HEADER    OXIDOREDUCTASE                          12-DEC-12   3ZFS              
TITLE     CRYO-EM STRUCTURE OF THE F420-REDUCING NIFE-HYDROGENASE FROM A        
TITLE    2 METHANOGENIC ARCHAEON WITH BOUND SUBSTRATE                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: F420-REDUCING HYDROGENASE, SUBUNIT ALPHA;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FRHA, COENZYME F420 HYDROGENASE ALPHA SUBUNIT;              
COMPND   5 EC: 1.12.98.1;                                                       
COMPND   6 OTHER_DETAILS: FRHA CONTAINS A NIFE CENTER;                          
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: F420-REDUCING HYDROGENASE, SUBUNIT GAMMA;                  
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: FRHG, COENZYME F420 HYDROGENASE GAMMA SUBUNIT;              
COMPND  11 EC: 1.12.98.1;                                                       
COMPND  12 OTHER_DETAILS: FRHG CONTAINS THREE 4FE4S CLUSTERS;                   
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: F420-REDUCING HYDROGENASE, SUBUNIT BETA;                   
COMPND  15 CHAIN: C;                                                            
COMPND  16 SYNONYM: FRHB, COENZYME F420 HYDROGENASE BETA SUBUNIT;               
COMPND  17 EC: 1.12.98.1;                                                       
COMPND  18 OTHER_DETAILS: FRHB CONTAINS FAD AND A 4FE4S CLUSTER                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER MARBURGENSIS;               
SOURCE   3 ORGANISM_TAXID: 145263;                                              
SOURCE   4 STRAIN: DSM 2133;                                                    
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER MARBURGENSIS;               
SOURCE   7 ORGANISM_TAXID: 145263;                                              
SOURCE   8 STRAIN: DSM 2133;                                                    
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER MARBURGENSIS;               
SOURCE  11 ORGANISM_TAXID: 145263;                                              
SOURCE  12 STRAIN: DSM 2133                                                     
KEYWDS    OXIDOREDUCTASE, METHANOGENESIS                                        
EXPDTA    ELECTRON MICROSCOPY                                                   
MDLTYP    CA ATOMS ONLY, CHAIN A, B, C                                          
AUTHOR    D.J.MILLS,S.VITT,M.STRAUSS,S.SHIMA,J.VONCK                            
REVDAT   4   02-OCT-19 3ZFS    1       CRYST1 SCALE                             
REVDAT   3   23-AUG-17 3ZFS    1       REMARK                                   
REVDAT   2   03-APR-13 3ZFS    1       JRNL                                     
REVDAT   1   06-MAR-13 3ZFS    0                                                
JRNL        AUTH   D.J.MILLS,S.VITT,M.STRAUSS,S.SHIMA,J.VONCK                   
JRNL        TITL   DE NOVO MODELING OF THE F420-REDUCING [NIFE]-HYDROGENASE     
JRNL        TITL 2 FROM A METHANOGENIC ARCHAEON BY CRYO-ELECTRON MICROSCOPY     
JRNL        REF    ELIFE                         V.   2   218 2013              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   23483797                                                     
JRNL        DOI    10.7554/ELIFE.00218                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : COOT, UCSF CHIMERA, EMAN                  
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 2WPN                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : REFINEMENT PROTOCOL--RIGID BODY                  
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : 1.190                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 4.000                          
REMARK   3   NUMBER OF PARTICLES               : 97290                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: FIT OF X-RAY MODEL      
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD   
REMARK   3  -2097.(DEPOSITION ID: 10788).                                       
REMARK   4                                                                      
REMARK   4 3ZFS 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_1290052442.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE - CRYO EM            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : F420-REDUCING HYDROGENASE         
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.70                              
REMARK 245   SAMPLE SUPPORT DETAILS         : HOLEY CARBON                      
REMARK 245   SAMPLE VITRIFICATION DETAILS   : LIQUID ETHANE                     
REMARK 245   SAMPLE BUFFER                  : 50 MM TRIS/HCL, 2 MM DTT, 0.025   
REMARK 245                                    MM FAD                            
REMARK 245   PH                             : 7.60                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 11-FEB-11                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 77.00                          
REMARK 245   MICROSCOPE MODEL                  : FEI POLARA 300                 
REMARK 245   DETECTOR TYPE                     : KODAK SO-163 FILM              
REMARK 245   MINIMUM DEFOCUS (NM)              : 1650.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3820.00                        
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)  : 15.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 59000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 61400                          
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 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     VAL A   387                                                      
REMARK 465     MET A   388                                                      
REMARK 465     VAL A   389                                                      
REMARK 465     VAL A   390                                                      
REMARK 465     ASP A   391                                                      
REMARK 465     ASP A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     ASP A   394                                                      
REMARK 465     LYS A   395                                                      
REMARK 465     SER A   396                                                      
REMARK 465     VAL A   397                                                      
REMARK 465     ILE A   398                                                      
REMARK 465     LYS A   399                                                      
REMARK 465     ASN A   400                                                      
REMARK 465     GLU A   401                                                      
REMARK 465     MET A   402                                                      
REMARK 465     VAL A   403                                                      
REMARK 465     LYS A   404                                                      
REMARK 465     ILE A   405                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     ILE B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     PHE B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     LEU B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     GLU B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     LYS B    18                                                      
