HEADER    MOTOR PROTEIN                           19-APR-12   4AQW              
TITLE     MODEL OF HUMAN KINESIN-5 MOTOR DOMAIN (1II6, 3HQD) AND MAMMALIAN      
TITLE    2 TUBULIN HETERODIMER (1JFF) DOCKED INTO THE 9.5-ANGSTROM CRYO-EM MAP  
TITLE    3 OF MICROTUBULE-BOUND KINESIN-5 MOTOR DOMAIN IN THE RIGOR STATE.      
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-5, KINESIN-LIKE PROTEIN 1, KINESIN-LIKE SPINDLE PRO 
COMPND  14 KINESIN-RELATED MOTOR PROTEIN EG5, THYROID RECEPTOR-INTERACTING      
COMPND  15 PROTEIN 5, TR-INTERACTING PROTEIN 5, TRIP-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_VECTOR: PET21A                                     
KEYWDS    MOTOR PROTEIN, MICROTUBULE, MITOSIS, CANCER                           
EXPDTA    ELECTRON MICROSCOPY                                                   
MDLTYP    CA ATOMS ONLY, CHAIN A, B, C                                          
AUTHOR    A.GOULET,W.M.BEHNKE-PARKS,C.V.SINDELAR,S.S.ROSENFELD,C.A.MOORES       
REVDAT   4   30-AUG-17 4AQW    1       REMARK                                   
REVDAT   3   19-APR-17 4AQW    1       REMARK                                   
REVDAT   2   16-JAN-13 4AQW    1       JRNL                                     
REVDAT   1   21-NOV-12 4AQW    0                                                
JRNL        AUTH   A.GOULET,W.M.BEHNKE-PARKS,C.V.SINDELAR,J.MAJOR,              
JRNL        AUTH 2 S.S.ROSENFELD,C.MOORES                                       
JRNL        TITL   THE STRUCTURAL BASIS OF FORCE GENERATION BY THE MITOTIC      
JRNL        TITL 2 MOTOR KINESIN-5.                                             
JRNL        REF    J.BIOL.CHEM.                  V. 287 44654 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   23135273                                                     
JRNL        DOI    10.1074/JBC.M112.404228                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    9.50 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                    : 1II6                                
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--RIGID BODY (1JFF). RIGID BODY AND        
REMARK   3  FLEXIBLE FITTING FOR THE CHIMERIC MODEL BUILT USING 1II6 AND        
REMARK   3  3HQD. REFINEMENT PROTOCOL--X-RAY                                    
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : 2.800                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 9.500                          
REMARK   3   NUMBER OF PARTICLES               : 6748                           
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: THE LOOP 5 (119-131) WAS MODELED WITH MODELLER.       
REMARK   3  SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-2078.           
REMARK   3  (DEPOSITION ID: 10752).                                             
REMARK   4                                                                      
REMARK   4 4AQW 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_1290052139.                                   
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                    : FILAMENT                          
REMARK 245   PARTICLE TYPE                  : HELICAL                           
REMARK 245   NAME OF SAMPLE                 : 13-PROTOFILAMENT MICROTUBULE      
REMARK 245                                    -BOUND HUMAN KINESIN-5 MOTOR      
REMARK 245                                    DOMAIN IN ABSENCE OF NUCLEOTIDES  
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 U/ML APYRASE              
REMARK 245   PH                             : 6.80                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 16-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)              : 2300.00                        
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 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, CYS 25 TO VAL                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, CYS 43 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, CYS 87 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, CYS 99 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, THR 126 TO CYS                        
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   438                                                      
REMARK 465     THR B   439                                                      
REMARK 465     ALA B   440                                                      
REMARK 465     ASP B   441                                                      
REMARK 465     GLU B   442                                                      
REMARK 465     GLN B   443                                                      
REMARK 465     GLY B   444                                                      
REMARK 465     GLU B   445                                                      
REMARK 465     PHE B   446                                                      
REMARK 465     GLU B   447                                                      
REMARK 465     GLU B   448                                                      
REMARK 465     GLU B   449                                                      
REMARK 465     GLU B   450                                                      
REMARK 465     GLY B   451                                                      
REMARK 465     GLU B   452                                                      
REMARK 465     ASP B   453                                                      
REMARK 465     GLU B   454                                                      
REMARK 465     ALA B   455                                                      
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     ASN C     6                                                      
REMARK 465     SER C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     LYS C    10                                                      
REMARK 465     LYS C    11                                                      
REMARK 465     LYS C    12                                                      
REMARK 465     GLU C    13                                                      
REMARK 465     GLU C    14                                                      
REMARK 465     LYS C    15                                                      
REMARK 465     ASN C   366                                                      
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 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 B 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1II6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MITOTIC KINESIN EG5 IN COMPLEXWITH MG-ADP.  
REMARK 900 RELATED ID: 1JFF   RELATED DB: PDB                                   
REMARK 900 REFINED STRUCTURE OF ALPHA-BETA TUBULIN FROM ZINC- INDUCEDSHEETS     
REMARK 900 STABILIZED WITH TAXOL                                                
REMARK 900 RELATED ID: 1Q0B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MOTOR PROTEIN KSP IN COMPLEX WITHADP AND    
REMARK 900 MONASTROL                                                            
REMARK 900 RELATED ID: 1SA0   RELATED DB: PDB                                   
REMARK 900 TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX                     
REMARK 900 RELATED ID: 1SA1   RELATED DB: PDB                                   
REMARK 900 TUBULIN-PODOPHYLLOTOXIN: STATHMIN-LIKE DOMAIN COMPLEX                
REMARK 900 RELATED ID: 1TVK   RELATED DB: PDB                                   
REMARK 900 THE BINDING MODE OF EPOTHILONE A ON A,B-TUBULIN BY                   
REMARK 900 ELECTRONCRYSTALLOGRAPHY                                              
REMARK 900 RELATED ID: 1X88   RELATED DB: PDB                                   
REMARK 900 HUMAN EG5 MOTOR DOMAIN BOUND TO MG-ADP AND MONASTROL                 
REMARK 900 RELATED ID: 1YRS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH INHIBITOR 1                 
REMARK 900 RELATED ID: 1Z2B   RELATED DB: PDB                                   
REMARK 900 TUBULIN-COLCHICINE-VINBLASTINE: STATHMIN-LIKE DOMAIN COMPLEX         
REMARK 900 RELATED ID: 2FKY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH INHIBITOR 13                
REMARK 900 RELATED ID: 2FL2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH INHIBITOR 19                
REMARK 900 RELATED ID: 2FL6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH INHIBITOR 6                 
REMARK 900 RELATED ID: 2G1Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH INHIBITOR 9H                
REMARK 900 RELATED ID: 2GM1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MITOTIC KINESIN EG5 IN COMPLEXWITH MG-ADP   
REMARK 900 AND N-(3-AMINOPROPYL)-N-((3- BENZYL-5-CHLORO-4-OXO-3,4-              
REMARK 900 DIHYDROPYRROLO[2,1-F][ 1,2,4]TRIAZIN-2-YL)(CYCLOPROPYL)METHYL)-4-    
REMARK 900 METHYLBENZAMIDE                                                      
REMARK 900 RELATED ID: 2UYI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH ADP AND THIOPHENE           
REMARK 900 CONTAINING INHIBITOR 33                                              
REMARK 900 RELATED ID: 2UYM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH ADP AND THIOPHENE           
REMARK 900 CONTAINING INHIBITOR 37                                              
REMARK 900 RELATED ID: 2WBE   RELATED DB: PDB                                   
REMARK 900 KINESIN-5-TUBULIN COMPLEX WITH AMPPNP                                
REMARK 900 RELATED ID: 2WOG   RELATED DB: PDB                                   
REMARK 900 INTERMEDIATE AND FINAL STATES OF HUMAN KINESIN EG5 IN COMPLEX WITH   
REMARK 900 S-TRITYL-L-CYSTEINE                                                  
REMARK 900 RELATED ID: 2X2R   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN KINESIN EG5 IN COMPLEX WITH (R)-2-AMINO-  
REMARK 900 3-((4-CHLOROPHENYL)DIPHENYLMETHYLTHIO) PROPANOIC ACID                
REMARK 900 RELATED ID: 2X7C   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN KINESIN EG5 IN COMPLEX WITH (S)-ENASTRON  
REMARK 900 RELATED ID: 2X7D   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN KINESIN EG5 IN COMPLEX WITH (S)-          
REMARK 900 DIMETHYLENASTRON                                                     
REMARK 900 RELATED ID: 2X7E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN KINESIN EG5 IN COMPLEX WITH (R)-          
REMARK 900 FLUORASTROL                                                          
REMARK 900 RELATED ID: 2XAE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN KINESIN EG5 IN COMPLEX WITH (R)-2-AMINO-  
REMARK 900 3-((S)-2-METHYL-1,1-DIPHENYLBUTYLTHIO )PROPANOIC ACID                
REMARK 900 RELATED ID: 2XRP   RELATED DB: PDB                                   
REMARK 900 HUMAN DOUBLECORTIN N-DC REPEAT (1MJD) AND MAMMALIAN TUBULIN (1JFF    
REMARK 900 AND 3HKE) DOCKED INTO THE 8-ANGSTROM CRYO-EM MAP OF DOUBLECORTIN-    
REMARK 900 STABILISED MICROTUBULES                                              
REMARK 900 RELATED ID: 4A1Z   RELATED DB: PDB                                   
REMARK 900 EG5-1                                                                
REMARK 900 RELATED ID: 4A28   RELATED DB: PDB                                   
REMARK 900 EG5-2                                                                
REMARK 900 RELATED ID: 4A2T   RELATED DB: PDB                                   
REMARK 900 EG5                                                                  
REMARK 900 RELATED ID: 4A50   RELATED DB: PDB                                   
REMARK 900 EG5-INHIBITOR COMPLEX                                                
REMARK 900 RELATED ID: 4A51   RELATED DB: PDB                                   
REMARK 900 EG5-INHIBITOR COMPLEX                                                
REMARK 900 RELATED ID: 4A5Y   RELATED DB: PDB                                   
REMARK 900 EG5-INHIBITOR COMPLEX                                                
REMARK 900 RELATED ID: 4AP0   RELATED DB: PDB                                   
REMARK 900 THE MITOTIC KINESIN EG5 IN COMPLEX WITH MG-ADP AND ISPINESIB         
REMARK 900 RELATED ID: 4AQV   RELATED DB: PDB                                   
REMARK 900 MODEL OF HUMAN KINESIN-5 MOTOR DOMAIN (3HQD) AND MAMMALIAN TUBULIN   
REMARK 900 HETERODIMER (1JFF) DOCKED INTO THE 9. 7-ANGSTROM CRYO-EM MAP OF      
REMARK 900 MICROTUBULE-BOUND KINESIN- 5 MOTOR DOMAIN IN THE AMPPPNP STATE.      
REMARK 900 RELATED ID: EMD-2078   RELATED DB: EMDB                              
REMARK 900 ELECTRON CRYO-MICROSCOPY OF MICROTUBULE-BOUND HUMAN KINESIN-5 MOTOR  
REMARK 900 DOMAIN IN RIGOR STATE.                                               
REMARK 900 RELATED ID: EMD-2077   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-2079   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-2080   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-2081   RELATED DB: EMDB                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CYS-LIGHT CONSTRUCT (C25V,C43S,C87A,C99A). THE MUTATION              
REMARK 999 T126C WAS INTRODUCED FOR GOLD-LABELLING.                             
DBREF  4AQW A    1   452  UNP    Q2HJ86   TBA1D_BOVIN      1    452             
DBREF  4AQW B    1   455  UNP    Q6B856   TBB2B_BOVIN      1    445             
DBREF  4AQW C    1   367  UNP    P52732   KIF11_HUMAN      1    367             
SEQADV 4AQW ILE A    7  UNP  Q2HJ86    VAL     7 CONFLICT                       
SEQADV 4AQW ILE A  114  UNP  Q2HJ86    LEU   114 CONFLICT                       
SEQADV 4AQW SER A  136  UNP  Q2HJ86    LEU   136 CONFLICT                       
SEQADV 4AQW VAL A  137  UNP  Q2HJ86    ILE   137 CONFLICT                       
SEQADV 4AQW GLY A  265  UNP  Q2HJ86    ILE   265 CONFLICT                       
SEQADV 4AQW GLU A  358  UNP  Q2HJ86    GLN   358 CONFLICT                       
SEQADV 4AQW VAL A  437  UNP  Q2HJ86    MET   437 CONFLICT                       
SEQADV 4AQW ALA B   57  UNP  Q6B856    THR    55 CONFLICT                       
SEQADV 4AQW VAL B  172  UNP  Q6B856    MET   170 CONFLICT                       
SEQADV 4AQW ALA B  298  UNP  Q6B856    SER   296 CONFLICT                       
SEQADV 4AQW VAL B  318  UNP  Q6B856    ILE   316 CONFLICT                       
SEQADV 4AQW VAL C   25  UNP  P52732    CYS    25 ENGINEERED MUTATION            
SEQADV 4AQW SER C   43  UNP  P52732    CYS    43 ENGINEERED MUTATION            
SEQADV 4AQW ALA C   87  UNP  P52732    CYS    87 ENGINEERED MUTATION            
SEQADV 4AQW ALA C   99  UNP  P52732    CYS    99 ENGINEERED MUTATION            
SEQADV 4AQW CYS C  126  UNP  P52732    THR   126 ENGINEERED MUTATION            
SEQADV 4AQW HIS C  368  UNP  P52732              EXPRESSION TAG                 
SEQADV 4AQW HIS C  369  UNP  P52732              EXPRESSION TAG                 
SEQADV 4AQW HIS C  370  UNP  P52732              EXPRESSION TAG                 
SEQADV 4AQW HIS C  371  UNP  P52732              EXPRESSION TAG                 
SEQADV 4AQW HIS C  372  UNP  P52732              EXPRESSION TAG                 
SEQADV 4AQW 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    GTP  A 500      32                                                       
HET     MG  A 501       1                                                       
HET    GDP  B 600      28                                                       
HET    TA1  B 601      62                                                       
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     TA1 TAXOL                                                            
FORMUL   4  GTP    C10 H16 N5 O14 P3                                            
FORMUL   5   MG    MG 2+                                                        
FORMUL   6  GDP    C10 H15 N5 O11 P2                                            
FORMUL   7  TA1    C47 H51 N O14                                                
LINK         O1G GTP A 500                MG    MG A 501     1555   1555  2.45  
SITE     1 AC1  9 GLY A  10  GLN A  11  ALA A  12  ALA A  99                    
SITE     2 AC1  9 ASN A 101  GLY A 143  GLY A 144  THR A 145                    
SITE     3 AC1  9  MG A 501                                                     
SITE     1 AC2  1 GTP A 500                                                     
SITE     1 AC3  4 GLY B  10  CYS B  12  THR B 145  GLY B 146                    
SITE     1 AC4  5 VAL B  23  LEU B 275  ARG B 278  PRO B 360                    
SITE     2 AC4  5 ARG B 369                                                     
