C  71     138.879 337.080 262.733  1.00 95.77           C  
ATOM    907  CA  LYS C  72     136.567 334.902 264.729  1.00145.17           C  
ATOM    908  CA  ASP C  73     139.588 332.785 265.502  1.00101.40           C  
ATOM    909  CA  VAL C  74     141.744 335.583 266.874  1.00119.66           C  
ATOM    910  CA  LEU C  75     138.919 336.837 268.994  1.00104.29           C  
ATOM    911  CA  ALA C  76     138.102 333.366 270.100  1.00 36.46           C  
ATOM    912  CA  GLY C  77     141.708 332.934 271.030  1.00 32.90           C  
ATOM    913  CA  TYR C  78     143.331 330.046 269.252  1.00 72.51           C  
ATOM    914  CA  ASN C  79     146.583 329.426 267.537  1.00120.07           C  
ATOM    915  CA  GLY C  80     146.583 329.575 263.807  1.00 31.25           C  
ATOM    916  CA  THR C  81     148.964 331.308 261.514  1.00 50.22           C  
ATOM    917  CA  ILE C  82     149.242 332.260 257.884  1.00118.48           C  
ATOM    918  CA  PHE C  83     152.091 332.446 255.436  1.00 64.06           C  
ATOM    919  CA  ALA C  84     152.872 333.228 251.835  1.00 39.59           C  
ATOM    920  CA  TYR C  85     154.489 330.852 249.429  1.00 63.17           C  
ATOM    921  CA  GLY C  86     155.458 332.302 246.131  1.00 25.36           C  
ATOM    922  CA  GLN C  87     158.526 332.082 244.018  1.00 96.25           C  
ATOM    923  CA  THR C  88     160.507 335.250 243.738  1.00124.94           C  
ATOM    924  CA  SER C  89     158.465 338.364 242.954  1.00 67.34           C  
ATOM    925  CA  SER C  90     155.489 336.128 242.833  1.00 53.55           C  
ATOM    926  CA  GLY C  91     153.621 338.813 244.668  1.00 45.69           C  
ATOM    927  CA  LYS C  92     153.365 337.456 248.186  1.00158.66           C  
ATOM    928  CA  THR C  93     154.448 340.556 250.095  1.00 53.97           C  
ATOM    929  CA  HIS C  94     152.126 342.712 247.988  1.00 35.90           C  
ATOM    930  CA  THR C  95     149.359 340.500 249.279  1.00 46.49           C  
ATOM    931  CA  MET C  96     150.047 340.752 252.982  1.00151.54           C  
ATOM    932  CA  GLU C  97     151.145 344.230 253.839  1.00147.05           C  
ATOM    933  CA  GLY C  98     150.042 345.839 250.633  1.00 46.11           C  
ATOM    934  CA  LYS C  99     149.944 349.477 251.374  1.00142.19           C  
ATOM    935  CA  LEU C 100     148.943 350.005 254.941  1.00146.01           C  
ATOM    936  CA  HIS C 101     147.666 353.533 254.488  1.00 41.76           C  
ATOM    937  CA  ASP C 102     145.335 353.179 251.551  1.00153.75           C  
ATOM    938  CA  PRO C 103     142.725 351.198 253.235  1.00 77.53           C  
ATOM    939  CA  GLN C 104     141.562 349.215 250.261  1.00130.92           C  
ATOM    940  CA  LEU C 105     145.126 348.551 249.336  1.00118.28           C  
ATOM    941  CA  MET C 106     145.787 347.163 252.766  1.00 96.12           C  
ATOM    942  CA  GLY C 107     145.511 343.460 252.971  1.00 30.23           C  
ATOM    943  CA  ILE C 108     143.753 340.842 254.942  1.00 39.37           C  
ATOM    944  CA  ILE C 109     146.194 340.992 257.809  1.00124.27           C  
ATOM    945  CA  PRO C 110     145.839 344.742 258.413  1.00148.08           C  
ATOM    946  CA  ARG C 111     142.088 344.567 258.046  1.00 58.53           C  
ATOM    947  CA  ILE C 112     141.882 341.705 260.456  1.00 97.48           C  
ATOM    948  CA  ALA C 113     143.718 343.644 263.157  1.00 30.99           C  
ATOM    949  CA  ARG C 114     141.299 346.529 263.341  1.00134.36           C  
ATOM    950  CA  ASP C 115     138.285 344.361 262.775  1.00 35.27           C  
ATOM    951  CA  ILE C 116     139.367 342.204 265.585  1.00 60.77           C  
ATOM    952  CA  PHE C 117     139.779 344.725 268.366  1.00 45.21           C  
ATOM    953  CA  ASN C 118     136.445 346.303 267.349  1.00 28.93           C  
ATOM    954  CA  HIS C 119     134.689 343.115 268.179  1.00 55.92           C  
ATOM    955  CA  ILE C 120     136.674 342.751 271.337  1.00185.94           C  
ATOM    956  CA  TYR C 121     135.236 346.176 271.976  1.00 54.78           C  
ATOM    957  CA  SER C 122     131.724 345.002 271.381  1.00 30.89           C  
ATOM    958  CA  MET C 123     132.634 341.956 273.344  1.00153.15           C  
ATOM    959  CA  ASP C 124     132.230 341.342 276.999  1.00126.83           C  
ATOM    960  CA  GLU C 125     134.067 343.657 279.307  1.00110.35           C  
ATOM    961  CA  ASN C 126     134.516 341.248 282.181  1.00 63.83           C  
ATOM    962  CA  LEU C 127     136.078 338.741 279.835  1.00133.21           C  
ATOM    963  CA  GLU C 128     139.539 340.011 280.456  1.00 79.08           C  
ATOM    964  CA  PHE C 129     141.706 340.266 277.393  1.00 62.18           C  
ATOM    965  CA  HIS C 130     145.428 340.530 277.124  1.00 55.00           C  
ATOM    966  CA  ILE C 131     146.859 341.122 273.707  1.00 92.90           C  
ATOM    967  CA  LYS C 132     150.449 341.223 272.685  1.00 78.08           C  
ATOM    968  CA  VAL C 133     152.361 340.845 269.485  1.00113.12           C  
ATOM    969  CA  SER C 134     155.831 340.440 268.074  1.00 89.19           C  
ATOM    970  CA  TYR C 135     157.574 341.372 264.865  1.00 73.78           C  
ATOM    971  CA  PHE C 136     160.965 339.881 264.214  1.00118.44           C  
ATOM    972  CA  GLU C 137     162.941 338.847 261.212  1.00275.61           C  
ATOM    973  CA  ILE C 138     165.000 335.944 260.118  1.00 79.74           C  
ATOM    974  CA  TYR C 139     168.069 337.129 258.366  1.00 47.84           C  
ATOM    975  CA  LEU C 140     171.460 335.536 258.154  1.00136.14           C  
ATOM    976  CA  ASP C 141     169.862 332.455 259.697  1.00 83.14           C  
ATOM    977  CA  LYS C 142     169.280 334.627 262.684  1.00167.59           C  
ATOM    978  CA  ILE C 143     166.214 335.922 264.318  1.00190.28           C  
