HEADER    MOTOR PROTEIN                           30-DEC-13   4CK7              
TITLE     PSEUDO-ATOMIC MODEL OF MICROTUBULE-BOUND HUMAN KINESIN-5 MOTOR DOMAIN 
TITLE    2 IN PRESENCE OF ADP.ALFX (NECK-LINKER IN ITS DISCONNECTED             
TITLE    3 CONFORMATION, BASED ON CRYO-ELECTRON MICROSCOPY EXPERIMENT           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUBULIN ALPHA-1D CHAIN;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA TUBULIN;                                              
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TUBULIN BETA-2B CHAIN;                                     
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: BETA TUBULIN;                                               
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: KINESIN-LIKE PROTEIN KIF11;                                
COMPND  11 CHAIN: C;                                                            
COMPND  12 FRAGMENT: MOTOR DOMAIN, RESIDUES 1-367;                              
COMPND  13 SYNONYM: KINESIN-LIKE PROTEIN 1, KINESIN-LIKE SPINDLE PROTEIN HKSP,  
COMPND  14 KINESIN-RELATED MOTOR PROTEIN EG5, THYROID RECEPTOR-INTERACTING      
COMPND  15 PROTEIN 5, TR-INTERACTING PROTEIN 5, TRIP-5, KINESIN-5;              
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 ORGAN: BRAIN;                                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   8 ORGANISM_COMMON: CATTLE;                                             
SOURCE   9 ORGANISM_TAXID: 9913;                                                
SOURCE  10 ORGAN: BRAIN;                                                        
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    MOTOR PROTEIN, KINESINS, MICROTUBULES, MITOSIS, MECHANOCHEMISTRY      
EXPDTA    ELECTRON MICROSCOPY                                                   
MDLTYP    CA ATOMS ONLY, CHAIN A, B, C                                          
AUTHOR    A.GOULET,J.MAJOR,Y.JUN,S.GROSS,S.ROSENFELD,C.MOORES                   
REVDAT   3   30-AUG-17 4CK7    1       REMARK                                   
REVDAT   2   19-FEB-14 4CK7    1       JRNL                                     
REVDAT   1   05-FEB-14 4CK7    0                                                
JRNL        AUTH   A.GOULET,J.MAJOR,Y.JUN,S.P.GROSS,S.S.ROSENFELD,C.A.MOORES    
JRNL        TITL   COMPREHENSIVE STRUCTURAL MODEL OF THE MECHANOCHEMICAL CYCLE  
JRNL        TITL 2 OF A MITOTIC MOTOR HIGHLIGHTS MOLECULAR ADAPTATIONS IN THE   
JRNL        TITL 3 KINESIN FAMILY.                                              
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111  1837 2014              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24449904                                                     
JRNL        DOI    10.1073/PNAS.1319848111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    9.20 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                    : 3HQD                                
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)  : 9.200                          
REMARK   3   NUMBER OF PARTICLES               : 10692                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: THE N-TERMINAL SEQUENCE WAS MODELLED USING            
REMARK   3  MODELLER. THE DISCONNECTED CONFORMATION OF THE NECK-LINKER WAS      
REMARK   3  CALCULATED USING A CONJUGATE-GRADIENT ENERGY MINIMIZATION.          
REMARK   3  SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-2533.           
REMARK   3  (DEPOSITION ID: 12198).                                             
REMARK   4                                                                      
REMARK   4 4CK7 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_1290059311.                                   
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                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : MICROTUBULE-BOUND HUMAN KINESIN   
REMARK 245                                    -5 MOTOR DOMAIN                   
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : HOLEY CARBON                      
REMARK 245   SAMPLE VITRIFICATION DETAILS   : LIQUID ETHANE                     
REMARK 245   SAMPLE BUFFER                  : 80 MM PIPES 5 MM MGCL2 1 MM       
REMARK 245                                    EGTA 1 MM TCEP                    
REMARK 245   PH                             : 6.80                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 10-MAR-11                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 90.00                          
REMARK 245   MICROSCOPE MODEL                  : FEI TECNAI F20                 
REMARK 245   DETECTOR TYPE                     : KODAK SO-163 FILM              
REMARK 245   MINIMUM DEFOCUS (NM)              : 700.00                         
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2500.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.00                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 18.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 50000                          
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 200                            
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: PQS                                                   
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     1                                                      
REMARK 465     GLN A    35                                                      
REMARK 465     MET A    36                                                      
REMARK 465     PRO A    37                                                      
REMARK 465     SER A    38                                                      
REMARK 465     ASP A    39                                                      
REMARK 465     LYS A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     ILE A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 465     GLY A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     ASP A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     SER A    48                                                      
REMARK 465     PHE A    49                                                      
REMARK 465     ASN A    50                                                      
REMARK 465     THR A    51                                                      
REMARK 465     PHE A    52                                                      
REMARK 465     PHE A    53                                                      
REMARK 465     SER A    54                                                      
REMARK 465     GLU A    55                                                      
REMARK 465     THR A    56                                                      
REMARK 465     GLY A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     LYS A    60                                                      
REMARK 465     VAL A   440                                                      
REMARK 465     GLU A   441                                                      
REMARK 465     GLY A   442                                                      
REMARK 465     GLU A   443                                                      
REMARK 465     GLY A   444                                                      
REMARK 465     GLU A   445                                                      
REMARK 465     GLU A   446                                                      
REMARK 465     GLU A   447                                                      
REMARK 465     GLU A   448                                                      
REMARK 465     GLY A   449                                                      
REMARK 465     GLU A   450                                                      
REMARK 465     GLU A   451                                                      
REMARK 465     TYR A   452                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   428                                                      
REMARK 465     THR B   429                                                      
REMARK 465     ALA B   430                                                      
REMARK 465     ASP B   431                                                      
REMARK 465     GLU B   432                                                      
REMARK 465     GLN B   433                                                      
REMARK 465     GLY B   434                                                      
REMARK 465     GLU B   435                                                      
REMARK 465     PHE B   436                                                      
REMARK 465     GLU B   437                                                      
REMARK 465     GLU B   438                                                      
REMARK 465     GLU B   439                                                      
REMARK 465     GLU B   440                                                      
REMARK 465     GLY B   441                                                      
REMARK 465     GLU B   442                                                      
REMARK 465     ASP B   443                                                      
REMARK 465     GLU B   444                                                      
REMARK 465     ALA B   445                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     GLN C   367                                                      
REMARK 465     HIS C   368                                                      
REMARK 465     HIS C   369                                                      
REMARK 465     HIS C   370                                                      
REMARK 465     HIS C   371                                                      
REMARK 465     HIS C   372                                                      
REMARK 465     HIS C   373                                                      
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                             AF3 C1206  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  MG C1205  MG                                                      
REMARK 620 2 AF3 C1206   F1   49.8                                              
REMARK 620 3 AF3 C1206   F2  140.2 120.5                                        
REMARK 620 4 AF3 C1206   F3   77.9 117.9 121.3                                  
REMARK 620 5 ADP C1207   O3B  66.1  88.5  76.0  99.6                            
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 MG A 1208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 1209                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 B 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 C 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 1207                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CK5   RELATED DB: PDB                                   
REMARK 900 PSEUDO-ATOMIC MODEL OF MICROTUBULE-BOUND HUMAN KINESIN- 5 MOTOR      
REMARK 900 DOMAIN IN THE ADP STATE, BASED ON CRYO- ELECTRON MICROSCOPY          
REMARK 900 EXPERIMENT.                                                          
REMARK 900 RELATED ID: 4CK6   RELATED DB: PDB                                   
REMARK 900 PSEUDO-ATOMIC MODEL OF MICROTUBULE-BOUND HUMAN KINESIN- 5 MOTOR      
REMARK 900 DOMAIN IN THE ADP.ALFX STATE, BASED ON CRYO-ELECTRON MICROSCOPY      
REMARK 900 EXPERIMENT.                                                          
REMARK 900 RELATED ID: EMD-2533   RELATED DB: EMDB                              
REMARK 900 ELECTRON CRYO-MICROSCOPY OF MICROTUBULE-BOUND HUMAN KINESIN-5 MOTOR  
REMARK 900 DOMAIN IN THE ADP.ALFX STATE                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CYS-LITE MUTANT CONTAINING THE SUBSTITUTION T126C                    
DBREF  4CK7 A    1   452  UNP    Q2HJ86   TBA1D_BOVIN      1    452             
DBREF  4CK7 B    1   445  UNP    Q6B856   TBB2B_BOVIN      1    445             
DBREF  4CK7 C    1   367  UNP    P52732   KIF11_HUMAN      1    367             
SEQADV 4CK7 ILE A    7  UNP  Q2HJ86    VAL     7 CONFLICT                       
SEQADV 4CK7 ILE A  114  UNP  Q2HJ86    LEU   114 CONFLICT                       
SEQADV 4CK7 SER A  136  UNP  Q2HJ86    LEU   136 CONFLICT                       
SEQADV 4CK7 VAL A  137  UNP  Q2HJ86    ILE   137 CONFLICT                       
SEQADV 4CK7 GLY A  265  UNP  Q2HJ86    ILE   265 CONFLICT                       
SEQADV 4CK7 GLU A  358  UNP  Q2HJ86    ASP   358 CONFLICT                       
SEQADV 4CK7 VAL A  437  UNP  Q2HJ86    MET   437 CONFLICT                       
SEQADV 4CK7 ALA B   55  UNP  Q6B856    THR    55 CONFLICT                       
SEQADV 4CK7 VAL B  170  UNP  Q6B856    MET   170 CONFLICT                       
SEQADV 4CK7 ALA B  296  UNP  Q6B856    SER   296 CONFLICT                       
SEQADV 4CK7 VAL B  316  UNP  Q6B856    ILE   316 CONFLICT                       
SEQADV 4CK7 VAL C   25  UNP  P52732    CYS    25 CONFLICT                       
SEQADV 4CK7 SER C   43  UNP  P52732    CYS    43 CONFLICT                       
SEQADV 4CK7 ALA C   87  UNP  P52732    CYS    87 CONFLICT                       
SEQADV 4CK7 ALA C   99  UNP  P52732    CYS    99 CONFLICT                       
SEQADV 4CK7 CYS C  126  UNP  P52732    THR   126 ENGINEERED MUTATION            
SEQADV 4CK7 HIS C  368  UNP  P52732              EXPRESSION TAG                 
SEQADV 4CK7 HIS C  369  UNP  P52732              EXPRESSION TAG                 
SEQADV 4CK7 HIS C  370  UNP  P52732              EXPRESSION TAG                 
SEQADV 4CK7 HIS C  371  UNP  P52732              EXPRESSION TAG                 
SEQADV 4CK7 HIS C  372  UNP  P52732              EXPRESSION TAG                 
SEQADV 4CK7 HIS C  373  UNP  P52732              EXPRESSION TAG                 
SEQRES   1 A  452  MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY          
SEQRES   2 A  452  VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU          
SEQRES   3 A  452  GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP          
SEQRES   4 A  452  LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE          
SEQRES   5 A  452  PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA          
SEQRES   6 A  452  VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL          
SEQRES   7 A  452  ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN          
SEQRES   8 A  452  LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA          
SEQRES   9 A  452  ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU          
SEQRES  10 A  452  VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR          
SEQRES  11 A  452  GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY          
SEQRES  12 A  452  GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG          
SEQRES  13 A  452  LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE          
SEQRES  14 A  452  SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL          
SEQRES  15 A  452  GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU          
SEQRES  16 A  452  GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA          
SEQRES  17 A  452  ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG          
SEQRES  18 A  452  PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE          
SEQRES  19 A  452  VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA          
SEQRES  20 A  452  LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL          
SEQRES  21 A  452  PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA          
SEQRES  22 A  452  PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU          
SEQRES  23 A  452  SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA          
SEQRES  24 A  452  ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR          
SEQRES  25 A  452  MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO          
SEQRES  26 A  452  LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS          
SEQRES  27 A  452  ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE          
SEQRES  28 A  452  LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO          
SEQRES  29 A  452  GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET          
SEQRES  30 A  452  LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG          
SEQRES  31 A  452  LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA          
SEQRES  32 A  452  PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY          
SEQRES  33 A  452  GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU          
SEQRES  34 A  452  LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY          
SEQRES  35 A  452  GLU GLY GLU GLU GLU GLU GLY GLU GLU TYR                      
SEQRES   1 B  445  MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY          
SEQRES   2 B  445  ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP          
SEQRES   3 B  445  GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP          
SEQRES   4 B  445  SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN          
SEQRES   5 B  445  GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU          
SEQRES   6 B  445  VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER          
SEQRES   7 B  445  GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL          
SEQRES   8 B  445  PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY          
SEQRES   9 B  445  HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU          
SEQRES  10 B  445  ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU          
SEQRES  11 B  445  GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR          
SEQRES  12 B  445  GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG          
SEQRES  13 B  445  GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL          
SEQRES  14 B  445  VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO          
SEQRES  15 B  445  TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN          
SEQRES  16 B  445  THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR          
SEQRES  17 B  445  ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR          
SEQRES  18 B  445  TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER          