REMARK 465     ARG B    19                                                      
REMARK 465     GLU B    20                                                      
REMARK 465     GLU B    21                                                      
REMARK 465     PRO B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     LYS B    24                                                      
REMARK 465     GLU B    25                                                      
REMARK 465     LYS B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     GLU B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     VAL B    30                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     ALA B    32                                                      
REMARK 465     SER B    33                                                      
REMARK 465     LYS B    34                                                      
REMARK 465     GLU B    35                                                      
REMARK 465     GLU B    36                                                      
REMARK 465     VAL B    37                                                      
REMARK 465     GLU B    38                                                      
REMARK 465     LYS B    39                                                      
REMARK 465     VAL B    40                                                      
REMARK 465     ALA B    41                                                      
REMARK 465     GLU B    42                                                      
REMARK 465     GLU B    43                                                      
REMARK 465     ASN B    44                                                      
REMARK 465     ALA B    45                                                      
REMARK 465     ASN B   188                                                      
REMARK 465     ASP B   189                                                      
REMARK 465     MET B   190                                                      
REMARK 465     ASP B   191                                                      
REMARK 465     TYR B   192                                                      
REMARK 465     LEU B   193                                                      
REMARK 465     GLN B   194                                                      
REMARK 465     PRO B   195                                                      
REMARK 465     MET B   196                                                      
REMARK 465     LEU B   197                                                      
REMARK 465     ASP B   198                                                      
REMARK 465     LEU B   199                                                      
REMARK 465     LEU B   273                                                      
REMARK 465     GLY B   274                                                      
REMARK 465     LEU B   275                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     PHE C   281                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CA   GLY C    26     O2A  FAD C   304              1.46            
REMARK 500   CA   ASP C    25     O4'  FAD C   304              1.71            
REMARK 500   CA   ASP C    25     C5'  FAD C   304              1.78            
REMARK 500   CA   CYS C   104     S3   SF4 C   303              2.04            
REMARK 500   CA   ASP C    25     C4'  FAD C   304              2.11            
REMARK 500   CA   GLY C    26     PA   FAD C   304              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 COENZYME F420 (F42): ONLY ISOALLOXAZINE RING                         
REMARK 600 CARBONMONOXIDE-(DICYANO) IRON (FCO): ONLY FE ION                     
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     FCO A 2989                                                       
REMARK 610     F42 C  285                                                       
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FCO A 2989                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 2990                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F42 C 285                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 304                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-2097   RELATED DB: EMDB                              
REMARK 900 CRYO-EM STRUCTURE OF THE F420-REDUCING [NIFE]-HYDROGENASE FROM A     
REMARK 900 METHANOGENIC ARCHAEON WITH BOUND SUBSTRATE                           
DBREF  3ZFS A    1   405  UNP    D9PYF9   D9PYF9_METTM     1    405             
DBREF  3ZFS B    1   275  UNP    D9PYF7   D9PYF7_METTM     1    275             
DBREF  3ZFS C    1   281  UNP    D9PYF6   D9PYF6_METTM     1    281             
SEQRES   1 A  405  MET SER GLU ARG ILE VAL ILE SER PRO THR SER ARG GLN          
SEQRES   2 A  405  GLU GLY HIS ALA GLU LEU VAL MET GLU VAL ASP ASP GLU          
SEQRES   3 A  405  GLY ILE VAL THR LYS GLY ARG TYR PHE SER ILE THR PRO          
SEQRES   4 A  405  VAL ARG GLY LEU GLU LYS MET VAL THR GLY LYS ALA PRO          
SEQRES   5 A  405  GLU THR ALA PRO VAL MET VAL GLN ARG ILE CYS GLY VAL          
SEQRES   6 A  405  CYS PRO ILE PRO HIS THR LEU ALA SER VAL GLU ALA ILE          
SEQRES   7 A  405  ASP ASP SER LEU ASP ILE GLU VAL PRO LYS ALA GLY ARG          
SEQRES   8 A  405  LEU LEU ARG GLU LEU THR LEU ALA ALA HIS HIS VAL ASN          
SEQRES   9 A  405  SER HIS ALA ILE HIS HIS PHE LEU ILE ALA PRO ASP PHE          
SEQRES  10 A  405  VAL PRO GLU ASN LEU MET ALA ASP ALA ILE ASN SER VAL          
SEQRES  11 A  405  SER GLU ILE ARG LYS ASN ALA GLN TYR VAL VAL ASP MET          
SEQRES  12 A  405  VAL ALA GLY GLU GLY ILE HIS PRO SER ASP VAL ARG ILE          
SEQRES  13 A  405  GLY GLY MET ALA ASP ASN ILE THR GLU LEU ALA ARG LYS          
SEQRES  14 A  405  ARG LEU TYR ALA ARG LEU LYS GLN LEU LYS PRO LYS VAL          
SEQRES  15 A  405  ASN GLU HIS VAL GLU LEU MET ILE GLY LEU ILE GLU ASP          
SEQRES  16 A  405  LYS GLY LEU PRO GLU GLY LEU GLY VAL HIS ASN GLN PRO          
SEQRES  17 A  405  THR LEU ALA SER HIS GLN ILE TYR GLY ASP ARG THR LYS          
SEQRES  18 A  405  PHE ASP LEU ASP ARG PHE THR GLU ILE MET PRO GLU SER          
SEQRES  19 A  405  TRP TYR ASP ASP PRO GLU ILE ALA LYS ARG ALA CYS SER          
SEQRES  20 A  405  THR ILE PRO LEU TYR ASP GLY ARG ASN VAL GLU VAL GLY          
SEQRES  21 A  405  PRO ARG ALA ARG MET VAL GLU PHE GLN GLY PHE LYS GLU          
SEQRES  22 A  405  ARG GLY VAL VAL ALA GLN HIS VAL ALA ARG ALA LEU GLU          
SEQRES  23 A  405  MET LYS THR ALA LEU SER ARG ALA ILE GLU ILE LEU ASP          
SEQRES  24 A  405  GLU LEU ASP THR SER ALA PRO VAL ARG ALA ASP PHE ASP          
SEQRES  25 A  405  GLU ARG GLY THR GLY LYS LEU GLY ILE GLY ALA ILE GLU          
SEQRES  26 A  405  ALA PRO ARG GLY LEU ASP VAL HIS MET ALA LYS VAL GLU          
SEQRES  27 A  405  ASN GLY LYS ILE GLN PHE TYR SER ALA LEU VAL PRO THR          