ATOM    979  CA  ARG C 144     166.809 339.552 264.538  1.00115.90           C  
ATOM    980  CA  ASP C 145     164.199 341.049 266.672  1.00 53.71           C  
ATOM    981  CA  LEU C 146     162.764 344.079 265.016  1.00 53.11           C  
ATOM    982  CA  LEU C 147     161.340 346.003 267.895  1.00 81.60           C  
ATOM    983  CA  ASP C 148     164.219 345.517 270.146  1.00 48.83           C  
ATOM    984  CA  VAL C 149     167.013 345.675 267.700  1.00 85.92           C  
ATOM    985  CA  THR C 150     169.500 344.820 270.400  1.00 38.05           C  
ATOM    986  CA  LYS C 151     169.049 341.078 270.493  1.00173.76           C  
ATOM    987  CA  THR C 152     169.996 340.293 266.993  1.00 58.07           C  
ATOM    988  CA  ASN C 153     170.951 336.705 267.420  1.00102.58           C  
ATOM    989  CA  LEU C 154     168.097 336.111 269.788  1.00128.78           C  
ATOM    990  CA  SER C 155     167.734 332.794 271.454  1.00106.05           C  
ATOM    991  CA  VAL C 156     164.978 330.403 270.766  1.00114.35           C  
ATOM    992  CA  HIS C 157     164.380 328.548 273.937  1.00 54.64           C  
ATOM    993  CA  GLU C 158     161.518 326.119 274.123  1.00102.92           C  
ATOM    994  CA  ASP C 159     158.724 325.492 276.537  1.00 71.34           C  
ATOM    995  CA  LYS C 160     157.090 322.556 278.301  1.00219.29           C  
ATOM    996  CA  ASN C 161     154.789 321.380 275.592  1.00265.46           C  
ATOM    997  CA  ARG C 162     158.029 321.842 273.775  1.00270.55           C  
ATOM    998  CA  VAL C 163     157.471 324.577 271.278  1.00135.36           C  
ATOM    999  CA  PRO C 164     160.135 326.986 270.541  1.00152.76           C  
ATOM   1000  CA  PHE C 165     159.561 330.662 271.022  1.00 82.03           C  
ATOM   1001  CA  VAL C 166     161.549 333.830 270.668  1.00155.00           C  
ATOM   1002  CA  LYS C 167     162.873 335.109 273.929  1.00152.52           C  
ATOM   1003  CA  GLY C 168     163.694 338.686 274.696  1.00 37.99           C  
ATOM   1004  CA  CYS C 169     161.190 339.654 272.051  1.00125.24           C  
ATOM   1005  CA  THR C 170     159.489 342.335 274.008  1.00254.98           C  
ATOM   1006  CA  GLU C 171     155.811 341.830 273.548  1.00 79.87           C  
ATOM   1007  CA  ARG C 172     154.014 345.099 273.846  1.00169.39           C  
ATOM   1008  CA  PHE C 173     150.456 344.676 274.978  1.00 58.95           C  
ATOM   1009  CA  VAL C 174     148.679 346.400 272.109  1.00110.23           C  
ATOM   1010  CA  SER C 175     145.224 347.593 273.172  1.00133.25           C  
ATOM   1011  CA  SER C 176     143.369 349.084 270.268  1.00108.90           C  
ATOM   1012  CA  PRO C 177     144.064 348.593 266.649  1.00 67.23           C  
ATOM   1013  CA  GLU C 178     146.172 351.697 266.628  1.00 78.23           C  
ATOM   1014  CA  GLU C 179     149.058 350.595 268.769  1.00 90.23           C  
ATOM   1015  CA  ILE C 180     149.176 347.601 266.503  1.00146.77           C  
ATOM   1016  CA  LEU C 181     149.799 349.736 263.431  1.00 47.03           C  
ATOM   1017  CA  ASP C 182     152.480 351.931 264.877  1.00 54.19           C  
ATOM   1018  CA  VAL C 183     154.379 349.005 266.206  1.00 96.99           C  
ATOM   1019  CA  ILE C 184     154.279 347.178 262.950  1.00 54.18           C  
ATOM   1020  CA  ASP C 185     155.394 349.994 260.708  1.00124.18           C  
ATOM   1021  CA  GLU C 186     158.505 350.511 262.720  1.00 47.42           C  
ATOM   1022  CA  GLY C 187     159.066 346.820 262.481  1.00 25.47           C  
ATOM   1023  CA  LYS C 188     158.471 347.335 258.811  1.00141.91           C  
ATOM   1024  CA  SER C 189     161.345 349.733 258.317  1.00 36.03           C  
ATOM   1025  CA  ASN C 190     163.732 347.499 260.190  1.00 81.68           C  
ATOM   1026  CA  ARG C 191     163.059 344.915 257.561  1.00118.70           C  
ATOM   1027  CA  HIS C 192     165.772 344.164 255.080  1.00 48.93           C  
ATOM   1028  CA  VAL C 193     165.170 344.613 251.397  1.00100.19           C  
ATOM   1029  CA  ALA C 194     167.927 343.755 249.050  1.00 39.05           C  
ATOM   1030  CA  VAL C 195     167.587 344.553 245.442  1.00 92.86           C  
ATOM   1031  CA  THR C 196     167.281 341.705 243.028  1.00 67.63           C  
ATOM   1032  CA  ASN C 197     167.192 341.872 239.295  1.00141.37           C  
ATOM   1033  CA  MET C 198     163.897 340.154 239.783  1.00128.18           C  
ATOM   1034  CA  ASN C 199     162.353 341.943 242.647  1.00152.67           C  
ATOM   1035  CA  GLU C 200     164.069 345.193 243.355  1.00 57.22           C  
ATOM   1036  CA  HIS C 201     162.331 345.113 246.673  1.00113.13           C  
ATOM   1037  CA  SER C 202     163.491 341.626 247.251  1.00141.98           C  
ATOM   1038  CA  SER C 203     162.674 340.795 250.797  1.00134.40           C  
ATOM   1039  CA  ARG C 204     165.675 339.015 252.135  1.00210.77           C  
ATOM   1040  CA  SER C 205     164.344 337.727 255.392  1.00 68.05           C  
ATOM   1041  CA  HIS C 206     161.196 335.995 256.424  1.00 63.54           C  
ATOM   1042  CA  SER C 207     159.023 338.199 258.513  1.00 92.39           C  
ATOM   1043  CA  ILE C 208     156.960 336.782 261.262  1.00 71.04           C  
ATOM   1044  CA  PHE C 209     154.217 338.781 262.772  1.00 71.89           C  
ATOM   1045  CA  LEU C 210     152.854 337.350 265.984  1.00191.06           C  
ATOM   1046  CA  ILE C 211     149.669 338.547 267.478  1.00103.43           C  
ATOM   1047  CA  ASN C 212     149.492 336.815 270.786  1.00 55.89           C  
ATOM   1048  CA  ILE C 213     146.132 337.009 272.405  1.00101.51           C  
ATOM   1049  CA  LYS C 214     144.849 335.921 275.750  1.00160.29           C  
ATOM   1050  CA  GLN C 215     141.547 336.120 277.498  1.00111.85           C  
ATOM   1051  CA  GLU C 216     140.215 335.083 280.828  1.00 72.81           C  
ATOM   1052  CA  ASN C 217     136.739 335.060 282.205  1.00 56.16           C  