SEQRES  19 B  445  GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN          
SEQRES  20 B  445  ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE          
SEQRES  21 B  445  PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU          
SEQRES  22 B  445  THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL          
SEQRES  23 B  445  PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET          
SEQRES  24 B  445  MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR          
SEQRES  25 B  445  VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU          
SEQRES  26 B  445  VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER          
SEQRES  27 B  445  SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR          
SEQRES  28 B  445  ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER          
SEQRES  29 B  445  ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU          
SEQRES  30 B  445  PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG          
SEQRES  31 B  445  ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET          
SEQRES  32 B  445  ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN          
SEQRES  33 B  445  ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR          
SEQRES  34 B  445  ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLU GLY GLU          
SEQRES  35 B  445  ASP GLU ALA                                                  
SEQRES   1 C  373  MET ALA SER GLN PRO ASN SER SER ALA LYS LYS LYS GLU          
SEQRES   2 C  373  GLU LYS GLY LYS ASN ILE GLN VAL VAL VAL ARG VAL ARG          
SEQRES   3 C  373  PRO PHE ASN LEU ALA GLU ARG LYS ALA SER ALA HIS SER          
SEQRES   4 C  373  ILE VAL GLU SER ASP PRO VAL ARG LYS GLU VAL SER VAL          
SEQRES   5 C  373  ARG THR GLY GLY LEU ALA ASP LYS SER SER ARG LYS THR          
SEQRES   6 C  373  TYR THR PHE ASP MET VAL PHE GLY ALA SER THR LYS GLN          
SEQRES   7 C  373  ILE ASP VAL TYR ARG SER VAL VAL ALA PRO ILE LEU ASP          
SEQRES   8 C  373  GLU VAL ILE MET GLY TYR ASN ALA THR ILE PHE ALA TYR          
SEQRES   9 C  373  GLY GLN THR GLY THR GLY LYS THR PHE THR MET GLU GLY          
SEQRES  10 C  373  GLU ARG SER PRO ASN GLU GLU TYR CYS TRP GLU GLU ASP          
SEQRES  11 C  373  PRO LEU ALA GLY ILE ILE PRO ARG THR LEU HIS GLN ILE          
SEQRES  12 C  373  PHE GLU LYS LEU THR ASP ASN GLY THR GLU PHE SER VAL          
SEQRES  13 C  373  LYS VAL SER LEU LEU GLU ILE TYR ASN GLU GLU LEU PHE          
SEQRES  14 C  373  ASP LEU LEU ASN PRO SER SER ASP VAL SER GLU ARG LEU          
SEQRES  15 C  373  GLN MET PHE ASP ASP PRO ARG ASN LYS ARG GLY VAL ILE          
SEQRES  16 C  373  ILE LYS GLY LEU GLU GLU ILE THR VAL HIS ASN LYS ASP          
SEQRES  17 C  373  GLU VAL TYR GLN ILE LEU GLU LYS GLY ALA ALA LYS ARG          
SEQRES  18 C  373  THR THR ALA ALA THR LEU MET ASN ALA TYR SER SER ARG          
SEQRES  19 C  373  SER HIS SER VAL PHE SER VAL THR ILE HIS MET LYS GLU          
SEQRES  20 C  373  THR THR ILE ASP GLY GLU GLU LEU VAL LYS ILE GLY LYS          
SEQRES  21 C  373  LEU ASN LEU VAL ASP LEU ALA GLY SER GLU ASN ILE GLY          
SEQRES  22 C  373  ARG SER GLY ALA VAL ASP LYS ARG ALA ARG GLU ALA GLY          
SEQRES  23 C  373  ASN ILE ASN GLN SER LEU LEU THR LEU GLY ARG VAL ILE          
SEQRES  24 C  373  THR ALA LEU VAL GLU ARG THR PRO HIS VAL PRO TYR ARG          
SEQRES  25 C  373  GLU SER LYS LEU THR ARG ILE LEU GLN ASP SER LEU GLY          
SEQRES  26 C  373  GLY ARG THR ARG THR SER ILE ILE ALA THR ILE SER PRO          
SEQRES  27 C  373  ALA SER LEU ASN LEU GLU GLU THR LEU SER THR LEU GLU          
SEQRES  28 C  373  TYR ALA HIS ARG ALA LYS ASN ILE LEU ASN LYS PRO GLU          
SEQRES  29 C  373  VAL ASN GLN HIS HIS HIS HIS HIS HIS                          
HET     MG  A1208       1                                                       
HET    GTP  A1209      32                                                       
HET    GDP  B1210      28                                                       
HET    TA1  B1211      62                                                       
HET     MG  C1205       1                                                       
HET    AF3  C1206       4                                                       
HET    ADP  C1207      27                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     TA1 TAXOL                                                            
HETNAM     AF3 ALUMINUM FLUORIDE                                                
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  GTP    C10 H16 N5 O14 P3                                            
FORMUL   6  GDP    C10 H15 N5 O11 P2                                            
FORMUL   7  TA1    C47 H51 N O14                                                
FORMUL   9  AF3    AL F3                                                        
FORMUL  10  ADP    C10 H15 N5 O10 P2                                            
LINK        MG    MG A1208                 O1G GTP A1209     1555   1555  2.45  
LINK        MG    MG C1205                 O3B ADP C1207     1555   1555  2.74  
LINK        AL   AF3 C1206                MG    MG C1205     1555   1555  2.70  
LINK        AL   AF3 C1206                 O3B ADP C1207     1555   1555  2.28  
SITE     1 AC1  1 GTP A1209                                                     
SITE     1 AC2  5 GLY A  10  GLN A  11  GLY A 143  PRO A 173                    
SITE     2 AC2  5  MG A1208                                                     
SITE     1 AC3  2 GLY B 141  GLY B 142                                          
SITE     1 AC4  3 VAL B  23  LEU B 228  GLY B 360                               
SITE     1 AC5  2 AF3 C1206  ADP C1207                                          
SITE     1 AC6  3 SER C 232   MG C1205  ADP C1207                               
SITE     1 AC7  6 ASN C  29  GLY C 108  GLY C 110  THR C 112                    
SITE     2 AC7  6  MG C1205  AF3 C1206                                          
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   2     197.415 276.426 371.079  1.00 90.72           C  
ATOM      2  CA  GLU A   3     197.747 276.838 374.741  1.00 76.37           C  
ATOM      3  CA  CYS A   4     196.472 274.400 377.309  1.00 53.93           C  
ATOM      4  CA  ILE A   5     196.000 274.957 380.959  1.00 42.08           C  
ATOM      5  CA  SER A   6     196.664 272.786 384.003  1.00 26.32           C  
ATOM      6  CA  ILE A   7     195.271 272.852 387.513  1.00 20.58           C  
ATOM      7  CA  HIS A   8     197.324 270.931 390.040  1.00 24.92           C  
ATOM      8  CA  VAL A   9     194.988 270.248 392.952  1.00 24.49           C  
ATOM      9  CA  GLY A  10     195.844 268.622 396.295  1.00 29.78           C  
ATOM     10  CA  GLN A  11     199.272 268.340 397.893  1.00 23.82           C  
ATOM     11  CA  ALA A  12     200.010 265.431 395.596  1.00 17.32           C  
ATOM     12  CA  GLY A  13     198.696 267.077 392.439  1.00 14.25           C  
ATOM     13  CA  VAL A  14     201.009 269.863 393.518  1.00 16.05           C  
ATOM     14  CA  GLN A  15     204.081 267.669 394.147  1.00 19.43           C  
ATOM     15  CA  ILE A  16     203.507 265.986 390.811  1.00 18.31           C  
ATOM     16  CA  GLY A  17     202.882 269.496 389.563  1.00 26.23           C  
ATOM     17  CA  ASN A  18     206.199 270.844 390.761  1.00 29.97           C  
ATOM     18  CA  ALA A  19     207.704 267.814 388.990  1.00 37.71           C  
ATOM     19  CA  CYS A  20     205.922 267.990 385.646  1.00 43.89           C  
ATOM     20  CA  TRP A  21     206.546 271.682 385.895  1.00 51.95           C  
ATOM     21  CA  GLU A  22     210.220 271.017 386.406  1.00 59.11           C  
ATOM     22  CA  LEU A  23     210.750 268.701 383.470  1.00 62.00           C  
ATOM     23  CA  TYR A  24     209.232 271.513 381.431  1.00 70.43           C  
ATOM     24  CA  CYS A  25     211.657 274.415 381.667  1.00 67.24           C  
ATOM     25  CA  LEU A  26     214.337 271.728 381.702  1.00 73.69           C  
ATOM     26  CA  GLU A  27     213.590 270.898 378.061  1.00 74.74           C  
ATOM     27  CA  HIS A  28     212.393 274.369 377.223  1.00 77.34           C  
ATOM     28  CA  GLY A  29     215.859 275.354 376.419  1.00 86.18           C  
ATOM     29  CA  ILE A  30     214.967 278.498 378.161  1.00 87.45           C  
ATOM     30  CA  GLN A  31     215.022 279.723 381.584  1.00 86.37           C  
ATOM     31  CA  PRO A  32     212.817 278.281 383.841  1.00 89.63           C  
ATOM     32  CA  ASP A  33     211.277 281.423 384.913  1.00 96.86           C  
ATOM     33  CA  GLY A  34     210.523 283.690 381.930  1.00 94.83           C  
ATOM     34  CA  HIS A  61     208.448 281.166 380.147  1.00 99.59           C  
ATOM     35  CA  VAL A  62     205.957 281.378 383.073  1.00 96.92           C  
ATOM     36  CA  PRO A  63     203.452 278.981 384.006  1.00 88.64           C  
ATOM     37  CA  ARG A  64     200.023 278.720 382.368  1.00 69.26           C  
ATOM     38  CA  ALA A  65     198.812 276.628 385.172  1.00 49.94           C  
ATOM     39  CA  VAL A  66     197.657 277.038 388.738  1.00 45.70           C  
ATOM     40  CA  PHE A  67     198.086 275.475 392.175  1.00 38.52           C  
ATOM     41  CA  VAL A  68     195.262 274.756 394.638  1.00 35.38           C  
ATOM     42  CA  ASP A  69     195.377 273.490 398.231  1.00 31.66           C  
ATOM     43  CA  LEU A  70     193.225 274.112 401.202  1.00 30.66           C  
ATOM     44  CA  GLU A  71     195.634 272.622 403.503  1.00 43.59           C  
ATOM     45  CA  PRO A  72     197.997 275.473 404.012  1.00 46.27           C  
ATOM     46  CA  THR A  73     201.007 273.708 405.528  1.00 48.55           C  
ATOM     47  CA  VAL A  74     201.985 272.227 402.122  1.00 58.12           C  
ATOM     48  CA  ILE A  75     201.945 275.313 399.868  1.00 63.45           C  
ATOM     49  CA  ASP A  76     203.618 276.861 402.872  1.00 69.97           C  
ATOM     50  CA  GLU A  77     206.539 274.529 402.100  1.00 70.62           C  
ATOM     51  CA  VAL A  78     206.934 276.528 398.923  1.00 70.09           C  
ATOM     52  CA  ARG A  79     206.592 279.614 401.094  1.00 74.67           C  
ATOM     53  CA  THR A  80     209.169 278.435 403.661  1.00 80.03           C  
ATOM     54  CA  GLY A  81     211.378 276.186 401.616  1.00 79.49           C  
ATOM     55  CA  THR A  82     211.889 276.886 398.098  1.00 76.49           C  
ATOM     56  CA  TYR A  83     210.697 279.600 397.523  1.00 71.97           C  
ATOM     57  CA  ARG A  84     208.929 282.844 398.476  1.00 84.74           C  
ATOM     58  CA  GLN A  85     210.490 285.250 396.305  1.00 84.53           C  
ATOM     59  CA  LEU A  86     209.882 284.882 392.670  1.00 77.11           C  
ATOM     60  CA  PHE A  87     206.211 284.768 391.767  1.00 75.47           C  
ATOM     61  CA  HIS A  88     202.960 286.015 393.062  1.00 78.06           C  
ATOM     62  CA  PRO A  89     200.149 284.083 394.534  1.00 83.61           C  
ATOM     63  CA  GLU A  90     198.133 284.386 391.386  1.00 78.49           C  
ATOM     64  CA  GLN A  91     198.787 280.941 390.051  1.00 69.51           C  
ATOM     65  CA  LEU A  92     199.222 279.787 393.545  1.00 68.73           C  
ATOM     66  CA  ILE A  93     195.920 279.495 395.425  1.00 68.32           C  
ATOM     67  CA  THR A  94     195.838 278.553 399.111  1.00 68.88           C  
ATOM     68  CA  GLY A  95     193.090 278.178 401.734  1.00 66.50           C  
ATOM     69  CA  LYS A  96     193.500 279.137 405.399  1.00 67.02           C  
ATOM     70  CA  GLU A  97     191.629 276.126 406.612  1.00 62.40           C  
ATOM     71  CA  ASP A  98     193.197 272.725 406.830  1.00 52.52           C  
ATOM     72  CA  ALA A  99     191.906 270.764 403.913  1.00 34.76           C  
ATOM     73  CA  ALA A 100     190.674 267.733 405.842  1.00 26.25           C  
ATOM     74  CA  ASN A 101     189.715 264.356 404.594  1.00 25.16           C  
ATOM     75  CA  ASN A 102     186.210 263.806 403.539  1.00 15.90           C  
ATOM     76  CA  TYR A 103     184.261 264.512 400.462  1.00  6.91           C  
ATOM     77  CA  ALA A 104     181.641 266.995 401.694  1.00  6.65           C  
ATOM     78  CA  ARG A 105     184.079 269.310 403.426  1.00 10.39           C  
ATOM     79  CA  GLY A 106     186.462 269.207 400.508  1.00 17.30           C  
ATOM     80  CA  HIS A 107     183.781 269.641 397.865  1.00 20.11           C  
ATOM     81  CA  TYR A 108     181.438 271.755 399.109  1.00 19.97           C  
ATOM     82  CA  THR A 109     182.423 273.592 402.437  1.00 14.79           C  
ATOM     83  CA  ILE A 110     185.855 275.146 402.047  1.00 22.39           C  
ATOM     84  CA  GLY A 111     186.978 274.465 398.486  1.00 31.58           C  
ATOM     85  CA  LYS A 112     183.822 276.289 397.380  1.00 37.27           C  
ATOM     86  CA  GLU A 113     184.898 279.741 398.530  1.00 41.42           C  
ATOM     87  CA  ILE A 114     187.912 279.699 396.203  1.00 32.89           C  
ATOM     88  CA  ILE A 115     186.421 278.145 393.059  1.00 24.51           C  
ATOM     89  CA  ASP A 116     184.913 281.384 391.708  1.00 26.78           C  
ATOM     90  CA  LEU A 117     188.282 283.077 391.922  1.00 23.76           C  
ATOM     91  CA  VAL A 118     189.897 279.929 390.528  1.00 24.82           C  
ATOM     92  CA  LEU A 119     187.555 279.863 387.550  1.00 27.75           C  
ATOM     93  CA  ASP A 120     188.097 283.563 386.971  1.00 39.11           C  
ATOM     94  CA  ARG A 121     191.686 282.815 385.979  1.00 44.01           C  
ATOM     95  CA  ILE A 122     190.767 279.909 383.716  1.00 48.00           C  
ATOM     96  CA  ARG A 123     188.340 282.369 382.115  1.00 54.11           C  
ATOM     97  CA  LYS A 124     190.793 285.275 382.205  1.00 44.21           C  
ATOM     98  CA  LEU A 125     193.628 283.077 380.895  1.00 49.40           C  
ATOM     99  CA  ALA A 126     191.203 281.329 378.533  1.00 56.85           C  
ATOM    100  CA  ASP A 127     190.235 284.624 376.933  1.00 68.82           C  
ATOM    101  CA  GLN A 128     193.656 286.176 376.383  1.00 79.45           C  
ATOM    102  CA  CYS A 129     194.883 283.374 374.112  1.00 86.84           C  
ATOM    103  CA  THR A 130     193.049 281.585 371.483  1.00 77.26           C  
ATOM    104  CA  GLY A 131     191.975 278.121 370.786  1.00 66.48           C  
ATOM    105  CA  LEU A 132     193.005 276.786 374.214  1.00 49.07           C  
ATOM    106  CA  GLN A 133     192.852 272.986 374.382  1.00 35.99           C  
ATOM    107  CA  GLY A 134     192.247 273.483 378.010  1.00 25.53           C  
ATOM    108  CA  PHE A 135     192.917 272.025 381.099  1.00 22.95           C  
ATOM    109  CA  SER A 136     195.225 269.220 382.155  1.00 11.40           C  
ATOM    110  CA  VAL A 137     194.022 268.736 385.755  1.00  6.65           C  
ATOM    111  CA  PHE A 138     196.326 267.115 388.353  1.00 13.94           C  
ATOM    112  CA  HIS A 139     194.703 265.572 391.434  1.00 22.19           C  
ATOM    113  CA  SER A 140     195.317 262.935 393.793  1.00 26.99           C  
ATOM    114  CA  PHE A 141     192.331 260.591 393.584  1.00 35.87           C  
ATOM    115  CA  GLY A 142     193.149 259.651 397.384  1.00 38.67           C  
ATOM    116  CA  GLY A 143     193.297 263.041 398.603  1.00 35.73           C  
ATOM    117  CA  GLY A 144     189.782 264.214 399.644  1.00 33.40           C  
ATOM    118  CA  THR A 145     190.408 267.846 398.920  1.00 20.53           C  
ATOM    119  CA  GLY A 146     192.048 267.083 395.535  1.00 15.71           C  
ATOM    120  CA  SER A 147     188.876 265.205 394.553  1.00 14.46           C  
ATOM    121  CA  GLY A 148     186.868 267.896 396.281  1.00 19.79           C  
ATOM    122  CA  PHE A 149     187.142 271.279 394.611  1.00 23.20           C  
ATOM    123  CA  THR A 150     187.086 270.065 391.012  1.00 22.10           C  
ATOM    124  CA  SER A 151     184.196 267.891 391.974  1.00 19.40           C  
ATOM    125  CA  LEU A 152     182.169 271.073 392.141  1.00 16.83           C  
ATOM    126  CA  LEU A 153     184.162 272.880 389.445  1.00 19.01           C  
ATOM    127  CA  MET A 154     183.335 270.265 386.836  1.00 24.75           C  
ATOM    128  CA  GLU A 155     180.010 270.253 388.619  1.00 28.50           C  
ATOM    129  CA  ARG A 156     179.349 273.932 387.965  1.00 30.73           C  
ATOM    130  CA  LEU A 157     180.600 273.459 384.351  1.00 30.23           C  
ATOM    131  CA  SER A 158     178.278 270.656 383.291  1.00 31.63           C  
ATOM    132  CA  VAL A 159     175.500 273.155 383.950  1.00 41.27           C  
ATOM    133  CA  ASP A 160     177.035 276.345 382.612  1.00 40.24           C  
ATOM    134  CA  TYR A 161     178.564 274.880 379.602  1.00 39.78           C  
ATOM    135  CA  GLY A 162     177.087 271.431 378.787  1.00 39.54           C  
ATOM    136  CA  LYS A 163     179.922 269.866 377.189  1.00 34.48           C  
ATOM    137  CA  LYS A 164     182.716 270.565 378.571  1.00 32.52           C  
ATOM    138  CA  SER A 165     185.532 268.237 378.411  1.00 22.09           C  
ATOM    139  CA  LYS A 166     188.916 268.017 380.010  1.00 18.88           C  
ATOM    140  CA  LEU A 167     191.707 265.474 380.655  1.00 13.86           C  
ATOM    141  CA  GLU A 168     192.293 264.898 384.328  1.00 15.54           C  
ATOM    142  CA  PHE A 169     195.496 263.185 385.301  1.00 18.38           C  
ATOM    143  CA  SER A 170     194.802 261.215 388.489  1.00 18.69           C  
ATOM    144  CA  ILE A 171     196.980 259.639 391.259  1.00 17.69           C  
ATOM    145  CA  TYR A 172     196.529 256.600 392.687  1.00 28.93           C  
ATOM    146  CA  PRO A 173     195.827 255.252 396.071  1.00 37.41           C  
ATOM    147  CA  ALA A 174     196.377 251.557 395.895  1.00 43.64           C  
ATOM    148  CA  PRO A 175     193.522 249.998 397.449  1.00 51.14           C  
ATOM    149  CA  GLN A 176     195.508 247.971 399.963  1.00 57.23           C  
ATOM    150  CA  VAL A 177     197.824 250.764 400.535  1.00 52.37           C  
ATOM    151  CA  SER A 178     195.469 253.573 400.947  1.00 51.22           C  
ATOM    152  CA  THR A 179     194.699 253.205 404.566  1.00 38.52           C  