SEQRES  28 A  405  THR TRP ASN ILE PRO THR MET GLY PRO ALA THR GLU GLY          
SEQRES  29 A  405  PHE HIS HIS GLU TYR GLY PRO HIS VAL ILE ARG ALA TYR          
SEQRES  30 A  405  ASP PRO CYS LEU SER CYS ALA THR HIS VAL MET VAL VAL          
SEQRES  31 A  405  ASP ASP GLU ASP LYS SER VAL ILE LYS ASN GLU MET VAL          
SEQRES  32 A  405  LYS ILE                                                      
SEQRES   1 B  275  MET SER LEU ILE ALA ARG ILE LYS ARG PHE LEU GLY LEU          
SEQRES   2 B  275  GLU ALA GLU ALA LYS ARG GLU GLU PRO GLU LYS GLU LYS          
SEQRES   3 B  275  SER GLU PRO VAL GLY ALA SER LYS GLU GLU VAL GLU LYS          
SEQRES   4 B  275  VAL ALA GLU GLU ASN ALA LYS PRO ARG ILE GLY TYR ILE          
SEQRES   5 B  275  HIS LEU SER GLY CYS THR GLY ASP ALA MET SER LEU THR          
SEQRES   6 B  275  GLU ASN TYR ASP ILE LEU ALA GLU LEU LEU THR ASN MET          
SEQRES   7 B  275  VAL ASP ILE VAL TYR GLY GLN THR LEU VAL ASP LEU TRP          
SEQRES   8 B  275  GLU MET PRO GLU MET ASP LEU ALA LEU VAL GLU GLY SER          
SEQRES   9 B  275  VAL CYS LEU GLN ASP GLU HIS SER LEU HIS GLU LEU LYS          
SEQRES  10 B  275  GLU LEU ARG GLU LYS ALA LYS LEU VAL CYS ALA PHE GLY          
SEQRES  11 B  275  SER CYS ALA ALA THR GLY CYS PHE THR ARG TYR SER ARG          
SEQRES  12 B  275  GLY GLY GLN GLN ALA GLN PRO SER HIS GLU SER PHE VAL          
SEQRES  13 B  275  PRO ILE ALA ASP LEU ILE ASP VAL ASP LEU ALA LEU PRO          
SEQRES  14 B  275  GLY CYS PRO PRO SER PRO GLU ILE ILE ALA LYS THR VAL          
SEQRES  15 B  275  VAL ALA LEU LEU ASN ASN ASP MET ASP TYR LEU GLN PRO          
SEQRES  16 B  275  MET LEU ASP LEU ALA GLY TYR THR GLU ALA CYS GLY CYS          
SEQRES  17 B  275  ASP LEU GLN THR LYS VAL VAL ASN GLN GLY LEU CYS ILE          
SEQRES  18 B  275  GLY CYS GLY THR CYS ALA MET ALA CYS GLN THR ARG ALA          
SEQRES  19 B  275  LEU ASP MET THR ASN GLY ARG PRO GLU LEU ASN SER ASP          
SEQRES  20 B  275  ARG CYS ILE LYS CYS GLY ILE CYS TYR VAL GLN CYS PRO          
SEQRES  21 B  275  ARG SER TRP TRP PRO GLU GLU GLN ILE LYS LYS GLU LEU          
SEQRES  22 B  275  GLY LEU                                                      
SEQRES   1 C  281  MET VAL LEU GLY THR TYR LYS GLU ILE VAL SER ALA ARG          
SEQRES   2 C  281  SER THR ASP ARG GLU ILE GLN LYS LEU ALA GLN ASP GLY          
SEQRES   3 C  281  GLY ILE VAL THR GLY LEU LEU ALA TYR ALA LEU ASP GLU          
SEQRES   4 C  281  GLY ILE ILE GLU GLY ALA VAL VAL ALA GLY PRO GLY GLU          
SEQRES   5 C  281  GLU PHE TRP LYS PRO GLN PRO MET VAL ALA MET SER SER          
SEQRES   6 C  281  ASP GLU LEU LYS ALA ALA ALA GLY THR LYS TYR THR PHE          
SEQRES   7 C  281  SER PRO ASN VAL MET MET LEU LYS LYS ALA VAL ARG GLN          
SEQRES   8 C  281  TYR GLY ILE GLU LYS LEU GLY THR VAL ALA ILE PRO CYS          
SEQRES   9 C  281  GLN THR MET GLY ILE ARG LYS MET GLN THR TYR PRO PHE          
SEQRES  10 C  281  GLY VAL ARG PHE LEU ALA ASP LYS ILE LYS LEU LEU VAL          
SEQRES  11 C  281  GLY ILE TYR CYS MET GLU ASN PHE PRO TYR THR SER LEU          
SEQRES  12 C  281  GLN THR PHE ILE CYS GLU LYS LEU GLY VAL SER MET GLU          
SEQRES  13 C  281  LEU VAL GLU LYS MET ASP ILE GLY LYS GLY LYS PHE TRP          
SEQRES  14 C  281  VAL TYR THR GLN ASP ASP VAL LEU THR LEU PRO LEU LYS          
SEQRES  15 C  281  GLU THR HIS GLY TYR GLU GLN ALA GLY CYS LYS ILE CYS          
SEQRES  16 C  281  LYS ASP TYR VAL ALA GLU LEU ALA ASP VAL SER THR GLY          
SEQRES  17 C  281  SER VAL GLY SER PRO ASP GLY TRP SER THR VAL ILE THR          
SEQRES  18 C  281  ARG THR ASP ALA GLY ASP SER ILE PHE LYS GLN ALA VAL          
SEQRES  19 C  281  GLU ALA GLY LEU PHE GLU THR LYS PRO ILE GLU GLU VAL          
SEQRES  20 C  281  LYS PRO GLY LEU GLY LEU LEU GLU LYS LEU ALA ALA GLN          
SEQRES  21 C  281  LYS LYS GLU LYS ALA GLU LYS ASN ILE ALA ALA ARG LYS          
SEQRES  22 C  281  GLU MET GLY LEU PRO THR PRO PHE                              
HET    FCO  A2989       1                                                       
HET     NI  A2990       1                                                       
HET    FE2  A2991       1                                                       
HET    SF4  B 300       8                                                       
HET    SF4  B 301       8                                                       
HET    SF4  B 302       8                                                       
HET    F42  C 285      19                                                       
HET    SF4  C 303       8                                                       
HET    FAD  C 304      53                                                       
HETNAM     FCO CARBONMONOXIDE-(DICYANO) IRON                                    
HETNAM      NI NICKEL (II) ION                                                  
HETNAM     FE2 FE (II) ION                                                      
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F42 COENZYME F420                                                    
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
FORMUL   4  FCO    C3 FE N2 O                                                   
FORMUL   5   NI    NI 2+                                                        
FORMUL   6  FE2    FE 2+                                                        
FORMUL   7  SF4    4(FE4 S4)                                                    
FORMUL  10  F42    C29 H36 N5 O18 P                                             
FORMUL  12  FAD    C27 H33 N9 O15 P2                                            
HELIX    1   1 LEU A   43  MET A   46  1                                   4    
HELIX    2   2 THR A   54  ILE A   62  1                                   9    
HELIX    3   3 PRO A   67  LEU A   82  1                                  16    
HELIX    4   4 LYS A   88  PHE A  111  1                                  24    
HELIX    5   5 LEU A  122  VAL A  141  1                                  20    
HELIX    6   6 GLU A  165  ILE A  193  1                                  29    
HELIX    7   7 PRO A  239  ARG A  244  1                                   6    
HELIX    8   8 PRO A  261  GLN A  269  1                                   9    
HELIX    9   9 VAL A  277  GLU A  300  1                                  24    
HELIX   10  10 PRO A  350  ASN A  354  1                                   5    
HELIX   11  11 MET A  358  THR A  362  1                                   5    
HELIX   12  12 HIS A  372  ALA A  376  1                                   5    
HELIX   13  13 LEU A  381  THR A  385  1                                   5    
HELIX   14  14 ARG A  262  GLU A  267  1                                   6    
HELIX   15  15 HIS A  372  ARG A  375  1                                   4    
HELIX   16  16 GLY B   59  THR B   65  1                                   7    
HELIX   17  17 LEU B   74  MET B   78  1                                   5    
HELIX   18  18 HIS B  111  GLU B  121  1                                  11    
HELIX   19  19 PRO B  175  LEU B  186  1                                  12    
HELIX   20  20 THR B  225  ALA B  229  1                                   5    