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     -17.728   3.062 -95.118  1.00 90.72           C  
ATOM      2  CA  GLU A   3     -17.703   2.398 -91.369  1.00 76.37           C  
ATOM      3  CA  CYS A   4     -19.198   4.272 -88.429  1.00 53.93           C  
ATOM      4  CA  ILE A   5     -17.495   4.267 -85.033  1.00 42.08           C  
ATOM      5  CA  SER A   6     -19.649   4.460 -81.913  1.00 26.32           C  
ATOM      6  CA  ILE A   7     -19.082   6.054 -78.534  1.00 20.58           C  
ATOM      7  CA  HIS A   8     -21.387   4.804 -75.814  1.00 24.92           C  
ATOM      8  CA  VAL A   9     -21.308   7.459 -73.104  1.00 24.49           C  
ATOM      9  CA  GLY A  10     -22.875   7.319 -69.644  1.00 29.78           C  
ATOM     10  CA  GLN A  11     -23.897   4.226 -67.700  1.00 23.82           C  
ATOM     11  CA  ALA A  12     -27.109   4.134 -69.691  1.00 17.32           C  
ATOM     12  CA  GLY A  13     -25.489   4.709 -73.075  1.00 14.25           C  
ATOM     13  CA  VAL A  14     -23.320   1.816 -71.983  1.00 16.05           C  
ATOM     14  CA  GLN A  15     -26.177  -0.489 -70.891  1.00 19.43           C  
ATOM     15  CA  ILE A  16     -27.967   0.268 -74.134  1.00 18.31           C  
ATOM     16  CA  GLY A  17     -24.554  -0.179 -75.693  1.00 26.23           C  
ATOM     17  CA  ASN A  18     -24.020  -3.638 -74.277  1.00 29.97           C  
ATOM     18  CA  ALA A  19     -27.496  -4.393 -75.661  1.00 37.71           C  
ATOM     19  CA  CYS A  20     -27.185  -2.983 -79.169  1.00 43.89           C  
ATOM     20  CA  TRP A  21     -23.783  -4.566 -79.133  1.00 51.95           C  
ATOM     21  CA  GLU A  22     -25.341  -7.873 -78.211  1.00 59.11           C  
ATOM     22  CA  LEU A  23     -27.990  -7.972 -80.903  1.00 62.00           C  
ATOM     23  CA  TYR A  24     -25.090  -7.435 -83.284  1.00 70.43           C  
ATOM     24  CA  CYS A  25     -22.922 -10.531 -83.025  1.00 67.24           C  
ATOM     25  CA  LEU A  26     -26.206 -12.370 -82.527  1.00 73.69           C  
ATOM     26  CA  GLU A  27     -27.161 -11.702 -86.152  1.00 74.74           C  
ATOM     27  CA  HIS A  28     -23.617 -11.961 -87.500  1.00 77.34           C  
ATOM     28  CA  GLY A  29     -22.670 -15.379 -86.135  1.00 86.18           C  
ATOM     29  CA  ILE A  30     -19.830 -14.055 -84.001  1.00 87.45           C  
ATOM     30  CA  GLN A  31     -20.165 -15.665 -80.540  1.00 86.37           C  
ATOM     31  CA  PRO A  32     -18.571 -14.352 -77.260  1.00 89.63           C  
ATOM     32  CA  ASP A  33     -15.041 -14.616 -78.550  1.00 96.86           C  
ATOM     33  CA  GLY A  34     -14.814 -14.181 -82.329  1.00 94.83           C  
ATOM     34  CA  HIS A  61     -13.631 -10.531 -84.129  1.00 99.59           C  
ATOM     35  CA  VAL A  62     -13.137  -7.029 -82.703  1.00 96.92           C  
ATOM     36  CA  PRO A  63     -15.792  -4.343 -82.043  1.00 88.64           C  
ATOM     37  CA  ARG A  64     -15.488  -0.848 -83.452  1.00 69.26           C  
ATOM     38  CA  ALA A  65     -16.483   1.451 -80.618  1.00 49.94           C  
ATOM     39  CA  VAL A  66     -15.646   2.729 -77.171  1.00 45.70           C  
ATOM     40  CA  PHE A  67     -17.139   3.012 -73.687  1.00 38.52           C  
ATOM     41  CA  VAL A  68     -16.980   6.110 -71.466  1.00 35.38           C  
ATOM     42  CA  ASP A  69     -18.097   6.627 -67.858  1.00 31.66           C  
ATOM     43  CA  LEU A  70     -16.941   8.434 -64.725  1.00 30.66           C  
ATOM     44  CA  GLU A  71     -18.302   5.639 -62.524  1.00 43.59           C  
ATOM     45  CA  PRO A  72     -16.150   2.528 -62.840  1.00 46.27           C  
ATOM     46  CA  THR A  73     -18.626  -0.047 -61.536  1.00 48.55           C  
ATOM     47  CA  VAL A  74     -20.785   0.278 -64.694  1.00 58.12           C  
ATOM     48  CA  ILE A  75     -18.200  -0.129 -67.478  1.00 63.45           C  
ATOM     49  CA  ASP A  76     -16.941  -2.835 -65.170  1.00 69.97           C  
ATOM     50  CA  GLU A  77     -20.214  -4.636 -65.947  1.00 70.62           C  
ATOM     51  CA  VAL A  78     -18.910  -4.899 -69.478  1.00 70.09           C  
ATOM     52  CA  ARG A  79     -15.639  -6.031 -67.941  1.00 74.67           C  
ATOM     53  CA  THR A  80     -17.283  -8.626 -65.665  1.00 80.03           C  
ATOM     54  CA  GLY A  81     -20.492  -9.706 -67.381  1.00 79.49           C  
ATOM     55  CA  THR A  82     -21.323 -11.062 -70.823  1.00 76.49           C  
ATOM     56  CA  TYR A  83     -19.414  -9.894 -73.908  1.00 71.97           C  
ATOM     57  CA  ARG A  84     -16.445  -9.632 -71.582  1.00 84.74           C  
ATOM     58  CA  GLN A  85     -13.576 -10.555 -73.928  1.00 84.53           C  
ATOM     59  CA  LEU A  86     -15.129  -9.161 -77.103  1.00 77.11           C  
ATOM     60  CA  PHE A  87     -13.629  -5.793 -76.173  1.00 75.47           C  
ATOM     61  CA  HIS A  88     -10.193  -4.311 -75.751  1.00 78.06           C  
ATOM     62  CA  PRO A  89      -9.512  -2.843 -72.325  1.00 83.61           C  
ATOM     63  CA  GLU A  90      -8.453   0.047 -74.539  1.00 78.49           C  
ATOM     64  CA  GLN A  91     -11.945   0.888 -75.858  1.00 69.51           C  
ATOM     65  CA  LEU A  92     -13.243   0.863 -72.288  1.00 68.73           C  
ATOM     66  CA  ILE A  93     -12.565   4.258 -70.695  1.00 68.32           C  
ATOM     67  CA  THR A  94     -13.313   4.884 -67.015  1.00 68.88           C  
ATOM     68  CA  GLY A  95     -12.669   7.615 -64.476  1.00 66.50           C  
ATOM     69  CA  LYS A  96     -12.647   5.842 -61.087  1.00 67.02           C  
ATOM     70  CA  GLU A  97     -13.528   9.268 -59.762  1.00 62.40           C  
ATOM     71  CA  ASP A  98     -17.092  10.459 -59.518  1.00 52.52           C  
ATOM     72  CA  ALA A  99     -20.026  10.455 -61.920  1.00 34.76           C  
ATOM     73  CA  ALA A 100     -22.262  13.190 -60.445  1.00 26.25           C  
ATOM     74  CA  ASN A 101     -25.713  13.590 -61.843  1.00 25.16           C  
ATOM     75  CA  ASN A 102     -24.792  17.046 -62.925  1.00 15.90           C  
ATOM     76  CA  TYR A 103     -23.836  18.342 -66.340  1.00  6.91           C  
ATOM     77  CA  ALA A 104     -21.248  20.911 -65.220  1.00  6.65           C  
ATOM     78  CA  ARG A 105     -19.099  18.481 -63.276  1.00 10.39           C  
ATOM     79  CA  GLY A 106     -19.264  15.916 -66.034  1.00 17.30           C  
ATOM     80  CA  HIS A 107     -18.637  18.390 -68.834  1.00 20.11           C  
ATOM     81  CA  TYR A 108     -16.263  20.888 -67.220  1.00 19.97           C  
ATOM     82  CA  THR A 109     -14.528  19.980 -63.933  1.00 14.79           C  
ATOM     83  CA  ILE A 110     -14.251  16.202 -63.868  1.00 22.39           C  
ATOM     84  CA  GLY A 111     -15.343  14.956 -67.283  1.00 31.58           C  
ATOM     85  CA  LYS A 112     -12.565  17.136 -68.715  1.00 37.27           C  
ATOM     86  CA  GLU A 113      -9.672  15.091 -67.356  1.00 41.42           C  
ATOM     87  CA  ILE A 114     -10.786  12.014 -69.305  1.00 32.89           C  
ATOM     88  CA  ILE A 115     -11.792  13.552 -72.644  1.00 24.51           C  
ATOM     89  CA  ASP A 116      -8.256  13.684 -74.084  1.00 26.78           C  
ATOM     90  CA  LEU A 117      -7.818   9.992 -73.424  1.00 23.76           C  
ATOM     91  CA  VAL A 118     -11.353   9.397 -74.692  1.00 24.82           C  
ATOM     92  CA  LEU A 119     -10.666  11.235 -77.932  1.00 27.75           C  
ATOM     93  CA  ASP A 120      -7.388   9.394 -78.346  1.00 39.11           C  
ATOM     94  CA  ARG A 121      -9.338   6.187 -78.918  1.00 44.01           C  
ATOM     95  CA  ILE A 122     -11.793   7.763 -81.346  1.00 48.00           C  
ATOM     96  CA  ARG A 123      -8.678   8.985 -83.164  1.00 54.11           C  
ATOM     97  CA  LYS A 124      -6.791   5.715 -82.709  1.00 44.21           C  
ATOM     98  CA  LEU A 125      -9.850   3.668 -83.721  1.00 49.40           C  
ATOM     99  CA  ALA A 126     -10.702   6.238 -86.402  1.00 56.85           C  
ATOM    100  CA  ASP A 127      -7.306   5.815 -88.024  1.00 68.82           C  
ATOM    101  CA  GLN A 128      -7.029   2.030 -88.119  1.00 79.45           C  
ATOM    102  CA  CYS A 129     -10.104   1.823 -90.403  1.00 86.84           C  
ATOM    103  CA  THR A 130     -10.603   2.584 -94.130  1.00 77.26           C  
ATOM    104  CA  GLY A 131     -12.483   5.727 -95.159  1.00 66.48           C  
ATOM    105  CA  LEU A 132     -15.093   5.901 -92.375  1.00 49.07           C  
ATOM    106  CA  GLN A 133     -18.411   7.764 -92.384  1.00 35.99           C  
ATOM    107  CA  GLY A 134     -18.913   8.850 -88.787  1.00 25.53           C  
ATOM    108  CA  PHE A 135     -19.486   8.031 -85.116  1.00 22.95           C  
ATOM    109  CA  SER A 136     -22.764   6.660 -83.822  1.00 11.40           C  
ATOM    110  CA  VAL A 137     -22.772   8.229 -80.335  1.00  6.65           C  
ATOM    111  CA  PHE A 138     -24.855   6.661 -77.523  1.00 13.94           C  
ATOM    112  CA  HIS A 139     -25.790   8.878 -74.574  1.00 22.19           C  
ATOM    113  CA  SER A 140     -28.582   9.466 -72.068  1.00 26.99           C  
ATOM    114  CA  PHE A 141     -29.453  13.152 -72.243  1.00 35.87           C  
ATOM    115  CA  GLY A 142     -30.311  13.607 -68.571  1.00 38.67           C  
ATOM    116  CA  GLY A 143     -27.275  12.236 -66.789  1.00 35.73           C  
ATOM    117  CA  GLY A 144     -23.919  13.450 -65.568  1.00 33.40           C  
ATOM    118  CA  THR A 145     -21.483  11.463 -67.682  1.00 20.53           C  
ATOM    119  CA  GLY A 146     -24.055  11.239 -70.428  1.00 15.71           C  
ATOM    120  CA  SER A 147     -25.138  14.844 -70.799  1.00 14.46           C  
ATOM    121  CA  GLY A 148     -22.059  16.795 -69.806  1.00 19.79           C  
ATOM    122  CA  PHE A 149     -19.124  14.728 -70.999  1.00 23.20           C  
ATOM    123  CA  THR A 150     -20.464  13.908 -74.459  1.00 22.10           C  
ATOM    124  CA  SER A 151     -21.369  17.529 -74.775  1.00 19.40           C  
ATOM    125  CA  LEU A 152     -17.663  18.176 -75.105  1.00 16.83           C  
ATOM    126  CA  LEU A 153     -16.885  14.830 -76.754  1.00 19.01           C  
ATOM    127  CA  MET A 154     -19.180  15.542 -79.677  1.00 24.75           C  
ATOM    128  CA  GLU A 155     -17.867  19.048 -79.219  1.00 28.50           C  
ATOM    129  CA  ARG A 156     -14.251  18.047 -79.786  1.00 30.73           C  
ATOM    130  CA  LEU A 157     -15.379  15.832 -82.730  1.00 30.23           C  
ATOM    131  CA  SER A 158     -17.204  18.455 -84.766  1.00 31.63           C  
ATOM    132  CA  VAL A 159     -13.830  20.174 -84.966  1.00 41.27           C  
ATOM    133  CA  ASP A 160     -11.512  17.216 -85.410  1.00 40.24           C  
ATOM    134  CA  TYR A 161     -13.670  15.626 -88.103  1.00 39.78           C  
ATOM    135  CA  GLY A 162     -16.145  18.259 -89.231  1.00 39.54           C  
ATOM    136  CA  LYS A 163     -15.949  16.315 -92.483  1.00 34.48           C  
ATOM    137  CA  LYS A 164     -18.110  13.383 -91.346  1.00 32.52           C  
ATOM    138  CA  SER A 165     -21.397  12.259 -89.850  1.00 22.09           C  
ATOM    139  CA  LYS A 166     -22.315  12.853 -86.236  1.00 18.88           C  
ATOM    140  CA  LEU A 167     -25.480  10.931 -85.567  1.00 13.86           C  
ATOM    141  CA  GLU A 168     -26.058  10.814 -81.849  1.00 15.54           C  
ATOM    142  CA  PHE A 169     -28.529   8.280 -80.578  1.00 18.38           C  
ATOM    143  CA  SER A 170     -30.119   9.729 -77.434  1.00 18.69           C  
ATOM    144  CA  ILE A 171     -32.545   8.534 -74.736  1.00 17.69           C  
ATOM    145  CA  TYR A 172     -34.137  11.820 -73.813  1.00 28.93           C  
ATOM    146  CA  PRO A 173     -36.043  12.434 -70.460  1.00 37.41           C  
ATOM    147  CA  ALA A 174     -39.217  10.464 -69.736  1.00 43.64           C  
ATOM    148  CA  PRO A 175     -42.133  12.937 -70.063  1.00 51.14           C  
ATOM    149  CA  GLN A 176     -43.364  12.329 -66.485  1.00 57.23           C  
ATOM    150  CA  VAL A 177     -41.305   9.420 -65.271  1.00 52.37           C  
ATOM    151  CA  SER A 178     -37.906  11.067 -65.030  1.00 51.22           C  
ATOM    152  CA  THR A 179     -35.363   9.843 -62.527  1.00 38.52           C  
ATOM    153  CA  ALA A 180     -32.730  12.404 -61.551  1.00 20.70           C  
ATOM    154  CA  VAL A 181     -34.161  15.360 -59.706  1.00  2.00           C  
ATOM    155  CA  VAL A 182     -32.293  17.740 -61.948  1.00  3.41           C  
ATOM    156  CA  GLU A 183     -32.655  15.868 -65.289  1.00 11.10           C  
ATOM    157  CA  PRO A 184     -33.726  19.016 -67.215  1.00  6.05           C  
ATOM    158  CA  TYR A 185     -30.682  20.963 -66.094  1.00  3.97           C  
ATOM    159  CA  ASN A 186     -28.657  18.133 -67.586  1.00  2.00           C  
ATOM    160  CA  SER A 187     -30.740  17.903 -70.765  1.00  6.16           C  
ATOM    161  CA  ILE A 188     -31.216  21.509 -71.656  1.00  8.44           C  
ATOM    162  CA  LEU A 189     -27.439  21.588 -71.388  1.00 10.17           C  
ATOM    163  CA  THR A 190     -26.595  18.577 -73.492  1.00  9.50           C  
ATOM    164  CA  THR A 191     -28.915  19.840 -76.199  1.00 18.93           C  
ATOM    165  CA  HIS A 192     -27.465  23.348 -76.521  1.00 23.95           C  
ATOM    166  CA  THR A 193     -23.866  22.212 -76.475  1.00 22.18           C  
ATOM    167  CA  THR A 194     -24.366  19.317 -78.882  1.00 30.97           C  
ATOM    168  CA  LEU A 195     -26.852  21.120 -81.157  1.00 33.77           C  
ATOM    169  CA  GLU A 196     -24.145  22.955 -83.027  1.00 39.79           C  
ATOM    170  CA  HIS A 197     -22.166  19.724 -83.407  1.00 34.63           C  
ATOM    171  CA  SER A 198     -24.397  16.777 -84.340  1.00 22.91           C  
ATOM    172  CA  ASP A 199     -25.545  15.724 -87.780  1.00 25.46           C  
ATOM    173  CA  CYS A 200     -28.714  13.850 -86.880  1.00 26.43           C  
ATOM    174  CA  ALA A 201     -29.800  13.066 -83.349  1.00 28.15           C  
ATOM    175  CA  PHE A 202     -31.981   9.984 -82.999  1.00 30.53           C  
ATOM    176  CA  MET A 203     -34.322   9.949 -80.056  1.00 30.61           C  
ATOM    177  CA  VAL A 204     -35.847   7.091 -78.095  1.00 20.65           C  
ATOM    178  CA  ASP A 205     -38.039   7.981 -75.114  1.00 29.43           C  
ATOM    179  CA  ASN A 206     -37.530   5.680 -72.142  1.00 22.56           C  
ATOM    180  CA  GLU A 207     -41.149   5.943 -70.894  1.00 20.12           C  
ATOM    181  CA  ALA A 208     -42.914   5.862 -74.253  1.00 11.03           C  
ATOM    182  CA  ILE A 209     -41.060   2.563 -74.759  1.00 10.08           C  
ATOM    183  CA  TYR A 210     -42.593   1.130 -71.608  1.00 22.92           C  
ATOM    184  CA  ASP A 211     -46.009   1.682 -73.075  1.00 23.58           C  
ATOM    185  CA  ILE A 212     -44.906  -0.499 -75.929  1.00 23.63           C  
ATOM    186  CA  CYS A 213     -43.898  -3.106 -73.333  1.00 28.44           C  
ATOM    187  CA  ARG A 214     -47.263  -2.841 -71.645  1.00 40.94           C  
ATOM    188  CA  ARG A 215     -49.539  -2.326 -74.665  1.00 38.84           C  
ATOM    189  CA  ASN A 216     -47.660  -4.049 -77.476  1.00 31.32           C  
ATOM    190  CA  LEU A 217     -46.039  -7.030 -75.844  1.00 40.55           C  
ATOM    191  CA  ASP A 218     -47.713  -7.182 -72.458  1.00 57.49           C  
ATOM    192  CA  ILE A 219     -45.355  -7.244 -69.459  1.00 59.12           C  
ATOM    193  CA  GLU A 220     -45.353  -5.125 -66.310  1.00 67.12           C  
ATOM    194  CA  ARG A 221     -41.939  -6.658 -65.654  1.00 69.11           C  
ATOM    195  CA  PRO A 222     -39.798  -4.660 -68.100  1.00 53.30           C  
ATOM    196  CA  THR A 223     -36.203  -4.647 -66.919  1.00 43.24           C  
ATOM    197  CA  TYR A 224     -33.929  -1.943 -68.269  1.00 35.46           C  
ATOM    198  CA  THR A 225     -32.354  -4.916 -69.982  1.00 40.10           C  
ATOM    199  CA  ASN A 226     -35.444  -4.931 -72.189  1.00 30.22           C  
ATOM    200  CA  LEU A 227     -35.788  -1.353 -73.321  1.00 16.19           C  
ATOM    201  CA  ASN A 228     -32.195  -1.910 -74.281  1.00 22.59           C  
ATOM    202  CA  ARG A 229     -33.113  -4.980 -76.362  1.00 16.14           C  
ATOM    203  CA  LEU A 230     -35.602  -2.784 -78.087  1.00  6.87           C  
ATOM    204  CA  ILE A 231     -33.471   0.189 -78.999  1.00 10.37           C  
ATOM    205  CA  GLY A 232     -30.977  -2.616 -79.402  1.00 21.17           C  
ATOM    206  CA  GLN A 233     -33.315  -3.536 -82.248  1.00 25.16           C  