ATOM    153  CA  ALA A 180     191.337 254.482 405.058  1.00 20.70           C  
ATOM    154  CA  VAL A 181     187.721 253.609 404.809  1.00  2.00           C  
ATOM    155  CA  VAL A 182     186.500 257.051 404.502  1.00  3.41           C  
ATOM    156  CA  GLU A 183     188.409 257.071 401.276  1.00 11.10           C  
ATOM    157  CA  PRO A 184     186.355 254.704 399.019  1.00  6.05           C  
ATOM    158  CA  TYR A 185     183.300 256.796 399.788  1.00  3.97           C  
ATOM    159  CA  ASN A 186     185.282 259.710 398.405  1.00  2.00           C  
ATOM    160  CA  SER A 187     186.596 257.792 395.392  1.00  6.16           C  
ATOM    161  CA  ILE A 188     183.544 255.942 394.246  1.00  8.44           C  
ATOM    162  CA  LEU A 189     182.013 259.406 394.270  1.00 10.17           C  
ATOM    163  CA  THR A 190     184.667 261.283 392.365  1.00  9.50           C  
ATOM    164  CA  THR A 191     184.654 258.587 389.715  1.00 18.93           C  
ATOM    165  CA  HIS A 192     180.907 258.568 389.025  1.00 23.95           C  
ATOM    166  CA  THR A 193     180.580 262.329 388.934  1.00 22.18           C  
ATOM    167  CA  THR A 194     183.668 262.914 386.806  1.00 30.97           C  
ATOM    168  CA  LEU A 195     183.340 259.853 384.465  1.00 33.77           C  
ATOM    169  CA  GLU A 196     180.743 261.558 382.283  1.00 39.79           C  
ATOM    170  CA  HIS A 197     181.992 265.026 382.634  1.00 34.63           C  
ATOM    171  CA  SER A 198     185.381 264.751 381.748  1.00 22.91           C  
ATOM    172  CA  ASP A 199     186.763 263.842 378.464  1.00 25.46           C  
ATOM    173  CA  CYS A 200     189.658 261.591 379.457  1.00 26.43           C  
ATOM    174  CA  ALA A 201     191.009 260.706 382.873  1.00 28.15           C  
ATOM    175  CA  PHE A 202     194.579 259.437 382.895  1.00 30.53           C  
ATOM    176  CA  MET A 203     195.495 257.151 385.736  1.00 30.61           C  
ATOM    177  CA  VAL A 204     198.930 256.118 387.036  1.00 20.65           C  
ATOM    178  CA  ASP A 205     199.488 253.383 389.666  1.00 29.43           C  
ATOM    179  CA  ASN A 206     201.648 254.102 392.638  1.00 22.56           C  
ATOM    180  CA  GLU A 207     202.104 250.391 393.498  1.00 20.12           C  
ATOM    181  CA  ALA A 208     202.543 249.040 389.979  1.00 11.03           C  
ATOM    182  CA  ILE A 209     205.409 251.549 389.745  1.00 10.08           C  
ATOM    183  CA  TYR A 210     207.111 250.004 392.755  1.00 22.92           C  
ATOM    184  CA  ASP A 211     207.249 246.721 390.932  1.00 23.58           C  
ATOM    185  CA  ILE A 212     209.178 248.527 388.257  1.00 23.63           C  
ATOM    186  CA  CYS A 213     211.524 249.748 391.004  1.00 28.44           C  
ATOM    187  CA  ARG A 214     211.926 246.238 392.331  1.00 40.94           C  
ATOM    188  CA  ARG A 215     211.879 244.238 389.079  1.00 38.84           C  
ATOM    189  CA  ASN A 216     213.332 246.516 386.479  1.00 31.32           C  
ATOM    190  CA  LEU A 217     215.381 248.941 388.222  1.00 40.55           C  
ATOM    191  CA  ASP A 218     215.842 246.809 391.205  1.00 57.49           C  
ATOM    192  CA  ILE A 219     216.367 249.343 393.892  1.00 59.12           C  
ATOM    193  CA  GLU A 220     214.912 249.443 397.287  1.00 67.12           C  
ATOM    194  CA  ARG A 221     215.244 253.167 397.316  1.00 69.11           C  
ATOM    195  CA  PRO A 222     212.721 255.178 395.342  1.00 53.30           C  
ATOM    196  CA  THR A 223     210.977 257.857 397.228  1.00 43.24           C  
ATOM    197  CA  TYR A 224     208.172 259.983 396.242  1.00 35.46           C  
ATOM    198  CA  THR A 225     210.426 262.271 394.257  1.00 40.10           C  
ATOM    199  CA  ASN A 226     210.958 259.297 391.958  1.00 30.22           C  
ATOM    200  CA  LEU A 227     207.475 258.057 391.231  1.00 16.19           C  
ATOM    201  CA  ASN A 228     206.987 261.675 390.337  1.00 22.59           C  
ATOM    202  CA  ARG A 229     209.918 261.581 387.888  1.00 16.14           C  
ATOM    203  CA  LEU A 230     208.235 258.619 386.341  1.00  6.87           C  
ATOM    204  CA  ILE A 231     204.732 259.926 385.848  1.00 10.37           C  
ATOM    205  CA  GLY A 232     206.747 263.055 385.214  1.00 21.17           C  
ATOM    206  CA  GLN A 233     207.883 261.041 382.202  1.00 25.16           C  
ATOM    207  CA  ILE A 234     204.757 259.257 381.004  1.00 17.99           C  
ATOM    208  CA  VAL A 235     203.039 262.636 381.219  1.00 12.48           C  
ATOM    209  CA  SER A 236     205.724 264.311 379.151  1.00 22.42           C  
ATOM    210  CA  SER A 237     204.784 261.847 376.449  1.00 23.30           C  
ATOM    211  CA  ILE A 238     201.167 262.913 376.619  1.00 23.29           C  
ATOM    212  CA  THR A 239     201.153 266.718 376.349  1.00 44.11           C  
ATOM    213  CA  ALA A 240     204.689 268.052 376.003  1.00 49.53           C  
ATOM    214  CA  SER A 241     205.955 266.092 372.984  1.00 59.69           C  
ATOM    215  CA  LEU A 242     202.580 265.359 371.437  1.00 65.02           C  
ATOM    216  CA  ARG A 243     201.579 268.999 371.498  1.00 68.97           C  
ATOM    217  CA  PHE A 244     204.744 269.885 369.750  1.00 81.08           C  
ATOM    218  CA  ASP A 245     204.647 268.713 366.181  1.00 74.39           C  
ATOM    219  CA  GLY A 246     205.924 265.335 364.978  1.00 59.02           C  
ATOM    220  CA  ALA A 247     205.606 263.458 361.736  1.00 50.29           C  
ATOM    221  CA  LEU A 248     202.281 262.212 362.820  1.00 38.92           C  
ATOM    222  CA  ASN A 249     201.438 265.606 364.149  1.00 32.91           C  
ATOM    223  CA  VAL A 250     198.952 263.727 366.233  1.00 30.37           C  
ATOM    224  CA  ASP A 251     196.352 266.044 367.769  1.00 25.27           C  
ATOM    225  CA  LEU A 252     194.764 265.660 371.215  1.00 17.06           C  
ATOM    226  CA  THR A 253     191.362 265.759 369.625  1.00 21.53           C  
ATOM    227  CA  GLU A 254     192.625 262.865 367.479  1.00 22.00           C  
ATOM    228  CA  PHE A 255     192.656 260.749 370.603  1.00 22.53           C  
ATOM    229  CA  GLN A 256     189.159 261.080 371.916  1.00 20.73           C  
ATOM    230  CA  THR A 257     188.014 260.718 368.290  1.00  9.52           C  
ATOM    231  CA  ASN A 258     190.034 257.633 367.411  1.00  6.03           C  
ATOM    232  CA  LEU A 259     189.852 256.468 371.054  1.00  6.83           C  
ATOM    233  CA  VAL A 260     186.346 256.834 372.237  1.00  9.49           C  
ATOM    234  CA  PRO A 261     183.318 256.574 370.237  1.00  7.37           C  
ATOM    235  CA  TYR A 262     182.022 258.547 373.059  1.00 16.29           C  
ATOM    236  CA  PRO A 263     180.997 261.156 375.111  1.00 16.05           C  
ATOM    237  CA  ARG A 264     182.516 259.155 378.079  1.00 22.39           C  
ATOM    238  CA  GLY A 265     185.076 258.512 379.770  1.00 23.25           C  
ATOM    239  CA  HIS A 266     185.681 254.858 378.859  1.00 11.08           C  
ATOM    240  CA  PHE A 267     188.845 253.781 380.500  1.00  8.40           C  
ATOM    241  CA  PRO A 268     192.339 253.959 379.155  1.00 17.01           C  
ATOM    242  CA  LEU A 269     195.146 252.250 380.858  1.00 12.30           C  
ATOM    243  CA  ALA A 270     198.629 253.772 380.645  1.00 11.58           C  
ATOM    244  CA  THR A 271     201.623 251.628 379.723  1.00 13.25           C  
ATOM    245  CA  TYR A 272     205.296 252.131 379.763  1.00 18.93           C  
ATOM    246  CA  ALA A 273     207.264 250.221 377.270  1.00 29.84           C  
ATOM    247  CA  PRO A 274     210.692 250.152 378.580  1.00 34.85           C  
ATOM    248  CA  VAL A 275     211.578 247.359 380.879  1.00 39.09           C  
ATOM    249  CA  ILE A 276     215.060 248.615 380.743  1.00 46.85           C  
ATOM    250  CA  SER A 277     216.821 250.795 383.173  1.00 55.16           C  
ATOM    251  CA  ALA A 278     220.145 252.162 382.081  1.00 66.26           C  
ATOM    252  CA  GLU A 279     222.323 249.948 384.192  1.00 78.70           C  
ATOM    253  CA  LYS A 280     219.920 247.515 385.207  1.00 82.76           C  
ATOM    254  CA  ALA A 281     218.174 246.196 382.333  1.00 79.12           C  
ATOM    255  CA  TYR A 282     220.041 244.806 379.431  1.00 80.90           C  
ATOM    256  CA  HIS A 283     218.727 244.743 375.920  1.00 75.09           C  
ATOM    257  CA  GLU A 284     220.298 247.326 376.170  1.00 59.49           C  
ATOM    258  CA  GLN A 285     219.096 248.977 372.943  1.00 39.32           C  
ATOM    259  CA  LEU A 286     215.514 248.318 372.434  1.00 34.04           C  
ATOM    260  CA  SER A 287     214.439 248.483 368.837  1.00 31.22           C  
ATOM    261  CA  VAL A 288     210.841 248.614 367.782  1.00 29.39           C  
ATOM    262  CA  ALA A 289     209.998 244.951 367.395  1.00 32.21           C  
ATOM    263  CA  GLU A 290     210.947 244.738 371.085  1.00 36.32           C  
ATOM    264  CA  ILE A 291     209.685 247.897 372.781  1.00 29.52           C  
ATOM    265  CA  THR A 292     206.196 247.258 371.382  1.00 17.98           C  
ATOM    266  CA  ASN A 293     205.969 243.771 372.711  1.00 34.10           C  
ATOM    267  CA  ALA A 294     207.070 245.211 376.051  1.00 30.79           C  
ATOM    268  CA  CYS A 295     203.869 247.179 376.261  1.00 13.70           C  
ATOM    269  CA  PHE A 296     201.410 244.322 376.379  1.00 21.47           C  
ATOM    270  CA  GLU A 297     203.575 242.202 378.717  1.00 31.40           C  
ATOM    271  CA  PRO A 298     202.214 242.243 382.176  1.00 27.43           C  
ATOM    272  CA  ALA A 299     205.048 243.971 383.953  1.00 26.57           C  
ATOM    273  CA  ASN A 300     205.013 247.193 381.926  1.00 27.39           C  
ATOM    274  CA  GLN A 301     201.260 247.798 381.905  1.00 35.05           C  
ATOM    275  CA  MET A 302     201.318 248.836 385.499  1.00 37.27           C  
ATOM    276  CA  VAL A 303     197.635 249.171 385.643  1.00 36.82           C  
ATOM    277  CA  LYS A 304     196.330 247.618 388.749  1.00 51.41           C  
ATOM    278  CA  CYS A 305     193.538 245.881 386.859  1.00 60.84           C  
ATOM    279  CA  ASP A 306     196.342 244.304 384.930  1.00 66.94           C  
ATOM    280  CA  PRO A 307     194.142 242.718 382.587  1.00 67.26           C  
ATOM    281  CA  ARG A 308     193.588 239.073 383.149  1.00 79.29           C  
ATOM    282  CA  HIS A 309     190.998 238.844 380.461  1.00 80.11           C  
ATOM    283  CA  GLY A 310     191.048 242.311 379.091  1.00 55.66           C  
ATOM    284  CA  LYS A 311     190.173 242.547 375.483  1.00 30.92           C  
ATOM    285  CA  TYR A 312     191.344 245.673 373.761  1.00 21.10           C  
ATOM    286  CA  MET A 313     189.012 247.908 371.769  1.00  9.30           C  
ATOM    287  CA  ALA A 314     191.382 250.717 370.870  1.00 10.29           C  
ATOM    288  CA  CYS A 315     195.015 251.479 371.595  1.00 12.21           C  
ATOM    289  CA  CYS A 316     196.913 254.705 371.013  1.00 15.81           C  
ATOM    290  CA  LEU A 317     200.498 253.712 370.527  1.00  8.50           C  
ATOM    291  CA  LEU A 318     202.411 256.884 371.208  1.00 15.06           C  
ATOM    292  CA  TYR A 319     206.022 256.429 370.172  1.00 21.99           C  
ATOM    293  CA  ARG A 320     208.806 258.920 370.661  1.00 31.61           C  
ATOM    294  CA  GLY A 321     212.426 258.978 369.562  1.00 40.46           C  
ATOM    295  CA  ASP A 322     213.884 257.457 366.423  1.00 51.76           C  
ATOM    296  CA  VAL A 323     211.533 255.151 364.807  1.00 45.09           C  
ATOM    297  CA  VAL A 324     211.430 254.511 361.068  1.00 43.42           C  
ATOM    298  CA  PRO A 325     207.849 254.078 360.251  1.00 48.35           C  
ATOM    299  CA  LYS A 326     207.886 250.694 358.512  1.00 35.28           C  
ATOM    300  CA  ASP A 327     209.733 249.215 361.458  1.00 25.97           C  
ATOM    301  CA  VAL A 328     206.724 250.315 363.468  1.00 23.06           C  
ATOM    302  CA  ASN A 329     204.089 249.658 360.827  1.00 29.42           C  
ATOM    303  CA  ALA A 330     205.344 246.077 361.089  1.00 22.83           C  
ATOM    304  CA  ALA A 331     206.447 245.628 364.676  1.00 23.95           C  
ATOM    305  CA  ILE A 332     202.872 246.576 365.489  1.00 18.32           C  
ATOM    306  CA  ALA A 333     201.505 244.372 362.711  1.00 16.38           C  
ATOM    307  CA  THR A 334     203.301 241.400 364.236  1.00 20.68           C  
ATOM    308  CA  ILE A 335     201.622 242.290 367.524  1.00 22.91           C  
ATOM    309  CA  LYS A 336     198.136 242.790 366.075  1.00 41.56           C  
ATOM    310  CA  THR A 337     198.327 239.240 364.537  1.00 64.14           C  
ATOM    311  CA  LYS A 338     199.772 237.356 367.484  1.00 77.19           C  
ATOM    312  CA  ARG A 339     195.750 238.105 368.969  1.00 89.49           C  
ATOM    313  CA  THR A 340     197.603 237.217 372.001  1.00 90.64           C  
ATOM    314  CA  ILE A 341     195.412 238.838 374.503  1.00 81.76           C  
ATOM    315  CA  GLN A 342     191.836 238.504 373.704  1.00 70.01           C  
ATOM    316  CA  PHE A 343     189.269 239.912 371.078  1.00 55.06           C  
ATOM    317  CA  VAL A 344     186.275 242.097 370.812  1.00 59.97           C  
ATOM    318  CA  ASP A 345     184.419 241.906 367.623  1.00 59.27           C  
ATOM    319  CA  TRP A 346     183.808 245.602 367.303  1.00 39.96           C  
ATOM    320  CA  CYS A 347     186.943 247.164 365.945  1.00 28.86           C  
ATOM    321  CA  PRO A 348     189.667 245.455 363.837  1.00 32.22           C  
ATOM    322  CA  THR A 349     191.200 248.831 363.472  1.00 30.77           C  
ATOM    323  CA  GLY A 350     192.109 251.871 365.476  1.00 18.15           C  
ATOM    324  CA  PHE A 351     195.586 251.135 366.565  1.00 14.27           C  
ATOM    325  CA  LYS A 352     196.267 254.863 366.637  1.00 12.21           C  
ATOM    326  CA  VAL A 353     199.962 255.177 365.820  1.00  2.00           C  
ATOM    327  CA  GLY A 354     201.349 258.373 367.319  1.00  8.12           C  
ATOM    328  CA  ILE A 355     204.931 259.166 366.361  1.00 23.70           C  
ATOM    329  CA  ASN A 356     206.854 262.079 367.875  1.00 42.13           C  
ATOM    330  CA  TYR A 357     210.391 262.506 367.081  1.00 64.11           C  
ATOM    331  CA  GLU A 358     211.556 264.426 369.759  1.00 58.76           C  
ATOM    332  CA  PRO A 359     213.347 262.616 372.262  1.00 58.21           C  
ATOM    333  CA  PRO A 360     212.052 262.271 375.638  1.00 62.52           C  
ATOM    334  CA  THR A 361     213.728 264.942 377.593  1.00 62.58           C  
ATOM    335  CA  VAL A 362     214.149 263.641 380.983  1.00 62.67           C  
ATOM    336  CA  VAL A 363     215.727 264.849 383.996  1.00 70.29           C  
ATOM    337  CA  PRO A 364     219.073 264.027 383.424  1.00 77.84           C  
ATOM    338  CA  GLY A 365     217.986 261.038 384.790  1.00 71.52           C  
ATOM    339  CA  GLY A 366     220.642 259.136 386.604  1.00 73.65           C  
ATOM    340  CA  ASP A 367     219.001 255.965 387.683  1.00 77.76           C  
ATOM    341  CA  LEU A 368     216.810 255.722 384.684  1.00 76.32           C  
ATOM    342  CA  ALA A 369     217.578 254.070 381.401  1.00 72.14           C  
ATOM    343  CA  LYS A 370     215.892 256.839 379.384  1.00 74.90           C  
ATOM    344  CA  VAL A 371     216.315 254.738 376.265  1.00 65.43           C  
ATOM    345  CA  GLN A 372     215.891 257.071 373.363  1.00 55.20           C  
ATOM    346  CA  ARG A 373     212.813 255.418 371.926  1.00 39.38           C  
ATOM    347  CA  ALA A 374     209.758 254.413 373.960  1.00 33.17           C  
ATOM    348  CA  VAL A 375     206.124 253.339 373.643  1.00 31.96           C  
ATOM    349  CA  CYS A 376     203.505 254.904 375.909  1.00 21.72           C  
ATOM    350  CA  MET A 377     200.541 252.885 374.778  1.00  7.45           C  
ATOM    351  CA  LEU A 378     197.236 253.494 376.440  1.00 12.52           C  
ATOM    352  CA  SER A 379     193.968 251.734 375.728  1.00 19.82           C  
ATOM    353  CA  ASN A 380     190.423 250.793 376.590  1.00 21.23           C  
ATOM    354  CA  THR A 381     190.309 247.130 377.540  1.00 19.77           C  
ATOM    355  CA  THR A 382     187.184 244.935 378.667  1.00  9.75           C  
ATOM    356  CA  ALA A 383     189.572 243.598 381.819  1.00  4.98           C  
ATOM    357  CA  ILE A 384     188.415 247.075 384.151  1.00  8.75           C  
ATOM    358  CA  ALA A 385     185.047 245.185 384.050  1.00 26.84           C  
ATOM    359  CA  GLU A 386     186.886 243.429 386.837  1.00 36.29           C  
ATOM    360  CA  ALA A 387     188.884 246.145 388.617  1.00 30.31           C  
ATOM    361  CA  TRP A 388     185.747 248.315 388.823  1.00 23.21           C  
ATOM    362  CA  ALA A 389     183.670 245.379 389.989  1.00 19.05           C  
ATOM    363  CA  ARG A 390     186.095 244.403 392.759  1.00 30.76           C  
ATOM    364  CA  LEU A 391     186.240 248.036 393.843  1.00 21.31           C  
ATOM    365  CA  ASP A 392     182.525 248.572 393.761  1.00 26.95           C  
ATOM    366  CA  HIS A 393     181.798 245.490 395.839  1.00 29.62           C  
ATOM    367  CA  LYS A 394     184.217 246.858 398.462  1.00 18.81           C  
ATOM    368  CA  PHE A 395     182.118 249.997 398.748  1.00 13.87           C  
ATOM    369  CA  ASP A 396     178.844 248.169 399.339  1.00 22.36           C  
ATOM    370  CA  LEU A 397     180.184 246.076 402.153  1.00 18.90           C  
ATOM    371  CA  MET A 398     180.890 249.251 404.109  1.00 15.44           C  
ATOM    372  CA  TYR A 399     177.998 251.342 402.900  1.00 26.50           C  
ATOM    373  CA  ALA A 400     175.751 248.368 403.758  1.00 24.37           C  
ATOM    374  CA  LYS A 401     177.646 248.039 407.034  1.00 28.08           C  
ATOM    375  CA  ARG A 402     176.475 251.339 408.370  1.00 21.94           C  
ATOM    376  CA  ALA A 403     176.400 253.909 409.481  1.00  8.20           C  
ATOM    377  CA  PHE A 404     179.609 254.960 407.942  1.00 16.11           C  
ATOM    378  CA  VAL A 405     177.312 256.786 405.823  1.00 14.70           C  
ATOM    379  CA  HIS A 406     176.322 259.286 408.608  1.00 13.33           C  