HELIX   21  21 GLU B  266  GLU B  272  1                                   7    
HELIX   22  22 ARG C   17  GLN C   20  1                                   4    
HELIX   23  23 GLY C   27  ASP C   38  1                                  12    
HELIX   24  24 SER C   64  ALA C   71  1                                   8    
HELIX   25  25 MET C   83  GLN C   91  1                                   9    
HELIX   26  26 THR C  106  THR C  114  1                                   9    
HELIX   27  27 TYR C  140  GLU C  149  1                                  10    
HELIX   28  28 MET C  155  LEU C  157  1                                   3    
HELIX   29  29 LYS C  182  GLY C  186  1                                   5    
HELIX   30  30 ASP C  224  GLU C  235  1                                  12    
HELIX   31  31 LEU C  251  GLU C  274  1                                  24    
SHEET    1   1 1 ARG A   4  PRO A   9  0                                        
SHEET    1   2 1 HIS A  16  GLU A  22  0                                        
SHEET    1   3 1 VAL A  29  PHE A  35  0                                        
SHEET    1   4 1 LYS A 318  ILE A 324  0                                        
SHEET    1   5 1 ASP A 331  LYS A 336  0                                        
SHEET    1   6 1 PHE A 344  VAL A 349  0                                        
SHEET    1   7 1 ARG B  48  ILE B  52  0                                        
SHEET    1   8 1 ASP B  80  TYR B  83  0                                        
SHEET    1   9 1 ASP B  97  GLU B 102  0                                        
SHEET    1  10 1 VAL B 126  GLY B 130  0                                        
SHEET    1  11 1 LEU B 166  PRO B 169  0                                        
SHEET    1  12 1 LEU B 235  THR B 238  0                                        
SHEET    1  13 1 PRO B 242  LEU B 244  0                                        
SHEET    1  14 1 GLU C   8  ARG C  13  0                                        
SHEET    1  15 1 GLU C  43  GLY C  49  0                                        
SHEET    1  16 1 PRO C  57  ALA C  62  0                                        
SHEET    1  17 1 LYS C  96  ILE C 102  0                                        
SHEET    1  18 1 LEU C 128  ILE C 132  0                                        
SHEET    1  19 1 GLU C 159  GLY C 164  0                                        
SHEET    1  20 1 LYS C 167  TYR C 171  0                                        
SHEET    1  21 1 VAL C 176  LEU C 181  0                                        
SHEET    1  22 1 VAL C 205  SER C 209  0                                        
SHEET    1  23 1 SER C 217  THR C 221  0                                        
SHEET    1  24 1 PHE C 239  LYS C 242  0                                        
SITE     1 AC1  1  NI A2990                                                     
SITE     1 AC2  1 FCO A2989                                                     
SITE     1 AC3  5 GLY B  56  CYS B  57  GLY B  59  CYS B 132                    
SITE     2 AC3  5 CYS B 171                                                     
SITE     1 AC4  4 CYS B 249  LYS B 251  CYS B 252  CYS B 255                    
SITE     1 AC5  6 ILE B 221  GLY B 222  CYS B 223  GLY B 224                    
SITE     2 AC5  6 THR B 225  CYS B 226                                          
SITE     1 AC6  5 GLY C 164  SER C 209  VAL C 210  SER C 217                    
SITE     2 AC6  5 FAD C 304                                                     
SITE     1 AC7  4 PRO C 103  CYS C 104  CYS C 134  MET C 135                    
SITE     1 AC8 14 GLN C  24  ASP C  25  GLY C  26  ILE C  28                    
SITE     2 AC8 14 VAL C  29  VAL C  47  ALA C  48  ALA C  72                    
SITE     3 AC8 14 THR C  74  TYR C  76  ILE C 132  GLY C 208                    
SITE     4 AC8 14 SER C 209  F42 C 285                                          
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  SER A   2     112.992 120.697 218.261  1.00 27.10           C  
ATOM      2  CA  GLU A   3     114.152 117.898 215.961  1.00 29.03           C  
ATOM      3  CA  ARG A   4     117.608 117.711 214.384  1.00 16.09           C  
ATOM      4  CA  ILE A   5     118.691 115.205 211.735  1.00 27.55           C  
ATOM      5  CA  VAL A   6     122.181 114.481 210.406  1.00 19.19           C  
ATOM      6  CA  ILE A   7     123.599 112.722 207.373  1.00 18.80           C  
ATOM      7  CA  SER A   8     127.340 112.076 207.335  1.00 20.85           C  
ATOM      8  CA  PRO A   9     128.336 111.738 204.767  1.00 14.68           C  
ATOM      9  CA  THR A  10     125.676 112.647 202.210  1.00 20.15           C  
ATOM     10  CA  SER A  11     125.912 110.382 199.169  1.00 19.71           C  
ATOM     11  CA  ARG A  12     128.237 111.412 196.341  1.00 15.62           C  
ATOM     12  CA  GLN A  13     129.864 114.098 198.474  1.00 18.48           C  
ATOM     13  CA  GLU A  14     133.205 112.801 197.216  1.00 30.00           C  
ATOM     14  CA  GLY A  15     134.363 113.377 200.785  1.00 20.03           C  
ATOM     15  CA  HIS A  16     133.283 112.790 204.363  1.00 19.59           C  
ATOM     16  CA  ALA A  17     130.667 115.432 204.942  1.00 23.67           C  
ATOM     17  CA  GLU A  18     127.888 116.361 207.373  1.00 22.82           C  
ATOM     18  CA  LEU A  19     124.561 118.213 207.403  1.00 16.67           C  
ATOM     19  CA  VAL A  20     122.062 118.652 210.273  1.00 19.87           C  
ATOM     20  CA  MET A  21     118.349 119.089 209.524  1.00 18.31           C  
ATOM     21  CA  GLU A  22     116.032 121.084 211.794  1.00 12.99           C  
ATOM     22  CA  VAL A  23     112.466 119.838 212.337  1.00 16.08           C  
ATOM     23  CA  ASP A  24     108.976 121.016 213.315  1.00 18.17           C  
ATOM     24  CA  ASP A  25     107.822 117.411 213.800  1.00 30.00           C  
ATOM     25  CA  GLU A  26     105.842 117.474 210.538  1.00 30.00           C  
ATOM     26  CA  GLY A  27     109.094 116.247 209.034  1.00 30.00           C  
ATOM     27  CA  ILE A  28     109.697 119.756 207.720  1.00 17.91           C  
ATOM     28  CA  VAL A  29     113.034 121.585 207.699  1.00 21.23           C  
ATOM     29  CA  THR A  30     113.881 125.071 208.943  1.00 19.54           C  
ATOM     30  CA  LYS A  31     117.647 125.186 209.348  1.00 24.43           C  
ATOM     31  CA  GLY A  32     120.835 123.657 207.900  1.00 14.38           C  
ATOM     32  CA  ARG A  33     124.603 123.497 208.510  1.00 19.08           C  
ATOM     33  CA  TYR A  34     127.155 121.962 206.113  1.00 18.73           C  
ATOM     34  CA  PHE A  35     130.592 120.711 207.184  1.00 12.16           C  
ATOM     35  CA  SER A  36     132.851 119.581 204.337  1.00 17.89           C  
ATOM     36  CA  ILE A  37     134.530 118.725 206.400  1.00 23.17           C  
ATOM     37  CA  THR A  38     138.092 119.255 207.660  1.00 17.35           C  
ATOM     38  CA  PRO A  39     140.838 118.281 207.796  1.00 20.00           C  
ATOM     39  CA  VAL A  40     142.053 120.211 204.737  1.00 30.00           C  