ATOM   1053  CA  MET C 218     136.205 336.591 285.590  1.00 61.35           C  
ATOM   1054  CA  GLU C 219     133.230 334.688 286.731  1.00 73.30           C  
ATOM   1055  CA  THR C 220     134.385 331.301 285.498  1.00 45.77           C  
ATOM   1056  CA  GLU C 221     137.969 332.508 285.516  1.00153.65           C  
ATOM   1057  CA  GLN C 222     138.843 330.260 282.654  1.00172.10           C  
ATOM   1058  CA  LYS C 223     141.845 331.471 280.816  1.00 59.84           C  
ATOM   1059  CA  LEU C 224     142.031 330.936 277.108  1.00 68.55           C  
ATOM   1060  CA  SER C 225     145.056 331.729 275.007  1.00 90.84           C  
ATOM   1061  CA  GLY C 226     145.625 331.424 271.283  1.00 21.68           C  
ATOM   1062  CA  LYS C 227     148.639 332.375 269.218  1.00156.25           C  
ATOM   1063  CA  LEU C 228     148.731 333.911 265.801  1.00112.46           C  
ATOM   1064  CA  TYR C 229     151.539 333.847 263.293  1.00 90.00           C  
ATOM   1065  CA  LEU C 230     151.713 335.998 260.244  1.00 79.32           C  
ATOM   1066  CA  VAL C 231     154.750 335.229 258.226  1.00133.92           C  
ATOM   1067  CA  ASP C 232     155.609 337.005 255.074  1.00 69.72           C  
ATOM   1068  CA  LEU C 233     158.006 334.437 253.689  1.00115.63           C  
ATOM   1069  CA  ALA C 234     160.604 335.143 251.094  1.00 50.59           C  
ATOM   1070  CA  GLY C 235     160.932 333.162 247.940  1.00 45.07           C  
ATOM   1071  CA  SER C 236     163.400 330.681 246.695  1.00 43.75           C  
ATOM   1072  CA  GLU C 237     165.403 332.498 244.111  1.00103.81           C  
ATOM   1073  CA  LYS C 238     167.065 331.210 241.012  1.00156.27           C  
ATOM   1074  CA  VAL C 239     170.431 332.828 241.021  1.00 91.92           C  
ATOM   1075  CA  SER C 240     170.975 333.577 237.359  1.00 89.86           C  
ATOM   1076  CA  LYS C 241     167.408 334.780 237.356  1.00199.31           C  
ATOM   1077  CA  THR C 242     168.024 336.729 240.554  1.00 53.49           C  
ATOM   1078  CA  GLY C 243     171.181 338.536 239.683  1.00 18.49           C  
ATOM   1079  CA  ALA C 244     172.411 338.598 243.222  1.00 31.46           C  
ATOM   1080  CA  GLU C 245     176.083 338.426 243.983  1.00 73.85           C  
ATOM   1081  CA  GLY C 246     178.299 338.791 246.996  1.00 20.44           C  
ATOM   1082  CA  ALA C 247     176.145 339.336 250.045  1.00 31.19           C  
ATOM   1083  CA  VAL C 248     172.692 338.960 248.596  1.00118.92           C  
ATOM   1084  CA  LEU C 249     174.027 335.739 247.193  1.00 48.25           C  
ATOM   1085  CA  ASP C 250     174.643 334.532 250.749  1.00 74.62           C  
ATOM   1086  CA  GLU C 251     171.178 335.727 251.611  1.00 58.56           C  
ATOM   1087  CA  ALA C 252     169.655 334.282 248.490  1.00 44.34           C  
ATOM   1088  CA  LYS C 253     171.293 331.030 249.496  1.00129.46           C  
ATOM   1089  CA  ASN C 254     169.863 331.298 252.987  1.00127.92           C  
ATOM   1090  CA  ILE C 255     166.307 331.716 251.814  1.00 59.93           C  
ATOM   1091  CA  ASN C 256     166.620 328.930 249.355  1.00 71.28           C  
ATOM   1092  CA  LYS C 257     167.748 326.358 251.825  1.00149.94           C  
ATOM   1093  CA  SER C 258     165.245 327.626 254.333  1.00 36.47           C  
ATOM   1094  CA  LEU C 259     162.445 327.354 251.826  1.00 85.94           C  
ATOM   1095  CA  SER C 260     163.689 323.964 250.777  1.00 28.61           C  
ATOM   1096  CA  ALA C 261     163.514 323.048 254.427  1.00 25.85           C  
ATOM   1097  CA  LEU C 262     159.835 323.636 254.106  1.00 76.51           C  
ATOM   1098  CA  GLY C 263     159.413 321.532 251.001  1.00 32.33           C  
ATOM   1099  CA  ASN C 264     161.172 318.782 252.814  1.00 84.38           C  
ATOM   1100  CA  VAL C 265     159.005 318.883 255.877  1.00 60.61           C  
ATOM   1101  CA  ILE C 266     155.713 319.103 254.094  1.00152.02           C  
ATOM   1102  CA  SER C 267     156.826 316.593 251.549  1.00 79.44           C  
ATOM   1103  CA  ALA C 268     157.400 314.502 254.636  1.00 40.89           C  
ATOM   1104  CA  LEU C 269     154.111 315.244 256.278  1.00140.41           C  
ATOM   1105  CA  ALA C 270     152.530 314.816 252.887  1.00 50.16           C  
ATOM   1106  CA  GLU C 271     153.634 311.246 252.940  1.00203.34           C  
ATOM   1107  CA  GLY C 272     151.244 309.397 255.168  1.00128.08           C  
ATOM   1108  CA  THR C 273     154.296 307.826 256.666  1.00131.88           C  
ATOM   1109  CA  LYS C 274     156.014 309.555 259.471  1.00166.67           C  
ATOM   1110  CA  SER C 275     159.628 310.392 259.607  1.00119.27           C  
ATOM   1111  CA  TYR C 276     160.981 312.810 262.138  1.00136.56           C  
ATOM   1112  CA  VAL C 277     160.715 315.989 260.054  1.00104.98           C  
ATOM   1113  CA  PRO C 278     163.233 318.639 259.189  1.00 73.34           C  
ATOM   1114  CA  TYR C 279     161.710 320.583 262.037  1.00 74.70           C  
ATOM   1115  CA  ARG C 280     164.654 319.795 264.278  1.00160.60           C  
ATOM   1116  CA  ASP C 281     166.711 321.237 261.460  1.00 42.31           C  
ATOM   1117  CA  SER C 282     165.906 324.831 260.802  1.00 38.99           C  
ATOM   1118  CA  LYS C 283     164.531 326.675 263.730  1.00108.62           C  
ATOM   1119  CA  MET C 284     162.002 328.501 261.648  1.00 73.20           C  
ATOM   1120  CA  THR C 285     160.671 325.016 261.201  1.00108.25           C  
ATOM   1121  CA  ARG C 286     160.668 324.074 264.841  1.00190.17           C  
ATOM   1122  CA  ILE C 287     158.229 326.894 264.849  1.00 96.03           C  
ATOM   1123  CA  LEU C 288     156.687 325.520 261.708  1.00126.15           C  
ATOM   1124  CA  GLN C 289     155.778 322.480 263.775  1.00 80.23           C  
ATOM   1125  CA  ASP C 290     152.614 323.528 265.570  1.00 35.09           C  