ATOM    380  CA  TRP A 407     179.273 261.545 407.959  1.00 12.68           C  
ATOM    381  CA  TYR A 408     178.026 262.613 404.588  1.00 24.39           C  
ATOM    382  CA  VAL A 409     174.290 262.549 405.082  1.00 29.93           C  
ATOM    383  CA  GLY A 410     174.583 265.032 407.928  1.00 34.36           C  
ATOM    384  CA  GLU A 411     177.039 267.027 406.001  1.00 28.17           C  
ATOM    385  CA  GLY A 412     174.542 267.687 403.430  1.00 30.26           C  
ATOM    386  CA  MET A 413     175.736 265.263 400.907  1.00 34.63           C  
ATOM    387  CA  GLU A 414     173.016 262.860 400.494  1.00 39.73           C  
ATOM    388  CA  GLU A 415     171.933 259.292 400.428  1.00 54.92           C  
ATOM    389  CA  GLY A 416     171.366 260.285 396.843  1.00 35.87           C  
ATOM    390  CA  GLU A 417     174.872 260.755 395.523  1.00 29.35           C  
ATOM    391  CA  PHE A 418     175.950 257.431 397.002  1.00 35.92           C  
ATOM    392  CA  SER A 419     173.010 255.209 396.091  1.00 40.42           C  
ATOM    393  CA  GLU A 420     172.676 257.030 392.806  1.00 34.69           C  
ATOM    394  CA  ALA A 421     176.373 256.615 391.929  1.00 28.13           C  
ATOM    395  CA  ARG A 422     176.205 252.985 392.849  1.00 25.50           C  
ATOM    396  CA  GLU A 423     173.380 252.425 390.374  1.00 31.02           C  
ATOM    397  CA  ASP A 424     175.690 254.356 388.046  1.00 30.57           C  
ATOM    398  CA  MET A 425     178.545 251.899 388.074  1.00 26.91           C  
ATOM    399  CA  ALA A 426     176.030 249.054 388.118  1.00 35.84           C  
ATOM    400  CA  ALA A 427     175.426 249.854 384.428  1.00 38.28           C  
ATOM    401  CA  LEU A 428     179.194 249.871 384.009  1.00 39.30           C  
ATOM    402  CA  GLU A 429     179.293 246.252 385.127  1.00 50.75           C  
ATOM    403  CA  LYS A 430     176.601 245.587 382.491  1.00 48.67           C  
ATOM    404  CA  ASP A 431     178.613 247.805 380.208  1.00 47.21           C  
ATOM    405  CA  TYR A 432     182.053 246.352 380.913  1.00 37.28           C  
ATOM    406  CA  GLU A 433     180.311 242.987 380.629  1.00 53.57           C  
ATOM    407  CA  GLU A 434     178.503 243.480 377.335  1.00 61.61           C  
ATOM    408  CA  VAL A 435     181.275 245.249 375.444  1.00 65.03           C  
ATOM    409  CA  GLY A 436     183.073 241.989 375.701  1.00 73.86           C  
ATOM    410  CA  VAL A 437     182.414 239.806 374.781  1.00 88.51           C  
ATOM    411  CA  ASP A 438     180.721 241.913 372.152  1.00 92.71           C  
ATOM    412  CA  SER A 439     177.383 240.887 370.629  1.00 87.57           C  
TER     413      SER A 439                                                      
ATOM    414  CA  ARG B   2     196.446 278.017 413.439  1.00 57.69           C  
ATOM    415  CA  GLU B   3     196.749 277.573 417.049  1.00 51.20           C  
ATOM    416  CA  ILE B   4     197.260 274.699 419.474  1.00 35.02           C  
ATOM    417  CA  VAL B   5     196.262 275.209 423.002  1.00 21.82           C  
ATOM    418  CA  HIS B   6     197.069 273.254 426.158  1.00 20.02           C  
ATOM    419  CA  ILE B   7     195.340 272.869 429.520  1.00 26.45           C  
ATOM    420  CA  GLN B   8     197.180 271.695 432.700  1.00 29.82           C  
ATOM    421  CA  ALA B   9     194.281 270.677 434.966  1.00 28.61           C  
ATOM    422  CA  GLY B  10     195.021 269.328 438.432  1.00 25.81           C  
ATOM    423  CA  GLN B  11     198.463 268.565 440.054  1.00 23.23           C  
ATOM    424  CA  CYS B  12     199.417 265.698 437.836  1.00 16.01           C  
ATOM    425  CA  GLY B  13     198.260 267.289 434.634  1.00 26.51           C  
ATOM    426  CA  ASN B  14     200.331 270.144 435.948  1.00 26.78           C  
ATOM    427  CA  GLN B  15     203.450 268.219 437.016  1.00 25.31           C  
ATOM    428  CA  ILE B  16     203.386 266.794 433.491  1.00 25.94           C  
ATOM    429  CA  GLY B  17     202.959 270.265 432.056  1.00 26.06           C  
ATOM    430  CA  ALA B  18     206.422 270.972 433.366  1.00 29.60           C  
ATOM    431  CA  LYS B  19     207.696 267.904 431.543  1.00 37.53           C  
ATOM    432  CA  PHE B  20     205.690 268.423 428.378  1.00 26.95           C  
ATOM    433  CA  TRP B  21     207.036 271.929 428.195  1.00 23.63           C  
ATOM    434  CA  GLU B  22     210.457 270.936 429.440  1.00 32.17           C  
ATOM    435  CA  VAL B  23     210.682 268.810 426.309  1.00 32.98           C  
ATOM    436  CA  ILE B  24     208.738 270.616 423.616  1.00 34.33           C  
ATOM    437  CA  SER B  25     210.753 273.776 424.277  1.00 47.08           C  
ATOM    438  CA  ASP B  26     214.100 272.061 423.597  1.00 58.11           C  
ATOM    439  CA  GLU B  27     212.396 270.409 420.677  1.00 61.30           C  
ATOM    440  CA  HIS B  28     212.004 273.883 419.379  1.00 62.52           C  
ATOM    441  CA  GLY B  29     215.573 274.468 420.740  1.00 75.22           C  
ATOM    442  CA  ILE B  30     214.583 277.819 421.916  1.00 81.60           C  
ATOM    443  CA  ASP B  31     214.756 277.867 425.619  1.00 89.43           C  
ATOM    444  CA  PRO B  32     213.491 281.147 426.747  1.00 90.13           C  
ATOM    445  CA  THR B  33     216.415 281.476 429.142  1.00 92.84           C  
ATOM    446  CA  GLY B  34     218.710 280.951 426.506  1.00 92.58           C  
ATOM    447  CA  SER B  35     222.018 280.361 425.061  1.00 96.36           C  
ATOM    448  CA  TYR B  36     222.128 278.746 422.312  1.00 99.20           C  
ATOM    449  CA  HIS B  37     222.809 275.021 421.912  1.00100.00           C  
ATOM    450  CA  GLY B  38     220.990 276.241 419.414  1.00 99.24           C  
ATOM    451  CA  ASP B  39     221.651 275.478 415.890  1.00 96.42           C  
ATOM    452  CA  SER B  40     218.843 274.206 414.047  1.00 92.02           C  
ATOM    453  CA  ASP B  41     217.912 276.059 410.964  1.00 85.29           C  
ATOM    454  CA  LEU B  42     214.819 275.135 410.259  1.00 82.58           C  
ATOM    455  CA  GLN B  43     213.030 275.526 413.398  1.00 78.10           C  
ATOM    456  CA  LEU B  44     214.800 278.778 413.400  1.00 74.03           C  
ATOM    457  CA  GLU B  45     212.821 279.971 410.537  1.00 73.64           C  
ATOM    458  CA  ARG B  46     209.658 279.110 412.160  1.00 71.38           C  
ATOM    459  CA  ILE B  47     209.627 280.907 414.941  1.00 67.67           C  
ATOM    460  CA  ASN B  48     209.703 283.906 413.181  1.00 63.33           C  
ATOM    461  CA  VAL B  49     206.604 283.588 411.008  1.00 57.47           C  
ATOM    462  CA  TYR B  50     203.871 283.604 413.226  1.00 58.87           C  
ATOM    463  CA  TYR B  51     203.756 286.268 414.807  1.00 66.14           C  
ATOM    464  CA  ASN B  52     202.909 288.791 417.459  1.00 80.80           C  
ATOM    465  CA  GLU B  53     205.019 289.210 420.519  1.00 96.22           C  
ATOM    466  CA  ALA B  54     204.677 292.406 422.387  1.00100.00           C  
ATOM    467  CA  ALA B  55     207.646 292.753 424.575  1.00100.00           C  
ATOM    468  CA  GLY B  56     209.825 290.515 422.586  1.00100.00           C  
ATOM    469  CA  ASN B  57     211.364 289.238 425.731  1.00 97.91           C  
ATOM    470  CA  LYS B  58     207.971 288.598 427.207  1.00 92.73           C  
ATOM    471  CA  TYR B  59     204.728 287.581 425.772  1.00 78.35           C  
ATOM    472  CA  VAL B  60     201.554 285.849 426.898  1.00 62.05           C  
ATOM    473  CA  PRO B  61     201.719 282.231 427.442  1.00 43.28           C  
ATOM    474  CA  ARG B  62     200.115 279.614 425.757  1.00 32.71           C  
ATOM    475  CA  ALA B  63     198.693 276.786 427.868  1.00 25.69           C  
ATOM    476  CA  ILE B  64     196.432 277.046 431.035  1.00 24.20           C  
ATOM    477  CA  LEU B  65     197.526 276.025 434.530  1.00 28.09           C  
ATOM    478  CA  VAL B  66     194.483 275.201 436.622  1.00 30.81           C  
ATOM    479  CA  ASP B  67     194.902 274.005 440.218  1.00 35.04           C  
ATOM    480  CA  LEU B  68     193.109 274.569 443.569  1.00 45.71           C  
ATOM    481  CA  GLU B  69     195.902 273.646 445.903  1.00 58.53           C  
ATOM    482  CA  PRO B  70     198.774 275.990 446.348  1.00 66.30           C  
ATOM    483  CA  GLY B  71     201.603 273.547 447.187  1.00 75.05           C  
ATOM    484  CA  THR B  72     201.729 272.510 443.523  1.00 81.80           C  
ATOM    485  CA  MET B  73     202.313 275.810 441.737  1.00 81.14           C  
ATOM    486  CA  ASP B  74     204.403 276.608 444.823  1.00 82.65           C  
ATOM    487  CA  SER B  75     206.697 273.720 443.865  1.00 78.89           C  
ATOM    488  CA  VAL B  76     206.830 274.705 440.222  1.00 77.54           C  
ATOM    489  CA  ARG B  77     207.406 278.360 441.112  1.00 78.78           C  
ATOM    490  CA  SER B  78     210.337 277.285 443.109  1.00 86.27           C  
ATOM    491  CA  GLY B  79     211.530 275.317 440.221  1.00 94.03           C  
ATOM    492  CA  PRO B  80     213.480 276.374 437.354  1.00 94.10           C  
ATOM    493  CA  PHE B  81     210.151 276.456 435.701  1.00 86.73           C  
ATOM    494  CA  GLY B  82     208.759 279.121 437.824  1.00 88.24           C  
ATOM    495  CA  GLN B  83     210.820 282.223 437.953  1.00 95.55           C  
ATOM    496  CA  ILE B  84     210.503 282.696 434.274  1.00 87.65           C  
ATOM    497  CA  PHE B  85     206.761 282.110 434.140  1.00 78.40           C  
ATOM    498  CA  ARG B  86     204.214 284.793 434.493  1.00 85.18           C  
ATOM    499  CA  PRO B  87     202.119 284.605 437.313  1.00 88.19           C  
ATOM    500  CA  ASP B  88     199.222 285.288 435.032  1.00 82.18           C  
ATOM    501  CA  ASN B  89     198.738 281.886 434.278  1.00 76.34           C  
ATOM    502  CA  PHE B  90     198.370 280.579 437.454  1.00 70.61           C  
ATOM    503  CA  VAL B  91     194.666 280.533 438.287  1.00 72.18           C  
ATOM    504  CA  PHE B  92     194.867 279.204 441.830  1.00 80.56           C  
ATOM    505  CA  GLY B  93     192.162 278.791 444.430  1.00 75.50           C  
ATOM    506  CA  GLN B  94     192.418 279.430 448.126  1.00 73.82           C  
ATOM    507  CA  SER B  95     191.204 275.988 448.710  1.00 69.76           C  
ATOM    508  CA  GLY B  96     192.072 273.520 449.565  1.00 66.97           C  
ATOM    509  CA  ALA B  97     190.265 271.104 447.235  1.00 57.56           C  
ATOM    510  CA  GLY B  98     191.745 268.108 448.884  1.00 39.29           C  
ATOM    511  CA  ASN B  99     190.523 265.011 447.164  1.00 26.36           C  
ATOM    512  CA  ASN B 100     186.874 265.174 445.951  1.00 22.28           C  
ATOM    513  CA  TRP B 101     185.654 264.924 442.450  1.00 16.37           C  
ATOM    514  CA  ALA B 102     182.820 266.957 443.719  1.00  5.22           C  
ATOM    515  CA  LYS B 103     184.715 269.651 445.540  1.00  4.60           C  
ATOM    516  CA  GLY B 104     186.305 270.678 442.265  1.00 12.37           C  
ATOM    517  CA  HIS B 105     183.297 270.287 440.004  1.00 13.18           C  
ATOM    518  CA  TYR B 106     180.326 271.646 441.968  1.00 18.05           C  
ATOM    519  CA  THR B 107     181.436 273.608 444.959  1.00 18.45           C  
ATOM    520  CA  GLU B 108     184.954 274.870 444.813  1.00 31.29           C  
ATOM    521  CA  GLY B 109     185.824 274.565 441.139  1.00 29.91           C  
ATOM    522  CA  ALA B 110     182.503 275.874 439.891  1.00 32.78           C  
ATOM    523  CA  GLU B 111     183.535 279.292 441.141  1.00 38.49           C  
ATOM    524  CA  LEU B 112     186.996 279.395 439.604  1.00 39.83           C  
ATOM    525  CA  VAL B 113     185.484 278.255 436.298  1.00 42.29           C  
ATOM    526  CA  ASP B 114     184.228 281.599 434.982  1.00 44.37           C  
ATOM    527  CA  SER B 115     187.666 283.103 435.666  1.00 40.63           C  
ATOM    528  CA  VAL B 116     189.023 280.285 433.505  1.00 33.60           C  
ATOM    529  CA  LEU B 117     186.589 280.285 430.590  1.00 36.30           C  
ATOM    530  CA  ASP B 118     187.435 283.975 430.501  1.00 42.58           C  
ATOM    531  CA  VAL B 119     190.986 283.161 429.518  1.00 44.32           C  
ATOM    532  CA  VAL B 120     190.179 280.050 427.451  1.00 56.75           C  
ATOM    533  CA  ARG B 121     188.371 282.656 425.302  1.00 68.40           C  
ATOM    534  CA  LYS B 122     191.175 285.186 425.393  1.00 66.99           C  
ATOM    535  CA  GLU B 123     193.391 282.424 423.988  1.00 66.66           C  
ATOM    536  CA  SER B 124     190.861 281.006 421.543  1.00 63.06           C  
ATOM    537  CA  GLU B 125     189.845 284.168 419.841  1.00 70.76           C  
ATOM    538  CA  SER B 126     193.111 285.790 419.808  1.00 73.77           C  
ATOM    539  CA  CYS B 127     194.483 284.778 416.575  1.00 76.00           C  
ATOM    540  CA  ASP B 128     193.831 282.887 413.371  1.00 68.67           C  
ATOM    541  CA  CYS B 129     192.151 279.558 413.205  1.00 61.48           C  
ATOM    542  CA  LEU B 130     191.927 277.741 416.453  1.00 38.17           C  
ATOM    543  CA  GLN B 131     191.955 273.967 416.000  1.00 26.44           C  
ATOM    544  CA  GLY B 132     191.352 272.610 419.517  1.00 14.57           C  
ATOM    545  CA  PHE B 133     192.663 272.341 423.086  1.00 11.67           C  
ATOM    546  CA  GLN B 134     194.982 269.821 424.740  1.00 18.92           C  
ATOM    547  CA  LEU B 135     193.930 268.656 428.195  1.00 22.98           C  
ATOM    548  CA  THR B 136     196.143 266.919 430.741  1.00 14.93           C  
ATOM    549  CA  HIS B 137     195.001 265.628 434.112  1.00  8.47           C  
ATOM    550  CA  SER B 138     194.352 262.595 436.271  1.00 11.41           C  
ATOM    551  CA  LEU B 139     191.036 261.040 436.892  1.00  6.65           C  
ATOM    552  CA  GLY B 140     192.574 260.234 440.205  1.00  6.55           C  
ATOM    553  CA  GLY B 141     191.945 263.558 441.769  1.00  9.94           C  
ATOM    554  CA  GLY B 142     190.249 266.841 442.218  1.00 14.56           C  
ATOM    555  CA  THR B 143     191.501 269.667 440.025  1.00 17.53           C  
ATOM    556  CA  GLY B 144     192.053 267.080 437.343  1.00 16.67           C  
ATOM    557  CA  SER B 145     189.077 264.812 436.875  1.00 22.04           C  
ATOM    558  CA  GLY B 146     186.446 266.965 438.525  1.00 29.36           C  
ATOM    559  CA  MET B 147     187.239 270.572 437.690  1.00 33.89           C  
ATOM    560  CA  GLY B 148     188.805 269.785 434.321  1.00 29.61           C  
ATOM    561  CA  THR B 149     185.953 267.501 433.424  1.00 20.03           C  
ATOM    562  CA  LEU B 150     183.701 270.444 434.122  1.00 23.56           C  
ATOM    563  CA  LEU B 151     185.749 272.858 432.079  1.00 21.87           C  
ATOM    564  CA  ILE B 152     184.930 270.737 429.085  1.00 28.64           C  
ATOM    565  CA  SER B 153     181.254 270.116 429.804  1.00 27.48           C  
ATOM    566  CA  LYS B 154     181.056 273.918 429.591  1.00 24.69           C  
ATOM    567  CA  ILE B 155     183.367 274.257 426.606  1.00 25.92           C  
ATOM    568  CA  ARG B 156     181.221 271.698 424.681  1.00 28.06           C  
ATOM    569  CA  GLU B 157     178.134 273.824 425.280  1.00 32.76           C  
ATOM    570  CA  GLU B 158     179.846 276.953 424.092  1.00 44.52           C  
ATOM    571  CA  TYR B 159     181.596 275.372 421.179  1.00 42.02           C  
ATOM    572  CA  PRO B 160     180.752 272.838 418.626  1.00 41.21           C  
ATOM    573  CA  ASP B 161     183.528 274.007 416.788  1.00 34.05           C  
ATOM    574  CA  ARG B 162     186.841 273.093 418.065  1.00 30.51           C  
ATOM    575  CA  ILE B 163     188.391 269.841 418.846  1.00 27.51           C  
ATOM    576  CA  MET B 164     189.213 268.499 422.310  1.00 28.59           C  
ATOM    577  CA  ASN B 165     191.991 266.007 422.877  1.00 16.68           C  
ATOM    578  CA  THR B 166     192.102 264.694 426.383  1.00  9.00           C  
ATOM    579  CA  PHE B 167     195.115 263.089 428.012  1.00  9.96           C  
ATOM    580  CA  SER B 168     193.799 261.215 431.044  1.00 21.96           C  
ATOM    581  CA  VAL B 169     195.391 258.862 433.714  1.00 12.49           C  
ATOM    582  CA  VAL B 170     193.445 256.125 434.263  1.00 18.70           C  
ATOM    583  CA  PRO B 171     193.751 255.824 438.047  1.00 26.85           C  
ATOM    584  CA  SER B 172     195.682 252.692 438.567  1.00 33.91           C  
ATOM    585  CA  PRO B 173     194.038 249.622 438.309  1.00 38.63           C  
ATOM    586  CA  LYS B 174     196.666 247.988 440.363  1.00 49.10           C  
ATOM    587  CA  VAL B 175     194.982 248.788 443.652  1.00 44.20           C  
ATOM    588  CA  SER B 176     192.811 251.516 444.927  1.00 35.51           C  
ATOM    589  CA  ASP B 177     194.826 254.315 446.407  1.00 27.24           C  
ATOM    590  CA  THR B 178     191.710 255.501 448.127  1.00 22.55           C  
ATOM    591  CA  VAL B 179     188.184 254.526 448.793  1.00  4.27           C  
ATOM    592  CA  VAL B 180     187.526 257.857 447.187  1.00  2.00           C  
ATOM    593  CA  GLU B 181     189.503 256.975 443.431  1.00  6.26           C  
ATOM    594  CA  PRO B 182     186.776 254.945 441.791  1.00  5.92           C  
ATOM    595  CA  TYR B 183     184.002 257.227 443.007  1.00  3.28           C  
ATOM    596  CA  ASN B 184     185.648 260.460 441.923  1.00  2.15           C  
ATOM    597  CA  ALA B 185     186.783 258.587 438.791  1.00 11.48           C  
ATOM    598  CA  THR B 186     183.825 256.674 437.463  1.00 11.42           C  
ATOM    599  CA  LEU B 187     181.945 259.933 437.917  1.00 21.39           C  
ATOM    600  CA  SER B 188     184.357 262.007 435.873  1.00 25.22           C  
ATOM    601  CA  VAL B 189     184.974 259.520 433.026  1.00 36.12           C  
ATOM    602  CA  HIS B 190     181.202 259.588 432.633  1.00 29.68           C  
ATOM    603  CA  GLN B 191     181.350 263.389 431.956  1.00 28.32           C  
ATOM    604  CA  LEU B 192     184.334 262.853 429.649  1.00 26.76           C  
ATOM    605  CA  VAL B 193     182.407 260.392 427.349  1.00 24.52           C  
ATOM    606  CA  GLU B 194     179.884 262.474 426.499  1.00 26.77           C  