ATOM    207  CA  ILE A 234     -34.292  -0.218 -83.801  1.00 17.99           C  
ATOM    208  CA  VAL A 235     -30.583   0.593 -83.808  1.00 12.48           C  
ATOM    209  CA  SER A 236     -29.710  -2.647 -85.547  1.00 22.42           C  
ATOM    210  CA  SER A 237     -31.949  -1.426 -88.332  1.00 23.30           C  
ATOM    211  CA  ILE A 238     -29.999   1.794 -88.600  1.00 23.29           C  
ATOM    212  CA  THR A 239     -26.326   0.807 -88.885  1.00 44.11           C  
ATOM    213  CA  ALA A 240     -25.941  -2.966 -88.814  1.00 49.53           C  
ATOM    214  CA  SER A 241     -28.260  -4.028 -91.652  1.00 59.69           C  
ATOM    215  CA  LEU A 242     -28.168  -0.776 -93.587  1.00 65.02           C  
ATOM    216  CA  ARG A 243     -24.388  -0.661 -93.877  1.00 68.97           C  
ATOM    217  CA  PHE A 244     -25.214  -4.187 -95.058  1.00 81.08           C  
ATOM    218  CA  ASP A 245     -25.989  -4.774 -98.784  1.00 74.39           C  
ATOM    219  CA  GLY A 246     -29.590  -4.756 -99.931  1.00 59.02           C  
ATOM    220  CA  ALA A 247     -32.108  -3.887-102.638  1.00 50.29           C  
ATOM    221  CA  LEU A 248     -32.156  -0.196-101.673  1.00 38.92           C  
ATOM    222  CA  ASN A 249     -29.079   0.637 -99.561  1.00 32.91           C  
ATOM    223  CA  VAL A 250     -28.988   3.766 -97.422  1.00 30.37           C  
ATOM    224  CA  ASP A 251     -25.649   5.217 -96.290  1.00 25.27           C  
ATOM    225  CA  LEU A 252     -25.289   7.126 -92.998  1.00 17.06           C  
ATOM    226  CA  THR A 253     -24.793  10.359 -94.846  1.00 21.53           C  
ATOM    227  CA  GLU A 254     -28.029   9.453 -96.662  1.00 22.00           C  
ATOM    228  CA  PHE A 255     -29.840   9.968 -93.389  1.00 22.53           C  
ATOM    229  CA  GLN A 256     -28.844  13.438 -92.379  1.00 20.73           C  
ATOM    230  CA  THR A 257     -29.338  14.398 -96.043  1.00  9.52           C  
ATOM    231  CA  ASN A 258     -32.770  12.858 -96.526  1.00  6.03           C  
ATOM    232  CA  LEU A 259     -33.565  13.459 -92.829  1.00  6.83           C  
ATOM    233  CA  VAL A 260     -32.559  16.951 -91.720  1.00  9.49           C  
ATOM    234  CA  PRO A 261     -34.122  19.945 -93.413  1.00  7.37           C  
ATOM    235  CA  TYR A 262     -32.082  22.321 -91.304  1.00 16.29           C  
ATOM    236  CA  PRO A 263     -28.640  22.589 -89.619  1.00 16.05           C  
ATOM    237  CA  ARG A 264     -30.082  22.283 -86.133  1.00 22.39           C  
ATOM    238  CA  GLY A 265     -28.745  18.785 -85.335  1.00 23.25           C  
ATOM    239  CA  HIS A 266     -32.376  17.872 -85.838  1.00 11.08           C  
ATOM    240  CA  PHE A 267     -33.742  15.026 -83.891  1.00  8.40           C  
ATOM    241  CA  PRO A 268     -35.880  12.440 -85.621  1.00 17.01           C  
ATOM    242  CA  LEU A 269     -37.744   9.694 -83.661  1.00 12.30           C  
ATOM    243  CA  ALA A 270     -37.157   5.939 -83.840  1.00 11.58           C  
ATOM    244  CA  THR A 271     -40.049   3.555 -84.450  1.00 13.25           C  
ATOM    245  CA  TYR A 272     -40.237  -0.155 -85.078  1.00 18.93           C  
ATOM    246  CA  ALA A 273     -43.061  -2.132 -86.647  1.00 29.84           C  
ATOM    247  CA  PRO A 274     -43.348  -5.820 -85.747  1.00 34.85           C  
ATOM    248  CA  VAL A 275     -43.211  -5.239 -82.018  1.00 39.09           C  
ATOM    249  CA  ILE A 276     -45.371  -8.265 -81.435  1.00 46.85           C  
ATOM    250  CA  SER A 277     -44.978 -10.636 -78.464  1.00 55.16           C  
ATOM    251  CA  ALA A 278     -43.217 -13.978 -78.960  1.00 66.26           C  
ATOM    252  CA  GLU A 279     -45.688 -15.873 -76.830  1.00 78.70           C  
ATOM    253  CA  LYS A 280     -49.060 -14.251 -76.588  1.00 82.76           C  
ATOM    254  CA  ALA A 281     -50.675 -13.367 -79.865  1.00 79.12           C  
ATOM    255  CA  TYR A 282     -49.579 -14.721 -83.197  1.00 80.90           C  
ATOM    256  CA  HIS A 283     -50.588 -13.183 -86.413  1.00 75.09           C  
ATOM    257  CA  GLU A 284     -46.844 -12.666 -87.145  1.00 59.49           C  
ATOM    258  CA  GLN A 285     -47.460 -13.009 -90.930  1.00 39.32           C  
ATOM    259  CA  LEU A 286     -48.399  -9.387 -91.175  1.00 34.04           C  
ATOM    260  CA  SER A 287     -47.594  -8.401 -94.773  1.00 31.22           C  
ATOM    261  CA  VAL A 288     -45.940  -5.063 -95.397  1.00 29.39           C  
ATOM    262  CA  ALA A 289     -49.250  -3.331 -95.961  1.00 32.21           C  
ATOM    263  CA  GLU A 290     -49.726  -3.855 -92.212  1.00 36.32           C  
ATOM    264  CA  ILE A 291     -46.358  -3.315 -90.538  1.00 29.52           C  
ATOM    265  CA  THR A 292     -46.045   0.079 -92.248  1.00 17.98           C  
ATOM    266  CA  ASN A 293     -49.358   1.330 -91.044  1.00 34.10           C  
ATOM    267  CA  ALA A 294     -48.278   0.195 -87.583  1.00 30.79           C  
ATOM    268  CA  CYS A 295     -45.535   2.774 -87.590  1.00 13.70           C  
ATOM    269  CA  PHE A 296     -47.647   5.898 -87.764  1.00 21.47           C  
ATOM    270  CA  GLU A 297     -50.086   4.973 -85.024  1.00 31.40           C  
ATOM    271  CA  PRO A 298     -48.610   6.945 -82.116  1.00 27.43           C  
ATOM    272  CA  ALA A 299     -48.683   3.972 -79.747  1.00 26.57           C  
ATOM    273  CA  ASN A 300     -45.567   2.428 -81.182  1.00 27.39           C  
ATOM    274  CA  GLN A 301     -42.851   4.975 -81.503  1.00 35.05           C  
ATOM    275  CA  MET A 302     -40.378   4.847 -78.665  1.00 37.27           C  
ATOM    276  CA  VAL A 303     -41.175   8.493 -77.882  1.00 36.82           C  
ATOM    277  CA  LYS A 304     -43.882  10.287 -75.896  1.00 51.41           C  
ATOM    278  CA  CYS A 305     -44.241  12.764 -78.730  1.00 60.84           C  
ATOM    279  CA  ASP A 306     -47.572  11.437 -79.997  1.00 66.94           C  
ATOM    280  CA  PRO A 307     -48.170  13.209 -83.363  1.00 67.26           C  
ATOM    281  CA  ARG A 308     -50.389  15.590 -81.401  1.00 79.29           C  
ATOM    282  CA  HIS A 309     -49.997  17.969 -84.350  1.00 80.11           C  
ATOM    283  CA  GLY A 310     -46.392  17.582 -85.372  1.00 55.66           C  
ATOM    284  CA  LYS A 311     -46.340  17.331 -89.136  1.00 30.92           C  
ATOM    285  CA  TYR A 312     -43.787  14.854 -90.369  1.00 21.10           C  
ATOM    286  CA  MET A 313     -41.230  16.502 -92.637  1.00  9.30           C  
ATOM    287  CA  ALA A 314     -39.187  13.487 -93.655  1.00 10.29           C  
ATOM    288  CA  CYS A 315     -39.286   9.797 -92.829  1.00 12.21           C  
ATOM    289  CA  CYS A 316     -36.696   7.139 -93.584  1.00 15.81           C  
ATOM    290  CA  LEU A 317     -38.583   3.904 -93.825  1.00  8.50           C  
ATOM    291  CA  LEU A 318     -35.938   1.272 -93.317  1.00 15.06           C  
ATOM    292  CA  TYR A 319     -37.365  -2.131 -94.147  1.00 21.99           C  
ATOM    293  CA  ARG A 320     -35.605  -5.437 -93.737  1.00 31.61           C  
ATOM    294  CA  GLY A 321     -36.543  -8.981 -94.673  1.00 40.46           C  
ATOM    295  CA  ASP A 322     -38.802 -10.176 -97.491  1.00 51.76           C  
ATOM    296  CA  VAL A 323     -40.236  -7.007 -99.034  1.00 45.09           C  
ATOM    297  CA  VAL A 324     -41.334  -6.313-102.629  1.00 43.42           C  
ATOM    298  CA  PRO A 325     -40.478  -2.747-103.664  1.00 48.35           C  
ATOM    299  CA  LYS A 326     -43.961  -2.381-105.147  1.00 35.28           C  
ATOM    300  CA  ASP A 327     -45.463  -3.498-101.865  1.00 25.97           C  
ATOM    301  CA  VAL A 328     -43.667  -0.504-100.411  1.00 23.06           C  
ATOM    302  CA  ASN A 329     -44.090   1.823-103.371  1.00 29.42           C  
ATOM    303  CA  ALA A 330     -47.798   1.313-102.681  1.00 22.83           C  
ATOM    304  CA  ALA A 331     -48.094   0.814 -98.948  1.00 23.95           C  
ATOM    305  CA  ILE A 332     -46.459   4.222 -98.750  1.00 18.32           C  
ATOM    306  CA  ALA A 333     -48.636   5.588-101.551  1.00 16.38           C  
ATOM    307  CA  THR A 334     -51.724   4.609 -99.576  1.00 20.68           C  
ATOM    308  CA  ILE A 335     -50.245   6.523 -96.647  1.00 22.91           C  
ATOM    309  CA  LYS A 336     -49.277   9.621 -98.638  1.00 41.56           C  
ATOM    310  CA  THR A 337     -53.018   9.943 -99.175  1.00 64.14           C  
ATOM    311  CA  LYS A 338     -54.379   9.389 -95.659  1.00 77.19           C  
ATOM    312  CA  ARG A 339     -54.061  13.139 -95.066  1.00 89.49           C  
ATOM    313  CA  THR A 340     -54.785  12.707 -91.362  1.00 90.64           C  
ATOM    314  CA  ILE A 341     -51.031  12.009 -91.464  1.00 81.76           C  
ATOM    315  CA  GLN A 342     -50.424  15.556 -92.754  1.00 70.01           C  
ATOM    316  CA  PHE A 343     -46.821  16.077 -93.973  1.00 55.06           C  
ATOM    317  CA  VAL A 344     -45.202  19.481 -94.068  1.00 59.97           C  
ATOM    318  CA  ASP A 345     -46.094  21.895 -96.861  1.00 59.27           C  
ATOM    319  CA  TRP A 346     -42.696  22.742 -98.282  1.00 39.96           C  
ATOM    320  CA  CYS A 347     -42.233  19.046 -98.624  1.00 28.86           C  
ATOM    321  CA  PRO A 348     -43.760  17.249-101.615  1.00 32.22           C  
ATOM    322  CA  THR A 349     -42.394  13.820-100.923  1.00 30.77           C  
ATOM    323  CA  GLY A 350     -40.496  12.990 -97.745  1.00 18.15           C  
ATOM    324  CA  PHE A 351     -40.209   9.209 -97.785  1.00 14.27           C  
ATOM    325  CA  LYS A 352     -36.777   7.618 -97.982  1.00 12.21           C  
ATOM    326  CA  VAL A 353     -37.460   3.946 -98.654  1.00  2.00           C  
ATOM    327  CA  GLY A 354     -34.587   1.839 -97.358  1.00  8.12           C  
ATOM    328  CA  ILE A 355     -34.795  -1.848 -98.215  1.00 23.70           C  
ATOM    329  CA  ASN A 356     -32.498  -4.465 -96.748  1.00 42.13           C  
ATOM    330  CA  TYR A 357     -32.530  -8.219 -97.315  1.00 64.11           C  
ATOM    331  CA  GLU A 358     -31.770 -10.217 -94.163  1.00 58.76           C  
ATOM    332  CA  PRO A 359     -34.900 -10.219 -91.932  1.00 58.21           C  
ATOM    333  CA  PRO A 360     -34.575  -8.988 -88.296  1.00 62.52           C  
ATOM    334  CA  THR A 361     -32.925 -11.136 -85.632  1.00 62.58           C  
ATOM    335  CA  VAL A 362     -34.643 -11.505 -82.295  1.00 62.67           C  
ATOM    336  CA  VAL A 363     -32.984 -12.539 -79.061  1.00 70.29           C  
ATOM    337  CA  PRO A 364     -33.171 -16.374 -78.775  1.00 77.84           C  
ATOM    338  CA  GLY A 365     -35.635 -16.137 -75.923  1.00 71.52           C  
ATOM    339  CA  GLY A 366     -36.318 -12.607 -74.765  1.00 73.65           C  
ATOM    340  CA  ASP A 367     -39.854 -11.479 -75.576  1.00 77.76           C  
ATOM    341  CA  LEU A 368     -39.613 -10.163 -79.138  1.00 76.32           C  
ATOM    342  CA  ALA A 369     -41.919 -11.964 -81.574  1.00 72.14           C  
ATOM    343  CA  LYS A 370     -39.523 -12.734 -84.454  1.00 74.90           C  
ATOM    344  CA  VAL A 371     -41.143 -11.855 -87.763  1.00 65.43           C  
ATOM    345  CA  GLN A 372     -39.721 -12.114 -91.284  1.00 55.20           C  
ATOM    346  CA  ARG A 373     -39.862  -8.410 -92.012  1.00 39.38           C  
ATOM    347  CA  ALA A 374     -39.892  -5.151 -90.044  1.00 33.17           C  
ATOM    348  CA  VAL A 375     -40.058  -1.373 -90.436  1.00 31.96           C  
ATOM    349  CA  CYS A 376     -37.696   0.823 -88.427  1.00 21.72           C  
ATOM    350  CA  MET A 377     -39.010   4.170 -89.522  1.00  7.45           C  
ATOM    351  CA  LEU A 378     -37.457   7.256 -88.068  1.00 12.52           C  
ATOM    352  CA  SER A 379     -38.411  10.842 -88.780  1.00 19.82           C  
ATOM    353  CA  ASN A 380     -38.363  14.528 -88.007  1.00 21.23           C  
ATOM    354  CA  THR A 381     -41.785  15.582 -86.769  1.00 19.77           C  
ATOM    355  CA  THR A 382     -42.910  19.072 -85.855  1.00  9.75           C  
ATOM    356  CA  ALA A 383     -44.144  17.041 -82.929  1.00  4.98           C  
ATOM    357  CA  ILE A 384     -41.084  17.416 -80.780  1.00  8.75           C  
ATOM    358  CA  ALA A 385     -42.150  21.078 -80.649  1.00 26.84           C  
ATOM    359  CA  GLU A 386     -43.918  19.521 -77.699  1.00 36.29           C  
ATOM    360  CA  ALA A 387     -41.351  17.233 -76.058  1.00 30.31           C  
ATOM    361  CA  TRP A 388     -38.801  20.077 -76.084  1.00 23.21           C  
ATOM    362  CA  ALA A 389     -41.370  22.525 -74.775  1.00 19.05           C  
ATOM    363  CA  ARG A 390     -42.437  20.291 -71.881  1.00 30.76           C  
ATOM    364  CA  LEU A 391     -38.781  19.714 -71.044  1.00 21.31           C  
ATOM    365  CA  ASP A 392     -37.800  23.330 -71.260  1.00 26.95           C  
ATOM    366  CA  HIS A 393     -40.615  24.471 -68.998  1.00 29.62           C  
ATOM    367  CA  LYS A 394     -39.371  21.951 -66.409  1.00 18.81           C  
ATOM    368  CA  PHE A 395     -35.985  23.648 -66.394  1.00 13.87           C  
ATOM    369  CA  ASP A 396     -37.352  27.132 -65.768  1.00 22.36           C  
ATOM    370  CA  LEU A 397     -39.389  26.111 -62.782  1.00 18.90           C  
ATOM    371  CA  MET A 398     -36.193  25.053 -61.031  1.00 15.44           C  
ATOM    372  CA  TYR A 399     -33.853  27.641 -62.454  1.00 26.50           C  
ATOM    373  CA  ALA A 400     -36.509  30.125 -61.447  1.00 24.37           C  
ATOM    374  CA  LYS A 401     -35.360  29.253 -57.914  1.00 28.08           C  
ATOM    375  CA  ARG A 402     -31.819  28.234 -58.723  1.00 21.94           C  
ATOM    376  CA  ALA A 403     -32.671  24.879 -57.185  1.00  8.20           C  
ATOM    377  CA  PHE A 404     -29.581  22.695 -57.579  1.00 16.11           C  
ATOM    378  CA  VAL A 405     -27.616  25.487 -59.169  1.00 14.70           C  
ATOM    379  CA  HIS A 406     -24.915  25.666 -56.542  1.00 13.33           C  
ATOM    380  CA  TRP A 407     -24.003  22.183 -57.666  1.00 12.68           C  
ATOM    381  CA  TYR A 408     -22.855  23.312 -61.056  1.00 24.39           C  
ATOM    382  CA  VAL A 409     -21.464  26.733 -60.305  1.00 29.93           C  
ATOM    383  CA  GLY A 410     -19.155  25.114 -57.818  1.00 34.36           C  
ATOM    384  CA  GLU A 411     -18.161  22.979 -60.762  1.00 28.17           C  
ATOM    385  CA  GLY A 412     -16.916  25.537 -63.249  1.00 30.26           C  
ATOM    386  CA  MET A 413     -20.087  26.893 -64.826  1.00 34.63           C  
ATOM    387  CA  GLU A 414     -21.899  30.170 -64.430  1.00 39.73           C  
ATOM    388  CA  GLU A 415     -25.240  31.948 -64.512  1.00 54.92           C  
ATOM    389  CA  GLY A 416     -24.162  32.287 -68.103  1.00 35.87           C  
ATOM    390  CA  GLU A 417     -24.150  28.716 -69.331  1.00 29.35           C  
ATOM    391  CA  PHE A 418     -27.593  28.123 -67.853  1.00 35.92           C  
ATOM    392  CA  SER A 419     -29.407  31.303 -68.856  1.00 40.42           C  
ATOM    393  CA  GLU A 420     -27.538  31.313 -72.134  1.00 34.69           C  
ATOM    394  CA  ALA A 421     -28.431  27.680 -72.921  1.00 28.13           C  
ATOM    395  CA  ARG A 422     -32.014  28.346 -72.037  1.00 25.50           C  
ATOM    396  CA  GLU A 423     -32.185  31.155 -74.586  1.00 31.02           C  
ATOM    397  CA  ASP A 424     -30.562  28.553 -76.839  1.00 30.57           C  
ATOM    398  CA  MET A 425     -33.372  26.049 -76.763  1.00 26.91           C  
ATOM    399  CA  ALA A 426     -35.864  28.913 -76.804  1.00 35.84           C  
ATOM    400  CA  ALA A 427     -34.971  29.313 -80.502  1.00 38.28           C  
ATOM    401  CA  LEU A 428     -35.446  25.566 -80.825  1.00 39.30           C  
ATOM    402  CA  GLU A 429     -39.054  25.971 -79.736  1.00 50.75           C  
ATOM    403  CA  LYS A 430     -39.422  28.686 -82.375  1.00 48.67           C  
ATOM    404  CA  ASP A 431     -37.416  26.744 -84.924  1.00 47.21           C  
ATOM    405  CA  TYR A 432     -39.460  23.547 -84.671  1.00 37.28           C  
ATOM    406  CA  GLU A 433     -42.466  25.865 -84.828  1.00 53.57           C  
ATOM    407  CA  GLU A 434     -41.527  27.921 -87.871  1.00 61.61           C  
ATOM    408  CA  VAL A 435     -40.330  25.032 -90.051  1.00 65.03           C  
ATOM    409  CA  GLY A 436     -43.915  23.880 -89.709  1.00 73.86           C  
ATOM    410  CA  VAL A 437     -47.427  24.946 -88.687  1.00 88.51           C  
ATOM    411  CA  ASP A 438     -46.957  27.571 -91.428  1.00 92.71           C  