ATOM   1126  CA  SER C 291     151.237 324.988 262.377  1.00 36.70           C  
ATOM   1127  CA  LEU C 292     152.093 322.329 259.845  1.00100.25           C  
ATOM   1128  CA  GLY C 293     151.257 318.998 261.385  1.00 68.03           C  
ATOM   1129  CA  GLY C 294     150.754 320.079 264.951  1.00 49.32           C  
ATOM   1130  CA  ASN C 295     147.683 321.850 266.222  1.00194.84           C  
ATOM   1131  CA  CYS C 296     147.132 324.945 264.220  1.00116.87           C  
ATOM   1132  CA  ARG C 297     144.654 326.095 261.748  1.00149.24           C  
ATOM   1133  CA  THR C 298     146.901 327.669 259.253  1.00147.79           C  
ATOM   1134  CA  THR C 299     146.549 328.344 255.617  1.00131.74           C  
ATOM   1135  CA  MET C 300     149.066 328.668 252.866  1.00104.67           C  
ATOM   1136  CA  PHE C 301     149.062 331.448 250.339  1.00 61.44           C  
ATOM   1137  CA  ILE C 302     150.412 330.393 246.988  1.00164.50           C  
ATOM   1138  CA  CYS C 303     151.797 333.020 244.756  1.00 94.93           C  
ATOM   1139  CA  CYS C 304     152.612 332.274 241.159  1.00 91.64           C  
ATOM   1140  CA  SER C 305     153.589 334.516 238.322  1.00 99.20           C  
ATOM   1141  CA  PRO C 306     152.067 333.844 235.042  1.00 82.50           C  
ATOM   1142  CA  SER C 307     155.295 334.163 233.142  1.00 96.81           C  
ATOM   1143  CA  SER C 308     156.409 331.249 231.014  1.00 81.78           C  
ATOM   1144  CA  TYR C 309     159.624 332.719 232.213  1.00 89.64           C  
ATOM   1145  CA  ASN C 310     158.863 331.308 235.566  1.00196.56           C  
ATOM   1146  CA  ASP C 311     156.485 328.923 233.922  1.00 54.37           C  
ATOM   1147  CA  ALA C 312     158.658 326.177 235.250  1.00 28.98           C  
ATOM   1148  CA  GLU C 313     158.957 326.857 238.962  1.00124.23           C  
ATOM   1149  CA  THR C 314     155.457 328.088 238.836  1.00 98.21           C  
ATOM   1150  CA  LYS C 315     154.599 324.504 238.416  1.00123.73           C  
ATOM   1151  CA  SER C 316     156.729 323.925 241.477  1.00 76.68           C  
ATOM   1152  CA  THR C 317     155.119 326.377 243.840  1.00120.86           C  
ATOM   1153  CA  LEU C 318     151.871 324.922 242.545  1.00 49.06           C  
ATOM   1154  CA  MET C 319     152.589 321.254 243.240  1.00149.86           C  
ATOM   1155  CA  PHE C 320     153.855 322.474 246.513  1.00 46.42           C  
ATOM   1156  CA  GLY C 321     150.574 324.161 247.318  1.00 20.78           C  
ATOM   1157  CA  GLN C 322     149.146 320.975 245.962  1.00 83.21           C  
ATOM   1158  CA  ARG C 323     150.607 318.376 248.304  1.00 65.64           C  
ATOM   1159  CA  ALA C 324     150.472 321.135 250.890  1.00 36.47           C  
ATOM   1160  CA  LYS C 325     146.742 320.711 251.278  1.00158.78           C  
ATOM   1161  CA  THR C 326     146.554 317.041 252.054  1.00 43.63           C  
ATOM   1162  CA  ILE C 327     148.450 317.404 255.262  1.00190.16           C  
ATOM   1163  CA  LYS C 328     146.036 317.708 258.065  1.00151.31           C  
ATOM   1164  CA  ASN C 329     146.424 318.963 261.553  1.00 74.06           C  
ATOM   1165  CA  THR C 330     145.662 318.262 265.155  1.00 46.09           C  
ATOM   1166  CA  ALA C 331     143.246 321.075 265.731  1.00 56.98           C  
ATOM   1167  CA  SER C 332     142.377 320.900 269.326  1.00 78.12           C  
ATOM   1168  CA  VAL C 333     140.913 323.861 271.017  1.00 85.23           C  
ATOM   1169  CA  ASN C 334     143.528 325.469 273.149  1.00 69.57           C  
ATOM   1170  CA  LEU C 335     142.631 324.665 276.689  1.00114.69           C  
ATOM   1171  CA  GLU C 336     145.404 326.817 278.003  1.00156.22           C  
ATOM   1172  CA  LEU C 337     143.219 327.041 281.049  1.00 65.65           C  
ATOM   1173  CA  THR C 338     143.978 328.838 284.236  1.00 61.73           C  
TER    1174      THR C 338                                                      
HETATM 1175 ZN    ZN A1413     204.630 288.018 215.598  1.00  2.00          ZN  
HETATM 1176 MG    MG A1414     190.812 317.751 242.725  1.00 18.63          MG  
HETATM 1177  PG  GTP A1415     187.175 318.139 242.679  1.00 29.97           P  
HETATM 1178  O1G GTP A1415     188.456 317.755 243.392  1.00 28.70           O  
HETATM 1179  O2G GTP A1415     186.735 319.575 242.991  1.00 34.97           O  
HETATM 1180  O3G GTP A1415     185.988 317.289 243.120  1.00 32.10           O  
HETATM 1181  O3B GTP A1415     187.537 317.890 241.080  1.00 35.17           O  
HETATM 1182  PB  GTP A1415     188.054 316.476 240.407  1.00 41.40           P  
HETATM 1183  O1B GTP A1415     189.481 316.534 240.124  1.00 41.17           O  
HETATM 1184  O2B GTP A1415     187.096 316.206 239.258  1.00 42.02           O  
HETATM 1185  O3A GTP A1415     187.687 315.403 241.432  1.00 39.24           O  
HETATM 1186  PA  GTP A1415     188.048 313.938 241.658  1.00 41.34           P  
HETATM 1187  O1A GTP A1415     187.358 313.494 242.902  1.00 43.37           O  
HETATM 1188  O2A GTP A1415     189.507 313.720 241.619  1.00 44.48           O  
HETATM 1189  O5' GTP A1415     187.304 313.169 240.409  1.00 34.27           O  
HETATM 1190  C5' GTP A1415     187.514 311.768 240.422  1.00 25.47           C  
HETATM 1191  C4' GTP A1415     186.862 310.995 239.321  1.00 17.26           C  
HETATM 1192  O4' GTP A1415     187.730 310.931 238.160  1.00 18.20           O  
HETATM 1193  C3' GTP A1415     186.684 309.567 239.783  1.00 18.14           C  
HETATM 1194  O3' GTP A1415     185.613 308.969 239.089  1.00 19.98           O  
HETATM 1195  C2' GTP A1415     188.036 308.957 239.448  1.00 17.50           C  
HETATM 1196  O2' GTP A1415     187.886 307.549 239.243  1.00 19.33           O  
HETATM 1197  C1' GTP A1415     188.457 309.693 238.167  1.00 18.43           C  
HETATM 1198  N9  GTP A1415     189.892 310.006 238.055  1.00  9.96           N  