ATOM    607  CA  ASN B 195     182.000 264.910 425.928  1.00 20.71           C  
ATOM    608  CA  THR B 196     185.489 265.353 424.199  1.00 23.25           C  
ATOM    609  CA  ASP B 197     186.024 263.278 421.267  1.00 13.99           C  
ATOM    610  CA  GLU B 198     189.749 262.368 421.481  1.00 15.97           C  
ATOM    611  CA  THR B 199     191.108 260.939 424.734  1.00  7.39           C  
ATOM    612  CA  TYR B 200     194.510 259.379 425.272  1.00 21.59           C  
ATOM    613  CA  CYS B 201     194.881 257.374 428.343  1.00 27.96           C  
ATOM    614  CA  ILE B 202     197.973 256.339 430.308  1.00 26.43           C  
ATOM    615  CA  ASP B 203     198.139 254.142 433.519  1.00 27.21           C  
ATOM    616  CA  ASN B 204     200.959 254.840 436.062  1.00 14.83           C  
ATOM    617  CA  GLU B 205     201.733 251.164 436.572  1.00 17.09           C  
ATOM    618  CA  ALA B 206     201.658 250.392 432.868  1.00 10.42           C  
ATOM    619  CA  LEU B 207     204.420 253.002 432.840  1.00  3.99           C  
ATOM    620  CA  TYR B 208     206.408 251.636 435.732  1.00  8.93           C  
ATOM    621  CA  ASP B 209     206.484 248.291 433.974  1.00 20.39           C  
ATOM    622  CA  ILE B 210     207.301 249.813 430.607  1.00 32.33           C  
ATOM    623  CA  CYS B 211     209.767 252.003 432.500  1.00 47.56           C  
ATOM    624  CA  PHE B 212     211.427 249.405 434.723  1.00 52.60           C  
ATOM    625  CA  ARG B 213     211.556 246.546 432.268  1.00 49.08           C  
ATOM    626  CA  THR B 214     213.015 248.694 429.616  1.00 38.75           C  
ATOM    627  CA  LEU B 215     215.297 250.659 431.796  1.00 36.97           C  
ATOM    628  CA  LYS B 216     218.131 249.439 433.950  1.00 44.63           C  
ATOM    629  CA  LEU B 217     216.682 251.285 436.871  1.00 44.21           C  
ATOM    630  CA  THR B 218     214.151 249.498 438.885  1.00 48.44           C  
ATOM    631  CA  THR B 219     211.884 252.182 439.867  1.00 49.51           C  
ATOM    632  CA  PRO B 220     211.046 254.911 437.835  1.00 38.42           C  
ATOM    633  CA  THR B 221     211.147 258.441 439.163  1.00 42.25           C  
ATOM    634  CA  TYR B 222     208.097 260.442 438.390  1.00 36.77           C  
ATOM    635  CA  GLY B 223     210.055 262.768 436.142  1.00 39.14           C  
ATOM    636  CA  ASP B 224     210.702 259.667 434.094  1.00 32.15           C  
ATOM    637  CA  LEU B 225     207.166 258.334 433.798  1.00 27.08           C  
ATOM    638  CA  ASN B 226     206.146 261.849 432.859  1.00 24.75           C  
ATOM    639  CA  HIS B 227     209.016 261.987 430.416  1.00 22.57           C  
ATOM    640  CA  LEU B 228     207.938 258.745 428.739  1.00 15.08           C  
ATOM    641  CA  VAL B 229     204.347 259.940 428.448  1.00 15.65           C  
ATOM    642  CA  SER B 230     205.349 263.344 427.076  1.00 16.58           C  
ATOM    643  CA  ALA B 231     207.301 261.334 424.506  1.00 21.00           C  
ATOM    644  CA  THR B 232     204.068 259.897 423.113  1.00 15.77           C  
ATOM    645  CA  MET B 233     202.032 263.119 423.087  1.00 23.03           C  
ATOM    646  CA  SER B 234     204.873 264.616 421.005  1.00 28.79           C  
ATOM    647  CA  GLY B 235     204.665 261.823 418.441  1.00 27.46           C  
ATOM    648  CA  VAL B 236     200.919 262.394 418.217  1.00 29.06           C  
ATOM    649  CA  THR B 237     200.398 266.120 417.736  1.00 40.62           C  
ATOM    650  CA  THR B 238     203.527 268.180 417.045  1.00 50.30           C  
ATOM    651  CA  CYS B 239     204.871 265.311 414.983  1.00 57.67           C  
ATOM    652  CA  LEU B 240     202.088 265.203 412.423  1.00 51.01           C  
ATOM    653  CA  ARG B 241     202.275 268.915 411.971  1.00 52.58           C  
ATOM    654  CA  PHE B 242     205.529 269.416 409.423  1.00 49.65           C  
ATOM    655  CA  PRO B 243     205.723 267.462 406.314  1.00 39.30           C  
ATOM    656  CA  GLY B 244     205.706 264.925 406.022  1.00 31.10           C  
ATOM    657  CA  GLN B 245     205.085 262.637 403.336  1.00 29.54           C  
ATOM    658  CA  LEU B 246     201.648 263.958 403.905  1.00 30.33           C  
ATOM    659  CA  ASN B 247     200.498 266.230 406.584  1.00 37.05           C  
ATOM    660  CA  ALA B 248     197.538 265.815 408.724  1.00 44.64           C  
ATOM    661  CA  ASP B 249     196.617 267.593 411.725  1.00 44.09           C  
ATOM    662  CA  LEU B 250     194.359 267.226 414.701  1.00 34.06           C  
ATOM    663  CA  ARG B 251     191.043 267.047 412.928  1.00 22.35           C  
ATOM    664  CA  LYS B 252     192.186 264.978 409.923  1.00 17.08           C  
ATOM    665  CA  LEU B 253     193.751 262.798 412.606  1.00 19.48           C  
ATOM    666  CA  ALA B 254     190.476 262.884 414.458  1.00 13.32           C  
ATOM    667  CA  VAL B 255     188.186 262.682 411.444  1.00  3.90           C  
ATOM    668  CA  ASN B 256     190.092 259.670 410.095  1.00  6.97           C  
ATOM    669  CA  MET B 257     190.621 257.861 413.328  1.00 20.47           C  
ATOM    670  CA  VAL B 258     187.224 257.990 414.878  1.00 14.83           C  
ATOM    671  CA  PRO B 259     184.430 258.143 412.582  1.00 18.97           C  
ATOM    672  CA  PHE B 260     182.587 258.261 415.747  1.00 21.66           C  
ATOM    673  CA  PRO B 261     184.121 260.565 416.971  1.00 28.77           C  
ATOM    674  CA  ARG B 262     182.963 261.095 420.331  1.00 33.46           C  
ATOM    675  CA  LEU B 263     184.305 258.286 422.280  1.00 20.85           C  
ATOM    676  CA  HIS B 264     186.434 255.632 422.301  1.00 17.05           C  
ATOM    677  CA  PHE B 265     189.762 255.452 424.318  1.00 15.04           C  
ATOM    678  CA  PHE B 266     193.020 254.525 422.706  1.00 14.55           C  
ATOM    679  CA  MET B 267     196.151 252.854 423.944  1.00  5.61           C  
ATOM    680  CA  PRO B 268     199.407 254.595 423.036  1.00  4.00           C  
ATOM    681  CA  GLY B 269     202.694 252.784 422.401  1.00 13.86           C  
ATOM    682  CA  PHE B 270     206.214 253.911 421.635  1.00 21.24           C  
ATOM    683  CA  ALA B 271     207.694 251.859 418.657  1.00 22.98           C  
ATOM    684  CA  PRO B 272     211.476 252.597 420.510  1.00 26.07           C  
ATOM    685  CA  LEU B 273     212.211 251.376 423.297  1.00 31.25           C  
ATOM    686  CA  THR B 274     215.588 250.165 424.963  1.00 46.02           C  
ATOM    687  CA  SER B 275     217.629 250.678 427.927  1.00 66.56           C  
ATOM    688  CA  ARG B 276     220.472 252.650 426.630  1.00 87.05           C  
ATOM    689  CA  GLY B 277     223.470 250.448 426.874  1.00 97.30           C  
ATOM    690  CA  SER B 278     222.401 246.841 426.248  1.00100.00           C  
ATOM    691  CA  GLN B 279     218.910 247.335 424.691  1.00100.00           C  
ATOM    692  CA  GLN B 280     219.381 250.180 422.176  1.00 97.58           C  
ATOM    693  CA  TYR B 281     220.470 248.534 419.271  1.00 97.75           C  
ATOM    694  CA  ARG B 282     219.214 251.150 417.807  1.00100.00           C  
ATOM    695  CA  ALA B 283     217.794 249.219 414.902  1.00 92.86           C  
ATOM    696  CA  LEU B 284     215.176 251.395 413.367  1.00 80.45           C  
ATOM    697  CA  THR B 285     214.313 249.273 410.624  1.00 66.34           C  
ATOM    698  CA  VAL B 286     210.825 247.836 410.980  1.00 44.62           C  
ATOM    699  CA  PRO B 287     210.218 244.693 412.715  1.00 42.51           C  
ATOM    700  CA  GLU B 288     211.578 245.650 416.078  1.00 43.33           C  
ATOM    701  CA  LEU B 289     209.322 248.675 416.384  1.00 31.88           C  
ATOM    702  CA  THR B 290     206.181 246.794 415.403  1.00 21.93           C  
ATOM    703  CA  GLN B 291     207.390 244.041 417.668  1.00 27.22           C  
ATOM    704  CA  GLN B 292     207.373 246.667 420.392  1.00 33.69           C  
ATOM    705  CA  MET B 293     204.243 248.775 419.759  1.00 23.21           C  
ATOM    706  CA  PHE B 294     201.715 245.977 418.872  1.00 26.97           C  
ATOM    707  CA  ASP B 295     202.824 243.549 421.768  1.00 40.24           C  
ATOM    708  CA  ALA B 296     200.672 242.547 424.656  1.00 39.02           C  
ATOM    709  CA  LYS B 297     203.624 243.740 426.609  1.00 32.50           C  
ATOM    710  CA  ASN B 298     204.606 247.207 426.445  1.00 28.60           C  
ATOM    711  CA  MET B 299     200.990 248.154 425.986  1.00 31.57           C  
ATOM    712  CA  MET B 300     199.905 251.283 427.722  1.00 21.60           C  
ATOM    713  CA  ALA B 301     196.810 249.502 428.479  1.00 29.61           C  
ATOM    714  CA  ALA B 302     196.866 246.392 430.537  1.00 39.22           C  
ATOM    715  CA  CYS B 303     194.236 245.231 428.162  1.00 47.77           C  
ATOM    716  CA  ASP B 304     195.730 243.376 425.245  1.00 48.33           C  
ATOM    717  CA  PRO B 305     195.845 244.179 421.723  1.00 40.81           C  
ATOM    718  CA  ARG B 306     195.140 240.597 420.765  1.00 48.63           C  
ATOM    719  CA  HIS B 307     191.801 240.898 422.271  1.00 41.86           C  
ATOM    720  CA  GLY B 308     191.020 244.375 421.177  1.00 23.13           C  
ATOM    721  CA  ARG B 309     189.470 245.282 417.911  1.00 18.23           C  
ATOM    722  CA  TYR B 310     189.569 248.348 416.227  1.00 18.02           C  
ATOM    723  CA  LEU B 311     188.430 251.546 415.741  1.00 12.59           C  
ATOM    724  CA  THR B 312     191.791 252.026 413.938  1.00 20.92           C  
ATOM    725  CA  VAL B 313     195.491 251.721 414.386  1.00 21.66           C  
ATOM    726  CA  ALA B 314     197.690 254.706 413.699  1.00 19.05           C  
ATOM    727  CA  ALA B 315     201.390 254.181 413.464  1.00  6.84           C  
ATOM    728  CA  VAL B 316     202.487 257.760 413.593  1.00  6.33           C  
ATOM    729  CA  PHE B 317     206.171 257.270 412.638  1.00 11.40           C  
ATOM    730  CA  ARG B 318     208.600 260.200 412.744  1.00 33.50           C  
ATOM    731  CA  GLY B 319     212.017 259.528 411.271  1.00 48.28           C  
ATOM    732  CA  ARG B 320     213.524 258.921 407.930  1.00 54.21           C  
ATOM    733  CA  MET B 321     212.160 255.898 406.157  1.00 34.07           C  
ATOM    734  CA  SER B 322     211.636 254.848 402.667  1.00 28.27           C  
ATOM    735  CA  MET B 323     208.154 254.667 401.236  1.00 29.79           C  
ATOM    736  CA  LYS B 324     208.909 251.185 400.015  1.00 26.85           C  
ATOM    737  CA  GLU B 325     210.167 249.517 403.193  1.00 25.85           C  
ATOM    738  CA  VAL B 326     207.266 251.234 404.920  1.00 26.70           C  
ATOM    739  CA  ASP B 327     204.498 250.622 402.464  1.00 44.49           C  
ATOM    740  CA  GLU B 328     205.845 247.088 402.120  1.00 51.41           C  
ATOM    741  CA  GLN B 329     206.223 245.965 405.732  1.00 48.07           C  
ATOM    742  CA  MET B 330     202.672 247.126 406.471  1.00 43.07           C  
ATOM    743  CA  LEU B 331     201.542 244.526 403.968  1.00 47.31           C  
ATOM    744  CA  ASN B 332     203.169 241.352 405.269  1.00 50.87           C  
ATOM    745  CA  VAL B 333     201.889 242.554 408.607  1.00 44.29           C  
ATOM    746  CA  GLN B 334     198.424 242.674 407.055  1.00 55.13           C  
ATOM    747  CA  ASN B 335     198.853 239.144 405.747  1.00 67.16           C  
ATOM    748  CA  LYS B 336     200.640 237.383 408.608  1.00 69.74           C  
ATOM    749  CA  ASN B 337     197.502 238.503 410.361  1.00 69.20           C  
ATOM    750  CA  SER B 338     195.273 236.194 408.510  1.00 69.00           C  
ATOM    751  CA  SER B 339     192.987 238.375 406.521  1.00 63.08           C  
ATOM    752  CA  TYR B 340     192.943 240.483 408.552  1.00 54.97           C  
ATOM    753  CA  PHE B 341     190.231 242.903 407.702  1.00 44.79           C  
ATOM    754  CA  VAL B 342     188.825 242.355 411.021  1.00 41.62           C  
ATOM    755  CA  GLU B 343     185.255 241.920 411.135  1.00 50.05           C  
ATOM    756  CA  TRP B 344     183.734 244.874 412.371  1.00 30.29           C  
ATOM    757  CA  ILE B 345     185.546 247.655 410.644  1.00 29.65           C  
ATOM    758  CA  PRO B 346     185.964 247.832 407.099  1.00 35.31           C  
ATOM    759  CA  ASN B 347     189.437 249.215 407.094  1.00 28.59           C  
ATOM    760  CA  ASN B 348     192.628 249.162 408.811  1.00 21.20           C  
ATOM    761  CA  VAL B 349     195.857 250.687 409.958  1.00 15.60           C  
ATOM    762  CA  LYS B 350     196.418 254.392 409.380  1.00  7.97           C  
ATOM    763  CA  THR B 351     200.034 254.817 408.397  1.00  2.00           C  
ATOM    764  CA  ALA B 352     201.342 258.261 409.200  1.00  7.32           C  
ATOM    765  CA  VAL B 353     204.838 259.489 408.481  1.00 17.66           C  
ATOM    766  CA  CYS B 354     206.620 262.547 409.799  1.00 41.06           C  
ATOM    767  CA  ASP B 355     209.846 263.568 408.259  1.00 55.40           C  
ATOM    768  CA  ILE B 356     212.107 263.947 411.138  1.00 59.96           C  
ATOM    769  CA  PRO B 357     213.742 261.605 413.322  1.00 58.14           C  
ATOM    770  CA  PRO B 358     214.077 262.245 416.886  1.00 59.42           C  
ATOM    771  CA  ARG B 359     217.437 263.315 417.990  1.00 68.33           C  
ATOM    772  CA  GLY B 360     218.870 259.999 419.250  1.00 59.28           C  
ATOM    773  CA  LEU B 361     216.514 257.765 417.528  1.00 55.07           C  
ATOM    774  CA  LYS B 362     216.538 256.950 413.942  1.00 49.45           C  
ATOM    775  CA  MET B 363     212.837 257.223 414.451  1.00 44.58           C  
ATOM    776  CA  SER B 364     209.803 256.861 416.732  1.00 40.19           C  
ATOM    777  CA  ALA B 365     206.808 255.662 415.745  1.00 35.52           C  
ATOM    778  CA  THR B 366     203.942 256.443 418.068  1.00 19.99           C  
ATOM    779  CA  PHE B 367     201.152 253.883 418.150  1.00  8.34           C  
ATOM    780  CA  ILE B 368     197.568 254.827 418.810  1.00 12.46           C  
ATOM    781  CA  GLY B 369     195.424 251.739 418.957  1.00 11.41           C  
ATOM    782  CA  ASN B 370     191.943 250.945 419.528  1.00  8.51           C  
ATOM    783  CA  SER B 371     191.296 247.625 421.250  1.00 19.03           C  
ATOM    784  CA  THR B 372     188.326 245.866 422.444  1.00 15.50           C  
ATOM    785  CA  ALA B 373     190.227 244.566 425.374  1.00  7.67           C  
ATOM    786  CA  ILE B 374     189.103 247.944 427.076  1.00  2.00           C  
ATOM    787  CA  GLN B 375     186.084 246.575 427.751  1.00 14.51           C  
ATOM    788  CA  GLU B 376     187.968 244.747 430.482  1.00 14.80           C  
ATOM    789  CA  LEU B 377     188.830 248.012 432.201  1.00 15.58           C  
ATOM    790  CA  PHE B 378     185.620 249.918 432.420  1.00 16.61           C  
ATOM    791  CA  LYS B 379     184.433 246.587 433.755  1.00 16.55           C  
ATOM    792  CA  ARG B 380     187.043 246.841 436.465  1.00 27.51           C  
ATOM    793  CA  ILE B 381     186.185 250.417 437.318  1.00 23.86           C  
ATOM    794  CA  SER B 382     182.467 249.712 437.146  1.00 26.53           C  
ATOM    795  CA  GLU B 383     182.946 246.758 439.479  1.00 34.87           C  
ATOM    796  CA  GLN B 384     184.831 248.718 442.163  1.00 27.14           C  
ATOM    797  CA  PHE B 385     181.956 251.177 442.105  1.00 19.69           C  
ATOM    798  CA  THR B 386     179.099 248.795 442.807  1.00 23.53           C  
ATOM    799  CA  ALA B 387     181.089 246.864 445.453  1.00 21.17           C  
ATOM    800  CA  MET B 388     181.340 250.155 447.321  1.00 16.25           C  
ATOM    801  CA  PHE B 389     178.367 251.995 446.045  1.00 26.94           C  
ATOM    802  CA  ARG B 390     176.218 249.159 447.334  1.00 43.42           C  
ATOM    803  CA  ARG B 391     177.736 249.275 450.758  1.00 35.47           C  
ATOM    804  CA  LYS B 392     176.695 252.874 450.865  1.00 20.61           C  
ATOM    805  CA  ALA B 393     178.496 253.639 453.891  1.00  9.52           C  
ATOM    806  CA  PHE B 394     180.455 255.878 451.622  1.00 15.71           C  
ATOM    807  CA  LEU B 395     177.341 256.906 449.847  1.00 18.28           C  
ATOM    808  CA  HIS B 396     176.198 259.629 452.424  1.00 19.93           C  
ATOM    809  CA  TRP B 397     179.032 262.144 451.940  1.00 24.76           C  
ATOM    810  CA  TYR B 398     177.986 262.412 448.319  1.00 30.69           C  
ATOM    811  CA  THR B 399     174.200 262.321 448.442  1.00 37.85           C  
ATOM    812  CA  GLY B 400     174.340 264.532 451.489  1.00 41.05           C  
ATOM    813  CA  GLU B 401     176.898 266.716 449.600  1.00 37.96           C  
ATOM    814  CA  GLY B 402     174.107 267.241 447.171  1.00 38.22           C  
ATOM    815  CA  MET B 403     175.764 264.958 444.637  1.00 39.38           C  
ATOM    816  CA  ASP B 404     172.818 263.072 443.350  1.00 41.26           C  
ATOM    817  CA  GLU B 405     171.958 259.514 444.066  1.00 45.59           C  
ATOM    818  CA  MET B 406     170.877 259.316 440.439  1.00 45.20           C  
ATOM    819  CA  GLU B 407     174.143 260.887 439.225  1.00 34.38           C  
ATOM    820  CA  PHE B 408     176.224 257.898 440.262  1.00 27.19           C  
ATOM    821  CA  THR B 409     173.572 255.607 438.846  1.00 27.27           C  
ATOM    822  CA  GLU B 410     173.813 257.448 435.570  1.00 38.93           C  
ATOM    823  CA  ALA B 411     177.562 257.238 435.107  1.00 38.51           C  
ATOM    824  CA  GLU B 412     177.965 253.612 436.056  1.00 39.60           C  
ATOM    825  CA  SER B 413     175.203 252.559 433.710  1.00 38.41           C  
ATOM    826  CA  ASN B 414     176.505 254.740 430.884  1.00 30.37           C  
ATOM    827  CA  MET B 415     180.102 253.661 431.290  1.00 30.27           C  
ATOM    828  CA  ASN B 416     178.747 250.195 432.094  1.00 30.82           C  
ATOM    829  CA  ASP B 417     176.846 250.059 428.797  1.00 28.66           C  
ATOM    830  CA  LEU B 418     180.038 251.309 427.187  1.00 23.70           C  
ATOM    831  CA  VAL B 419     181.512 247.918 428.166  1.00 26.78           C  
ATOM    832  CA  SER B 420     178.613 246.157 426.546  1.00 36.87           C  
ATOM    833  CA  GLU B 421     178.917 247.831 423.144  1.00 46.33           C  