ATOM     40  CA  ARG A  41     145.434 120.081 202.964  1.00  1.00           C  
ATOM     41  CA  GLY A  42     146.548 123.647 203.712  1.00  1.00           C  
ATOM     42  CA  LEU A  43     147.714 124.266 200.159  1.00 17.20           C  
ATOM     43  CA  GLU A  44     147.382 127.999 199.787  1.00 23.45           C  
ATOM     44  CA  LYS A  45     150.017 128.192 202.551  1.00 14.89           C  
ATOM     45  CA  MET A  46     151.982 125.119 201.578  1.00 16.69           C  
ATOM     46  CA  VAL A  47     152.468 126.732 198.116  1.00 19.01           C  
ATOM     47  CA  THR A  48     154.134 129.904 199.617  1.00 16.60           C  
ATOM     48  CA  GLY A  49     157.838 130.376 198.951  1.00 17.68           C  
ATOM     49  CA  LYS A  50     157.854 127.353 196.698  1.00 13.50           C  
ATOM     50  CA  ALA A  51     159.159 127.737 193.190  1.00 27.42           C  
ATOM     51  CA  PRO A  52     156.199 129.366 191.464  1.00 23.24           C  
ATOM     52  CA  GLU A  53     156.215 126.627 188.861  1.00 17.76           C  
ATOM     53  CA  THR A  54     154.643 124.576 191.631  1.00 19.85           C  
ATOM     54  CA  ALA A  55     151.082 125.808 191.224  1.00 23.76           C  
ATOM     55  CA  PRO A  56     149.461 123.616 188.557  1.00 22.13           C  
ATOM     56  CA  VAL A  57     151.471 120.613 189.740  1.00 22.51           C  
ATOM     57  CA  MET A  58     150.721 121.811 193.258  1.00 24.15           C  
ATOM     58  CA  VAL A  59     147.188 123.126 192.751  1.00 20.11           C  
ATOM     59  CA  GLN A  60     145.930 120.184 190.667  1.00 22.16           C  
ATOM     60  CA  ARG A  61     146.210 117.852 193.689  1.00 20.71           C  
ATOM     61  CA  ILE A  62     143.510 119.999 195.312  1.00 21.72           C  
ATOM     62  CA  CYS A  63     141.006 117.837 193.432  1.00 16.66           C  
ATOM     63  CA  GLY A  64     141.545 114.803 191.172  1.00 18.21           C  
ATOM     64  CA  VAL A  65     138.076 115.077 189.584  1.00 15.39           C  
ATOM     65  CA  CYS A  66     138.474 118.674 188.332  1.00 14.78           C  
ATOM     66  CA  PRO A  67     142.114 118.801 187.205  1.00 18.59           C  
ATOM     67  CA  ILE A  68     141.357 121.209 184.355  1.00 15.22           C  
ATOM     68  CA  PRO A  69     139.769 123.927 186.504  1.00 24.59           C  
ATOM     69  CA  HIS A  70     142.600 124.041 189.027  1.00 19.94           C  
ATOM     70  CA  THR A  71     145.421 123.448 186.574  1.00 24.21           C  
ATOM     71  CA  LEU A  72     144.032 125.891 184.020  1.00 17.36           C  
ATOM     72  CA  ALA A  73     143.264 128.502 186.644  1.00 22.54           C  
ATOM     73  CA  SER A  74     146.706 128.064 188.141  1.00 16.10           C  
ATOM     74  CA  VAL A  75     148.321 128.509 184.752  1.00 21.25           C  
ATOM     75  CA  GLU A  76     146.303 131.639 184.091  1.00 22.50           C  
ATOM     76  CA  ALA A  77     147.175 133.117 187.481  1.00 25.98           C  
ATOM     77  CA  ILE A  78     150.842 132.209 187.068  1.00 19.55           C  
ATOM     78  CA  ASP A  79     150.827 133.800 183.620  1.00 19.91           C  
ATOM     79  CA  ASP A  80     149.293 137.007 184.966  1.00 24.46           C  
ATOM     80  CA  SER A  81     152.058 137.351 187.550  1.00 20.64           C  
ATOM     81  CA  LEU A  82     154.503 136.541 184.761  1.00 13.48           C  
ATOM     82  CA  ASP A  83     152.700 138.955 182.450  1.00 17.60           C  
ATOM     83  CA  ILE A  84     153.416 136.487 179.646  1.00 14.98           C  
ATOM     84  CA  GLU A  85     150.950 136.171 176.756  1.00 27.88           C  
ATOM     85  CA  VAL A  86     149.968 132.820 175.224  1.00 17.74           C  
ATOM     86  CA  PRO A  87     149.947 132.074 171.481  1.00 23.43           C  
ATOM     87  CA  LYS A  88     146.564 131.853 169.745  1.00 20.95           C  
ATOM     88  CA  ALA A  89     147.122 128.149 169.083  1.00 16.70           C  
ATOM     89  CA  GLY A  90     148.024 127.644 172.743  1.00 23.83           C  
ATOM     90  CA  ARG A  91     144.828 129.284 173.946  1.00 20.10           C  
ATOM     91  CA  LEU A  92     142.853 126.930 171.695  1.00 15.01           C  
ATOM     92  CA  LEU A  93     144.465 123.995 173.501  1.00 22.43           C  
ATOM     93  CA  ARG A  94     143.560 125.295 176.955  1.00 16.21           C  
ATOM     94  CA  GLU A  95     139.952 125.644 175.813  1.00 15.42           C  
ATOM     95  CA  LEU A  96     140.025 122.161 174.282  1.00 21.72           C  
ATOM     96  CA  THR A  97     141.246 120.568 177.512  1.00 16.16           C  
ATOM     97  CA  LEU A  98     138.780 122.480 179.683  1.00 25.55           C  
ATOM     98  CA  ALA A  99     135.780 121.354 177.637  1.00 20.67           C  
ATOM     99  CA  ALA A 100     136.839 117.713 177.395  1.00 19.41           C  
ATOM    100  CA  HIS A 101     137.592 117.745 181.117  1.00 17.79           C  
ATOM    101  CA  HIS A 102     134.156 119.151 181.771  1.00 22.19           C  
ATOM    102  CA  VAL A 103     132.316 116.605 179.822  1.00 19.75           C  
ATOM    103  CA  ASN A 104     134.329 113.840 181.475  1.00 17.50           C  
ATOM    104  CA  SER A 105     133.725 115.037 185.030  1.00 22.09           C  
ATOM    105  CA  HIS A 106     130.028 115.637 184.371  1.00 15.77           C  
ATOM    106  CA  ALA A 107     129.385 112.343 182.580  1.00 17.97           C  
ATOM    107  CA  ILE A 108     131.025 110.845 185.668  1.00 15.85           C  
ATOM    108  CA  HIS A 109     129.176 112.712 188.388  1.00 19.90           C  
ATOM    109  CA  HIS A 110     125.933 112.582 186.461  1.00 18.42           C  
ATOM    110  CA  PHE A 111     126.079 108.907 185.516  1.00 16.93           C  
ATOM    111  CA  LEU A 112     126.965 107.786 189.037  1.00 15.43           C  
ATOM    112  CA  ILE A 113     124.746 110.440 190.519  1.00 17.94           C  
ATOM    113  CA  ALA A 114     121.193 109.194 190.104  1.00 16.47           C  
ATOM    114  CA  PRO A 115     120.987 105.699 191.593  1.00 16.12           C  
ATOM    115  CA  ASP A 116     117.611 106.779 192.984  1.00 16.43           C  
ATOM    116  CA  PHE A 117     116.319 107.942 189.599  1.00 13.87           C  
ATOM    117  CA  VAL A 118     116.638 104.440 188.157  1.00 23.89           C  
ATOM    118  CA  PRO A 119     115.437 101.511 190.279  1.00 19.28           C  
ATOM    119  CA  GLU A 120     116.471  98.432 188.263  1.00 15.57           C  
ATOM    120  CA  ASN A 121     117.576  97.026 184.904  1.00 26.11           C  
ATOM    121  CA  LEU A 122     117.748 100.446 183.268  1.00 21.56           C  
ATOM    122  CA  MET A 123     120.398 101.701 185.696  1.00 12.49           C  
ATOM    123  CA  ALA A 124     123.002  98.990 184.942  1.00 24.62           C  
ATOM    124  CA  ASP A 125     122.265  99.776 181.295  1.00 18.79           C  
ATOM    125  CA  ALA A 126     122.894 103.505 181.681  1.00 22.56           C  
ATOM    126  CA  ILE A 127     125.971 103.199 183.894  1.00 23.27           C  
ATOM    127  CA  ASN A 128     127.459 101.203 181.019  1.00 13.57           C  
ATOM    128  CA  SER A 129     126.262 103.257 178.052  1.00 18.06           C  