ATOM    412  CA  SER A 439     -47.204  27.584 -95.232  1.00 87.57           C  
TER     413      SER A 439                                                      
ATOM    414  CA  ARG B   2     -14.116   4.904 -52.253  1.00 57.69           C  
ATOM    415  CA  GLU B   3     -13.983   5.038 -48.430  1.00 51.20           C  
ATOM    416  CA  ILE B   4     -15.245   6.495 -45.119  1.00 35.02           C  
ATOM    417  CA  VAL B   5     -14.060   6.596 -41.486  1.00 21.82           C  
ATOM    418  CA  HIS B   6     -16.647   6.160 -38.745  1.00 20.02           C  
ATOM    419  CA  ILE B   7     -16.459   8.266 -35.586  1.00 26.45           C  
ATOM    420  CA  GLN B   8     -17.848   7.081 -32.190  1.00 29.82           C  
ATOM    421  CA  ALA B   9     -18.066  10.355 -30.236  1.00 28.61           C  
ATOM    422  CA  GLY B  10     -19.140  10.132 -26.606  1.00 25.81           C  
ATOM    423  CA  GLN B  11     -20.703   7.122 -24.882  1.00 23.23           C  
ATOM    424  CA  CYS B  12     -23.913   6.959 -26.841  1.00 16.01           C  
ATOM    425  CA  GLY B  13     -22.246   7.502 -30.166  1.00 26.51           C  
ATOM    426  CA  ASN B  14     -19.945   4.840 -28.826  1.00 26.78           C  
ATOM    427  CA  GLN B  15     -22.540   2.378 -27.494  1.00 25.31           C  
ATOM    428  CA  ILE B  16     -24.079   2.620 -30.962  1.00 25.94           C  
ATOM    429  CA  GLY B  17     -20.691   2.072 -32.544  1.00 26.06           C  
ATOM    430  CA  ALA B  18     -20.820  -1.386 -31.043  1.00 29.60           C  
ATOM    431  CA  LYS B  19     -24.198  -1.925 -32.673  1.00 37.53           C  
ATOM    432  CA  PHE B  20     -23.349  -0.286 -35.974  1.00 26.95           C  
ATOM    433  CA  TRP B  21     -20.312  -2.491 -36.197  1.00 23.63           C  
ATOM    434  CA  GLU B  22     -22.074  -5.474 -34.703  1.00 32.17           C  
ATOM    435  CA  VAL B  23     -24.345  -5.311 -37.737  1.00 32.98           C  
ATOM    436  CA  ILE B  24     -22.246  -4.039 -40.610  1.00 34.33           C  
ATOM    437  CA  SER B  25     -19.670  -6.758 -39.936  1.00 47.08           C  
ATOM    438  CA  ASP B  26     -22.207  -9.583 -40.341  1.00 58.11           C  
ATOM    439  CA  GLU B  27     -23.350  -7.631 -43.417  1.00 61.30           C  
ATOM    440  CA  HIS B  28     -19.756  -8.176 -44.478  1.00 62.52           C  
ATOM    441  CA  GLY B  29     -18.888 -11.531 -42.887  1.00 75.22           C  
ATOM    442  CA  ILE B  30     -16.248 -10.200 -40.509  1.00 81.60           C  
ATOM    443  CA  ASP B  31     -16.046 -12.183 -37.265  1.00 89.43           C  
ATOM    444  CA  PRO B  32     -14.604 -10.545 -34.109  1.00 90.13           C  
ATOM    445  CA  THR B  33     -10.952 -10.641 -35.183  1.00 92.84           C  
ATOM    446  CA  GLY B  34     -11.672 -13.191 -37.895  1.00 92.58           C  
ATOM    447  CA  SER B  35     -11.793 -12.319 -41.575  1.00 96.36           C  
ATOM    448  CA  TYR B  36     -14.311 -12.576 -44.360  1.00 99.20           C  
ATOM    449  CA  HIS B  37     -16.491 -15.666 -43.821  1.00100.00           C  
ATOM    450  CA  GLY B  38     -18.917 -13.973 -46.194  1.00 99.24           C  
ATOM    451  CA  ASP B  39     -21.676 -16.307 -47.286  1.00 96.42           C  
ATOM    452  CA  SER B  40     -21.072 -14.685 -50.666  1.00 92.02           C  
ATOM    453  CA  ASP B  41     -18.187 -13.099 -52.580  1.00 85.29           C  
ATOM    454  CA  LEU B  42     -19.774  -9.688 -53.155  1.00 82.58           C  
ATOM    455  CA  GLN B  43     -19.616  -8.607 -49.502  1.00 78.10           C  
ATOM    456  CA  LEU B  44     -15.892  -8.105 -50.068  1.00 74.03           C  
ATOM    457  CA  GLU B  47     -15.144  -6.269 -53.307  1.00 73.64           C  
ATOM    458  CA  ARG B  48     -16.184  -3.031 -51.622  1.00 71.38           C  
ATOM    459  CA  ILE B  49     -15.449  -3.555 -47.905  1.00 67.67           C  
ATOM    460  CA  ASN B  50     -12.499  -1.160 -47.979  1.00 63.33           C  
ATOM    461  CA  VAL B  51     -15.067   1.569 -47.359  1.00 57.47           C  
ATOM    462  CA  TYR B  52     -14.895   0.545 -43.669  1.00 58.87           C  
ATOM    463  CA  TYR B  53     -11.747  -1.533 -43.096  1.00 66.14           C  
ATOM    464  CA  ASN B  54      -8.001  -1.903 -43.660  1.00 80.80           C  
ATOM    465  CA  GLU B  55      -5.669  -4.647 -44.896  1.00 96.22           C  
ATOM    466  CA  ALA B  56      -2.870  -5.665 -42.507  1.00100.00           C  
ATOM    467  CA  ALA B  57      -2.703  -9.375 -41.720  1.00100.00           C  
ATOM    468  CA  GLY B  58      -4.915 -11.182 -44.233  1.00100.00           C  
ATOM    469  CA  ASN B  59      -7.772 -12.257 -41.990  1.00 97.91           C  
ATOM    470  CA  LYS B  60      -7.833  -9.073 -39.961  1.00 92.73           C  
ATOM    471  CA  TYR B  61      -9.805  -6.340 -41.699  1.00 78.35           C  
ATOM    472  CA  VAL B  62     -10.046  -3.787 -38.898  1.00 62.05           C  
ATOM    473  CA  PRO B  63     -12.900  -1.294 -38.700  1.00 43.28           C  
ATOM    474  CA  ARG B  64     -11.636   2.152 -39.583  1.00 32.71           C  
ATOM    475  CA  ALA B  65     -13.501   4.198 -36.994  1.00 25.69           C  
ATOM    476  CA  ILE B  66     -12.558   6.407 -34.076  1.00 24.20           C  
ATOM    477  CA  LEU B  67     -13.616   5.944 -30.453  1.00 28.09           C  
ATOM    478  CA  VAL B  68     -13.624   9.294 -28.694  1.00 30.81           C  
ATOM    479  CA  ASP B  69     -14.692   9.534 -25.043  1.00 35.04           C  
ATOM    480  CA  LEU B  70     -13.650  11.137 -21.735  1.00 45.71           C  
ATOM    481  CA  GLU B  71     -15.118   8.309 -19.639  1.00 58.53           C  
ATOM    482  CA  PRO B  72     -12.969   5.193 -19.539  1.00 66.30           C  
ATOM    483  CA  GLY B  73     -15.588   2.710 -18.256  1.00 75.05           C  
ATOM    484  CA  THR B  74     -17.550   3.179 -21.489  1.00 81.80           C  
ATOM    485  CA  MET B  75     -14.994   2.287 -24.156  1.00 81.14           C  
ATOM    486  CA  ASP B  76     -13.821  -0.249 -21.560  1.00 82.65           C  
ATOM    487  CA  SER B  77     -17.234  -1.924 -21.838  1.00 78.89           C  
ATOM    488  CA  VAL B  78     -17.272  -1.787 -25.611  1.00 77.54           C  
ATOM    489  CA  ARG B  79     -13.719  -3.087 -25.699  1.00 78.78           C  
ATOM    490  CA  SER B  80     -14.374  -5.763 -23.054  1.00 86.27           C  
ATOM    491  CA  GLY B  81     -17.462  -7.338 -24.608  1.00 94.03           C  
ATOM    492  CA  PRO B  82     -18.353  -8.981 -27.969  1.00 94.10           C  
ATOM    493  CA  PHE B  83     -16.847  -7.471 -31.138  1.00 86.73           C  
ATOM    494  CA  GLY B  84     -14.970  -5.151 -28.801  1.00 88.24           C  
ATOM    495  CA  GLN B  85     -11.652  -6.794 -29.675  1.00 95.55           C  
ATOM    496  CA  ILE B  86     -11.550  -5.906 -33.387  1.00 87.65           C  
ATOM    497  CA  PHE B  87     -10.658  -2.230 -33.099  1.00 78.40           C  
ATOM    498  CA  ARG B  88      -6.911  -1.622 -33.177  1.00 85.18           C  
ATOM    499  CA  PRO B  89      -6.105  -0.035 -29.762  1.00 88.19           C  
ATOM    500  CA  ASP B  90      -4.766   2.948 -31.670  1.00 82.18           C  
ATOM    501  CA  ASN B  91      -8.453   3.723 -32.375  1.00 76.34           C  
ATOM    502  CA  PHE B  92      -9.290   4.301 -28.711  1.00 70.61           C  
ATOM    503  CA  VAL B  93      -8.814   8.015 -28.072  1.00 72.18           C  
ATOM    504  CA  PHE B  94      -9.837   8.132 -24.426  1.00 80.56           C  
ATOM    505  CA  GLY B  95      -9.794  11.006 -21.964  1.00 75.50           C  
ATOM    506  CA  GLN B  96      -9.559   9.548 -18.462  1.00 73.82           C  
ATOM    507  CA  SER B  97     -10.393  13.071 -17.258  1.00 69.76           C  
ATOM    508  CA  GLY B  98     -13.767  13.793 -15.678  1.00 66.97           C  
ATOM    509  CA  ALA B  99     -16.123  13.269 -18.628  1.00 57.56           C  
ATOM    510  CA  GLY B 100     -18.478  15.813 -17.040  1.00 39.29           C  
ATOM    511  CA  ASN B 101     -21.893  16.132 -18.648  1.00 26.36           C  
ATOM    512  CA  ASN B 102     -21.027  19.618 -19.818  1.00 22.28           C  
ATOM    513  CA  TRP B 103     -20.908  20.597 -23.492  1.00 16.37           C  
ATOM    514  CA  ALA B 104     -18.388  23.151 -22.387  1.00  5.22           C  
ATOM    515  CA  LYS B 105     -16.361  20.562 -20.529  1.00  4.60           C  
ATOM    516  CA  GLY B 106     -15.890  18.429 -23.616  1.00 12.37           C  
ATOM    517  CA  HIS B 107     -15.560  21.186 -26.185  1.00 13.18           C  
ATOM    518  CA  TYR B 108     -13.416  23.885 -24.561  1.00 18.05           C  
ATOM    519  CA  THR B 109     -11.712  22.613 -21.478  1.00 18.45           C  
ATOM    520  CA  GLU B 110     -11.409  18.895 -21.251  1.00 31.29           C  
ATOM    521  CA  GLY B 111     -12.049  17.761 -24.808  1.00 29.91           C  
ATOM    522  CA  ALA B 112      -9.966  20.478 -26.415  1.00 32.78           C  
ATOM    523  CA  GLU B 113      -6.894  18.721 -25.076  1.00 38.49           C  
ATOM    524  CA  LEU B 114      -7.741  15.215 -26.231  1.00 39.83           C  
ATOM    525  CA  VAL B 115      -8.559  16.626 -29.677  1.00 42.29           C  
ATOM    526  CA  ASP B 116      -5.049  16.823 -31.136  1.00 44.37           C  
ATOM    527  CA  SER B 117      -4.468  13.200 -30.093  1.00 40.63           C  
ATOM    528  CA  VAL B 118      -7.611  12.412 -32.079  1.00 33.60           C  
ATOM    529  CA  LEU B 119      -7.077  14.448 -35.240  1.00 36.30           C  
ATOM    530  CA  ASP B 120      -3.738  12.663 -35.259  1.00 42.58           C  
ATOM    531  CA  VAL B 121      -5.475   9.368 -35.848  1.00 44.32           C  
ATOM    532  CA  VAL B 122      -8.337  10.739 -37.973  1.00 56.75           C  
ATOM    533  CA  ARG B 123      -5.424  11.575 -40.318  1.00 68.40           C  
ATOM    534  CA  LYS B 124      -3.706   8.232 -39.939  1.00 66.99           C  
ATOM    535  CA  GLU B 125      -6.992   6.683 -41.083  1.00 66.66           C  
ATOM    536  CA  SER B 126      -7.786   9.230 -43.779  1.00 63.06           C  
ATOM    537  CA  GLU B 127      -4.338   8.892 -45.331  1.00 70.76           C  
ATOM    538  CA  SER B 128      -4.930   5.145 -45.204  1.00 73.77           C  
ATOM    539  CA  CYS B 129      -5.277   4.493 -48.908  1.00 76.00           C  
ATOM    540  CA  ASP B 130      -7.255   4.906 -52.128  1.00 68.67           C  
ATOM    541  CA  CYS B 131      -9.703   7.819 -52.088  1.00 61.48           C  
ATOM    542  CA  LEU B 132     -11.632   9.104 -49.085  1.00 38.17           C  
ATOM    543  CA  GLN B 133     -15.336   9.895 -49.427  1.00 26.44           C  
ATOM    544  CA  GLY B 134     -16.337  11.156 -45.963  1.00 14.57           C  
ATOM    545  CA  PHE B 135     -16.703  10.313 -42.263  1.00 11.67           C  
ATOM    546  CA  GLN B 136     -19.595   8.818 -40.292  1.00 18.92           C  
ATOM    547  CA  LEU B 137     -20.308  10.461 -36.946  1.00 22.98           C  
ATOM    548  CA  THR B 138     -22.363   8.980 -34.121  1.00 14.93           C  
ATOM    549  CA  HIS B 139     -23.185  10.726 -30.865  1.00  8.47           C  
ATOM    550  CA  SER B 140     -25.877  12.272 -28.712  1.00 11.41           C  
ATOM    551  CA  LEU B 141     -26.567  15.971 -28.462  1.00  6.65           C  
ATOM    552  CA  GLY B 142     -27.349  15.611 -24.785  1.00  6.55           C  
ATOM    553  CA  GLY B 143     -24.003  15.312 -23.012  1.00  9.94           C  
ATOM    554  CA  GLY B 144     -20.337  16.263 -22.872  1.00 14.56           C  
ATOM    555  CA  THR B 145     -18.282  13.779 -24.867  1.00 17.53           C  
ATOM    556  CA  GLY B 146     -21.122  13.709 -27.340  1.00 16.67           C  
ATOM    557  CA  SER B 147     -22.306  17.162 -28.290  1.00 22.04           C  
ATOM    558  CA  GLY B 148     -19.273  19.132 -27.201  1.00 29.36           C  
ATOM    559  CA  MET B 149     -16.217  17.033 -27.962  1.00 33.89           C  
ATOM    560  CA  GLY B 150     -17.757  15.300 -30.968  1.00 29.61           C  
ATOM    561  CA  THR B 151     -19.036  18.571 -32.319  1.00 20.03           C  
ATOM    562  CA  LEU B 152     -15.463  19.764 -32.112  1.00 23.56           C  
ATOM    563  CA  LEU B 153     -14.044  16.711 -33.802  1.00 21.87           C  
ATOM    564  CA  ILE B 154     -16.018  17.702 -36.846  1.00 28.64           C  
ATOM    565  CA  SER B 155     -15.324  21.435 -36.796  1.00 27.48           C  
ATOM    566  CA  LYS B 156     -11.705  20.286 -37.131  1.00 24.69           C  
ATOM    567  CA  ILE B 157     -12.404  17.541 -39.649  1.00 25.92           C  
ATOM    568  CA  ARG B 158     -14.257  20.086 -41.874  1.00 28.06           C  
ATOM    569  CA  GLU B 159     -11.187  22.316 -41.898  1.00 32.76           C  
ATOM    570  CA  GLU B 160      -8.912  19.469 -42.827  1.00 44.52           C  
ATOM    571  CA  TYR B 161     -10.912  18.133 -45.757  1.00 42.02           C  
ATOM    572  CA  PRO B 162     -13.710  20.529 -46.787  1.00 41.21           C  
ATOM    573  CA  ASP B 163     -13.932  18.155 -49.747  1.00 34.05           C  
ATOM    574  CA  ARG B 164     -14.827  14.805 -48.222  1.00 30.51           C  
ATOM    575  CA  ILE B 165     -18.400  14.586 -46.887  1.00 27.51           C  
ATOM    576  CA  MET B 166     -19.707  14.454 -43.316  1.00 28.59           C  
ATOM    577  CA  ASN B 167     -22.728  12.396 -42.375  1.00 16.68           C  
ATOM    578  CA  THR B 168     -23.846  12.950 -38.843  1.00  9.00           C  
ATOM    579  CA  PHE B 169     -26.001  10.570 -36.844  1.00  9.96           C  
ATOM    580  CA  SER B 170     -27.369  12.586 -33.927  1.00 21.96           C  
ATOM    581  CA  VAL B 171     -29.590  11.377 -31.131  1.00 12.49           C  
ATOM    582  CA  VAL B 172     -31.490  14.627 -30.729  1.00 18.70           C  
ATOM    583  CA  PRO B 173     -33.021  14.983 -27.207  1.00 26.85           C  
ATOM    584  CA  SER B 174     -36.240  13.001 -27.137  1.00 33.91           C  
ATOM    585  CA  PRO B 175     -39.328  15.001 -26.125  1.00 38.63           C  
ATOM    586  CA  LYS B 176     -41.649  13.379 -23.530  1.00 49.10           C  
ATOM    587  CA  VAL B 177     -38.745  12.648 -21.140  1.00 44.20           C  
ATOM    588  CA  SER B 178     -35.158  13.886 -21.174  1.00 35.51           C  
ATOM    589  CA  ASP B 179     -32.515  11.366 -20.154  1.00 27.24           C  
ATOM    590  CA  THR B 180     -30.507  14.303 -18.823  1.00 22.55           C  
ATOM    591  CA  VAL B 181     -31.230  17.735 -17.356  1.00  4.27           C  
ATOM    592  CA  VAL B 182     -29.231  20.358 -19.175  1.00  2.00           C  
ATOM    593  CA  GLU B 183     -29.989  18.453 -22.371  1.00  6.26           C  
ATOM    594  CA  PRO B 184     -31.110  21.579 -24.332  1.00  5.92           C  
ATOM    595  CA  TYR B 185     -27.818  23.160 -23.300  1.00  3.28           C  
ATOM    596  CA  ASN B 186     -25.620  20.352 -24.571  1.00  2.15           C  
ATOM    597  CA  ALA B 187     -27.991  20.131 -27.561  1.00 11.48           C  
ATOM    598  CA  THR B 188     -28.609  23.633 -28.797  1.00 11.42           C  
ATOM    599  CA  LEU B 189     -24.843  24.006 -28.578  1.00 21.39           C  
ATOM    600  CA  SER B 190     -24.072  20.990 -30.723  1.00 25.22           C  
ATOM    601  CA  VAL B 191     -26.771  21.489 -33.396  1.00 36.12           C  
ATOM    602  CA  HIS B 192     -25.192  24.908 -33.839  1.00 29.68           C  
ATOM    603  CA  GLN B 193     -21.839  23.232 -34.758  1.00 28.32           C  
ATOM    604  CA  LEU B 194     -23.694  20.763 -36.990  1.00 26.76           C  
ATOM    605  CA  VAL B 195     -25.647  23.301 -39.117  1.00 24.52           C  
ATOM    606  CA  GLU B 196     -22.219  24.556 -39.999  1.00 26.77           C  
ATOM    607  CA  ASN B 197     -19.855  21.683 -40.640  1.00 20.71           C  
ATOM    608  CA  THR B 198     -21.358  18.233 -41.405  1.00 23.25           C  
ATOM    609  CA  ASP B 199     -23.493  18.204 -44.596  1.00 13.99           C  
ATOM    610  CA  GLU B 200     -25.837  15.255 -43.912  1.00 15.97           C  
ATOM    611  CA  THR B 201     -27.362  14.603 -40.490  1.00  7.39           C  
ATOM    612  CA  TYR B 202     -29.618  11.723 -39.529  1.00 21.59           C  
ATOM    613  CA  CYS B 203     -31.490  12.592 -36.293  1.00 27.96           C  
ATOM    614  CA  ILE B 204     -32.778   9.691 -34.238  1.00 26.43           C  
ATOM    615  CA  ASP B 205     -35.019   9.859 -31.132  1.00 27.21           C  
ATOM    616  CA  ASN B 206     -34.797   7.284 -28.372  1.00 14.83           C  
ATOM    617  CA  GLU B 207     -38.593   7.585 -27.959  1.00 17.09           C  