ATOM    834  CA  TYR B 422     182.678 247.251 422.893  1.00 37.74           C  
ATOM    835  CA  GLN B 423     181.899 243.518 423.024  1.00 41.57           C  
ATOM    836  CA  GLN B 424     179.526 243.899 420.076  1.00 51.40           C  
ATOM    837  CA  TYR B 425     182.665 243.851 417.927  1.00 56.61           C  
ATOM    838  CA  GLN B 426     184.807 241.347 419.814  1.00 63.11           C  
ATOM    839  CA  ASP B 427     182.019 239.014 418.788  1.00 74.59           C  
TER     840      ASP B 427                                                      
ATOM    841  CA  ASN C   6     168.858 225.138 415.129  1.00 20.73           C  
ATOM    842  CA  SER C   7     165.528 223.904 416.309  1.00106.22           C  
ATOM    843  CA  SER C   8     163.075 226.668 416.903  1.00216.13           C  
ATOM    844  CA  ALA C   9     159.430 226.913 417.708  1.00225.15           C  
ATOM    845  CA  LYS C  10     157.229 229.189 415.710  1.00263.25           C  
ATOM    846  CA  LYS C  11     155.431 231.759 417.762  1.00233.38           C  
ATOM    847  CA  LYS C  12     152.273 233.434 416.650  1.00306.98           C  
ATOM    848  CA  GLU C  13     151.705 237.010 417.614  1.00218.86           C  
ATOM    849  CA  GLU C  14     148.096 237.598 418.448  1.00 83.72           C  
ATOM    850  CA  LYS C  15     148.976 241.127 419.409  1.00185.36           C  
ATOM    851  CA  GLY C  16     149.025 243.513 416.509  1.00 70.50           C  
ATOM    852  CA  LYS C  17     152.527 244.044 415.251  1.00113.85           C  
ATOM    853  CA  ASN C  18     151.723 247.371 413.781  1.00 85.68           C  
ATOM    854  CA  ILE C  19     152.478 250.578 415.491  1.00214.38           C  
ATOM    855  CA  GLN C  20     150.083 252.773 413.722  1.00 20.00           C  
ATOM    856  CA  VAL C  21     151.615 254.581 410.702  1.00 16.64           C  
ATOM    857  CA  VAL C  22     149.524 256.664 408.322  1.00 15.50           C  
ATOM    858  CA  VAL C  23     150.515 258.798 405.357  1.00 14.71           C  
ATOM    859  CA  ARG C  24     149.092 262.161 404.371  1.00 14.10           C  
ATOM    860  CA  VAL C  25     149.787 263.677 400.956  1.00 13.97           C  
ATOM    861  CA  ARG C  26     149.346 267.487 401.087  1.00 11.21           C  
ATOM    862  CA  PRO C  27     147.621 269.986 398.915  1.00 12.02           C  
ATOM    863  CA  PHE C  28     149.488 271.877 396.439  1.00 16.09           C  
ATOM    864  CA  ASN C  29     151.807 274.730 396.328  1.00 20.48           C  
ATOM    865  CA  LEU C  30     153.817 277.055 394.092  1.00 26.43           C  
ATOM    866  CA  ALA C  31     157.057 275.100 393.822  1.00 22.89           C  
ATOM    867  CA  GLU C  32     155.173 272.076 392.485  1.00 21.77           C  
ATOM    868  CA  ARG C  33     153.321 274.079 389.834  1.00 24.21           C  
ATOM    869  CA  LYS C  34     156.454 275.898 388.699  1.00 28.66           C  
ATOM    870  CA  ALA C  35     158.194 272.533 388.520  1.00 27.80           C  
ATOM    871  CA  SER C  36     155.445 271.418 386.173  1.00 29.80           C  
ATOM    872  CA  ALA C  37     156.497 267.857 386.813  1.00 27.46           C  
ATOM    873  CA  HIS C  38     154.144 265.041 387.457  1.00 23.01           C  
ATOM    874  CA  SER C  39     153.994 262.960 390.470  1.00 17.62           C  
ATOM    875  CA  ILE C  40     155.537 259.843 390.982  1.00 16.06           C  
ATOM    876  CA  VAL C  41     153.226 259.879 393.844  1.00 17.55           C  
ATOM    877  CA  GLU C  42     150.125 257.785 393.257  1.00 20.09           C  
ATOM    878  CA  SER C  43     147.779 257.409 396.214  1.00 20.78           C  
ATOM    879  CA  ASP C  44     144.946 254.910 396.250  1.00 23.12           C  
ATOM    880  CA  PRO C  45     143.097 255.551 399.472  1.00 23.39           C  
ATOM    881  CA  VAL C  46     140.419 252.952 399.166  1.00 27.33           C  
ATOM    882  CA  ARG C  47     143.243 250.519 398.644  1.00 26.05           C  
ATOM    883  CA  LYS C  48     145.262 252.328 401.122  1.00 24.01           C  
ATOM    884  CA  GLU C  49     148.154 252.100 398.769  1.00 21.65           C  
ATOM    885  CA  VAL C  50     150.870 254.592 397.910  1.00 20.25           C  
ATOM    886  CA  SER C  51     152.994 253.781 394.857  1.00 18.60           C  
ATOM    887  CA  VAL C  52     156.226 255.515 394.004  1.00 16.88           C  
ATOM    888  CA  ARG C  53     157.832 255.547 390.556  1.00 21.09           C  
ATOM    889  CA  THR C  54     161.450 254.618 391.351  1.00 27.10           C  
ATOM    890  CA  GLY C  55     162.569 255.976 388.009  1.00 39.42           C  
ATOM    891  CA  GLY C  56     160.516 259.129 387.953  1.00 49.15           C  
ATOM    892  CA  LEU C  57     160.642 260.067 384.230  1.00 54.32           C  
ATOM    893  CA  ALA C  58     163.059 257.347 382.889  1.00 52.00           C  
ATOM    894  CA  ASP C  59     161.322 254.619 384.593  1.00 48.56           C  
ATOM    895  CA  LYS C  60     157.554 255.064 384.339  1.00 45.90           C  
ATOM    896  CA  SER C  61     156.613 251.478 384.489  1.00 39.79           C  
ATOM    897  CA  SER C  62     158.168 250.532 387.602  1.00 34.16           C  
ATOM    898  CA  ARG C  63     156.915 251.407 391.025  1.00 31.82           C  
ATOM    899  CA  LYS C  64     157.390 250.770 394.744  1.00 28.75           C  
ATOM    900  CA  THR C  65     154.068 250.153 396.449  1.00 22.39           C  
ATOM    901  CA  TYR C  66     153.324 250.296 400.157  1.00 23.21           C  
ATOM    902  CA  THR C  67     150.128 249.411 401.952  1.00 22.53           C  
ATOM    903  CA  PHE C  68     149.226 251.669 404.860  1.00 18.80           C  
ATOM    904  CA  ASP C  69     147.253 251.314 407.947  1.00 20.39           C  
ATOM    905  CA  MET C  70     145.724 254.505 406.715  1.00 20.23           C  
ATOM    906  CA  VAL C  71     146.351 256.665 403.666  1.00 19.42           C  
ATOM    907  CA  PHE C  72     145.116 260.234 403.207  1.00 18.86           C  
ATOM    908  CA  GLY C  73     145.771 261.987 400.221  1.00 16.11           C  
ATOM    909  CA  ALA C  74     145.608 265.326 398.799  1.00 18.84           C  
ATOM    910  CA  SER C  75     141.819 265.808 399.230  1.00 22.02           C  
ATOM    911  CA  THR C  76     141.942 264.883 402.791  1.00 23.53           C  
ATOM    912  CA  LYS C  77     140.963 267.875 404.848  1.00 23.00           C  
ATOM    913  CA  GLN C  78     142.000 268.709 408.369  1.00 21.18           C  
ATOM    914  CA  ILE C  79     138.804 267.321 409.904  1.00 25.93           C  
ATOM    915  CA  ASP C  80     139.368 264.054 408.015  1.00 25.13           C  
ATOM    916  CA  VAL C  81     142.824 263.573 409.525  1.00 23.79           C  
ATOM    917  CA  TYR C  82     141.461 264.347 412.969  1.00 27.62           C  
ATOM    918  CA  ARG C  83     138.392 262.084 412.855  1.00 28.63           C  
ATOM    919  CA  SER C  84     140.436 259.215 411.450  1.00 25.82           C  
ATOM    920  CA  VAL C  85     143.648 259.589 413.457  1.00 26.48           C  
ATOM    921  CA  VAL C  86     143.191 261.756 416.559  1.00 28.96           C  
ATOM    922  CA  ALA C  87     139.728 260.881 417.853  1.00 35.22           C  
ATOM    923  CA  PRO C  88     140.699 257.252 418.606  1.00 32.06           C  
ATOM    924  CA  ILE C  89     143.920 258.453 420.239  1.00 31.34           C  
ATOM    925  CA  LEU C  90     142.053 260.930 422.414  1.00 29.57           C  
ATOM    926  CA  ASP C  91     139.854 258.215 423.900  1.00 29.62           C  
ATOM    927  CA  GLU C  92     142.926 256.146 424.718  1.00 25.71           C  
ATOM    928  CA  VAL C  93     144.345 259.090 426.632  1.00 22.08           C  
ATOM    929  CA  ILE C  94     141.081 259.314 428.573  1.00 24.31           C  
ATOM    930  CA  MET C  95     141.648 255.632 429.262  1.00 23.81           C  
ATOM    931  CA  GLY C  96     144.820 256.578 430.940  1.00 21.06           C  
ATOM    932  CA  TYR C  97     147.341 255.496 428.369  1.00 21.45           C  
ATOM    933  CA  ASN C  98     150.545 256.953 427.554  1.00 16.83           C  
ATOM    934  CA  ALA C  99     150.090 257.959 423.929  1.00 17.24           C  
ATOM    935  CA  THR C 100     152.140 259.709 421.307  1.00 16.07           C  
ATOM    936  CA  ILE C 101     151.409 261.077 417.865  1.00 17.14           C  
ATOM    937  CA  PHE C 102     154.156 262.643 415.814  1.00 14.89           C  
ATOM    938  CA  ALA C 103     154.235 264.126 412.311  1.00 13.02           C  
ATOM    939  CA  TYR C 104     157.254 263.140 410.208  1.00 11.51           C  
ATOM    940  CA  GLY C 105     158.380 264.243 406.756  1.00 12.42           C  
ATOM    941  CA  GLN C 106     160.186 266.662 404.547  1.00 12.57           C  
ATOM    942  CA  THR C 107     159.508 270.375 404.891  1.00  8.96           C  
ATOM    943  CA  GLY C 108     156.682 271.684 402.826  1.00  8.64           C  
ATOM    944  CA  THR C 109     154.540 268.803 403.868  1.00  8.01           C  
ATOM    945  CA  GLY C 110     152.303 270.806 406.054  1.00  7.39           C  
ATOM    946  CA  LYS C 111     153.243 268.970 409.245  1.00 10.19           C  
ATOM    947  CA  THR C 112     152.965 272.232 411.137  1.00 10.64           C  
ATOM    948  CA  PHE C 113     150.036 273.398 409.047  1.00 11.38           C  
ATOM    949  CA  THR C 114     148.308 270.148 410.014  1.00 12.37           C  
ATOM    950  CA  MET C 115     149.231 270.073 413.714  1.00 15.95           C  
ATOM    951  CA  GLU C 116     148.823 273.790 414.437  1.00 19.12           C  
ATOM    952  CA  GLY C 117     146.325 274.432 411.631  1.00 35.33           C  
ATOM    953  CA  GLU C 118     145.374 277.910 410.511  1.00 45.54           C  
ATOM    954  CA  ARG C 119     142.442 280.171 411.186  1.00152.44           C  
ATOM    955  CA  SER C 120     139.864 281.402 408.768  1.00 80.48           C  
ATOM    956  CA  PRO C 121     140.542 284.885 407.682  1.00 84.36           C  
ATOM    957  CA  ASN C 122     138.434 287.829 408.726  1.00192.35           C  
ATOM    958  CA  GLU C 123     137.155 285.751 411.558  1.00285.87           C  
ATOM    959  CA  GLU C 124     135.262 287.925 413.966  1.00271.28           C  
ATOM    960  CA  TYR C 125     132.093 287.875 415.986  1.00144.21           C  
ATOM    961  CA  CYS C 126     130.506 286.420 412.941  1.00 95.11           C  
ATOM    962  CA  TRP C 127     131.653 282.883 413.256  1.00198.23           C  
ATOM    963  CA  GLU C 128     133.933 281.703 410.527  1.00263.14           C  
ATOM    964  CA  GLU C 129     134.479 278.218 409.277  1.00244.07           C  
ATOM    965  CA  ASP C 130     136.375 275.865 411.538  1.00164.54           C  
ATOM    966  CA  PRO C 131     138.033 273.594 408.971  1.00220.18           C  
ATOM    967  CA  LEU C 132     141.478 275.215 408.983  1.00 73.07           C  
ATOM    968  CA  ALA C 133     142.244 274.244 412.568  1.00 41.83           C  
ATOM    969  CA  GLY C 134     144.884 271.586 412.954  1.00 26.81           C  
ATOM    970  CA  ILE C 135     144.957 268.304 414.859  1.00 19.17           C  
ATOM    971  CA  ILE C 136     146.250 270.068 417.964  1.00 20.44           C  
ATOM    972  CA  PRO C 137     143.558 272.762 418.202  1.00 24.10           C  
ATOM    973  CA  ARG C 138     140.874 270.065 417.763  1.00 22.18           C  
ATOM    974  CA  THR C 139     142.416 267.746 420.332  1.00 25.48           C  
ATOM    975  CA  LEU C 140     142.594 270.360 423.087  1.00 28.80           C  
ATOM    976  CA  HIS C 141     138.887 271.020 422.502  1.00 29.95           C  
ATOM    977  CA  GLN C 142     137.964 267.335 422.419  1.00 27.14           C  
ATOM    978  CA  ILE C 143     140.113 266.448 425.445  1.00 22.70           C  
ATOM    979  CA  PHE C 144     137.899 268.495 427.763  1.00 18.70           C  
ATOM    980  CA  GLU C 145     134.690 267.347 426.107  1.00 21.68           C  
ATOM    981  CA  LYS C 146     135.538 263.694 426.682  1.00 19.85           C  
ATOM    982  CA  LEU C 147     136.940 264.262 430.165  1.00 19.06           C  
ATOM    983  CA  THR C 148     133.852 266.153 431.332  1.00 17.67           C  
ATOM    984  CA  ASP C 149     131.675 263.487 429.722  1.00 19.60           C  
ATOM    985  CA  ASN C 150     133.719 260.806 431.495  1.00 22.91           C  
ATOM    986  CA  GLY C 151     133.025 262.438 434.810  1.00 22.45           C  
ATOM    987  CA  THR C 152     136.058 261.123 436.476  1.00 22.25           C  
ATOM    988  CA  GLU C 153     137.378 263.629 438.980  1.00 24.29           C  
ATOM    989  CA  PHE C 154     140.064 265.070 436.742  1.00 24.83           C  
ATOM    990  CA  SER C 155     142.940 267.484 436.493  1.00 24.24           C  
ATOM    991  CA  VAL C 156     144.540 268.551 433.217  1.00 22.46           C  
ATOM    992  CA  LYS C 157     148.132 269.710 432.895  1.00 23.08           C  
ATOM    993  CA  VAL C 158     149.921 270.896 429.738  1.00 21.03           C  
ATOM    994  CA  SER C 159     153.487 271.650 428.664  1.00 20.37           C  
ATOM    995  CA  LEU C 160     155.133 272.773 425.443  1.00 17.11           C  
ATOM    996  CA  LEU C 161     158.816 272.688 424.636  1.00 11.56           C  
ATOM    997  CA  GLU C 162     160.873 272.770 421.500  1.00 10.30           C  
ATOM    998  CA  ILE C 163     164.078 270.947 420.787  1.00  9.88           C  
ATOM    999  CA  TYR C 164     166.292 273.504 419.068  1.00 10.79           C  
ATOM   1000  CA  ASN C 165     169.754 272.288 418.113  1.00 10.83           C  
ATOM   1001  CA  GLU C 166     169.540 269.659 420.711  1.00 11.99           C  
ATOM   1002  CA  GLU C 167     168.750 272.010 423.486  1.00 15.43           C  
ATOM   1003  CA  LEU C 168     165.389 272.195 425.251  1.00 13.61           C  
ATOM   1004  CA  PHE C 169     163.435 275.428 425.681  1.00 13.92           C  
ATOM   1005  CA  ASP C 170     160.121 275.854 427.518  1.00 15.41           C  
ATOM   1006  CA  LEU C 171     157.822 277.611 425.231  1.00 15.88           C  
ATOM   1007  CA  LEU C 172     154.976 278.003 427.729  1.00 21.73           C  
ATOM   1008  CA  ASN C 173     157.306 279.711 429.983  1.00 29.29           C  
ATOM   1009  CA  PRO C 174     156.313 282.893 431.361  1.00 33.75           C  
ATOM   1010  CA  SER C 175     159.705 284.126 432.102  1.00 33.54           C  
ATOM   1011  CA  SER C 176     161.333 286.445 429.692  1.00 35.16           C  
ATOM   1012  CA  ASP C 177     164.341 284.290 429.203  1.00 33.82           C  
ATOM   1013  CA  VAL C 178     164.210 281.026 427.538  1.00 26.51           C  
ATOM   1014  CA  SER C 179     164.042 278.657 430.260  1.00 24.32           C  
ATOM   1015  CA  GLU C 180     166.623 276.529 431.943  1.00 23.89           C  
ATOM   1016  CA  ARG C 181     167.558 273.314 430.600  1.00 20.12           C  
ATOM   1017  CA  LEU C 182     166.170 270.116 431.893  1.00 17.00           C  
ATOM   1018  CA  GLN C 183     168.170 267.467 433.389  1.00 22.57           C  
ATOM   1019  CA  MET C 184     167.167 263.912 432.844  1.00 25.98           C  
ATOM   1020  CA  PHE C 185     167.050 260.884 435.171  1.00 30.99           C  
ATOM   1021  CA  ASP C 186     165.881 257.270 434.883  1.00 36.94           C  
ATOM   1022  CA  ASP C 187     162.629 256.112 436.355  1.00 46.23           C  
ATOM   1023  CA  PRO C 188     163.191 253.408 438.844  1.00 53.19           C  
ATOM   1024  CA  ARG C 189     159.561 252.879 438.453  1.00 56.65           C  
ATOM   1025  CA  ASN C 190     159.561 251.881 434.891  1.00 55.73           C  
ATOM   1026  CA  LYS C 191     162.052 249.561 433.544  1.00 53.41           C  
ATOM   1027  CA  ARG C 192     163.050 251.990 430.850  1.00 50.92           C  
ATOM   1028  CA  GLY C 193     162.302 255.517 430.608  1.00 43.74           C  
ATOM   1029  CA  VAL C 194     163.045 258.776 432.033  1.00 31.08           C  
ATOM   1030  CA  ILE C 195     162.107 261.739 434.168  1.00 23.81           C  
ATOM   1031  CA  ILE C 196     162.732 265.293 433.036  1.00 20.53           C  
ATOM   1032  CA  LYS C 197     162.992 267.089 436.282  1.00 24.05           C  
ATOM   1033  CA  GLY C 198     162.298 270.661 436.441  1.00 22.72           C  
ATOM   1034  CA  LEU C 199     159.705 270.997 433.889  1.00 21.25           C  
ATOM   1035  CA  GLU C 200     157.048 273.307 435.020  1.00 22.99           C  
ATOM   1036  CA  GLU C 201     153.714 272.730 433.382  1.00 23.32           C  
ATOM   1037  CA  ILE C 202     150.343 274.521 433.581  1.00 22.56           C  
ATOM   1038  CA  THR C 203     147.110 273.261 435.100  1.00 23.34           C  
ATOM   1039  CA  VAL C 204     144.253 274.109 432.736  1.00 23.17           C  
ATOM   1040  CA  HIS C 205     140.580 273.939 433.539  1.00 27.37           C  
ATOM   1041  CA  ASN C 206     139.694 273.987 429.899  1.00 32.15           C  
ATOM   1042  CA  LYS C 207     140.691 275.071 426.427  1.00 36.16           C  
ATOM   1043  CA  ASP C 208     140.584 278.836 426.939  1.00 36.42           C  
ATOM   1044  CA  GLU C 209     143.167 278.647 429.712  1.00 29.90           C  
ATOM   1045  CA  VAL C 210     145.327 276.359 427.598  1.00 30.44           C  
ATOM   1046  CA  TYR C 211     144.925 278.419 424.434  1.00 32.11           C  
ATOM   1047  CA  GLN C 212     146.185 281.603 426.079  1.00 34.92           C  
ATOM   1048  CA  ILE C 213     149.262 279.772 427.362  1.00 29.81           C  
ATOM   1049  CA  LEU C 214     149.817 277.877 424.095  1.00 27.07           C  
ATOM   1050  CA  GLU C 215     149.802 280.822 421.675  1.00 31.31           C  
ATOM   1051  CA  LYS C 216     152.250 282.769 423.822  1.00 31.28           C  
ATOM   1052  CA  GLY C 217     154.415 279.680 424.134  1.00 27.04           C  
ATOM   1053  CA  ALA C 218     154.460 278.726 420.452  1.00 26.09           C  
ATOM   1054  CA  ALA C 219     155.006 282.374 419.584  1.00 24.58           C  
ATOM   1055  CA  LYS C 220     158.366 282.475 421.341  1.00 23.55           C  
ATOM   1056  CA  ARG C 221     159.325 279.073 419.835  1.00 14.63           C  
ATOM   1057  CA  THR C 222     162.011 279.931 417.557  1.00 14.32           C  
ATOM   1058  CA  THR C 223     162.025 280.570 414.145  1.00 15.60           C  
ATOM   1059  CA  ALA C 224     164.295 281.043 411.139  1.00 12.97           C  
ATOM   1060  CA  ALA C 225     164.420 281.379 407.445  1.00 15.05           C  
ATOM   1061  CA  THR C 226     165.730 278.735 405.255  1.00 15.24           C  