HETATM 1199  C8  GTP A1415     190.648 310.745 238.933  1.00 11.60           C  
HETATM 1200  N7  GTP A1415     191.898 310.859 238.575  1.00  7.31           N  
HETATM 1201  C5  GTP A1415     191.985 310.147 237.404  1.00  2.00           C  
HETATM 1202  C6  GTP A1415     193.076 309.906 236.570  1.00  3.48           C  
HETATM 1203  O6  GTP A1415     194.222 310.319 236.728  1.00  2.56           O  
HETATM 1204  N1  GTP A1415     192.755 309.121 235.440  1.00  2.00           N  
HETATM 1205  C2  GTP A1415     191.502 308.619 235.165  1.00  2.00           C  
HETATM 1206  N2  GTP A1415     191.383 307.903 234.085  1.00  2.00           N  
HETATM 1207  N3  GTP A1415     190.450 308.831 235.956  1.00  2.00           N  
HETATM 1208  C4  GTP A1415     190.745 309.604 237.052  1.00  3.56           C  
HETATM 1209  PB  GDP B1427     187.929 317.417 282.235  1.00 22.28           P  
HETATM 1210  O1B GDP B1427     187.541 318.231 281.068  1.00 23.59           O  
HETATM 1211  O2B GDP B1427     189.301 317.217 282.418  1.00 23.44           O  
HETATM 1212  O3B GDP B1427     187.164 318.011 283.552  1.00 25.30           O  
HETATM 1213  O3A GDP B1427     187.352 315.975 281.971  1.00 19.52           O  
HETATM 1214  PA  GDP B1427     188.136 314.501 281.892  1.00 20.51           P  
HETATM 1215  O1A GDP B1427     189.038 314.493 280.707  1.00 23.36           O  
HETATM 1216  O2A GDP B1427     188.820 314.312 283.236  1.00 18.00           O  
HETATM 1217  O5' GDP B1427     186.942 313.545 281.612  1.00 16.66           O  
HETATM 1218  C5' GDP B1427     187.007 312.129 281.961  1.00  7.65           C  
HETATM 1219  C4' GDP B1427     186.808 311.215 280.850  1.00  2.51           C  
HETATM 1220  O4' GDP B1427     187.919 311.397 279.885  1.00  2.00           O  
HETATM 1221  C3' GDP B1427     186.954 309.690 281.201  1.00  3.46           C  
HETATM 1222  O3' GDP B1427     185.936 308.993 280.394  1.00  2.32           O  
HETATM 1223  C2' GDP B1427     188.349 309.195 280.752  1.00  2.23           C  
HETATM 1224  O2' GDP B1427     188.500 307.838 280.300  1.00  2.00           O  
HETATM 1225  C1' GDP B1427     188.703 310.155 279.619  1.00  2.00           C  
HETATM 1226  N9  GDP B1427     190.117 310.526 279.554  1.00  5.88           N  
HETATM 1227  C8  GDP B1427     190.688 311.421 280.617  1.00  9.42           C  
HETATM 1228  N7  GDP B1427     191.972 311.426 280.043  1.00 10.36           N  
HETATM 1229  C5  GDP B1427     192.220 310.740 278.932  1.00 10.45           C  
HETATM 1230  C6  GDP B1427     193.193 310.374 277.978  1.00 13.51           C  
HETATM 1231  O6  GDP B1427     194.421 310.890 278.158  1.00 11.34           O  
HETATM 1232  N1  GDP B1427     192.962 309.583 276.907  1.00 10.31           N  
HETATM 1233  C2  GDP B1427     191.591 309.036 276.721  1.00  5.81           C  
HETATM 1234  N2  GDP B1427     191.601 308.286 275.640  1.00  6.23           N  
HETATM 1235  N3  GDP B1427     190.675 309.311 277.553  1.00  4.23           N  
HETATM 1236  C4  GDP B1427     190.945 310.132 278.585  1.00  7.64           C  
HETATM 1237  O01 TA1 B1428     205.221 301.780 267.574  1.00 63.75           O  
HETATM 1238  C01 TA1 B1428     205.028 301.500 266.174  1.00 63.37           C  
HETATM 1239  C02 TA1 B1428     203.874 300.351 266.098  1.00 64.56           C  
HETATM 1240  O02 TA1 B1428     202.731 301.024 266.756  1.00 73.61           O  
HETATM 1241  C03 TA1 B1428     202.348 300.590 268.047  1.00 82.30           C  
HETATM 1242  O03 TA1 B1428     202.879 299.678 268.632  1.00 81.04           O  
HETATM 1243  C04 TA1 B1428     201.236 301.336 268.577  1.00 85.16           C  
HETATM 1244  C05 TA1 B1428     201.481 301.754 269.957  1.00 85.81           C  
HETATM 1245  C06 TA1 B1428     200.364 302.530 270.580  1.00 88.17           C  
HETATM 1246  C07 TA1 B1428     199.171 302.822 269.862  1.00 88.93           C  
HETATM 1247  C08 TA1 B1428     199.072 302.415 268.681  1.00 87.81           C  
HETATM 1248  C09 TA1 B1428     200.031 301.669 267.944  1.00 86.96           C  
HETATM 1249  C10 TA1 B1428     203.372 299.837 264.644  1.00 60.76           C  
HETATM 1250  C11 TA1 B1428     201.773 299.708 264.499  1.00 59.46           C  
HETATM 1251  O04 TA1 B1428     201.086 301.020 264.641  1.00 58.42           O  
HETATM 1252  C12 TA1 B1428     201.216 302.019 263.704  1.00 58.87           C  
HETATM 1253  O05 TA1 B1428     201.874 301.955 262.709  1.00 60.49           O  
HETATM 1254  C13 TA1 B1428     200.387 303.213 264.130  1.00 55.92           C  
HETATM 1255  C14 TA1 B1428     200.975 298.824 265.494  1.00 60.18           C  
HETATM 1256  O06 TA1 B1428     200.421 298.004 264.439  1.00 59.01           O  
HETATM 1257  C15 TA1 B1428     201.121 298.775 263.439  1.00 59.51           C  
HETATM 1258  C16 TA1 B1428     202.057 297.883 262.558  1.00 60.03           C  
HETATM 1259  C17 TA1 B1428     203.525 298.288 262.608  1.00 61.43           C  
HETATM 1260  O07 TA1 B1428     204.303 297.370 261.796  1.00 62.13           O  
HETATM 1261  C18 TA1 B1428     204.098 298.416 264.101  1.00 62.13           C  
HETATM 1262  C19 TA1 B1428     203.698 297.148 264.914  1.00 63.64           C  
HETATM 1263  C20 TA1 B1428     205.718 298.341 264.076  1.00 65.31           C  
HETATM 1264  O08 TA1 B1428     206.272 297.395 264.612  1.00 68.11           O  
HETATM 1265  C21 TA1 B1428     206.578 299.429 263.421  1.00 63.59           C  
HETATM 1266  O09 TA1 B1428     208.009 299.049 263.607  1.00 58.93           O  
HETATM 1267  C22 TA1 B1428     208.777 298.690 262.519  1.00 56.05           C  
HETATM 1268  O10 TA1 B1428     208.397 298.653 261.389  1.00 57.49           O  
HETATM 1269  C23 TA1 B1428     210.174 298.343 262.954  1.00 54.68           C  
HETATM 1270  C24 TA1 B1428     206.272 300.796 264.036  1.00 63.31           C  
HETATM 1271  C25 TA1 B1428     205.711 301.794 263.245  1.00 62.60           C  