ATOM    618  CA  ALA B 208     -39.484   7.677 -31.635  1.00 10.42           C  
ATOM    619  CA  LEU B 209     -37.672   4.339 -31.584  1.00  3.99           C  
ATOM    620  CA  TYR B 210     -39.371   2.911 -28.540  1.00  8.93           C  
ATOM    621  CA  ASP B 211     -42.699   3.617 -30.188  1.00 20.39           C  
ATOM    622  CA  ILE B 212     -41.589   2.274 -33.547  1.00 32.33           C  
ATOM    623  CA  CYS B 213     -40.022  -0.580 -31.580  1.00 47.56           C  
ATOM    624  CA  PHE B 214     -42.856  -1.404 -29.188  1.00 52.60           C  
ATOM    625  CA  ARG B 215     -45.767  -1.122 -31.623  1.00 49.08           C  
ATOM    626  CA  THR B 216     -44.120  -1.875 -34.989  1.00 38.75           C  
ATOM    627  CA  LEU B 217     -42.272  -4.731 -33.289  1.00 36.97           C  
ATOM    628  CA  LYS B 218     -44.601  -6.056 -30.615  1.00 44.63           C  
ATOM    629  CA  LEU B 219     -41.299  -5.997 -28.676  1.00 44.21           C  
ATOM    630  CA  THR B 220     -42.258  -5.538 -24.998  1.00 48.44           C  
ATOM    631  CA  THR B 221     -38.776  -5.033 -23.480  1.00 49.51           C  
ATOM    632  CA  PRO B 222     -36.914  -2.775 -25.927  1.00 38.42           C  
ATOM    633  CA  THR B 223     -33.498  -2.617 -24.330  1.00 42.25           C  
ATOM    634  CA  TYR B 224     -31.071   0.054 -25.533  1.00 36.77           C  
ATOM    635  CA  GLY B 225     -29.146  -2.570 -27.459  1.00 39.14           C  
ATOM    636  CA  ASP B 226     -32.284  -2.839 -29.533  1.00 32.15           C  
ATOM    637  CA  LEU B 227     -32.888   0.828 -30.276  1.00 27.08           C  
ATOM    638  CA  ASN B 228     -29.229   1.029 -31.194  1.00 24.75           C  
ATOM    639  CA  HIS B 229     -29.626  -2.080 -33.290  1.00 22.57           C  
ATOM    640  CA  LEU B 230     -32.568  -0.599 -35.197  1.00 15.08           C  
ATOM    641  CA  VAL B 231     -30.684   2.632 -35.847  1.00 15.65           C  
ATOM    642  CA  SER B 232     -27.527   0.832 -36.972  1.00 16.58           C  
ATOM    643  CA  ALA B 233     -29.845  -0.983 -39.378  1.00 21.00           C  
ATOM    644  CA  THR B 234     -30.598   2.282 -41.179  1.00 15.77           C  
ATOM    645  CA  MET B 235     -27.036   3.634 -41.315  1.00 23.03           C  
ATOM    646  CA  SER B 236     -26.102   0.335 -43.007  1.00 28.79           C  
ATOM    647  CA  GLY B 237     -28.761   0.776 -45.680  1.00 27.46           C  
ATOM    648  CA  VAL B 238     -27.461   4.283 -46.302  1.00 29.06           C  
ATOM    649  CA  THR B 239     -23.696   4.013 -46.702  1.00 40.62           C  
ATOM    650  CA  THR B 240     -22.285   0.484 -46.958  1.00 50.30           C  
ATOM    651  CA  CYS B 241     -25.335  -0.511 -48.960  1.00 57.67           C  
ATOM    652  CA  LEU B 242     -24.853   1.919 -51.820  1.00 51.01           C  
ATOM    653  CA  ARG B 243     -21.275   0.755 -51.938  1.00 52.58           C  
ATOM    654  CA  PHE B 244     -22.826  -2.308 -53.493  1.00 49.65           C  
ATOM    655  CA  PRO B 245     -23.938  -2.777 -57.102  1.00 39.30           C  
ATOM    656  CA  GLY B 246     -27.405  -1.784 -58.269  1.00 31.10           C  
ATOM    657  CA  GLN B 247     -29.489  -1.079 -61.335  1.00 29.54           C  
ATOM    658  CA  LEU B 248     -29.405   2.499 -60.117  1.00 30.33           C  
ATOM    659  CA  ASN B 249     -26.868   3.054 -57.382  1.00 37.05           C  
ATOM    660  CA  ALA B 250     -25.953   6.216 -55.587  1.00 44.64           C  
ATOM    661  CA  ASP B 251     -23.368   7.098 -52.910  1.00 44.09           C  
ATOM    662  CA  LEU B 252     -23.111   9.631 -50.088  1.00 34.06           C  
ATOM    663  CA  ARG B 253     -22.755  12.425 -52.581  1.00 22.35           C  
ATOM    664  CA  LYS B 254     -25.705  11.478 -54.826  1.00 17.08           C  
ATOM    665  CA  LEU B 255     -27.549  11.252 -51.515  1.00 19.48           C  
ATOM    666  CA  ALA B 256     -26.113  14.600 -50.587  1.00 13.32           C  
ATOM    667  CA  VAL B 257     -26.358  16.222 -54.006  1.00  3.90           C  
ATOM    668  CA  ASN B 258     -30.013  15.189 -54.324  1.00  6.97           C  
ATOM    669  CA  MET B 259     -31.092  15.899 -50.811  1.00 20.47           C  
ATOM    670  CA  VAL B 260     -29.754  19.253 -49.842  1.00 14.83           C  
ATOM    671  CA  PRO B 261     -31.404  22.100 -51.706  1.00 18.97           C  
ATOM    672  CA  PHE B 262     -29.901  24.710 -49.419  1.00 21.66           C  
ATOM    673  CA  PRO B 263     -26.398  24.651 -47.768  1.00 28.77           C  
ATOM    674  CA  ARG B 264     -27.600  24.688 -44.151  1.00 33.46           C  
ATOM    675  CA  LEU B 265     -26.760  20.984 -44.305  1.00 20.85           C  
ATOM    676  CA  HIS B 266     -30.253  20.074 -43.338  1.00 17.05           C  
ATOM    677  CA  PHE B 267     -31.138  17.107 -41.250  1.00 15.04           C  
ATOM    678  CA  PHE B 268     -33.012  14.052 -42.354  1.00 14.55           C  
ATOM    679  CA  MET B 269     -35.028  11.351 -40.678  1.00  5.61           C  
ATOM    680  CA  PRO B 270     -34.161   7.743 -41.512  1.00  4.00           C  
ATOM    681  CA  GLY B 271     -36.729   4.956 -41.871  1.00 13.86           C  
ATOM    682  CA  PHE B 272     -36.203   1.249 -42.488  1.00 21.24           C  
ATOM    683  CA  ALA B 273     -38.427  -0.918 -44.684  1.00 22.98           C  
ATOM    684  CA  PRO B 274     -39.361  -4.377 -43.502  1.00 26.07           C  
ATOM    685  CA  LEU B 275     -40.145  -3.619 -39.914  1.00 31.25           C  
ATOM    686  CA  THR B 276     -42.354  -6.544 -38.965  1.00 46.02           C  
ATOM    687  CA  SER B 277     -42.501  -8.435 -35.642  1.00 66.56           C  
ATOM    688  CA  ARG B 278     -40.683 -11.786 -35.646  1.00 87.05           C  
ATOM    689  CA  GLY B 279     -42.833 -14.925 -35.969  1.00 97.30           C  
ATOM    690  CA  SER B 280     -46.409 -14.013 -36.966  1.00100.00           C  
ATOM    691  CA  GLN B 281     -46.165 -10.711 -38.811  1.00100.00           C  
ATOM    692  CA  GLN B 282     -43.604 -12.418 -41.159  1.00 97.58           C  
ATOM    693  CA  TYR B 283     -46.227 -11.633 -43.720  1.00 97.75           C  
ATOM    694  CA  ARG B 284     -43.752 -11.168 -46.512  1.00100.00           C  
ATOM    695  CA  ALA B 285     -46.078  -8.469 -47.800  1.00 92.86           C  
ATOM    696  CA  LEU B 286     -42.918  -6.957 -49.206  1.00 80.45           C  
ATOM    697  CA  THR B 287     -43.761  -7.013 -52.930  1.00 66.34           C  
ATOM    698  CA  VAL B 288     -42.850  -3.270 -52.803  1.00 44.62           C  
ATOM    699  CA  PRO B 289     -46.032  -1.273 -52.343  1.00 42.51           C  
ATOM    700  CA  GLU B 290     -45.628  -2.678 -48.890  1.00 43.33           C  
ATOM    701  CA  LEU B 291     -42.232  -1.076 -48.388  1.00 31.88           C  
ATOM    702  CA  THR B 292     -43.349   2.343 -49.577  1.00 21.93           C  
ATOM    703  CA  GLN B 293     -46.452   1.804 -47.515  1.00 27.22           C  
ATOM    704  CA  GLN B 294     -44.085   1.384 -44.591  1.00 33.69           C  
ATOM    705  CA  MET B 295     -41.339   3.994 -45.119  1.00 23.21           C  
ATOM    706  CA  PHE B 296     -43.784   6.787 -45.936  1.00 26.97           C  
ATOM    707  CA  ASP B 297     -46.134   6.486 -42.973  1.00 40.24           C  
ATOM    708  CA  ALA B 298     -45.876   8.770 -39.948  1.00 39.02           C  
ATOM    709  CA  LYS B 299     -44.852   6.222 -37.358  1.00 32.50           C  
ATOM    710  CA  ASN B 300     -41.747   4.473 -38.646  1.00 28.60           C  
ATOM    711  CA  MET B 301     -39.798   7.711 -38.924  1.00 31.57           C  
ATOM    712  CA  MET B 302     -36.934   7.398 -36.439  1.00 21.60           C  
ATOM    713  CA  ALA B 303     -37.411  11.126 -35.950  1.00 29.61           C  
ATOM    714  CA  ALA B 304     -39.771  12.425 -33.281  1.00 39.22           C  
ATOM    715  CA  CYS B 305     -41.740  14.719 -35.491  1.00 47.77           C  
ATOM    716  CA  ASP B 306     -44.303  13.422 -37.938  1.00 48.33           C  
ATOM    717  CA  PRO B 307     -43.847  14.097 -41.681  1.00 40.81           C  
ATOM    718  CA  ARG B 308     -47.582  14.596 -41.965  1.00 48.63           C  
ATOM    719  CA  HIS B 309     -46.810  17.845 -40.119  1.00 41.86           C  
ATOM    720  CA  GLY B 310     -44.735  19.436 -42.867  1.00 23.13           C  
ATOM    721  CA  ARG B 311     -43.783  19.109 -46.545  1.00 18.23           C  
ATOM    722  CA  TYR B 312     -40.698  17.321 -47.778  1.00 18.02           C  
ATOM    723  CA  LEU B 313     -37.882  18.806 -49.825  1.00 12.59           C  
ATOM    724  CA  THR B 314     -36.247  15.585 -50.759  1.00 20.92           C  
ATOM    725  CA  VAL B 315     -36.614  11.905 -50.178  1.00 21.66           C  
ATOM    726  CA  ALA B 316     -34.279   9.039 -50.917  1.00 19.05           C  
ATOM    727  CA  ALA B 317     -35.670   5.561 -50.931  1.00  6.84           C  
ATOM    728  CA  VAL B 318     -32.443   3.654 -50.948  1.00  6.33           C  
ATOM    729  CA  PHE B 319     -33.846   0.159 -51.680  1.00 11.40           C  
ATOM    730  CA  ARG B 320     -31.565  -2.888 -51.615  1.00 33.50           C  
ATOM    731  CA  GLY B 321     -33.118  -6.108 -52.923  1.00 48.28           C  
ATOM    732  CA  ARG B 322     -33.972  -7.287 -56.464  1.00 54.21           C  
ATOM    733  CA  MET B 323     -37.031  -5.378 -57.774  1.00 34.07           C  
ATOM    734  CA  SER B 324     -38.504  -3.848 -60.922  1.00 28.27           C  
ATOM    735  CA  MET B 325     -37.165  -0.430 -61.800  1.00 29.79           C  
ATOM    736  CA  LYS B 326     -40.748  -0.124 -62.922  1.00 26.85           C  
ATOM    737  CA  GLU B 327     -42.625  -1.114 -59.766  1.00 25.85           C  
ATOM    738  CA  VAL B 328     -40.147   1.083 -57.927  1.00 26.70           C  
ATOM    739  CA  ASP B 329     -40.037   4.085 -60.175  1.00 44.49           C  
ATOM    740  CA  GLU B 330     -43.810   3.769 -60.459  1.00 51.41           C  
ATOM    741  CA  GLN B 331     -44.917   3.448 -56.839  1.00 48.07           C  
ATOM    742  CA  MET B 332     -42.816   6.490 -55.922  1.00 43.07           C  
ATOM    743  CA  LEU B 333     -45.066   8.459 -58.238  1.00 47.31           C  
ATOM    744  CA  ASN B 334     -48.533   7.656 -56.914  1.00 50.87           C  
ATOM    745  CA  VAL B 335     -46.957   8.320 -53.556  1.00 44.29           C  
ATOM    746  CA  GLN B 336     -45.933  11.728 -54.886  1.00 55.13           C  
ATOM    747  CA  ASN B 337     -49.475  12.362 -56.074  1.00 67.16           C  
ATOM    748  CA  LYS B 338     -51.592  10.913 -53.262  1.00 69.74           C  
ATOM    749  CA  ASN B 339     -49.706  13.306 -51.007  1.00 69.20           C  
ATOM    750  CA  SER B 340     -49.065  16.245 -53.335  1.00 69.00           C  
ATOM    751  CA  SER B 341     -50.263  18.216 -50.327  1.00 63.08           C  
ATOM    752  CA  TYR B 342     -47.097  17.581 -48.359  1.00 54.97           C  
ATOM    753  CA  PHE B 343     -44.148  17.108 -50.649  1.00 44.79           C  
ATOM    754  CA  VAL B 344     -43.320  20.707 -51.634  1.00 41.62           C  
ATOM    755  CA  GLU B 345     -43.872  21.747 -55.245  1.00 50.05           C  
ATOM    756  CA  TRP B 346     -40.891  23.694 -56.539  1.00 30.29           C  
ATOM    757  CA  ILE B 347     -39.221  20.311 -56.976  1.00 29.65           C  
ATOM    758  CA  PRO B 348     -40.962  18.352 -59.710  1.00 35.31           C  
ATOM    759  CA  ASN B 349     -39.495  15.061 -58.444  1.00 28.59           C  
ATOM    760  CA  ASN B 350     -38.652  15.313 -54.747  1.00 21.20           C  
ATOM    761  CA  VAL B 351     -38.001  11.632 -54.515  1.00 15.60           C  
ATOM    762  CA  LYS B 352     -34.577  10.189 -55.272  1.00  7.97           C  
ATOM    763  CA  THR B 353     -35.076   6.540 -56.089  1.00  2.00           C  
ATOM    764  CA  ALA B 354     -31.986   4.486 -55.415  1.00  7.32           C  
ATOM    765  CA  VAL B 355     -31.660   0.774 -56.020  1.00 17.66           C  
ATOM    766  CA  CYS B 356     -29.022  -1.632 -54.788  1.00 41.06           C  
ATOM    767  CA  ASP B 357     -29.198  -5.351 -55.527  1.00 55.40           C  
ATOM    768  CA  ILE B 358     -28.106  -7.528 -52.629  1.00 59.96           C  
ATOM    769  CA  PRO B 359     -30.466  -7.037 -49.644  1.00 58.14           C  
ATOM    770  CA  PRO B 360     -29.932  -7.170 -45.875  1.00 59.42           C  
ATOM    771  CA  ARG B 369     -28.235 -10.542 -45.424  1.00 68.33           C  
ATOM    772  CA  GLY B 370     -31.240 -12.504 -44.169  1.00 59.28           C  
ATOM    773  CA  LEU B 371     -34.024 -10.522 -45.819  1.00 55.07           C  
ATOM    774  CA  LYS B 372     -35.559 -10.608 -49.312  1.00 49.45           C  
ATOM    775  CA  MET B 373     -36.255  -6.914 -49.816  1.00 44.58           C  
ATOM    776  CA  SER B 374     -35.628  -3.721 -47.828  1.00 40.19           C  
ATOM    777  CA  ALA B 375     -35.346   0.034 -48.458  1.00 35.52           C  
ATOM    778  CA  THR B 376     -33.764   2.722 -46.334  1.00 19.99           C  
ATOM    779  CA  PHE B 377     -35.588   6.038 -46.254  1.00  8.34           C  
ATOM    780  CA  ILE B 378     -33.791   9.317 -45.835  1.00 12.46           C  
ATOM    781  CA  GLY B 379     -36.274  12.134 -45.624  1.00 11.41           C  
ATOM    782  CA  ASN B 380     -35.495  15.827 -45.708  1.00  8.51           C  
ATOM    783  CA  SER B 381     -38.831  17.079 -44.480  1.00 19.03           C  
ATOM    784  CA  THR B 382     -39.644  20.540 -43.223  1.00 15.50           C  
ATOM    785  CA  ALA B 383     -41.321  18.770 -40.357  1.00  7.67           C  
ATOM    786  CA  ILE B 384     -38.092  18.632 -38.430  1.00  2.00           C  
ATOM    787  CA  GLN B 385     -38.777  22.278 -37.832  1.00 14.51           C  
ATOM    788  CA  GLU B 386     -41.015  21.163 -34.985  1.00 14.80           C  
ATOM    789  CA  LEU B 387     -38.069  19.662 -33.132  1.00 15.58           C  
ATOM    790  CA  PHE B 388     -35.415  22.297 -33.153  1.00 16.61           C  
ATOM    791  CA  LYS B 389     -38.337  24.397 -31.991  1.00 16.55           C  
ATOM    792  CA  ARG B 390     -38.743  22.056 -29.063  1.00 27.51           C  
ATOM    793  CA  ILE B 391     -35.065  22.060 -28.214  1.00 23.86           C  
ATOM    794  CA  SER B 392     -34.811  25.806 -28.720  1.00 26.53           C  
ATOM    795  CA  GLU B 393     -37.786  26.293 -26.413  1.00 34.87           C  
ATOM    796  CA  GLN B 394     -36.359  24.221 -23.538  1.00 27.14           C  
ATOM    797  CA  PHE B 395     -33.254  26.370 -23.795  1.00 19.69           C  
ATOM    798  CA  THR B 396     -34.841  29.784 -23.389  1.00 23.53           C  
ATOM    799  CA  ALA B 397     -37.205  28.584 -20.623  1.00 21.17           C  
ATOM    800  CA  MET B 398     -34.079  27.681 -18.672  1.00 16.25           C  
ATOM    801  CA  PHE B 399     -31.551  29.975 -20.160  1.00 26.94           C  
ATOM    802  CA  ARG B 400     -33.710  32.859 -19.054  1.00 43.42           C  
ATOM    803  CA  ARG B 401     -32.799  31.850 -15.488  1.00 35.47           C  
ATOM    804  CA  LYS B 402     -29.262  30.690 -16.363  1.00 20.61           C  
ATOM    805  CA  ALA B 403     -30.235  27.399 -14.715  1.00  9.52           C  
ATOM    806  CA  PHE B 404     -27.216  25.117 -14.698  1.00 15.71           C  
ATOM    807  CA  LEU B 405     -25.115  27.691 -16.432  1.00 18.28           C  
ATOM    808  CA  HIS B 406     -22.374  27.943 -13.816  1.00 19.93           C  
ATOM    809  CA  TRP B 407     -21.205  24.462 -14.872  1.00 24.76           C  
ATOM    810  CA  TYR B 408     -20.514  25.887 -18.304  1.00 30.69           C  
ATOM    811  CA  THR B 409     -19.076  29.323 -17.599  1.00 37.85           C  
ATOM    812  CA  GLY B 410     -17.106  27.968 -14.644  1.00 41.05           C  
ATOM    813  CA  GLU B 411     -15.511  25.813 -17.314  1.00 37.96           C  
ATOM    814  CA  GLY B 412     -14.414  28.776 -19.352  1.00 38.22           C  
ATOM    815  CA  MET B 413     -17.427  29.527 -21.507  1.00 39.38           C  
ATOM    816  CA  ASP B 414     -19.254  32.687 -22.542  1.00 41.26           C  
ATOM    817  CA  GLU B 415     -22.689  34.197 -21.863  1.00 45.59           C  
ATOM    818  CA  MET B 416     -22.632  35.151 -25.531  1.00 45.20           C  
ATOM    819  CA  GLU B 417     -21.794  31.578 -26.600  1.00 34.38           C  
ATOM    820  CA  PHE B 418     -25.167  30.230 -25.526  1.00 27.19           C  
ATOM    821  CA  THR B 419     -26.825  33.254 -27.071  1.00 27.27           C  
ATOM    822  CA  GLU B 420     -25.065  32.492 -30.311  1.00 38.93           C  