ATOM   1062  CA  LEU C 227     165.153 278.998 401.313  1.00 16.02           C  
ATOM   1063  CA  MET C 228     162.010 277.343 401.862  1.00 17.98           C  
ATOM   1064  CA  ASN C 229     160.618 279.259 404.304  1.00 14.80           C  
ATOM   1065  CA  ALA C 230     160.305 282.376 406.131  1.00 16.41           C  
ATOM   1066  CA  TYR C 231     158.747 281.398 409.128  1.00 20.01           C  
ATOM   1067  CA  SER C 232     159.898 278.154 409.855  1.00 13.41           C  
ATOM   1068  CA  SER C 233     159.714 276.661 413.332  1.00 11.66           C  
ATOM   1069  CA  ARG C 234     163.177 275.526 414.008  1.00 11.26           C  
ATOM   1070  CA  SER C 235     162.569 273.014 416.747  1.00  8.14           C  
ATOM   1071  CA  HIS C 236     160.913 269.726 417.095  1.00  8.03           C  
ATOM   1072  CA  SER C 237     157.794 270.745 419.013  1.00 11.09           C  
ATOM   1073  CA  VAL C 238     156.604 268.575 421.896  1.00 12.26           C  
ATOM   1074  CA  PHE C 239     153.208 269.323 423.414  1.00 15.31           C  
ATOM   1075  CA  SER C 240     152.260 267.125 426.368  1.00 16.31           C  
ATOM   1076  CA  VAL C 241     148.909 266.814 428.118  1.00 17.89           C  
ATOM   1077  CA  THR C 242     148.858 264.910 431.380  1.00 17.39           C  
ATOM   1078  CA  ILE C 243     145.510 263.881 432.817  1.00 21.32           C  
ATOM   1079  CA  HIS C 244     145.091 262.775 436.428  1.00 27.14           C  
ATOM   1080  CA  MET C 245     141.873 260.834 436.857  1.00 26.88           C  
ATOM   1081  CA  LYS C 246     140.266 259.541 440.066  1.00 29.54           C  
ATOM   1082  CA  GLU C 247     136.889 257.812 440.215  1.00 30.98           C  
ATOM   1083  CA  THR C 248     134.889 255.670 442.627  1.00 33.97           C  
ATOM   1084  CA  THR C 249     133.195 252.697 441.051  1.00 34.93           C  
ATOM   1085  CA  ILE C 250     130.004 250.836 441.331  1.00 35.39           C  
ATOM   1086  CA  ASP C 251     132.154 248.553 443.299  1.00 38.13           C  
ATOM   1087  CA  GLY C 252     133.097 251.621 445.136  1.00 38.20           C  
ATOM   1088  CA  GLU C 253     136.642 250.985 444.725  1.00 42.34           C  
ATOM   1089  CA  GLU C 254     138.504 254.159 444.196  1.00 44.12           C  
ATOM   1090  CA  LEU C 255     140.718 253.893 441.134  1.00 41.79           C  
ATOM   1091  CA  VAL C 256     143.364 256.129 439.886  1.00 36.44           C  
ATOM   1092  CA  LYS C 257     144.996 256.578 436.708  1.00 31.01           C  
ATOM   1093  CA  ILE C 258     147.544 258.703 435.236  1.00 25.16           C  
ATOM   1094  CA  GLY C 259     147.762 259.037 431.472  1.00 21.95           C  
ATOM   1095  CA  LYS C 260     149.960 261.270 429.405  1.00 21.72           C  
ATOM   1096  CA  LEU C 261     150.249 262.025 425.776  1.00 19.93           C  
ATOM   1097  CA  ASN C 262     152.802 263.517 423.655  1.00 17.80           C  
ATOM   1098  CA  LEU C 263     153.068 264.859 420.261  1.00 13.84           C  
ATOM   1099  CA  VAL C 264     156.078 265.725 418.372  1.00 10.68           C  
ATOM   1100  CA  ASP C 265     155.715 267.616 415.326  1.00 11.05           C  
ATOM   1101  CA  LEU C 266     159.409 267.110 414.623  1.00 10.20           C  
ATOM   1102  CA  ALA C 267     160.892 269.099 411.729  1.00 11.56           C  
ATOM   1103  CA  GLY C 268     160.384 268.705 409.136  1.00 11.02           C  
ATOM   1104  CA  SER C 269     163.536 269.974 408.045  1.00 15.90           C  
ATOM   1105  CA  GLU C 270     165.210 270.866 405.002  1.00 15.90           C  
ATOM   1106  CA  ASN C 271     168.590 269.883 404.313  1.00 17.75           C  
ATOM   1107  CA  ILE C 272     171.053 272.526 403.542  1.00 22.33           C  
ATOM   1108  CA  GLY C 273     171.752 270.976 400.168  1.00 25.21           C  
ATOM   1109  CA  ARG C 274     168.277 272.163 399.221  1.00 23.12           C  
ATOM   1110  CA  SER C 275     167.964 275.219 401.494  1.00 23.31           C  
ATOM   1111  CA  GLY C 276     171.475 276.271 400.453  1.00 24.08           C  
ATOM   1112  CA  ALA C 277     171.947 277.028 403.949  1.00 24.47           C  
ATOM   1113  CA  VAL C 278     175.107 277.993 405.376  1.00 29.29           C  
ATOM   1114  CA  ASP C 279     176.739 277.968 408.945  1.00 28.13           C  
ATOM   1115  CA  LYS C 280     174.050 278.222 411.633  1.00 22.61           C  
ATOM   1116  CA  ARG C 281     171.398 276.700 409.351  1.00 22.32           C  
ATOM   1117  CA  ALA C 282     173.912 274.086 408.199  1.00 19.06           C  
ATOM   1118  CA  ARG C 283     174.835 273.278 411.801  1.00 19.86           C  
ATOM   1119  CA  GLU C 284     171.150 272.649 412.479  1.00 16.63           C  
ATOM   1120  CA  ALA C 285     170.814 270.477 409.366  1.00 13.25           C  
ATOM   1121  CA  GLY C 286     173.828 268.459 410.487  1.00 12.54           C  
ATOM   1122  CA  ASN C 287     172.214 267.696 413.837  1.00 13.54           C  
ATOM   1123  CA  ILE C 288     168.824 267.183 412.237  1.00 12.60           C  
ATOM   1124  CA  ASN C 289     170.168 264.699 409.661  1.00 11.88           C  
ATOM   1125  CA  GLN C 290     172.283 262.895 412.236  1.00 10.94           C  
ATOM   1126  CA  SER C 291     169.400 262.554 414.666  1.00 11.57           C  
ATOM   1127  CA  LEU C 292     167.066 261.256 411.933  1.00 12.59           C  
ATOM   1128  CA  LEU C 293     169.778 258.882 410.793  1.00 13.34           C  
ATOM   1129  CA  THR C 294     170.014 257.579 414.375  1.00 11.20           C  
ATOM   1130  CA  LEU C 295     166.226 257.168 414.224  1.00 13.21           C  
ATOM   1131  CA  GLY C 296     166.603 255.125 411.045  1.00 12.05           C  
ATOM   1132  CA  ARG C 297     169.215 252.900 412.687  1.00 13.40           C  
ATOM   1133  CA  VAL C 298     166.953 252.354 415.698  1.00  9.81           C  
ATOM   1134  CA  ILE C 299     164.116 251.339 413.371  1.00  9.84           C  
ATOM   1135  CA  THR C 300     166.367 249.044 411.365  1.00 13.83           C  
ATOM   1136  CA  ALA C 301     167.843 247.548 414.535  1.00 13.20           C  
ATOM   1137  CA  LEU C 302     164.376 246.681 415.815  1.00 13.42           C  
ATOM   1138  CA  VAL C 303     163.187 245.129 412.542  1.00 14.01           C  
ATOM   1139  CA  GLU C 304     166.366 243.084 412.159  1.00 15.25           C  
ATOM   1140  CA  ARG C 305     165.886 242.356 415.738  1.00 20.02           C  
ATOM   1141  CA  THR C 306     169.556 242.935 415.605  1.00 18.34           C  
ATOM   1142  CA  PRO C 307     170.506 243.457 419.029  1.00 17.51           C  
ATOM   1143  CA  HIS C 308     172.766 246.471 418.901  1.00 21.03           C  
ATOM   1144  CA  VAL C 309     173.548 249.450 416.812  1.00 17.82           C  
ATOM   1145  CA  PRO C 310     175.918 252.226 417.391  1.00 14.61           C  
ATOM   1146  CA  TYR C 311     173.797 255.310 417.132  1.00 18.01           C  
ATOM   1147  CA  ARG C 312     175.888 257.030 417.899  1.00 19.32           C  
ATOM   1148  CA  GLU C 313     174.854 260.520 417.974  1.00 15.81           C  
ATOM   1149  CA  SER C 314     171.448 261.564 419.139  1.00 12.82           C  
ATOM   1150  CA  LYS C 315     170.083 261.269 422.600  1.00 12.48           C  
ATOM   1151  CA  LEU C 316     167.202 261.012 421.357  1.00 10.85           C  
ATOM   1152  CA  THR C 317     166.364 257.395 420.101  1.00  8.48           C  
ATOM   1153  CA  ARG C 318     167.438 256.144 423.521  1.00 14.80           C  
ATOM   1154  CA  ILE C 319     164.542 258.074 425.039  1.00 14.10           C  
ATOM   1155  CA  LEU C 320     162.252 257.188 422.162  1.00 15.58           C  
ATOM   1156  CA  GLN C 321     162.339 253.473 422.614  1.00 18.10           C  
ATOM   1157  CA  ASP C 322     160.114 253.280 425.596  1.00 17.37           C  
ATOM   1158  CA  SER C 323     157.800 255.765 424.027  1.00 13.74           C  
ATOM   1159  CA  LEU C 324     157.672 254.225 420.542  1.00 13.67           C  
ATOM   1160  CA  GLY C 325     157.422 250.502 420.424  1.00 15.96           C  
ATOM   1161  CA  GLY C 326     157.245 250.455 424.105  1.00 17.88           C  
ATOM   1162  CA  ARG C 327     154.262 249.972 426.234  1.00 22.41           C  
ATOM   1163  CA  THR C 328     153.346 253.384 424.705  1.00 20.30           C  
ATOM   1164  CA  ARG C 329     150.674 253.692 422.310  1.00 20.61           C  
ATOM   1165  CA  THR C 330     152.224 255.440 419.290  1.00 16.24           C  
ATOM   1166  CA  SER C 331     150.941 256.724 415.948  1.00 17.40           C  
ATOM   1167  CA  ILE C 332     152.992 258.262 413.143  1.00 12.78           C  
ATOM   1168  CA  ILE C 333     151.703 260.654 410.510  1.00 10.86           C  
ATOM   1169  CA  ALA C 334     154.118 260.656 407.566  1.00 11.62           C  
ATOM   1170  CA  THR C 335     153.611 263.763 405.449  1.00 10.55           C  
ATOM   1171  CA  ILE C 336     154.621 263.835 401.788  1.00 10.37           C  
ATOM   1172  CA  SER C 337     154.184 266.095 398.833  1.00 12.38           C  
ATOM   1173  CA  PRO C 338     152.806 264.753 395.965  1.00 12.28           C  
ATOM   1174  CA  ALA C 339     155.719 265.908 393.653  1.00 14.71           C  
ATOM   1175  CA  SER C 340     158.196 263.427 392.070  1.00 19.04           C  
ATOM   1176  CA  LEU C 341     161.084 265.655 392.665  1.00 20.65           C  
ATOM   1177  CA  ASN C 342     161.386 264.461 396.211  1.00 19.36           C  
ATOM   1178  CA  LEU C 343     161.814 260.889 394.999  1.00 18.58           C  
ATOM   1179  CA  GLU C 344     164.725 259.848 397.216  1.00 18.70           C  
ATOM   1180  CA  GLU C 345     163.298 261.488 400.326  1.00 16.45           C  
ATOM   1181  CA  THR C 346     159.854 259.982 399.736  1.00 13.75           C  
ATOM   1182  CA  LEU C 347     161.256 256.484 399.168  1.00 15.76           C  
ATOM   1183  CA  SER C 348     163.380 256.840 402.308  1.00 13.99           C  
ATOM   1184  CA  THR C 349     160.316 257.779 404.358  1.00 12.18           C  
ATOM   1185  CA  LEU C 350     158.187 254.972 402.930  1.00 13.52           C  
ATOM   1186  CA  GLU C 351     160.949 252.371 403.275  1.00 13.87           C  
ATOM   1187  CA  TYR C 352     161.602 252.986 406.974  1.00 12.52           C  
ATOM   1188  CA  ALA C 353     157.921 253.504 407.719  1.00 12.30           C  
ATOM   1189  CA  HIS C 354     157.279 250.174 406.023  1.00 17.33           C  
ATOM   1190  CA  ARG C 355     159.934 248.417 408.094  1.00 14.15           C  
ATOM   1191  CA  ALA C 356     158.334 249.878 411.209  1.00 15.76           C  
ATOM   1192  CA  LYS C 357     155.162 247.925 410.433  1.00 19.71           C  
ATOM   1193  CA  ASN C 358     157.091 244.767 411.129  1.00 21.04           C  
ATOM   1194  CA  ILE C 359     158.400 245.297 414.878  1.00 17.26           C  
ATOM   1195  CA  LEU C 360     156.778 242.342 417.203  1.00 21.71           C  
ATOM   1196  CA  ASN C 361     156.277 242.657 421.055  1.00 20.29           C  
ATOM   1197  CA  LYS C 362     155.276 240.025 423.631  1.00 24.02           C  
ATOM   1198  CA  PRO C 363     152.512 240.059 425.687  1.00 27.18           C  
ATOM   1199  CA  GLU C 364     153.866 238.765 429.109  1.00 37.56           C  
ATOM   1200  CA  VAL C 365     152.010 238.963 432.338  1.00 41.22           C  
ATOM   1201  CA  ASN C 366     153.457 240.387 435.511  1.00 47.67           C  
TER    1202      ASN C 366                                                      
HETATM 1203 MG    MG A1208     197.452 267.250 402.079  1.00 18.63          MG  
HETATM 1204  PG  GTP A1209     193.977 266.352 401.376  1.00 29.97           P  
HETATM 1205  O1G GTP A1209     195.206 266.289 402.258  1.00 28.70           O  
HETATM 1206  O2G GTP A1209     192.990 267.439 401.819  1.00 34.97           O  
HETATM 1207  O3G GTP A1209     193.157 265.067 401.435  1.00 32.10           O  
HETATM 1208  O3B GTP A1209     194.603 266.603 399.864  1.00 35.17           O  
HETATM 1209  PB  GTP A1209     195.698 265.641 399.088  1.00 41.40           P  
HETATM 1210  O1B GTP A1209     197.020 266.251 399.108  1.00 41.17           O  
HETATM 1211  O2B GTP A1209     195.068 265.316 397.744  1.00 42.02           O  
HETATM 1212  O3A GTP A1209     195.639 264.309 399.838  1.00 39.24           O  
HETATM 1213  PA  GTP A1209     196.499 263.050 399.896  1.00 41.34           P  
HETATM 1214  O1A GTP A1209     195.878 262.131 400.893  1.00 43.37           O  
HETATM 1215  O2A GTP A1209     197.923 263.367 400.111  1.00 44.48           O  
HETATM 1216  O5' GTP A1209     196.264 262.366 398.418  1.00 34.27           O  
HETATM 1217  C5' GTP A1209     196.987 261.160 398.250  1.00 25.47           C  
HETATM 1218  C4' GTP A1209     196.820 260.472 396.934  1.00 17.26           C  
HETATM 1219  O4' GTP A1209     197.787 260.969 395.973  1.00 18.20           O  
HETATM 1220  C3' GTP A1209     197.142 259.004 397.118  1.00 18.14           C  
HETATM 1221  O3' GTP A1209     196.473 258.242 396.139  1.00 19.98           O  
HETATM 1222  C2' GTP A1209     198.655 258.992 396.966  1.00 17.50           C  
HETATM 1223  O2' GTP A1209     199.077 257.702 396.514  1.00 19.33           O  
HETATM 1224  C1' GTP A1209     198.923 260.093 395.925  1.00 18.43           C  
HETATM 1225  N9  GTP A1209     200.133 260.900 396.151  1.00  9.96           N  
HETATM 1226  C8  GTP A1209     200.436 261.641 397.267  1.00 11.60           C  
HETATM 1227  N7  GTP A1209     201.581 262.259 397.187  1.00  7.31           N  
HETATM 1228  C5  GTP A1209     202.077 261.899 395.957  1.00  2.00           C  
HETATM 1229  C6  GTP A1209     203.275 262.241 395.329  1.00  3.48           C  
HETATM 1230  O6  GTP A1209     204.149 262.979 395.775  1.00  2.56           O  
HETATM 1231  N1  GTP A1209     203.420 261.666 394.049  1.00  2.00           N  
HETATM 1232  C2  GTP A1209     202.495 260.831 393.456  1.00  2.00           C  
HETATM 1233  N2  GTP A1209     202.796 260.375 392.273  1.00  2.00           N  
HETATM 1234  N3  GTP A1209     201.352 260.484 394.043  1.00  2.00           N  
HETATM 1235  C4  GTP A1209     201.192 261.051 395.286  1.00  3.56           C  
HETATM 1236  PB  GDP B1210     194.598 266.334 442.219  1.00 22.28           P  
HETATM 1237  O1B GDP B1210     193.884 266.877 441.048  1.00 23.59           O  
HETATM 1238  O2B GDP B1210     195.888 266.829 442.437  1.00 23.44           O  
HETATM 1239  O3B GDP B1210     193.616 266.451 443.519  1.00 25.30           O  
HETATM 1240  O3A GDP B1210     194.806 264.799 441.929  1.00 19.52           O  
HETATM 1241  PA  GDP B1210     196.213 263.898 441.859  1.00 20.51           P  
HETATM 1242  O1A GDP B1210     197.027 264.359 440.699  1.00 23.36           O  
HETATM 1243  O2A GDP B1210     196.875 264.044 443.220  1.00 18.00           O  
HETATM 1244  O5' GDP B1210     195.645 262.488 441.541  1.00 16.66           O  
HETATM 1245  C5' GDP B1210     196.388 261.276 441.880  1.00  7.65           C  
HETATM 1246  C4' GDP B1210     196.685 260.406 440.757  1.00  2.51           C  
HETATM 1247  O4' GDP B1210     197.584 261.127 439.825  1.00  2.00           O  
HETATM 1248  C3' GDP B1210     197.551 259.140 441.101  1.00  3.46           C  
HETATM 1249  O3' GDP B1210     197.021 258.051 440.261  1.00  2.32           O  
HETATM 1250  C2' GDP B1210     199.020 259.401 440.688  1.00  2.23           C  
HETATM 1251  O2' GDP B1210     199.824 258.300 440.228  1.00  2.00           O  
HETATM 1252  C1' GDP B1210     198.881 260.433 439.571  1.00  2.00           C  
HETATM 1253  N9  GDP B1210     199.933 261.448 439.548  1.00  5.88           N  
HETATM 1254  C8  GDP B1210     199.971 262.488 440.630  1.00  9.42           C  
HETATM 1255  N7  GDP B1210     201.098 263.133 440.090  1.00 10.36           N  
HETATM 1256  C5  GDP B1210     201.673 262.678 438.984  1.00 10.45           C  
HETATM 1257  C6  GDP B1210     202.720 262.853 438.051  1.00 13.51           C  
HETATM 1258  O6  GDP B1210     203.533 263.902 438.268  1.00 11.34           O  
HETATM 1259  N1  GDP B1210     202.924 262.072 436.968  1.00 10.31           N  
HETATM 1260  C2  GDP B1210     202.001 260.927 436.743  1.00  5.81           C  
HETATM 1261  N2  GDP B1210     202.400 260.299 435.656  1.00  6.23           N  
HETATM 1262  N3  GDP B1210     201.054 260.703 437.551  1.00  4.23           N  
HETATM 1263  C4  GDP B1210     200.865 261.530 438.596  1.00  7.64           C  
HETATM 1264  O01 TA1 B1211     217.000 260.080 427.889  1.00 63.75           O  
HETATM 1265  C01 TA1 B1211     216.975 259.699 426.500  1.00 63.37           C  
HETATM 1266  C02 TA1 B1211     216.499 258.140 426.468  1.00 64.56           C  
HETATM 1267  O02 TA1 B1211     215.168 258.214 427.111  1.00 73.61           O  
HETATM 1268  C03 TA1 B1211     215.022 257.692 428.417  1.00 82.30           C  
HETATM 1269  O03 TA1 B1211     215.915 257.157 429.027  1.00 81.04           O  
HETATM 1270  C04 TA1 B1211     213.685 257.841 428.930  1.00 85.16           C  
HETATM 1271  C05 TA1 B1211     213.690 258.367 430.295  1.00 85.81           C  
HETATM 1272  C06 TA1 B1211     212.334 258.544 430.899  1.00 88.17           C  
HETATM 1273  C07 TA1 B1211     211.151 258.216 430.179  1.00 88.93           C  
HETATM 1274  C08 TA1 B1211     211.267 257.774 429.013  1.00 87.81           C  
HETATM 1275  C09 TA1 B1211     212.472 257.546 428.293  1.00 86.96           C  
HETATM 1276  C10 TA1 B1211     216.313 257.405 425.033  1.00 60.76           C  
HETATM 1277  C11 TA1 B1211     214.965 256.534 424.902  1.00 59.46           C  
HETATM 1278  O04 TA1 B1211     213.740 257.369 425.007  1.00 58.42           O  
HETATM 1279  C12 TA1 B1211     213.392 258.283 424.038  1.00 58.87           C  
HETATM 1280  O05 TA1 B1211     214.012 258.506 423.041  1.00 60.49           O  
HETATM 1281  C13 TA1 B1211     212.095 258.957 424.431  1.00 55.92           C  
HETATM 1282  C14 TA1 B1211     214.668 255.409 425.930  1.00 60.18           C  
HETATM 1283  O06 TA1 B1211     214.577 254.392 424.905  1.00 59.01           O  
HETATM 1284  C15 TA1 B1211     214.841 255.370 423.877  1.00 59.51           C  
HETATM 1285  C16 TA1 B1211     216.095 254.999 423.019  1.00 60.03           C  
HETATM 1286  C17 TA1 B1211     217.198 256.049 423.048  1.00 61.43           C  
HETATM 1287  O07 TA1 B1211     218.324 255.582 422.260  1.00 62.13           O  
HETATM 1288  C18 TA1 B1211     217.629 256.478 424.532  1.00 62.13           C  