HETATM 1272  C26 TA1 B1428     205.279 303.098 263.983  1.00 60.57           C  
HETATM 1273  O11 TA1 B1428     204.375 303.959 263.206  1.00 60.54           O  
HETATM 1274  C27 TA1 B1428     204.916 304.933 262.486  1.00 60.84           C  
HETATM 1275  O12 TA1 B1428     206.072 305.201 262.378  1.00 60.71           O  
HETATM 1276  C28 TA1 B1428     203.806 305.745 261.768  1.00 63.49           C  
HETATM 1277  O13 TA1 B1428     204.429 306.795 261.051  1.00 63.94           O  
HETATM 1278  C29 TA1 B1428     202.809 306.257 262.838  1.00 64.93           C  
HETATM 1279  N01 TA1 B1428     203.594 306.942 263.858  1.00 68.46           N  
HETATM 1280  C30 TA1 B1428     203.192 307.057 265.145  1.00 75.26           C  
HETATM 1281  O14 TA1 B1428     202.127 306.612 265.559  1.00 72.57           O  
HETATM 1282  C31 TA1 B1428     204.173 307.750 266.027  1.00 80.56           C  
HETATM 1283  C32 TA1 B1428     204.599 309.062 265.834  1.00 83.75           C  
HETATM 1284  C33 TA1 B1428     205.547 309.662 266.707  1.00 86.03           C  
HETATM 1285  C34 TA1 B1428     206.072 308.909 267.794  1.00 87.21           C  
HETATM 1286  C35 TA1 B1428     205.655 307.604 267.993  1.00 85.33           C  
HETATM 1287  C36 TA1 B1428     204.722 307.005 267.139  1.00 84.57           C  
HETATM 1288  C37 TA1 B1428     201.698 307.122 262.205  1.00 65.34           C  
HETATM 1289  C38 TA1 B1428     200.510 306.483 261.814  1.00 66.62           C  
HETATM 1290  C39 TA1 B1428     199.452 307.221 261.219  1.00 67.56           C  
HETATM 1291  C40 TA1 B1428     199.593 308.605 261.021  1.00 66.79           C  
HETATM 1292  C41 TA1 B1428     200.761 309.239 261.407  1.00 68.49           C  
HETATM 1293  C42 TA1 B1428     201.827 308.506 262.003  1.00 66.75           C  
HETATM 1294  C43 TA1 B1428     204.531 302.773 265.333  1.00 61.38           C  
HETATM 1295  C44 TA1 B1428     205.396 301.694 261.756  1.00 62.81           C  
HETATM 1296  C45 TA1 B1428     206.517 301.043 265.605  1.00 63.04           C  
HETATM 1297  C46 TA1 B1428     207.625 302.178 265.781  1.00 62.66           C  
HETATM 1298  C47 TA1 B1428     207.083 299.885 266.459  1.00 61.96           C  
HETATM 1299  PB  ADP C1339     157.678 338.717 246.732  1.00144.64           P  
HETATM 1300  O1B ADP C1339     156.682 337.724 246.221  1.00144.64           O  
HETATM 1301  O2B ADP C1339     157.410 338.984 248.204  1.00144.64           O  
HETATM 1302  O3B ADP C1339     159.086 338.075 246.511  1.00144.64           O  
HETATM 1303  PA  ADP C1339     156.548 341.363 246.052  1.00144.64           P  
HETATM 1304  O1A ADP C1339     157.340 342.437 246.687  1.00144.64           O  
HETATM 1305  O2A ADP C1339     155.364 341.040 246.912  1.00144.64           O  
HETATM 1306  O3A ADP C1339     157.483 340.069 245.891  1.00144.64           O  
HETATM 1307  O5' ADP C1339     156.013 341.847 244.667  1.00144.64           O  
HETATM 1308  C5' ADP C1339     156.914 342.309 243.643  1.00144.64           C  
HETATM 1309  C4' ADP C1339     156.230 343.386 242.843  1.00144.64           C  
HETATM 1310  O4' ADP C1339     155.044 342.873 242.208  1.00144.64           O  
HETATM 1311  C3' ADP C1339     155.811 344.654 243.598  1.00144.64           C  
HETATM 1312  O3' ADP C1339     156.227 345.796 242.862  1.00144.64           O  
HETATM 1313  C2' ADP C1339     154.298 344.472 243.771  1.00144.64           C  
HETATM 1314  O2' ADP C1339     153.590 345.688 243.974  1.00144.64           O  
HETATM 1315  C1' ADP C1339     153.935 343.706 242.495  1.00144.64           C  
HETATM 1316  N9  ADP C1339     152.769 342.834 242.609  1.00144.64           N  
HETATM 1317  C8  ADP C1339     152.709 341.654 243.310  1.00144.64           C  
HETATM 1318  N7  ADP C1339     151.542 341.083 243.264  1.00144.64           N  
HETATM 1319  C5  ADP C1339     150.764 341.939 242.521  1.00144.64           C  
HETATM 1320  C6  ADP C1339     149.441 341.844 242.040  1.00144.64           C  
HETATM 1321  N6  ADP C1339     148.559 340.918 242.474  1.00144.64           N  
HETATM 1322  N1  ADP C1339     148.995 342.833 241.238  1.00144.64           N  
HETATM 1323  C2  ADP C1339     149.835 343.821 240.901  1.00144.64           C  
HETATM 1324  N3  ADP C1339     151.123 343.988 241.242  1.00144.64           N  
HETATM 1325  C4  ADP C1339     151.525 343.011 242.062  1.00144.64           C  
HETATM 1326 MG    MG C1340     158.504 340.383 249.311  1.00  4.06          MG  
HETATM 1327 AL   ALF C1341     160.737 338.319 247.540  1.00 35.15          AL  
HETATM 1328  F1  ALF C1341     160.094 337.605 249.024  1.00 35.15           F  
HETATM 1329  F2  ALF C1341     161.610 338.950 246.106  1.00 35.15           F  
HETATM 1330  F3  ALF C1341     161.491 336.719 247.206  1.00 35.15           F  
HETATM 1331  F4  ALF C1341     160.280 339.970 248.048  1.00 35.15           F  
HETATM 1332  N7  ANP C1343     150.715 338.863 244.601  1.00  9.01           N  
CONECT 1176 1178                                                                
CONECT 1177 1178 1179 1180 1181                                                 
CONECT 1178 1176 1177                                                           
CONECT 1179 1177                                                                
CONECT 1180 1177                                                                
CONECT 1181 1177 1182                                                           
CONECT 1182 1181 1183 1184 1185                                                 
CONECT 1183 1182                                                                
CONECT 1184 1182                                                                
CONECT 1185 1182 1186                                                           
CONECT 1186 1185 1187 1188 1189                                                 
CONECT 1187 1186                                                                
CONECT 1188 1186                                                                