ATOM    129  CA  VAL A 130     127.687 106.376 179.705  1.00 14.92           C  
ATOM    130  CA  SER A 131     131.025 105.008 180.886  1.00 30.33           C  
ATOM    131  CA  GLU A 132     131.212 104.184 177.183  1.00 14.02           C  
ATOM    132  CA  ILE A 133     131.607 107.938 176.684  1.00 21.83           C  
ATOM    133  CA  ARG A 134     134.050 108.765 179.478  1.00 16.14           C  
ATOM    134  CA  LYS A 135     136.689 106.941 177.531  1.00 19.45           C  
ATOM    135  CA  ASN A 136     136.555 109.296 174.634  1.00 24.26           C  
ATOM    136  CA  ALA A 137     136.797 112.355 176.881  1.00 13.83           C  
ATOM    137  CA  GLN A 138     139.405 111.081 179.335  1.00 19.30           C  
ATOM    138  CA  TYR A 139     141.013 110.300 175.788  1.00 20.08           C  
ATOM    139  CA  VAL A 140     140.253 113.989 175.232  1.00 18.29           C  
ATOM    140  CA  VAL A 141     142.272 115.052 178.262  1.00 21.65           C  
ATOM    141  CA  ASP A 142     145.419 113.110 177.511  1.00  0.00           C  
ATOM    142  CA  MET A 143     145.937 114.164 173.926  1.00 18.55           C  
ATOM    143  CA  VAL A 144     146.318 117.675 175.290  1.00 16.23           C  
ATOM    144  CA  ALA A 145     146.989 116.400 178.778  1.00 23.38           C  
ATOM    145  CA  GLY A 146     149.274 113.364 178.864  1.00 20.24           C  
ATOM    146  CA  GLU A 147     147.041 111.516 181.317  1.00 20.53           C  
ATOM    147  CA  GLY A 148     143.841 111.792 183.338  1.00 19.38           C  
ATOM    148  CA  ILE A 149     143.073 112.553 185.951  1.00 17.87           C  
ATOM    149  CA  HIS A 150     145.942 114.997 186.472  1.00 18.59           C  
ATOM    150  CA  PRO A 151     147.252 116.632 183.315  1.00 20.73           C  
ATOM    151  CA  SER A 152     150.987 116.999 182.659  1.00 23.05           C  
ATOM    152  CA  ASP A 153     150.303 119.116 179.555  1.00 23.72           C  
ATOM    153  CA  VAL A 154     149.532 122.572 180.994  1.00 24.13           C  
ATOM    154  CA  ARG A 155     152.424 124.601 182.456  1.00 23.26           C  
ATOM    155  CA  ILE A 156     153.255 128.296 182.827  1.00 21.86           C  
ATOM    156  CA  GLY A 157     154.083 129.329 179.268  1.00 23.58           C  
ATOM    157  CA  GLY A 158     151.392 127.319 177.462  1.00 20.89           C  
ATOM    158  CA  MET A 159     151.036 123.642 176.644  1.00 23.21           C  
ATOM    159  CA  ALA A 160     153.878 121.067 176.642  1.00 24.30           C  
ATOM    160  CA  ASP A 161     152.661 119.025 173.676  1.00 26.90           C  
ATOM    161  CA  ASN A 162     150.991 119.000 170.255  1.00 25.03           C  
ATOM    162  CA  ILE A 163     149.069 116.442 168.229  1.00 28.17           C  
ATOM    163  CA  THR A 164     150.943 118.343 165.594  1.00 16.56           C  
ATOM    164  CA  GLU A 165     149.258 117.137 163.368  1.00 26.28           C  
ATOM    165  CA  LEU A 166     148.323 113.463 163.699  1.00 21.62           C  
ATOM    166  CA  ALA A 167     146.328 113.794 166.882  1.00  0.00           C  
ATOM    167  CA  ARG A 168     143.223 115.668 165.823  1.00 21.74           C  
ATOM    168  CA  LYS A 169     142.104 113.175 163.177  1.00 13.68           C  
ATOM    169  CA  ARG A 170     142.221 110.093 165.371  1.00 16.05           C  
ATOM    170  CA  LEU A 171     141.305 112.274 168.277  1.00 15.24           C  
ATOM    171  CA  TYR A 172     138.739 114.018 166.083  1.00 19.32           C  
ATOM    172  CA  ALA A 173     137.334 110.556 165.392  1.00 19.07           C  
ATOM    173  CA  ARG A 174     136.959 110.036 169.137  1.00 22.20           C  
ATOM    174  CA  LEU A 175     134.701 113.085 169.346  1.00 20.14           C  
ATOM    175  CA  LYS A 176     132.868 112.246 166.118  1.00 22.41           C  
ATOM    176  CA  GLN A 177     131.868 108.805 167.572  1.00 20.24           C  
ATOM    177  CA  LEU A 178     131.329 110.165 171.140  1.00 25.37           C  
ATOM    178  CA  LYS A 179     128.668 112.826 170.650  1.00 24.80           C  
ATOM    179  CA  PRO A 180     125.836 111.093 168.792  1.00 21.73           C  
ATOM    180  CA  LYS A 181     125.230 108.294 171.295  1.00 11.14           C  
ATOM    181  CA  VAL A 182     126.690 109.401 174.629  1.00 17.93           C  
ATOM    182  CA  ASN A 183     125.239 112.903 174.342  1.00 21.68           C  
ATOM    183  CA  GLU A 184     122.108 111.644 172.611  1.00 18.47           C  
ATOM    184  CA  HIS A 185     120.973 108.975 175.037  1.00 25.23           C  
ATOM    185  CA  VAL A 186     122.256 110.114 178.402  1.00 15.85           C  
ATOM    186  CA  GLU A 187     120.948 113.636 178.072  1.00 20.76           C  
ATOM    187  CA  LEU A 188     117.579 112.451 176.939  1.00 23.09           C  
ATOM    188  CA  MET A 189     117.245 109.992 179.770  1.00 21.87           C  
ATOM    189  CA  ILE A 190     118.332 112.522 182.338  1.00 20.16           C  
ATOM    190  CA  GLY A 191     115.738 115.036 181.204  1.00 22.58           C  
ATOM    191  CA  LEU A 192     112.966 112.399 181.035  1.00 12.63           C  
ATOM    192  CA  ILE A 193     113.382 110.650 184.412  1.00 14.55           C  
ATOM    193  CA  GLU A 194     113.686 114.051 186.097  1.00 16.85           C  
ATOM    194  CA  ASP A 195     109.923 113.809 186.545  1.00 26.15           C  
ATOM    195  CA  LYS A 196     110.418 111.122 189.196  1.00 16.76           C  
ATOM    196  CA  GLY A 197     111.595 113.822 191.578  1.00 13.21           C  
ATOM    197  CA  LEU A 198     108.518 115.835 192.537  1.00 12.12           C  
ATOM    198  CA  PRO A 199     107.716 118.938 194.590  1.00 15.48           C  
ATOM    199  CA  GLU A 200     107.573 119.964 196.994  1.00 17.06           C  
ATOM    200  CA  GLY A 201     110.527 120.714 194.744  1.00 14.85           C  
ATOM    201  CA  LEU A 202     111.322 123.453 197.220  1.00  8.31           C  
ATOM    202  CA  GLY A 203     112.666 120.998 197.413  1.00 22.86           C  
ATOM    203  CA  VAL A 204     114.437 123.081 196.632  1.00 12.81           C  
ATOM    204  CA  HIS A 205     114.563 126.709 195.517  1.00 16.71           C  
ATOM    205  CA  ASN A 206     117.749 128.800 195.483  1.00 24.84           C  
ATOM    206  CA  GLN A 207     118.200 132.579 195.627  1.00 20.06           C  
ATOM    207  CA  PRO A 208     120.029 134.604 194.844  1.00 21.23           C  
ATOM    208  CA  THR A 209     122.972 133.433 192.718  1.00 27.31           C  
ATOM    209  CA  LEU A 210     124.720 135.075 189.767  1.00 29.65           C  
ATOM    210  CA  ALA A 211     128.236 133.836 189.042  1.00 18.86           C  
ATOM    211  CA  SER A 212     131.062 132.931 186.680  1.00 18.61           C  
ATOM    212  CA  HIS A 213     132.466 134.208 183.401  1.00 24.61           C  
ATOM    213  CA  GLN A 214     130.381 131.841 181.378  1.00 20.11           C  
ATOM    214  CA  ILE A 215     132.340 128.881 180.043  1.00 16.14           C  
ATOM    215  CA  TYR A 216     134.216 130.921 179.603  1.00 26.16           C  
ATOM    216  CA  GLY A 217     133.728 134.706 179.518  1.00 19.17           C  
ATOM    217  CA  ASP A 218     136.305 134.717 180.773  1.00 19.08           C  