HETATM 1289  C19 TA1 B1211     217.866 255.197 425.387  1.00 63.64           C  
HETATM 1290  C20 TA1 B1211     219.092 257.176 424.500  1.00 65.31           C  
HETATM 1291  O08 TA1 B1211     220.022 256.620 425.062  1.00 68.11           O  
HETATM 1292  C21 TA1 B1211     219.344 258.520 423.805  1.00 63.59           C  
HETATM 1293  O09 TA1 B1211     220.783 258.865 423.995  1.00 58.93           O  
HETATM 1294  C22 TA1 B1211     221.641 258.877 422.913  1.00 56.05           C  
HETATM 1295  O10 TA1 B1211     221.334 258.631 421.788  1.00 57.49           O  
HETATM 1296  C23 TA1 B1211     223.032 259.244 423.352  1.00 54.68           C  
HETATM 1297  C24 TA1 B1211     218.424 259.599 424.378  1.00 63.31           C  
HETATM 1298  C25 TA1 B1211     217.466 260.189 423.559  1.00 62.60           C  
HETATM 1299  C26 TA1 B1211     216.464 261.158 424.258  1.00 60.57           C  
HETATM 1300  O11 TA1 B1211     215.268 261.466 423.460  1.00 60.54           O  
HETATM 1301  C27 TA1 B1211     215.293 262.557 422.706  1.00 60.84           C  
HETATM 1302  O12 TA1 B1211     216.188 263.335 422.583  1.00 60.71           O  
HETATM 1303  C28 TA1 B1211     213.939 262.729 421.968  1.00 63.49           C  
HETATM 1304  O13 TA1 B1211     214.000 263.925 421.215  1.00 63.94           O  
HETATM 1305  C29 TA1 B1211     212.808 262.743 423.028  1.00 64.93           C  
HETATM 1306  N01 TA1 B1211     213.167 263.748 424.021  1.00 68.46           N  
HETATM 1307  C30 TA1 B1211     212.745 263.699 425.306  1.00 75.26           C  
HETATM 1308  O14 TA1 B1211     212.013 262.817 425.740  1.00 72.57           O  
HETATM 1309  C31 TA1 B1211     213.276 264.799 426.160  1.00 80.56           C  
HETATM 1310  C32 TA1 B1211     213.035 266.151 425.922  1.00 83.75           C  
HETATM 1311  C33 TA1 B1211     213.579 267.154 426.770  1.00 86.03           C  
HETATM 1312  C34 TA1 B1211     214.386 266.771 427.877  1.00 87.21           C  
HETATM 1313  C35 TA1 B1211     214.632 265.431 428.121  1.00 85.33           C  
HETATM 1314  C36 TA1 B1211     214.100 264.437 427.292  1.00 84.57           C  
HETATM 1315  C37 TA1 B1211     211.426 262.961 422.375  1.00 65.34           C  
HETATM 1316  C38 TA1 B1211     210.683 261.826 422.011  1.00 66.62           C  
HETATM 1317  C39 TA1 B1211     209.408 261.959 421.399  1.00 67.56           C  
HETATM 1318  C40 TA1 B1211     208.881 263.240 421.157  1.00 66.79           C  
HETATM 1319  C41 TA1 B1211     209.610 264.361 421.516  1.00 68.49           C  
HETATM 1320  C42 TA1 B1211     210.889 264.235 422.129  1.00 66.75           C  
HETATM 1321  C43 TA1 B1211     215.945 260.561 425.622  1.00 61.38           C  
HETATM 1322  C44 TA1 B1211     217.250 259.907 422.076  1.00 62.81           C  
HETATM 1323  C45 TA1 B1211     218.508 259.981 425.937  1.00 63.04           C  
HETATM 1324  C46 TA1 B1211     218.948 261.509 426.069  1.00 62.66           C  
HETATM 1325  C47 TA1 B1211     219.546 259.254 426.823  1.00 61.96           C  
HETATM 1326 MG    MG C1205     156.220 276.195 408.160  1.00 54.43          MG  
HETATM 1327 AL   AF3 C1206     158.405 274.607 408.184  1.00 76.31          AL  
HETATM 1328  F1  AF3 C1206     158.099 276.218 407.301  1.00 81.79           F  
HETATM 1329  F2  AF3 C1206     159.100 273.210 407.308  1.00 65.69           F  
HETATM 1330  F3  AF3 C1206     157.774 274.437 409.957  1.00 61.96           F  
HETATM 1331  PB  ADP C1207     155.488 272.778 406.837  1.00 44.09           P  
HETATM 1332  O1B ADP C1207     155.990 271.496 406.239  1.00 50.00           O  
HETATM 1333  O2B ADP C1207     154.695 272.495 408.090  1.00 57.89           O  
HETATM 1334  O3B ADP C1207     156.627 273.720 407.059  1.00 42.78           O  
HETATM 1335  PA  ADP C1207     154.021 274.462 405.040  1.00 52.69           P  
HETATM 1336  O1A ADP C1207     152.971 275.207 405.841  1.00 58.36           O  
HETATM 1337  O2A ADP C1207     155.261 275.339 404.862  1.00 51.43           O  
HETATM 1338  O3A ADP C1207     154.408 273.118 405.767  1.00 50.13           O  
HETATM 1339  O5' ADP C1207     153.455 274.061 403.670  1.00 54.39           O  
HETATM 1340  C5' ADP C1207     154.317 274.434 402.623  1.00 57.48           C  
HETATM 1341  C4' ADP C1207     153.581 274.664 401.383  1.00 58.30           C  
HETATM 1342  O4' ADP C1207     152.642 273.609 401.151  1.00 53.47           O  
HETATM 1343  C3' ADP C1207     152.858 275.983 401.319  1.00 67.74           C  
HETATM 1344  O3' ADP C1207     153.631 276.906 400.529  1.00 78.48           O  
HETATM 1345  C2' ADP C1207     151.396 275.578 400.875  1.00 65.49           C  
HETATM 1346  O2' ADP C1207     150.931 276.152 399.625  1.00 82.19           O  
HETATM 1347  C1' ADP C1207     151.367 274.030 400.846  1.00 54.44           C  
HETATM 1348  N9  ADP C1207     150.327 273.462 401.765  1.00 41.27           N  
HETATM 1349  C8  ADP C1207     150.434 272.808 402.946  1.00 42.88           C  
HETATM 1350  N7  ADP C1207     149.234 272.494 403.511  1.00 37.91           N  
HETATM 1351  C5  ADP C1207     148.301 272.984 402.631  1.00 31.81           C  
HETATM 1352  C6  ADP C1207     146.853 272.952 402.616  1.00 35.93           C  
HETATM 1353  N6  ADP C1207     146.093 272.402 403.577  1.00 44.19           N  
HETATM 1354  N1  ADP C1207     146.219 273.550 401.533  1.00 35.81           N  
HETATM 1355  C2  ADP C1207     146.996 274.120 400.537  1.00 42.98           C  
HETATM 1356  N3  ADP C1207     148.322 274.193 400.457  1.00 37.51           N  
HETATM 1357  C4  ADP C1207     148.939 273.587 401.542  1.00 40.50           C  
CONECT 1203 1205                                                                
CONECT 1204 1205 1206 1207 1208                                                 
CONECT 1205 1203 1204                                                           
CONECT 1206 1204                                                                
CONECT 1207 1204                                                                
CONECT 1208 1204 1209                                                           
CONECT 1209 1208 1210 1211 1212                                                 
CONECT 1210 1209                                                                
CONECT 1211 1209                                                                
CONECT 1212 1209 1213                                                           
CONECT 1213 1212 1214 1215 1216                                                 
CONECT 1214 1213                                                                
CONECT 1215 1213                                                                
CONECT 1216 1213 1217                                                           
CONECT 1217 1216 1218                                                           
CONECT 1218 1217 1219 1220                                                      
CONECT 1219 1218 1224                                                           
CONECT 1220 1218 1221 1222                                                      
CONECT 1221 1220                                                                
CONECT 1222 1220 1223 1224                                                      
CONECT 1223 1222                                                                
CONECT 1224 1219 1222 1225                                                      
CONECT 1225 1224 1226 1235                                                      
CONECT 1226 1225 1227                                                           
CONECT 1227 1226 1228                                                           
CONECT 1228 1227 1229 1235                                                      
CONECT 1229 1228 1230 1231                                                      
CONECT 1230 1229                                                                
CONECT 1231 1229 1232                                                           
CONECT 1232 1231 1233 1234                                                      
CONECT 1233 1232                                                                
CONECT 1234 1232 1235                                                           
CONECT 1235 1225 1228 1234                                                      
CONECT 1236 1237 1238 1239 1240                                                 
CONECT 1237 1236                                                                
CONECT 1238 1236                                                                
CONECT 1239 1236                                                                
CONECT 1240 1236 1241                                                           
CONECT 1241 1240 1242 1243 1244                                                 
CONECT 1242 1241                                                                
CONECT 1243 1241                                                                
CONECT 1244 1241 1245                                                           
CONECT 1245 1244 1246                                                           
CONECT 1246 1245 1247 1248                                                      
CONECT 1247 1246 1252                                                           
CONECT 1248 1246 1249 1250                                                      
CONECT 1249 1248                                                                
CONECT 1250 1248 1251 1252                                                      
CONECT 1251 1250                                                                
CONECT 1252 1247 1250 1253                                                      
CONECT 1253 1252 1254 1263                                                      
CONECT 1254 1253 1255                                                           
CONECT 1255 1254 1256                                                           
CONECT 1256 1255 1257 1263                                                      
CONECT 1257 1256 1258 1259                                                      
CONECT 1258 1257                                                                
CONECT 1259 1257 1260                                                           
CONECT 1260 1259 1261 1262                                                      
CONECT 1261 1260                                                                
CONECT 1262 1260 1263                                                           
CONECT 1263 1253 1256 1262                                                      
CONECT 1264 1265                                                                
CONECT 1265 1264 1266 1321 1323                                                 
CONECT 1266 1265 1267 1276                                                      
CONECT 1267 1266 1268                                                           
CONECT 1268 1267 1269 1270                                                      
CONECT 1269 1268                                                                
CONECT 1270 1268 1271 1275                                                      
CONECT 1271 1270 1272                                                           
CONECT 1272 1271 1273                                                           
CONECT 1273 1272 1274                                                           
CONECT 1274 1273 1275                                                           
CONECT 1275 1270 1274                                                           
CONECT 1276 1266 1277 1288                                                      
CONECT 1277 1276 1278 1282 1284                                                 
CONECT 1278 1277 1279                                                           
CONECT 1279 1278 1280 1281                                                      
CONECT 1280 1279                                                                
CONECT 1281 1279                                                                
CONECT 1282 1277 1283                                                           
CONECT 1283 1282 1284                                                           
CONECT 1284 1277 1283 1285                                                      
CONECT 1285 1284 1286                                                           
CONECT 1286 1285 1287 1288                                                      
CONECT 1287 1286                                                                
CONECT 1288 1276 1286 1289 1290                                                 
CONECT 1289 1288                                                                
CONECT 1290 1288 1291 1292                                                      
CONECT 1291 1290                                                                
CONECT 1292 1290 1293 1297                                                      
CONECT 1293 1292 1294                                                           
CONECT 1294 1293 1295 1296                                                      
CONECT 1295 1294                                                                
CONECT 1296 1294                                                                
CONECT 1297 1292 1298 1323                                                      
CONECT 1298 1297 1299 1322                                                      
CONECT 1299 1298 1300 1321                                                      
CONECT 1300 1299 1301                                                           
CONECT 1301 1300 1302 1303                                                      
CONECT 1302 1301                                                                
CONECT 1303 1301 1304 1305                                                      
CONECT 1304 1303                                                                
CONECT 1305 1303 1306 1315                                                      
CONECT 1306 1305 1307                                                           
CONECT 1307 1306 1308 1309                                                      
CONECT 1308 1307                                                                
CONECT 1309 1307 1310 1314                                                      
CONECT 1310 1309 1311                                                           
CONECT 1311 1310 1312                                                           
CONECT 1312 1311 1313                                                           
CONECT 1313 1312 1314                                                           
CONECT 1314 1309 1313                                                           
CONECT 1315 1305 1316 1320                                                      
CONECT 1316 1315 1317                                                           
CONECT 1317 1316 1318                                                           
CONECT 1318 1317 1319                                                           
CONECT 1319 1318 1320                                                           
CONECT 1320 1315 1319                                                           
CONECT 1321 1265 1299                                                           
CONECT 1322 1298                                                                
CONECT 1323 1265 1297 1324 1325                                                 
CONECT 1324 1323                                                                
CONECT 1325 1323                                                                
CONECT 1326 1327 1334                                                           
CONECT 1327 1326 1328 1329 1330                                                 
CONECT 1327 1334                                                                
CONECT 1328 1327                                                                
CONECT 1329 1327                                                                
CONECT 1330 1327                                                                
CONECT 1331 1332 1333 1334 1338                                                 
CONECT 1332 1331                                                                
CONECT 1333 1331                                                                
CONECT 1334 1326 1327 1331                                                      
CONECT 1335 1336 1337 1338 1339                                                 
CONECT 1336 1335                                                                
CONECT 1337 1335                                                                
CONECT 1338 1331 1335                                                           
CONECT 1339 1335 1340                                                           
CONECT 1340 1339 1341                                                           
CONECT 1341 1340 1342 1343                                                      
CONECT 1342 1341 1347                                                           
CONECT 1343 1341 1344 1345                                                      
CONECT 1344 1343                                                                
CONECT 1345 1343 1346 1347                                                      
CONECT 1346 1345                                                                
CONECT 1347 1342 1345 1348                                                      
CONECT 1348 1347 1349 1357                                                      
CONECT 1349 1348 1350                                                           
CONECT 1350 1349 1351                                                           
CONECT 1351 1350 1352 1357                                                      
CONECT 1352 1351 1353 1354                                                      
CONECT 1353 1352                                                                
CONECT 1354 1352 1355                                                           
CONECT 1355 1354 1356                                                           
CONECT 1356 1355 1357                                                           
CONECT 1357 1348 1351 1356                                                      
MASTER      237    0    7    0    0    0    9    6 1354    3  156   99          
END                                                                             