CONECT 1189 1186 1190                                                           
CONECT 1190 1189 1191                                                           
CONECT 1191 1190 1192 1193                                                      
CONECT 1192 1191 1197                                                           
CONECT 1193 1191 1194 1195                                                      
CONECT 1194 1193                                                                
CONECT 1195 1193 1196 1197                                                      
CONECT 1196 1195                                                                
CONECT 1197 1192 1195 1198                                                      
CONECT 1198 1197 1199 1208                                                      
CONECT 1199 1198 1200                                                           
CONECT 1200 1199 1201                                                           
CONECT 1201 1200 1202 1208                                                      
CONECT 1202 1201 1203 1204                                                      
CONECT 1203 1202                                                                
CONECT 1204 1202 1205                                                           
CONECT 1205 1204 1206 1207                                                      
CONECT 1206 1205                                                                
CONECT 1207 1205 1208                                                           
CONECT 1208 1198 1201 1207                                                      
CONECT 1209 1210 1211 1212 1213                                                 
CONECT 1210 1209                                                                
CONECT 1211 1209                                                                
CONECT 1212 1209                                                                
CONECT 1213 1209 1214                                                           
CONECT 1214 1213 1215 1216 1217                                                 
CONECT 1215 1214                                                                
CONECT 1216 1214                                                                
CONECT 1217 1214 1218                                                           
CONECT 1218 1217 1219                                                           
CONECT 1219 1218 1220 1221                                                      
CONECT 1220 1219 1225                                                           
CONECT 1221 1219 1222 1223                                                      
CONECT 1222 1221                                                                
CONECT 1223 1221 1224 1225                                                      
CONECT 1224 1223                                                                
CONECT 1225 1220 1223 1226                                                      
CONECT 1226 1225 1227 1236                                                      
CONECT 1227 1226 1228                                                           
CONECT 1228 1227 1229                                                           
CONECT 1229 1228 1230 1236                                                      
CONECT 1230 1229 1231 1232                                                      
CONECT 1231 1230                                                                
CONECT 1232 1230 1233                                                           
CONECT 1233 1232 1234 1235                                                      
CONECT 1234 1233                                                                
CONECT 1235 1233 1236                                                           
CONECT 1236 1226 1229 1235                                                      
CONECT 1237 1238                                                                
CONECT 1238 1237 1239 1294 1296                                                 
CONECT 1239 1238 1240 1249                                                      
CONECT 1240 1239 1241                                                           
CONECT 1241 1240 1242 1243                                                      
CONECT 1242 1241                                                                
CONECT 1243 1241 1244 1248                                                      
CONECT 1244 1243 1245                                                           
CONECT 1245 1244 1246                                                           
CONECT 1246 1245 1247                                                           
CONECT 1247 1246 1248                                                           
CONECT 1248 1243 1247                                                           
CONECT 1249 1239 1250 1261                                                      
CONECT 1250 1249 1251 1255 1257                                                 
CONECT 1251 1250 1252                                                           
CONECT 1252 1251 1253 1254                                                      
CONECT 1253 1252                                                                
CONECT 1254 1252                                                                
CONECT 1255 1250 1256                                                           
CONECT 1256 1255 1257                                                           
CONECT 1257 1250 1256 1258                                                      
CONECT 1258 1257 1259                                                           
CONECT 1259 1258 1260 1261                                                      
CONECT 1260 1259                                                                
CONECT 1261 1249 1259 1262 1263                                                 