ATOM    218  CA  ARG A 219     137.859 138.059 181.767  1.00 25.45           C  
ATOM    219  CA  THR A 220     137.777 140.345 183.496  1.00 18.33           C  
ATOM    220  CA  LYS A 221     134.036 140.426 184.182  1.00 17.37           C  
ATOM    221  CA  PHE A 222     132.751 139.012 187.453  1.00 30.00           C  
ATOM    222  CA  ASP A 223     135.058 138.870 190.454  1.00 13.48           C  
ATOM    223  CA  LEU A 224     136.871 140.881 190.913  1.00 30.00           C  
ATOM    224  CA  ASP A 225     134.695 142.651 191.186  1.00 24.47           C  
ATOM    225  CA  ARG A 226     134.058 142.714 194.936  1.00 18.56           C  
ATOM    226  CA  PHE A 227     134.582 139.598 197.046  1.00 17.25           C  
ATOM    227  CA  THR A 228     135.213 138.496 200.629  1.00 15.02           C  
ATOM    228  CA  GLU A 229     136.308 135.490 202.675  1.00 14.28           C  
ATOM    229  CA  ILE A 230     135.219 135.331 206.314  1.00 21.15           C  
ATOM    230  CA  MET A 231     134.797 133.046 209.319  1.00 30.00           C  
ATOM    231  CA  PRO A 232     133.022 130.811 209.071  1.00 15.12           C  
ATOM    232  CA  GLU A 233     132.557 131.904 212.683  1.00 28.33           C  
ATOM    233  CA  SER A 234     129.243 133.307 211.463  1.00 16.73           C  
ATOM    234  CA  TRP A 235     127.744 129.888 210.748  1.00 20.06           C  
ATOM    235  CA  TYR A 236     125.360 129.280 212.090  1.00 16.74           C  
ATOM    236  CA  ASP A 237     125.141 129.676 215.866  1.00  1.00           C  
ATOM    237  CA  ASP A 238     126.799 126.948 217.958  1.00  1.00           C  
ATOM    238  CA  PRO A 239     130.586 126.524 218.189  1.00 24.62           C  
ATOM    239  CA  GLU A 240     130.435 122.831 217.247  1.00 18.79           C  
ATOM    240  CA  ILE A 241     129.430 124.195 213.849  1.00 22.56           C  
ATOM    241  CA  ALA A 242     132.531 126.307 214.439  1.00 23.27           C  
ATOM    242  CA  LYS A 243     134.234 122.953 214.971  1.00 13.57           C  
ATOM    243  CA  ARG A 244     133.029 122.473 211.398  1.00 18.06           C  
ATOM    244  CA  ALA A 245     135.068 125.568 210.669  1.00 14.92           C  
ATOM    245  CA  CYS A 246     137.735 124.050 208.495  1.00 17.49           C  
ATOM    246  CA  SER A 247     135.491 125.706 205.924  1.00 18.16           C  
ATOM    247  CA  THR A 248     135.473 129.446 205.221  1.00 19.32           C  
ATOM    248  CA  ILE A 249     132.417 131.457 204.098  1.00 20.43           C  
ATOM    249  CA  PRO A 250     132.574 133.011 200.571  1.00 21.79           C  
ATOM    250  CA  LEU A 251     130.142 135.826 199.729  1.00 23.36           C  
ATOM    251  CA  TYR A 252     129.465 137.797 196.577  1.00 24.80           C  
ATOM    252  CA  ASP A 253     128.470 141.373 197.423  1.00 23.70           C  
ATOM    253  CA  GLY A 254     127.897 139.985 200.939  1.00 24.74           C  
ATOM    254  CA  ARG A 255     125.273 137.526 199.694  1.00 25.01           C  
ATOM    255  CA  ASN A 256     125.521 133.702 199.974  1.00 25.28           C  
ATOM    256  CA  VAL A 257     125.496 132.310 196.414  1.00 24.89           C  
ATOM    257  CA  GLU A 258     125.590 129.130 194.305  1.00 21.55           C  
ATOM    258  CA  VAL A 259     127.180 128.555 190.875  1.00 22.51           C  
ATOM    259  CA  GLY A 260     126.103 125.802 188.483  1.00 12.72           C  
ATOM    260  CA  PRO A 261     124.458 124.828 185.195  1.00 16.78           C  
ATOM    261  CA  ARG A 262     122.308 127.898 185.869  1.00 16.77           C  
ATOM    262  CA  ALA A 263     125.251 130.236 185.282  1.00 28.05           C  
ATOM    263  CA  ARG A 264     126.113 128.723 181.900  1.00 20.40           C  
ATOM    264  CA  MET A 265     122.529 129.422 180.835  1.00 25.43           C  
ATOM    265  CA  VAL A 266     121.153 132.376 182.782  1.00 18.68           C  
ATOM    266  CA  GLU A 267     124.688 133.682 182.479  1.00 26.76           C  
ATOM    267  CA  PHE A 268     125.399 134.620 179.743  1.00 28.38           C  
ATOM    268  CA  GLN A 269     123.064 132.684 177.387  1.00 16.86           C  
ATOM    269  CA  GLY A 270     119.743 132.491 179.080  1.00 14.39           C  
ATOM    270  CA  PHE A 271     117.539 129.859 180.639  1.00 24.55           C  
ATOM    271  CA  LYS A 272     115.037 131.442 183.028  1.00 27.05           C  
ATOM    272  CA  GLU A 273     113.234 128.804 185.116  1.00 21.19           C  
ATOM    273  CA  ARG A 274     115.079 127.095 187.872  1.00 32.49           C  
ATOM    274  CA  GLY A 275     114.096 124.112 190.044  1.00 37.27           C  
ATOM    275  CA  VAL A 276     115.959 121.859 192.435  1.00 15.48           C  
ATOM    276  CA  VAL A 277     115.375 119.508 189.533  1.00 15.76           C  
ATOM    277  CA  ALA A 278     116.419 122.242 187.077  1.00 16.26           C  
ATOM    278  CA  GLN A 279     120.153 122.406 187.869  1.00 22.44           C  
ATOM    279  CA  HIS A 280     120.827 118.781 186.895  1.00 12.75           C  
ATOM    280  CA  VAL A 281     119.064 119.356 183.578  1.00 25.96           C  
ATOM    281  CA  ALA A 282     121.207 122.441 183.045  1.00 17.38           C  
ATOM    282  CA  ARG A 283     124.333 120.364 183.703  1.00 19.57           C  
ATOM    283  CA  ALA A 284     123.143 117.790 181.178  1.00 17.66           C  
ATOM    284  CA  LEU A 285     122.629 120.567 178.630  1.00 18.61           C  
ATOM    285  CA  GLU A 286     126.149 121.756 179.420  1.00 16.50           C  
ATOM    286  CA  MET A 287     127.718 118.336 178.796  1.00 19.66           C  
ATOM    287  CA  LYS A 288     126.471 118.329 175.183  1.00 23.34           C  
ATOM    288  CA  THR A 289     127.724 121.881 174.656  1.00 16.49           C  
ATOM    289  CA  ALA A 290     131.225 120.589 175.389  1.00 25.23           C  
ATOM    290  CA  LEU A 291     131.177 118.505 172.208  1.00 20.57           C  
ATOM    291  CA  SER A 292     130.654 121.626 170.098  1.00 17.73           C  
ATOM    292  CA  ARG A 293     133.588 123.357 171.789  1.00 23.11           C  
ATOM    293  CA  ALA A 294     135.838 120.414 170.927  1.00 17.30           C  
ATOM    294  CA  ILE A 295     134.604 120.377 167.330  1.00 14.69           C  
ATOM    295  CA  GLU A 296     135.112 124.094 166.705  1.00 30.70           C  
ATOM    296  CA  ILE A 297     138.549 123.670 168.278  1.00 22.79           C  
ATOM    297  CA  LEU A 298     140.144 120.820 166.366  1.00 20.02           C  
ATOM    298  CA  ASP A 299     138.826 122.082 163.037  1.00 21.97           C  
ATOM    299  CA  GLU A 300     139.479 125.578 164.380  1.00 13.67           C  
ATOM    300  CA  LEU A 301     142.921 124.639 165.678  1.00 18.61           C  
ATOM    301  CA  ASP A 302     145.689 124.575 163.083  1.00 11.92           C  
ATOM    302  CA  THR A 303     147.648 122.701 165.750  1.00 30.00           C  
ATOM    303  CA  SER A 304     151.052 124.226 164.862  1.00 30.00           C  
ATOM    304  CA  ALA A 305     152.480 126.948 167.026  1.00 30.00           C  
ATOM    305  CA  PRO A 306     155.618 127.905 168.943  1.00 17.68           C  
ATOM    306  CA  VAL A 307     153.441 127.306 171.985  1.00 20.55           C  