ATOM    823  CA  ALA B 421     -26.075  28.860 -30.632  1.00 38.51           C  
ATOM    824  CA  GLU B 422     -29.708  29.284 -29.716  1.00 39.60           C  
ATOM    825  CA  SER B 423     -30.131  32.113 -32.180  1.00 38.41           C  
ATOM    826  CA  ASN B 424     -28.266  30.260 -34.925  1.00 30.37           C  
ATOM    827  CA  MET B 425     -30.097  26.997 -34.400  1.00 30.27           C  
ATOM    828  CA  ASN B 426     -33.194  29.097 -33.692  1.00 30.82           C  
ATOM    829  CA  ASP B 427     -32.902  30.849 -37.061  1.00 28.66           C  
ATOM    830  CA  LEU B 428     -32.361  27.400 -38.531  1.00 23.70           C  
ATOM    831  CA  VAL B 429     -35.992  26.731 -37.542  1.00 26.78           C  
ATOM    832  CA  SER B 430     -37.080  29.873 -39.295  1.00 36.87           C  
ATOM    833  CA  GLU B 431     -35.495  29.078 -42.660  1.00 46.33           C  
ATOM    834  CA  TYR B 432     -36.868  25.527 -42.775  1.00 37.74           C  
ATOM    835  CA  GLN B 433     -40.348  27.092 -42.724  1.00 41.57           C  
ATOM    836  CA  GLN B 434     -39.452  29.209 -45.755  1.00 51.40           C  
ATOM    837  CA  TYR B 435     -40.164  26.068 -47.783  1.00 56.61           C  
ATOM    838  CA  GLN B 436     -43.080  24.591 -45.850  1.00 63.11           C  
ATOM    839  CA  ASP B 437     -44.643  27.685 -47.446  1.00 74.59           C  
TER     840      ASP B 437                                                      
ATOM    841  CA  GLY C  16     -39.162  50.860 -54.080  1.00 56.94           C  
ATOM    842  CA  LYS C  17     -35.727  51.041 -52.556  1.00 52.64           C  
ATOM    843  CA  ASN C  18     -33.284  53.735 -51.821  1.00 47.09           C  
ATOM    844  CA  ILE C  19     -30.773  51.324 -53.294  1.00 41.53           C  
ATOM    845  CA  GLN C  20     -29.157  52.935 -56.350  1.00 33.88           C  
ATOM    846  CA  VAL C  21     -27.287  51.279 -59.238  1.00 24.18           C  
ATOM    847  CA  VAL C  22     -25.147  53.391 -61.576  1.00 18.33           C  
ATOM    848  CA  VAL C  23     -22.569  52.769 -64.315  1.00 17.82           C  
ATOM    849  CA  ARG C  24     -19.289  54.575 -65.009  1.00 17.53           C  
ATOM    850  CA  VAL C  25     -17.449  54.025 -68.294  1.00 19.53           C  
ATOM    851  CA  ARG C  26     -13.762  54.910 -68.207  1.00 19.95           C  
ATOM    852  CA  PRO C  27     -11.723  56.116 -71.167  1.00 19.71           C  
ATOM    853  CA  PHE C  28      -9.026  53.784 -72.461  1.00 19.75           C  
ATOM    854  CA  ASN C  29      -5.778  52.953 -71.251  1.00 20.30           C  
ATOM    855  CA  LEU C  30      -2.873  52.540 -73.668  1.00 22.09           C  
ATOM    856  CA  ALA C  31      -2.639  48.736 -73.398  1.00 21.20           C  
ATOM    857  CA  GLU C  32      -6.202  48.306 -74.698  1.00 20.50           C  
ATOM    858  CA  ARG C  33      -5.465  50.577 -77.696  1.00 23.38           C  
ATOM    859  CA  LYS C  34      -2.292  48.669 -78.606  1.00 20.41           C  
ATOM    860  CA  ALA C  35      -4.272  45.452 -78.203  1.00 19.03           C  
ATOM    861  CA  SER C  36      -6.639  47.117 -80.543  1.00 20.41           C  
ATOM    862  CA  ALA C  37      -9.580  46.923 -78.493  1.00 20.04           C  
ATOM    863  CA  HIS C  38     -12.081  49.258 -80.045  1.00 19.64           C  
ATOM    864  CA  SER C  39     -14.043  51.722 -78.101  1.00 21.02           C  
ATOM    865  CA  ILE C  40     -17.227  49.743 -78.514  1.00 20.84           C  
ATOM    866  CA  VAL C  41     -18.866  51.424 -75.564  1.00 20.43           C  
ATOM    867  CA  GLU C  42     -21.130  54.421 -76.153  1.00 27.08           C  
ATOM    868  CA  SER C  43     -22.432  56.467 -73.206  1.00 26.77           C  
ATOM    869  CA  ASP C  44     -25.484  58.715 -73.502  1.00 29.44           C  
ATOM    870  CA  PRO C  45     -25.649  60.293 -70.161  1.00 32.02           C  
ATOM    871  CA  VAL C  46     -28.800  62.161 -71.199  1.00 33.24           C  
ATOM    872  CA  ARG C  47     -30.501  58.915 -72.061  1.00 30.34           C  
ATOM    873  CA  LYS C  48     -28.700  57.317 -69.230  1.00 29.02           C  
ATOM    874  CA  GLU C  49     -28.080  54.571 -71.709  1.00 26.51           C  
ATOM    875  CA  VAL C  50     -24.930  52.558 -72.394  1.00 23.72           C  
ATOM    876  CA  SER C  51     -24.645  50.609 -75.652  1.00 26.06           C  
ATOM    877  CA  VAL C  52     -21.994  47.981 -76.422  1.00 23.71           C  
ATOM    878  CA  ARG C  53     -20.886  46.691 -79.861  1.00 29.61           C  
ATOM    879  CA  THR C  54     -21.067  43.012 -79.099  1.00 34.47           C  
ATOM    880  CA  GLY C  55     -20.068  41.669 -82.364  1.00 40.58           C  
ATOM    881  CA  GLY C  56     -16.809  41.067 -84.014  1.00 43.50           C  
ATOM    882  CA  LEU C  57     -16.567  42.733 -87.352  1.00 45.12           C  
ATOM    883  CA  ALA C  58     -19.913  42.684 -89.117  1.00 45.67           C  
ATOM    884  CA  ASP C  59     -21.536  41.881 -85.874  1.00 46.98           C  
ATOM    885  CA  LYS C  60     -20.149  45.037 -84.310  1.00 50.20           C  
ATOM    886  CA  SER C  61     -23.399  46.351 -85.623  1.00 50.26           C  
ATOM    887  CA  SER C  62     -25.116  44.231 -83.178  1.00 47.69           C  
ATOM    888  CA  ARG C  63     -25.060  46.208 -80.027  1.00 45.40           C  
ATOM    889  CA  LYS C  64     -26.829  45.770 -76.691  1.00 35.41           C  
ATOM    890  CA  THR C  65     -28.347  48.761 -74.899  1.00 28.60           C  
ATOM    891  CA  TYR C  66     -29.011  49.159 -71.174  1.00 24.56           C  
ATOM    892  CA  THR C  67     -30.699  51.915 -69.194  1.00 24.23           C  
ATOM    893  CA  PHE C  68     -29.873  52.933 -65.691  1.00 23.21           C  
ATOM    894  CA  ASP C  69     -30.619  55.141 -62.800  1.00 23.05           C  
ATOM    895  CA  MET C  70     -27.509  57.128 -63.522  1.00 26.74           C  
ATOM    896  CA  VAL C  71     -25.003  56.671 -66.340  1.00 25.51           C  
ATOM    897  CA  PHE C  72     -21.567  58.291 -66.434  1.00 24.61           C  
ATOM    898  CA  GLY C  73     -19.650  58.292 -69.662  1.00 23.71           C  
ATOM    899  CA  ALA C  74     -15.930  58.207 -69.918  1.00 26.26           C  
ATOM    900  CA  SER C  75     -16.316  61.927 -69.707  1.00 29.38           C  
ATOM    901  CA  THR C  76     -17.814  61.437 -66.305  1.00 26.82           C  
ATOM    902  CA  LYS C  77     -14.941  62.135 -63.997  1.00 26.30           C  
ATOM    903  CA  GLN C  78     -14.232  62.000 -60.323  1.00 23.24           C  
ATOM    904  CA  ILE C  79     -16.199  64.929 -58.896  1.00 27.51           C  
ATOM    905  CA  ASP C  80     -19.301  63.869 -60.788  1.00 28.53           C  
ATOM    906  CA  VAL C  81     -19.250  60.339 -59.402  1.00 24.54           C  
ATOM    907  CA  TYR C  82     -18.901  61.860 -55.942  1.00 23.22           C  
ATOM    908  CA  ARG C  83     -21.782  64.313 -56.356  1.00 28.84           C  
ATOM    909  CA  SER C  84     -24.255  61.819 -57.790  1.00 27.74           C  
ATOM    910  CA  VAL C  85     -23.394  58.811 -55.643  1.00 25.45           C  
ATOM    911  CA  VAL C  86     -21.753  59.724 -52.333  1.00 22.84           C  
ATOM    912  CA  ALA C  87     -23.360  63.073 -51.403  1.00 28.43           C  
ATOM    913  CA  PRO C  88     -26.864  61.719 -50.721  1.00 26.80           C  
ATOM    914  CA  ILE C  89     -25.302  58.916 -48.661  1.00 27.18           C  
ATOM    915  CA  LEU C  90     -22.978  61.079 -46.571  1.00 29.28           C  
ATOM    916  CA  ASP C  91     -26.056  63.120 -45.611  1.00 32.43           C  
ATOM    917  CA  GLU C  92     -27.585  60.017 -44.051  1.00 35.61           C  
ATOM    918  CA  VAL C  93     -24.344  59.233 -42.241  1.00 30.03           C  
ATOM    919  CA  ILE C  94     -24.097  62.728 -40.758  1.00 31.58           C  
ATOM    920  CA  MET C  95     -27.622  61.954 -39.502  1.00 36.26           C  
ATOM    921  CA  GLY C  96     -26.410  59.116 -37.373  1.00 33.55           C  
ATOM    922  CA  TYR C  97     -26.944  56.535 -40.031  1.00 34.72           C  
ATOM    923  CA  ASN C  98     -25.153  53.546 -41.401  1.00 34.65           C  
ATOM    924  CA  ALA C  99     -24.707  53.390 -45.191  1.00 28.79           C  
ATOM    925  CA  THR C 100     -22.630  51.558 -47.825  1.00 26.24           C  
ATOM    926  CA  ILE C 101     -21.273  52.305 -51.327  1.00 21.60           C  
ATOM    927  CA  PHE C 102     -19.771  49.604 -53.608  1.00 22.25           C  
ATOM    928  CA  ALA C 103     -17.441  49.634 -56.643  1.00 18.23           C  
ATOM    929  CA  TYR C 104     -18.019  46.644 -58.943  1.00 20.61           C  
ATOM    930  CA  GLY C 105     -16.406  45.612 -62.216  1.00 20.12           C  
ATOM    931  CA  GLN C 106     -13.624  43.987 -64.217  1.00 22.08           C  
ATOM    932  CA  THR C 107     -10.042  44.586 -63.098  1.00 20.48           C  
ATOM    933  CA  GLY C 108      -8.697  47.763 -64.721  1.00 19.36           C  
ATOM    934  CA  THR C 109     -12.059  49.465 -65.286  1.00 18.57           C  
ATOM    935  CA  GLY C 110     -11.835  52.043 -62.464  1.00 18.76           C  
ATOM    936  CA  LYS C 111     -12.910  50.631 -59.071  1.00 19.01           C  
ATOM    937  CA  THR C 112      -9.937  51.958 -57.085  1.00 21.03           C  
ATOM    938  CA  PHE C 113      -9.805  55.108 -59.225  1.00 20.70           C  
ATOM    939  CA  THR C 114     -13.403  55.764 -58.268  1.00 20.03           C  
ATOM    940  CA  MET C 115     -13.198  54.777 -54.588  1.00 25.89           C  
ATOM    941  CA  GLU C 116      -9.741  56.143 -53.843  1.00 28.03           C  
ATOM    942  CA  GLY C 117      -9.530  58.606 -56.556  1.00 31.97           C  
ATOM    943  CA  GLU C 118      -5.953  58.634 -57.738  1.00 42.59           C  
ATOM    944  CA  ARG C 119      -3.029  60.464 -56.219  1.00 57.06           C  
ATOM    945  CA  SER C 120      -4.330  59.072 -53.077  1.00 67.84           C  
ATOM    946  CA  PRO C 121      -2.748  56.131 -51.318  1.00 73.45           C  
ATOM    947  CA  ASN C 122      -2.746  53.828 -54.246  1.00 77.57           C  
ATOM    948  CA  GLU C 123      -1.055  54.344 -57.510  1.00 80.36           C  
ATOM    949  CA  GLU C 124      -0.652  57.944 -56.938  1.00 81.23           C  
ATOM    950  CA  TYR C 125       0.377  60.127 -59.803  1.00 80.16           C  
ATOM    951  CA  CYS C 126      -1.216  62.756 -61.768  1.00 77.76           C  
ATOM    952  CA  TRP C 127      -3.656  62.331 -64.544  1.00 74.44           C  
ATOM    953  CA  GLU C 128      -6.484  64.464 -65.860  1.00 66.65           C  
ATOM    954  CA  GLU C 129     -10.083  64.162 -64.904  1.00 57.03           C  
ATOM    955  CA  ASP C 130     -12.144  65.683 -62.207  1.00 47.92           C  
ATOM    956  CA  PRO C 131      -9.864  66.059 -59.348  1.00 40.18           C  
ATOM    957  CA  LEU C 132      -7.717  63.505 -57.730  1.00 33.95           C  
ATOM    958  CA  ALA C 133      -9.567  62.632 -54.675  1.00 27.52           C  
ATOM    959  CA  GLY C 134     -11.956  59.769 -55.126  1.00 25.26           C  
ATOM    960  CA  ILE C 135     -14.882  58.834 -52.927  1.00 23.75           C  
ATOM    961  CA  ILE C 136     -13.015  57.984 -49.710  1.00 26.24           C  
ATOM    962  CA  PRO C 137     -11.065  61.299 -49.713  1.00 29.59           C  
ATOM    963  CA  ARG C 138     -14.066  63.519 -50.524  1.00 26.91           C  
ATOM    964  CA  THR C 139     -16.279  61.699 -48.026  1.00 27.95           C  
ATOM    965  CA  LEU C 140     -13.950  62.336 -45.061  1.00 31.85           C  
ATOM    966  CA  HIS C 141     -13.580  65.944 -46.160  1.00 37.81           C  
ATOM    967  CA  GLN C 142     -17.349  66.490 -46.203  1.00 32.70           C  
ATOM    968  CA  ILE C 143     -17.995  64.771 -42.865  1.00 29.20           C  
ATOM    969  CA  PHE C 144     -15.643  67.196 -41.136  1.00 29.46           C  
ATOM    970  CA  GLU C 145     -16.900  70.216 -43.094  1.00 28.73           C  
ATOM    971  CA  LYS C 146     -20.597  69.499 -42.552  1.00 25.98           C  
ATOM    972  CA  LEU C 147     -20.436  68.432 -38.885  1.00 27.49           C  
ATOM    973  CA  THR C 148     -18.093  71.280 -38.001  1.00 30.20           C  
ATOM    974  CA  ASP C 149     -20.312  73.897 -39.632  1.00 29.85           C  
ATOM    975  CA  ASN C 150     -23.328  72.644 -37.697  1.00 30.93           C  
ATOM    976  CA  GLY C 151     -20.892  72.566 -34.863  1.00 32.09           C  
ATOM    977  CA  THR C 152     -21.752  69.105 -33.837  1.00 31.21           C  
ATOM    978  CA  GLU C 153     -19.176  68.261 -31.229  1.00 30.54           C  
ATOM    979  CA  PHE C 154     -17.750  65.271 -33.061  1.00 29.34           C  
ATOM    980  CA  SER C 155     -15.043  62.626 -33.307  1.00 32.44           C  
ATOM    981  CA  VAL C 156     -13.952  60.676 -36.386  1.00 33.49           C  
ATOM    982  CA  LYS C 157     -12.376  57.218 -36.572  1.00 33.72           C  
ATOM    983  CA  VAL C 158     -11.705  54.936 -39.537  1.00 33.95           C  
ATOM    984  CA  SER C 159     -10.744  51.317 -40.191  1.00 35.07           C  
ATOM    985  CA  LEU C 160      -9.507  49.373 -43.197  1.00 35.08           C  
ATOM    986  CA  LEU C 161      -9.738  45.615 -43.552  1.00 37.58           C  
ATOM    987  CA  GLU C 162      -9.248  43.322 -46.530  1.00 41.22           C  
ATOM    988  CA  ILE C 163     -11.063  40.100 -47.366  1.00 42.29           C  
ATOM    989  CA  TYR C 164      -8.876  37.621 -49.256  1.00 47.31           C  
ATOM    990  CA  ASN C 165      -9.545  33.906 -49.645  1.00 50.84           C  
ATOM    991  CA  GLU C 166     -12.336  34.543 -47.130  1.00 52.42           C  
ATOM    992  CA  GLU C 167      -9.939  35.754 -44.430  1.00 52.10           C  
ATOM    993  CA  LEU C 168     -10.002  39.177 -42.751  1.00 48.48           C  
ATOM    994  CA  PHE C 169      -6.757  41.141 -42.664  1.00 47.12           C  
ATOM    995  CA  ASP C 170      -6.360  44.444 -40.808  1.00 45.80           C  
ATOM    996  CA  LEU C 171      -4.723  46.909 -43.174  1.00 41.82           C  
ATOM    997  CA  LEU C 172      -5.563  50.068 -41.506  1.00 46.19           C  
ATOM    998  CA  ASN C 173      -4.154  49.591 -38.132  1.00 55.76           C  
ATOM    999  CA  PRO C 174      -0.579  48.528 -37.709  1.00 63.02           C  
ATOM   1000  CA  SER C 175      -2.045  46.502 -34.984  1.00 69.71           C  
ATOM   1001  CA  SER C 176      -2.869  43.196 -36.343  1.00 74.91           C  
ATOM   1002  CA  ASP C 177      -1.703  44.772 -39.498  1.00 78.14           C  
ATOM   1003  CA  VAL C 178      -0.262  41.381 -40.220  1.00 79.77           C  
ATOM   1004  CA  SER C 179      -0.668  38.042 -42.042  1.00 78.55           C  
ATOM   1005  CA  GLU C 180      -2.461  36.920 -38.986  1.00 76.03           C  
ATOM   1006  CA  ARG C 181      -6.136  36.801 -39.503  1.00 71.55           C  
ATOM   1007  CA  LEU C 182      -7.983  39.318 -37.567  1.00 65.54           C  
ATOM   1008  CA  GLN C 183     -11.121  37.560 -36.203  1.00 62.99           C  
ATOM   1009  CA  MET C 184     -14.902  38.316 -35.394  1.00 63.95           C  
ATOM   1010  CA  PHE C 185     -18.328  37.047 -34.041  1.00 66.19           C  
ATOM   1011  CA  ASP C 186     -21.962  37.966 -33.388  1.00 69.99           C  
ATOM   1012  CA  ASP C 187     -21.985  40.324 -30.411  1.00 73.18           C  
ATOM   1013  CA  PRO C 188     -24.612  40.355 -27.644  1.00 75.52           C  
ATOM   1014  CA  ARG C 189     -26.905  43.230 -28.652  1.00 76.49           C  
ATOM   1015  CA  ASN C 190     -29.858  43.532 -31.031  1.00 76.55           C  
ATOM   1016  CA  LYS C 191     -29.284  41.412 -34.150  1.00 73.13           C  
ATOM   1017  CA  ARG C 192     -27.911  42.526 -37.537  1.00 67.38           C  
ATOM   1018  CA  GLY C 193     -24.471  43.601 -36.372  1.00 60.93           C  
ATOM   1019  CA  VAL C 194     -21.177  41.815 -35.774  1.00 55.04           C  
ATOM   1020  CA  ILE C 195     -17.959  42.674 -33.954  1.00 51.80           C  
ATOM   1021  CA  ILE C 196     -14.539  42.558 -35.594  1.00 49.50           C  
ATOM   1022  CA  LYS C 197     -11.896  42.511 -32.860  1.00 48.63           C  
ATOM   1023  CA  GLY C 198      -8.245  43.265 -33.583  1.00 44.26           C  
ATOM   1024  CA  LEU C 199      -9.180  46.116 -35.909  1.00 41.53           C  
ATOM   1025  CA  GLU C 200      -8.579  49.472 -34.318  1.00 42.31           C  
ATOM   1026  CA  GLU C 201     -10.096  52.585 -35.395  1.00 43.34           C  
ATOM   1027  CA  ILE C 202      -7.489  55.134 -36.174  1.00 41.26           C  
ATOM   1028  CA  THR C 203      -8.763  58.456 -34.854  1.00 41.29           C  