CONECT 1262 1261                                                                
CONECT 1263 1261 1264 1265                                                      
CONECT 1264 1263                                                                
CONECT 1265 1263 1266 1270                                                      
CONECT 1266 1265 1267                                                           
CONECT 1267 1266 1268 1269                                                      
CONECT 1268 1267                                                                
CONECT 1269 1267                                                                
CONECT 1270 1265 1271 1296                                                      
CONECT 1271 1270 1272 1295                                                      
CONECT 1272 1271 1273 1294                                                      
CONECT 1273 1272 1274                                                           
CONECT 1274 1273 1275 1276                                                      
CONECT 1275 1274                                                                
CONECT 1276 1274 1277 1278                                                      
CONECT 1277 1276                                                                
CONECT 1278 1276 1279 1288                                                      
CONECT 1279 1278 1280                                                           
CONECT 1280 1279 1281 1282                                                      
CONECT 1281 1280                                                                
CONECT 1282 1280 1283 1287                                                      
CONECT 1283 1282 1284                                                           
CONECT 1284 1283 1285                                                           
CONECT 1285 1284 1286                                                           
CONECT 1286 1285 1287                                                           
CONECT 1287 1282 1286                                                           
CONECT 1288 1278 1289 1293                                                      
CONECT 1289 1288 1290                                                           
CONECT 1290 1289 1291                                                           
CONECT 1291 1290 1292                                                           
CONECT 1292 1291 1293                                                           
CONECT 1293 1288 1292                                                           
CONECT 1294 1238 1272                                                           
CONECT 1295 1271                                                                
CONECT 1296 1238 1270 1297 1298                                                 
CONECT 1297 1296                                                                
CONECT 1298 1296                                                                
CONECT 1299 1300 1301 1302 1306                                                 
CONECT 1300 1299                                                                
CONECT 1301 1299 1326                                                           
CONECT 1302 1299 1327                                                           
CONECT 1303 1304 1305 1306 1307                                                 
CONECT 1304 1303                                                                
CONECT 1305 1303                                                                
CONECT 1306 1299 1303                                                           
CONECT 1307 1303 1308                                                           
CONECT 1308 1307 1309                                                           
CONECT 1309 1308 1310 1311                                                      
CONECT 1310 1309 1315                                                           
CONECT 1311 1309 1312 1313                                                      
CONECT 1312 1311                                                                
CONECT 1313 1311 1314 1315                                                      
CONECT 1314 1313                                                                
CONECT 1315 1310 1313 1316                                                      
CONECT 1316 1315 1317 1325                                                      
CONECT 1317 1316 1318                                                           
CONECT 1318 1317 1319                                                           
CONECT 1319 1318 1320 1325                                                      
CONECT 1320 1319 1321 1322                                                      
CONECT 1321 1320                                                                
CONECT 1322 1320 1323                                                           
CONECT 1323 1322 1324                                                           
CONECT 1324 1323 1325                                                           
CONECT 1325 1316 1319 1324                                                      
CONECT 1326 1301                                                                
CONECT 1327 1302 1328 1329 1330                                                 
CONECT 1327 1331                                                                
CONECT 1328 1327                                                                
CONECT 1329 1327                                                                
CONECT 1330 1327                                                                
CONECT 1331 1327                                                                
MASTER      230    0    9    0    0    0   14    6 1329    3  157   95          
END                                                                             