ATOM   1029  CA  VAL C 204      -8.638  60.501 -37.934  1.00 44.66           C  
ATOM   1030  CA  HIS C 205      -8.605  64.171 -38.190  1.00 27.37           C  
ATOM   1031  CA  ASN C 206      -8.062  64.371 -41.792  1.00 32.15           C  
ATOM   1032  CA  LYS C 207      -6.919  62.981 -45.130  1.00 36.16           C  
ATOM   1033  CA  ASP C 208      -3.200  62.967 -44.331  1.00 36.42           C  
ATOM   1034  CA  GLU C 209      -3.712  60.585 -41.424  1.00 29.90           C  
ATOM   1035  CA  VAL C 210      -5.935  58.383 -43.567  1.00 30.44           C  
ATOM   1036  CA  TYR C 211      -3.627  58.491 -46.582  1.00 32.11           C  
ATOM   1037  CA  GLN C 212      -0.635  57.213 -44.617  1.00 34.92           C  
ATOM   1038  CA  ILE C 213      -2.698  54.302 -43.285  1.00 29.81           C  
ATOM   1039  CA  LEU C 214      -4.366  53.613 -46.648  1.00 27.07           C  
ATOM   1040  CA  GLU C 215      -1.249  53.346 -48.830  1.00 31.31           C  
ATOM   1041  CA  LYS C 216       0.417  50.965 -46.386  1.00 31.28           C  
ATOM   1042  CA  GLY C 217      -2.784  48.959 -46.177  1.00 27.04           C  
ATOM   1043  CA  ALA C 218      -3.458  48.705 -49.914  1.00 26.09           C  
ATOM   1044  CA  ALA C 219       0.213  47.954 -50.456  1.00 24.58           C  
ATOM   1045  CA  LYS C 220       0.025  44.716 -48.489  1.00 23.55           C  
ATOM   1046  CA  ARG C 221      -3.270  43.566 -50.155  1.00 14.63           C  
ATOM   1047  CA  THR C 222      -3.416  39.870 -50.768  1.00 14.32           C  
ATOM   1048  CA  THR C 223      -3.095  38.521 -54.105  1.00 15.60           C  
ATOM   1049  CA  ALA C 224      -3.526  35.362 -56.160  1.00 12.97           C  
ATOM   1050  CA  ALA C 225      -2.780  34.197 -59.577  1.00 15.05           C  
ATOM   1051  CA  THR C 226      -4.566  34.512 -62.801  1.00 15.24           C  
ATOM   1052  CA  LEU C 227      -3.491  33.080 -66.113  1.00 16.02           C  
ATOM   1053  CA  MET C 228      -2.932  36.663 -67.219  1.00 17.98           C  
ATOM   1054  CA  ASN C 229      -0.601  38.064 -64.614  1.00 14.80           C  
ATOM   1055  CA  ALA C 230       0.271  38.081 -60.875  1.00 16.41           C  
ATOM   1056  CA  TYR C 231      -2.290  39.681 -61.094  1.00 20.01           C  
ATOM   1057  CA  SER C 232      -5.005  39.751 -58.963  1.00 13.41           C  
ATOM   1058  CA  SER C 233      -6.153  41.523 -55.818  1.00 11.66           C  
ATOM   1059  CA  ARG C 234      -8.617  39.123 -54.398  1.00 11.26           C  
ATOM   1060  CA  SER C 235     -10.106  40.744 -51.560  1.00  8.14           C  
ATOM   1061  CA  HIS C 236     -12.968  43.190 -51.009  1.00 32.84           C  
ATOM   1062  CA  SER C 237     -11.380  46.256 -49.399  1.00 31.57           C  
ATOM   1063  CA  VAL C 238     -13.630  47.642 -46.646  1.00 30.04           C  
ATOM   1064  CA  PHE C 239     -12.916  51.212 -45.587  1.00 31.62           C  
ATOM   1065  CA  SER C 240     -15.314  52.331 -42.858  1.00 31.80           C  
ATOM   1066  CA  VAL C 241     -15.676  55.738 -41.200  1.00 32.00           C  
ATOM   1067  CA  THR C 242     -17.652  56.138 -37.957  1.00 31.91           C  
ATOM   1068  CA  ILE C 243     -18.877  59.512 -36.670  1.00 32.44           C  
ATOM   1069  CA  HIS C 244     -19.852  60.347 -33.079  1.00 34.93           C  
ATOM   1070  CA  MET C 245     -21.893  63.556 -32.993  1.00 36.40           C  
ATOM   1071  CA  LYS C 246     -23.488  65.674 -30.274  1.00 41.17           C  
ATOM   1072  CA  GLU C 247     -25.098  68.967 -31.250  1.00 45.89           C  
ATOM   1073  CA  THR C 248     -26.713  71.512 -28.948  1.00 44.88           C  
ATOM   1074  CA  THR C 249     -29.080  74.406 -29.510  1.00 45.98           C  
ATOM   1075  CA  ILE C 250     -30.377  76.768 -26.827  1.00 44.78           C  
ATOM   1076  CA  ASP C 251     -34.108  76.081 -26.415  1.00 50.22           C  
ATOM   1077  CA  GLY C 252     -33.857  73.018 -28.656  1.00 58.06           C  
ATOM   1078  CA  GLU C 253     -32.544  70.021 -26.656  1.00 63.92           C  
ATOM   1079  CA  GLU C 254     -29.268  68.145 -27.174  1.00 63.20           C  
ATOM   1080  CA  LEU C 255     -28.916  65.277 -29.634  1.00 58.18           C  
ATOM   1081  CA  VAL C 256     -26.427  62.415 -29.579  1.00 50.70           C  
ATOM   1082  CA  LYS C 257     -25.821  60.715 -32.946  1.00 41.79           C  
ATOM   1083  CA  ILE C 258     -23.524  58.076 -34.424  1.00 36.05           C  
ATOM   1084  CA  GLY C 259     -23.073  57.651 -38.168  1.00 30.78           C  
ATOM   1085  CA  LYS C 260     -21.229  55.159 -40.335  1.00 28.47           C  
ATOM   1086  CA  LEU C 261     -20.292  54.869 -44.019  1.00 25.32           C  
ATOM   1087  CA  ASN C 262     -18.767  51.766 -45.600  1.00 23.90           C  
ATOM   1088  CA  LEU C 263     -16.882  52.299 -48.870  1.00 24.09           C  
ATOM   1089  CA  VAL C 264     -16.265  48.970 -50.581  1.00 22.19           C  
ATOM   1090  CA  ASP C 265     -13.671  48.597 -53.356  1.00 23.69           C  
ATOM   1091  CA  LEU C 266     -14.451  45.110 -54.544  1.00 10.20           C  
ATOM   1092  CA  ALA C 267     -11.791  43.284 -56.358  1.00 11.56           C  
ATOM   1093  CA  GLY C 268     -11.868  42.725 -60.012  1.00 11.02           C  
ATOM   1094  CA  SER C 269     -13.849  39.731 -61.095  1.00 15.90           C  
ATOM   1095  CA  GLU C 270     -12.378  36.528 -62.433  1.00 15.90           C  
ATOM   1096  CA  ASN C 271     -14.147  33.955 -64.494  1.00 17.75           C  
ATOM   1097  CA  ILE C 272     -12.190  30.786 -64.701  1.00 22.33           C  
ATOM   1098  CA  GLY C 273     -12.566  30.677 -68.461  1.00 25.21           C  
ATOM   1099  CA  ARG C 274     -10.456  33.825 -68.475  1.00 23.12           C  
ATOM   1100  CA  SER C 275      -8.390  33.274 -65.307  1.00 23.31           C  
ATOM   1101  CA  GLY C 276      -7.498  29.856 -66.606  1.00 24.08           C  
ATOM   1102  CA  ALA C 277      -8.707  28.831 -63.253  1.00 24.47           C  
ATOM   1103  CA  VAL C 278      -8.316  25.242 -62.475  1.00 29.29           C  
ATOM   1104  CA  ASP C 279      -8.526  23.762 -58.976  1.00 28.13           C  
ATOM   1105  CA  LYS C 280      -7.467  26.384 -56.420  1.00 22.61           C  
ATOM   1106  CA  ARG C 281      -8.291  29.261 -58.789  1.00 22.32           C  
ATOM   1107  CA  ALA C 282     -11.525  27.506 -59.765  1.00 19.06           C  
ATOM   1108  CA  ARG C 283     -12.429  26.978 -56.109  1.00 19.86           C  
ATOM   1109  CA  GLU C 284     -12.016  30.720 -55.583  1.00 16.63           C  
ATOM   1110  CA  ALA C 285     -14.122  31.509 -58.660  1.00 13.25           C  
ATOM   1111  CA  GLY C 286     -16.839  29.203 -57.356  1.00 12.54           C  
ATOM   1112  CA  ASN C 287     -17.023  31.089 -54.068  1.00 13.54           C  
ATOM   1113  CA  ILE C 288     -16.655  34.432 -55.807  1.00 12.60           C  
ATOM   1114  CA  ASN C 289     -19.497  33.710 -58.266  1.00 11.88           C  
ATOM   1115  CA  GLN C 290     -21.716  32.266 -55.558  1.00 10.94           C  
ATOM   1116  CA  SER C 291     -21.181  35.226 -53.253  1.00 11.57           C  
ATOM   1117  CA  LEU C 292     -21.894  37.715 -56.063  1.00 12.59           C  
ATOM   1118  CA  LEU C 293     -24.949  35.706 -57.018  1.00 13.34           C  
ATOM   1119  CA  THR C 294     -26.144  35.972 -53.402  1.00 11.20           C  
ATOM   1120  CA  LEU C 295     -25.521  39.720 -53.717  1.00 13.21           C  
ATOM   1121  CA  GLY C 296     -27.697  39.788 -56.832  1.00 12.05           C  
ATOM   1122  CA  ARG C 297     -30.490  37.943 -55.018  1.00 13.40           C  
ATOM   1123  CA  VAL C 298     -30.298  40.384 -52.104  1.00  9.81           C  
ATOM   1124  CA  ILE C 299     -30.588  43.300 -54.538  1.00  9.84           C  
ATOM   1125  CA  THR C 300     -33.476  41.679 -56.384  1.00 13.83           C  
ATOM   1126  CA  ALA C 301     -35.206  40.787 -53.118  1.00 13.20           C  
ATOM   1127  CA  LEU C 302     -35.059  44.406 -51.978  1.00 13.42           C  
ATOM   1128  CA  VAL C 303     -36.342  45.846 -55.268  1.00 14.01           C  
ATOM   1129  CA  GLU C 304     -39.104  43.229 -55.289  1.00 15.25           C  
ATOM   1130  CA  ARG C 305     -39.585  43.954 -51.640  1.00 20.02           C  
ATOM   1131  CA  THR C 306     -39.646  40.283 -50.907  1.00 18.34           C  
ATOM   1132  CA  PRO C 307     -38.939  40.731 -47.420  1.00 17.51           C  
ATOM   1133  CA  HIS C 308     -35.722  38.862 -46.732  1.00 21.03           C  
ATOM   1134  CA  VAL C 309     -33.481  36.239 -48.138  1.00 17.82           C  
ATOM   1135  CA  PRO C 310     -31.435  33.651 -46.499  1.00 14.61           C  
ATOM   1136  CA  TYR C 311     -28.753  35.998 -45.244  1.00 49.57           C  
ATOM   1137  CA  ARG C 312     -26.066  34.514 -43.610  1.00 50.92           C  
ATOM   1138  CA  GLU C 313     -23.498  32.911 -45.583  1.00 48.18           C  
ATOM   1139  CA  SER C 314     -20.794  35.130 -46.984  1.00 42.57           C  
ATOM   1140  CA  LYS C 315     -18.161  36.953 -44.918  1.00 39.73           C  
ATOM   1141  CA  LEU C 316     -18.606  40.139 -46.963  1.00 36.49           C  
ATOM   1142  CA  THR C 317     -22.368  40.423 -46.433  1.00 36.67           C  
ATOM   1143  CA  ARG C 318     -22.101  39.369 -42.779  1.00 42.55           C  
ATOM   1144  CA  ILE C 319     -19.725  42.225 -41.971  1.00 41.77           C  
ATOM   1145  CA  LEU C 320     -21.906  44.795 -43.758  1.00 38.49           C  
ATOM   1146  CA  GLN C 321     -25.156  43.331 -42.439  1.00 40.67           C  
ATOM   1147  CA  ASP C 322     -25.623  46.131 -39.897  1.00 46.54           C  
ATOM   1148  CA  SER C 323     -25.362  48.494 -42.835  1.00 46.85           C  
ATOM   1149  CA  LEU C 324     -27.715  46.913 -45.367  1.00 45.32           C  
ATOM   1150  CA  GLY C 325     -30.460  45.924 -42.937  1.00 51.24           C  
ATOM   1151  CA  GLY C 326     -31.477  48.797 -40.685  1.00 55.18           C  
ATOM   1152  CA  ARG C 327     -32.853  50.979 -43.465  1.00 53.69           C  
ATOM   1153  CA  THR C 328     -30.382  53.274 -45.174  1.00 45.50           C  
ATOM   1154  CA  ARG C 329     -29.222  54.269 -48.615  1.00 38.16           C  
ATOM   1155  CA  THR C 330     -27.011  51.852 -50.524  1.00 32.78           C  
ATOM   1156  CA  SER C 331     -25.399  52.400 -53.908  1.00 30.84           C  
ATOM   1157  CA  ILE C 332     -23.441  50.341 -56.411  1.00 25.79           C  
ATOM   1158  CA  ILE C 333     -21.120  51.895 -58.984  1.00 19.39           C  
ATOM   1159  CA  ALA C 334     -20.445  49.460 -61.834  1.00 18.76           C  
ATOM   1160  CA  THR C 335     -17.330  50.289 -63.838  1.00 16.49           C  
ATOM   1161  CA  ILE C 336     -16.748  49.216 -67.462  1.00 15.83           C  
ATOM   1162  CA  SER C 337     -14.221  49.475 -70.247  1.00 16.14           C  
ATOM   1163  CA  PRO C 338     -15.093  50.527 -73.628  1.00 15.98           C  
ATOM   1164  CA  ALA C 339     -13.051  47.903 -75.115  1.00 15.84           C  
ATOM   1165  CA  SER C 340     -14.531  45.590 -77.534  1.00 17.55           C  
ATOM   1166  CA  LEU C 341     -11.845  43.530 -76.003  1.00 22.15           C  
ATOM   1167  CA  ASN C 342     -13.629  44.204 -72.770  1.00 22.50           C  
ATOM   1168  CA  LEU C 343     -16.931  43.378 -74.422  1.00 21.58           C  
ATOM   1169  CA  GLU C 344     -17.557  40.407 -72.125  1.00 23.66           C  
ATOM   1170  CA  GLU C 345     -17.113  42.186 -68.779  1.00 20.60           C  
ATOM   1171  CA  THR C 346     -18.986  45.270 -69.953  1.00 16.67           C  
ATOM   1172  CA  LEU C 347     -21.990  43.134 -70.874  1.00 19.55           C  
ATOM   1173  CA  SER C 348     -21.706  41.313 -67.545  1.00 21.98           C  
ATOM   1174  CA  THR C 349     -21.710  44.623 -65.664  1.00 19.45           C  
ATOM   1175  CA  LEU C 350     -24.733  45.923 -67.583  1.00 20.95           C  
ATOM   1176  CA  GLU C 351     -26.604  42.644 -66.938  1.00 28.12           C  
ATOM   1177  CA  TYR C 352     -25.839  42.747 -63.207  1.00 25.93           C  
ATOM   1178  CA  ALA C 353     -27.104  46.356 -63.081  1.00 25.09           C  
ATOM   1179  CA  HIS C 354     -30.228  45.452 -65.061  1.00 26.44           C  
ATOM   1180  CA  ARG C 355     -30.990  42.618 -62.627  1.00 31.68           C  
ATOM   1181  CA  ALA C 356     -30.673  44.967 -59.629  1.00 29.35           C  
ATOM   1182  CA  LYS C 357     -33.465  47.186 -60.900  1.00 29.78           C  
ATOM   1183  CA  ASN C 358     -35.211  46.669 -64.145  1.00 35.55           C  
ATOM   1184  CA  ILE C 359     -34.409  49.696 -66.182  1.00 38.18           C  
ATOM   1185  CA  LEU C 360     -35.637  48.906 -69.595  1.00 39.37           C  
ATOM   1186  CA  ASN C 361     -34.031  50.374 -72.614  1.00 35.96           C  
ATOM   1187  CA  LYS C 362     -35.505  53.716 -72.694  1.00 39.57           C  
ATOM   1188  CA  PRO C 363     -37.087  54.411 -75.785  1.00 49.91           C  
ATOM   1189  CA  GLU C 364     -34.974  55.378 -78.628  1.00 61.28           C  
ATOM   1190  CA  VAL C 365     -32.750  52.865 -76.908  1.00 65.98           C  
TER    1191      VAL C 365                                                      
HETATM 1192  PG  GTP A 500     -24.030   9.888 -64.580  1.00 29.97           P  
HETATM 1193  O1G GTP A 500     -24.044   8.596 -63.787  1.00 28.70           O  
HETATM 1194  O2G GTP A 500     -25.118  10.858 -64.128  1.00 32.10           O  
HETATM 1195  O3G GTP A 500     -22.730  10.681 -64.392  1.00 34.97           O  
HETATM 1196  O3B GTP A 500     -24.280   9.383 -66.140  1.00 35.17           O  
HETATM 1197  PB  GTP A 500     -25.559   8.500 -66.685  1.00 41.40           P  
HETATM 1198  O1B GTP A 500     -26.126   9.294 -67.851  1.00 42.02           O  
HETATM 1199  O2B GTP A 500     -25.171   7.115 -66.911  1.00 41.17           O  
HETATM 1200  O3A GTP A 500     -26.627   8.656 -65.600  1.00 39.24           O  
HETATM 1201  PA  GTP A 500     -27.941   7.965 -65.254  1.00 41.34           P  
HETATM 1202  O1A GTP A 500     -27.797   6.496 -65.214  1.00 44.48           O  
HETATM 1203  O2A GTP A 500     -28.466   8.599 -64.012  1.00 43.37           O  
HETATM 1204  O5' GTP A 500     -28.943   8.426 -66.475  1.00 34.27           O  
HETATM 1205  C5' GTP A 500     -30.246   7.884 -66.350  1.00 25.47           C  
HETATM 1206  C4' GTP A 500     -31.221   8.263 -67.419  1.00 17.26           C  
HETATM 1207  O4' GTP A 500     -31.139   7.339 -68.534  1.00 18.20           O  
HETATM 1208  C3' GTP A 500     -32.619   8.116 -66.861  1.00 18.14           C  
HETATM 1209  O3' GTP A 500     -33.503   8.968 -67.556  1.00 19.98           O  
HETATM 1210  C2' GTP A 500     -32.897   6.639 -67.094  1.00 17.50           C  
HETATM 1211  O2' GTP A 500     -34.308   6.431 -67.202  1.00 19.33           O  
HETATM 1212  C1' GTP A 500     -32.158   6.335 -68.406  1.00 18.43           C  
HETATM 1213  N9  GTP A 500     -31.510   5.014 -68.480  1.00  9.96           N  
HETATM 1214  C8  GTP A 500     -30.556   4.511 -67.626  1.00 11.60           C  
HETATM 1215  N7  GTP A 500     -30.160   3.308 -67.938  1.00  7.31           N  
HETATM 1216  C5  GTP A 500     -30.898   2.983 -69.050  1.00  2.00           C  
HETATM 1217  C6  GTP A 500     -30.913   1.819 -69.817  1.00  3.48           C  
HETATM 1218  O6  GTP A 500     -30.223   0.818 -69.641  1.00  2.56           O  
HETATM 1219  N1  GTP A 500     -31.820   1.874 -70.899  1.00  2.00           N  
HETATM 1220  C2  GTP A 500     -32.630   2.949 -71.190  1.00  2.00           C  
HETATM 1221  N2  GTP A 500     -33.417   2.826 -72.219  1.00  2.00           N  
HETATM 1222  N3  GTP A 500     -32.635   4.065 -70.461  1.00  2.00           N  
HETATM 1223  C4  GTP A 500     -31.750   4.031 -69.414  1.00  3.56           C  
HETATM 1224 MG    MG A 501     -23.509   6.275 -64.350  1.00 18.63          MG  
HETATM 1225  PB  GDP B 600     -21.863  11.464 -23.069  1.00 22.28           P  
HETATM 1226  O1B GDP B 600     -21.400  12.438 -21.840  1.00 25.30           O  
HETATM 1227  O2B GDP B 600     -21.705  10.101 -22.802  1.00 23.44           O  
HETATM 1228  O3B GDP B 600     -21.243  11.960 -24.312  1.00 23.59           O  
HETATM 1229  O3A GDP B 600     -23.416  11.652 -23.252  1.00 19.52           O  
HETATM 1230  PA  GDP B 600     -24.652  10.528 -23.180  1.00 20.51           P  
HETATM 1231  O1A GDP B 600     -24.582   9.911 -21.794  1.00 18.00           O  
HETATM 1232  O2A GDP B 600     -24.507   9.573 -24.315  1.00 23.36           O  
HETATM 1233  O5' GDP B 600     -25.890  11.429 -23.448  1.00 16.66           O  
HETATM 1234  C5' GDP B 600     -27.221  11.044 -22.991  1.00  7.65           C  
HETATM 1235  C4' GDP B 600     -28.220  10.938 -24.038  1.00  2.51           C  
HETATM 1236  O4' GDP B 600     -27.827   9.843 -24.957  1.00  2.00           O  
HETATM 1237  C3' GDP B 600     -29.638  10.448 -23.567  1.00  3.46           C  
HETATM 1238  O3' GDP B 600     -30.614  11.209 -24.371  1.00  2.32           O  
HETATM 1239  C2' GDP B 600     -29.797   8.946 -23.906  1.00  2.23           C  
HETATM 1240  O2' GDP B 600     -31.098   8.440 -24.247  1.00  2.00           O  
HETATM 1241  C1' GDP B 600     -28.849   8.763 -25.090  1.00  2.00           C  
HETATM 1242  N9  GDP B 600     -28.143   7.481 -25.110  1.00  5.88           N  
HETATM 1243  C8  GDP B 600     -27.071   7.220 -24.090  1.00  9.42           C  
HETATM 1244  N7  GDP B 600     -26.782   5.940 -24.597  1.00 10.36           N  
HETATM 1245  C5  GDP B 600     -27.450   5.458 -25.639  1.00 10.45           C  
HETATM 1246  C6  GDP B 600     -27.620   4.362 -26.513  1.00 13.51           C  
HETATM 1247  O6  GDP B 600     -26.805   3.312 -26.310  1.00 11.34           O  
HETATM 1248  N1  GDP B 600     -28.507   4.321 -27.532  1.00 10.31           N  
HETATM 1249  C2  GDP B 600     -29.388   5.500 -27.745  1.00  5.81           C  
HETATM 1250  N2  GDP B 600     -30.175   5.234 -28.765  1.00  6.23           N  
HETATM 1251  N3  GDP B 600     -29.299   6.509 -26.984  1.00  4.23           N  
HETATM 1252  C4  GDP B 600     -28.376   6.518 -26.004  1.00  7.64           C  
HETATM 1253  O01 TA1 B 601     -33.566 -10.077 -35.620  1.00 63.75           O  
HETATM 1254  C01 TA1 B 601     -33.969 -10.053 -37.003  1.00 63.37           C  
HETATM 1255  C02 TA1 B 601     -35.372  -9.223 -37.050  1.00 64.56           C  
HETATM 1256  O02 TA1 B 601     -34.966  -7.908 -36.504  1.00 73.61           O  
HETATM 1257  C03 TA1 B 601     -35.402  -7.556 -35.205  1.00 82.30           C  
HETATM 1258  O03 TA1 B 601     -36.116  -8.254 -34.527  1.00 81.04           O  
HETATM 1259  C04 TA1 B 601     -34.925  -6.263 -34.789  1.00 85.16           C  
HETATM 1260  C05 TA1 B 601     -34.941  -5.058 -35.507  1.00 86.96           C  
HETATM 1261  C06 TA1 B 601     -34.413  -3.899 -34.875  1.00 87.81           C  
HETATM 1262  C07 TA1 B 601     -33.924  -3.815 -33.725  1.00 88.93           C  
HETATM 1263  C08 TA1 B 601     -33.866  -4.992 -32.928  1.00 88.17           C  
HETATM 1264  C09 TA1 B 601     -34.377  -6.304 -33.434  1.00 85.81           C  
HETATM 1265  C10 TA1 B 601     -36.081  -8.961 -38.486  1.00 60.76           C  
HETATM 1266  C11 TA1 B 601     -36.612  -7.455 -38.701  1.00 59.46           C  
HETATM 1267  O04 TA1 B 601     -35.506  -6.461 -38.693  1.00 58.42           O  
HETATM 1268  C12 TA1 B 601     -34.564  -6.406 -39.695  1.00 58.87           C  
HETATM 1269  O05 TA1 B 601     -34.522  -7.125 -40.648  1.00 60.49           O  
HETATM 1270  C13 TA1 B 601     -33.591  -5.283 -39.402  1.00 55.92           C  
HETATM 1271  C14 TA1 B 601     -37.605  -6.832 -37.685  1.00 60.18           C  
HETATM 1272  O06 TA1 B 601     -38.598  -6.569 -38.701  1.00 59.01           O  
HETATM 1273  C15 TA1 B 601     -37.740  -7.125 -39.720  1.00 59.51           C  
HETATM 1274  C16 TA1 B 601     -38.422  -8.309 -40.482  1.00 60.03           C  
HETATM 1275  C17 TA1 B 601     -37.664  -9.625 -40.388  1.00 61.43           C  
HETATM 1276  O07 TA1 B 601     -38.406 -10.656 -41.089  1.00 62.13           O  
HETATM 1277  C18 TA1 B 601     -37.307 -10.047 -38.883  1.00 62.13           C  
HETATM 1278  C19 TA1 B 601     -38.582  -9.916 -37.998  1.00 63.64           C  
HETATM 1279  C20 TA1 B 601     -36.977 -11.634 -38.819  1.00 65.31           C  
HETATM 1280  O08 TA1 B 601     -37.723 -12.365 -38.187  1.00 68.11           O  
HETATM 1281  C21 TA1 B 601     -35.752 -12.244 -39.512  1.00 63.59           C  
HETATM 1282  O09 TA1 B 601     -35.753 -13.708 -39.224  1.00 58.93           O  
HETATM 1283  C22 TA1 B 601     -35.974 -14.614 -40.242  1.00 56.05           C  
HETATM 1284  O10 TA1 B 601     -36.173 -14.332 -41.384  1.00 57.49           O  
HETATM 1285  C23 TA1 B 601     -35.936 -16.020 -39.712  1.00 54.68           C  
HETATM 1286  C24 TA1 B 601     -34.469 -11.572 -39.016  1.00 63.31           C  
HETATM 1287  C25 TA1 B 601     -33.692 -10.839 -39.908  1.00 62.60           C  
HETATM 1288  C26 TA1 B 601     -32.494 -10.053 -39.292  1.00 60.57           C  
HETATM 1289  O11 TA1 B 601     -31.933  -9.022 -40.176  1.00 60.54           O  
HETATM 1290  C27 TA1 B 601     -30.900  -9.355 -40.939  1.00 60.84           C  
HETATM 1291  O12 TA1 B 601     -30.361 -10.415 -41.008  1.00 60.71           O  
HETATM 1292  C28 TA1 B 601     -30.434  -8.131 -41.771  1.00 63.49           C  
HETATM 1293  O13 TA1 B 601     -29.308  -8.525 -42.532  1.00 63.94           O  
HETATM 1294  C29 TA1 B 601     -30.124  -6.969 -40.795  1.00 64.93           C  
HETATM 1295  N01 TA1 B 601     -29.205  -7.492 -39.791  1.00 68.46           N  
HETATM 1296  C30 TA1 B 601     -29.115  -6.988 -38.538  1.00 75.26           C  
HETATM 1297  O14 TA1 B 601     -29.786  -6.039 -38.146  1.00 72.57           O  
HETATM 1298  C31 TA1 B 601     -28.148  -7.707 -37.661  1.00 80.56           C  
HETATM 1299  C32 TA1 B 601     -28.665  -8.346 -36.471  1.00 84.57           C  
HETATM 1300  C33 TA1 B 601     -27.803  -9.044 -35.617  1.00 85.33           C  
HETATM 1301  C34 TA1 B 601     -26.449  -9.141 -35.893  1.00 87.21           C  
HETATM 1302  C35 TA1 B 601     -25.917  -8.523 -37.059  1.00 86.03           C  
HETATM 1303  C36 TA1 B 601     -26.786  -7.811 -37.931  1.00 83.75           C  
HETATM 1304  C37 TA1 B 601     -29.601  -5.726 -41.547  1.00 65.34           C  
HETATM 1305  C38 TA1 B 601     -28.244  -5.525 -41.845  1.00 66.75           C  
HETATM 1306  C39 TA1 B 601     -27.836  -4.356 -42.547  1.00 68.49           C  
HETATM 1307  C40 TA1 B 601     -28.762  -3.406 -42.944  1.00 66.79           C  
HETATM 1308  C41 TA1 B 601     -30.124  -3.595 -42.649  1.00 67.56           C  
HETATM 1309  C42 TA1 B 601     -30.538  -4.758 -41.948  1.00 66.62           C  
HETATM 1310  C43 TA1 B 601     -32.913  -9.318 -37.961  1.00 61.38           C  
HETATM 1311  C44 TA1 B 601     -33.957 -10.660 -41.399  1.00 62.81           C  
HETATM 1312  C45 TA1 B 601     -34.075 -11.643 -37.460  1.00 63.04           C  
HETATM 1313  C46 TA1 B 601     -32.691 -12.425 -37.314  1.00 62.66           C  
HETATM 1314  C47 TA1 B 601     -35.002 -12.417 -36.495  1.00 61.96           C  
CONECT 1192 1193 1194 1195 1196                                                 
CONECT 1193 1192 1224                                                           
CONECT 1194 1192                                                                
CONECT 1195 1192                                                                
CONECT 1196 1192 1197                                                           
CONECT 1197 1196 1198 1199 1200                                                 
CONECT 1198 1197                                                                
CONECT 1199 1197                                                                
CONECT 1200 1197 1201                                                           
CONECT 1201 1200 1202 1203 1204                                                 
CONECT 1202 1201                                                                
CONECT 1203 1201                                                                
CONECT 1204 1201 1205                                                           
CONECT 1205 1204 1206                                                           
CONECT 1206 1205 1207 1208                                                      
CONECT 1207 1206 1212                                                           
CONECT 1208 1206 1209 1210                                                      
CONECT 1209 1208                                                                
CONECT 1210 1208 1211 1212                                                      
CONECT 1211 1210                                                                
CONECT 1212 1207 1210 1213                                                      
CONECT 1213 1212 1214 1223                                                      
CONECT 1214 1213 1215                                                           
CONECT 1215 1214 1216                                                           
CONECT 1216 1215 1217 1223                                                      
CONECT 1217 1216 1218 1219                                                      
CONECT 1218 1217                                                                
CONECT 1219 1217 1220                                                           
CONECT 1220 1219 1221 1222                                                      
CONECT 1221 1220                                                                
CONECT 1222 1220 1223                                                           
CONECT 1223 1213 1216 1222                                                      
CONECT 1224 1193                                                                
CONECT 1225 1226 1227 1228 1229                                                 
CONECT 1226 1225                                                                
CONECT 1227 1225                                                                
CONECT 1228 1225                                                                
CONECT 1229 1225 1230                                                           
CONECT 1230 1229 1231 1232 1233                                                 
CONECT 1231 1230                                                                
CONECT 1232 1230                                                                
CONECT 1233 1230 1234                                                           
CONECT 1234 1233 1235                                                           
CONECT 1235 1234 1236 1237                                                      
CONECT 1236 1235 1241                                                           
CONECT 1237 1235 1238 1239                                                      
CONECT 1238 1237                                                                
CONECT 1239 1237 1240 1241                                                      
CONECT 1240 1239                                                                
CONECT 1241 1236 1239 1242                                                      
CONECT 1242 1241 1243 1252                                                      
CONECT 1243 1242 1244                                                           
CONECT 1244 1243 1245                                                           
CONECT 1245 1244 1246 1252                                                      
CONECT 1246 1245 1247 1248                                                      
CONECT 1247 1246                                                                
CONECT 1248 1246 1249                                                           
CONECT 1249 1248 1250 1251                                                      
CONECT 1250 1249                                                                
CONECT 1251 1249 1252                                                           
CONECT 1252 1242 1245 1251                                                      
CONECT 1253 1254                                                                
CONECT 1254 1253 1255 1310 1312                                                 
CONECT 1255 1254 1256 1265                                                      
CONECT 1256 1255 1257                                                           
CONECT 1257 1256 1258 1259                                                      
CONECT 1258 1257                                                                
CONECT 1259 1257 1260 1264                                                      
CONECT 1260 1259 1261                                                           
CONECT 1261 1260 1262                                                           
CONECT 1262 1261 1263                                                           
CONECT 1263 1262 1264                                                           
CONECT 1264 1259 1263                                                           
CONECT 1265 1255 1266 1277                                                      
CONECT 1266 1265 1267 1271 1273                                                 
CONECT 1267 1266 1268                                                           
CONECT 1268 1267 1269 1270                                                      
CONECT 1269 1268                                                                
CONECT 1270 1268                                                                
CONECT 1271 1266 1272                                                           
CONECT 1272 1271 1273                                                           
CONECT 1273 1266 1272 1274                                                      
CONECT 1274 1273 1275                                                           
CONECT 1275 1274 1276 1277                                                      
CONECT 1276 1275                                                                
CONECT 1277 1265 1275 1278 1279                                                 
CONECT 1278 1277                                                                
CONECT 1279 1277 1280 1281                                                      
CONECT 1280 1279                                                                
CONECT 1281 1279 1282 1286                                                      
CONECT 1282 1281 1283                                                           
CONECT 1283 1282 1284 1285                                                      
CONECT 1284 1283                                                                
CONECT 1285 1283                                                                
CONECT 1286 1281 1287 1312                                                      
CONECT 1287 1286 1288 1311                                                      
CONECT 1288 1287 1289 1310                                                      
CONECT 1289 1288 1290                                                           
CONECT 1290 1289 1291 1292                                                      
CONECT 1291 1290                                                                
CONECT 1292 1290 1293 1294                                                      
CONECT 1293 1292                                                                
CONECT 1294 1292 1295 1304                                                      
CONECT 1295 1294 1296                                                           
CONECT 1296 1295 1297 1298                                                      
CONECT 1297 1296                                                                
CONECT 1298 1296 1299 1303                                                      
CONECT 1299 1298 1300                                                           
CONECT 1300 1299 1301                                                           
CONECT 1301 1300 1302                                                           
CONECT 1302 1301 1303                                                           
CONECT 1303 1298 1302                                                           
CONECT 1304 1294 1305 1309                                                      
CONECT 1305 1304 1306                                                           
CONECT 1306 1305 1307                                                           
CONECT 1307 1306 1308                                                           
CONECT 1308 1307 1309                                                           
CONECT 1309 1304 1308                                                           
CONECT 1310 1254 1288                                                           
CONECT 1311 1287                                                                
CONECT 1312 1254 1286 1313 1314                                                 
CONECT 1313 1312                                                                
CONECT 1314 1312                                                                
MASTER      306    0    4    0    0    0    7    6 1311    3  123   99          
END                                                                             