ATOM    307  CA  ARG A 308     156.280 128.158 174.362  1.00 15.83           C  
ATOM    308  CA  ALA A 309     156.582 131.836 175.233  1.00 17.31           C  
ATOM    309  CA  ASP A 310     159.109 132.409 178.026  1.00 18.94           C  
ATOM    310  CA  PHE A 311     157.892 133.758 181.396  1.00 20.28           C  
ATOM    311  CA  ASP A 312     160.852 134.099 183.818  1.00 16.25           C  
ATOM    312  CA  GLU A 313     160.506 134.644 187.585  1.00 15.51           C  
ATOM    313  CA  ARG A 314     160.632 138.405 188.072  1.00 14.03           C  
ATOM    314  CA  GLY A 315     159.114 139.961 190.069  1.00 30.00           C  
ATOM    315  CA  THR A 316     156.982 142.881 188.938  1.00 13.73           C  
ATOM    316  CA  GLY A 317     154.519 141.970 191.693  1.00 30.00           C  
ATOM    317  CA  LYS A 318     151.388 142.264 189.653  1.00 30.00           C  
ATOM    318  CA  LEU A 319     149.271 139.386 190.936  1.00 12.87           C  
ATOM    319  CA  GLY A 320     147.066 138.111 188.110  1.00 13.51           C  
ATOM    320  CA  ILE A 321     143.899 136.143 188.891  1.00 22.72           C  
ATOM    321  CA  GLY A 322     142.402 133.830 186.275  1.00 17.87           C  
ATOM    322  CA  ALA A 323     138.742 132.912 186.434  1.00 19.89           C  
ATOM    323  CA  ILE A 324     138.194 129.664 184.597  1.00 18.82           C  
ATOM    324  CA  GLU A 325     134.812 127.978 184.758  1.00 17.72           C  
ATOM    325  CA  ALA A 326     134.604 124.621 186.491  1.00 19.74           C  
ATOM    326  CA  PRO A 327     131.388 122.804 185.615  1.00 16.86           C  
ATOM    327  CA  ARG A 328     130.182 122.846 189.338  1.00 13.67           C  
ATOM    328  CA  GLY A 329     131.343 126.501 189.848  1.00 15.29           C  
ATOM    329  CA  LEU A 330     133.575 129.410 188.859  1.00 23.39           C  
ATOM    330  CA  ASP A 331     137.142 129.174 190.183  1.00 20.74           C  
ATOM    331  CA  VAL A 332     139.481 132.107 190.831  1.00 23.91           C  
ATOM    332  CA  HIS A 333     143.045 131.441 192.084  1.00 18.26           C  
ATOM    333  CA  MET A 334     145.210 134.487 193.153  1.00 16.07           C  
ATOM    334  CA  ALA A 335     148.852 134.629 194.164  1.00 14.69           C  
ATOM    335  CA  LYS A 336     151.405 137.349 194.906  1.00 16.84           C  
ATOM    336  CA  VAL A 337     155.077 137.051 193.957  1.00 21.35           C  
ATOM    337  CA  GLU A 338     157.966 139.019 195.424  1.00 23.38           C  
ATOM    338  CA  ASN A 339     161.528 137.880 194.698  1.00 20.31           C  
ATOM    339  CA  GLY A 340     160.327 135.463 192.012  1.00 15.63           C  
ATOM    340  CA  LYS A 341     158.674 133.091 194.462  1.00 19.25           C  
ATOM    341  CA  ILE A 342     155.193 132.716 195.979  1.00 19.86           C  
ATOM    342  CA  GLN A 343     154.320 134.989 198.901  1.00 18.72           C  
ATOM    343  CA  PHE A 344     150.545 134.529 198.915  1.00 19.51           C  
ATOM    344  CA  TYR A 345     148.195 132.186 197.113  1.00 17.61           C  
ATOM    345  CA  SER A 346     144.504 131.754 197.824  1.00 17.45           C  
ATOM    346  CA  ALA A 347     142.423 129.405 195.685  1.00 17.56           C  
ATOM    347  CA  LEU A 348     138.624 129.591 195.780  1.00 18.26           C  
ATOM    348  CA  VAL A 349     136.654 126.524 194.734  1.00 20.34           C  
ATOM    349  CA  PRO A 350     133.292 126.421 192.991  1.00 19.06           C  
ATOM    350  CA  THR A 351     132.414 124.006 195.787  1.00 21.78           C  
ATOM    351  CA  THR A 352     133.247 126.458 198.577  1.00 20.95           C  
ATOM    352  CA  TRP A 353     130.661 128.783 197.040  1.00 16.70           C  
ATOM    353  CA  ASN A 354     127.915 126.114 197.028  1.00 19.10           C  
ATOM    354  CA  ILE A 355     127.118 125.244 200.685  1.00 18.61           C  
ATOM    355  CA  PRO A 356     125.378 128.415 201.931  1.00 17.28           C  
ATOM    356  CA  THR A 357     122.945 127.875 199.081  1.00 17.73           C  
ATOM    357  CA  MET A 358     123.053 124.235 200.270  1.00 16.62           C  
ATOM    358  CA  GLY A 359     122.047 125.338 203.755  1.00 18.62           C  
ATOM    359  CA  PRO A 360     119.321 127.106 201.798  1.00 23.15           C  
ATOM    360  CA  ALA A 361     117.815 123.932 200.266  1.00 18.83           C  
ATOM    361  CA  THR A 362     116.119 122.805 203.511  1.00 14.23           C  
ATOM    362  CA  GLU A 363     113.938 124.384 204.324  1.00 11.29           C  
ATOM    363  CA  GLY A 364     112.136 124.330 202.215  1.00 27.46           C  
ATOM    364  CA  PHE A 365     109.493 121.823 203.302  1.00 17.31           C  
ATOM    365  CA  HIS A 366     109.172 118.103 203.923  1.00 30.00           C  
ATOM    366  CA  HIS A 367     112.920 117.969 203.737  1.00 22.21           C  
ATOM    367  CA  GLU A 368     112.623 114.811 205.757  1.00 21.36           C  
ATOM    368  CA  TYR A 369     113.026 114.700 203.012  1.00 15.78           C  
ATOM    369  CA  GLY A 370     114.174 112.392 202.185  1.00 22.10           C  
ATOM    370  CA  PRO A 371     115.835 115.136 200.151  1.00 15.35           C  
ATOM    371  CA  HIS A 372     118.310 114.712 197.317  1.00 20.48           C  
ATOM    372  CA  VAL A 373     118.405 118.469 196.937  1.00 24.06           C  
ATOM    373  CA  ILE A 374     121.781 118.441 198.674  1.00 15.59           C  
ATOM    374  CA  ARG A 375     122.625 115.718 196.166  1.00 17.23           C  
ATOM    375  CA  ALA A 376     121.516 118.029 193.356  1.00 14.42           C  
ATOM    376  CA  TYR A 377     124.376 120.489 194.053  1.00 20.56           C  
ATOM    377  CA  ASP A 378     127.819 119.633 192.727  1.00 21.52           C  
ATOM    378  CA  PRO A 379     130.226 120.192 195.611  1.00 20.25           C  
ATOM    379  CA  CYS A 380     133.826 119.090 196.049  1.00 18.95           C  
ATOM    380  CA  LEU A 381     135.115 118.663 199.590  1.00 22.65           C  
ATOM    381  CA  SER A 382     138.635 118.771 198.206  1.00 16.42           C  
ATOM    382  CA  CYS A 383     137.971 121.895 196.088  1.00 19.15           C  
ATOM    383  CA  ALA A 384     135.868 123.599 198.788  1.00 19.57           C  
ATOM    384  CA  THR A 385     138.646 123.294 201.363  1.00 14.61           C  
ATOM    385  CA  HIS A 386     141.450 121.807 199.280  1.00 18.34           C  
TER     386      HIS A 386                                                      
ATOM    387  CA  LYS B  46     131.715  88.777 195.617  1.00 30.00           C  
ATOM    388  CA  PRO B  47     132.440  90.489 198.945  1.00 22.55           C  
ATOM    389  CA  ARG B  48     133.640  92.202 200.775  1.00 30.00           C  
ATOM    390  CA  ILE B  49     135.624  95.310 200.026  1.00 16.82           C  
ATOM    391  CA  GLY B  50     134.698  98.652 201.520  1.00 17.26           C  
ATOM    392  CA  TYR B  51     136.899 101.595 200.629  1.00 17.40           C  
ATOM    393  CA  ILE B  52     137.790 104.238 203.212  1.00 19.69           C  
ATOM    394  CA  HIS B  53     139.112 107.614 202.145  1.00 21.75           C  
ATOM    395  CA  LEU B  54     140.519 109.902 204.816  1.00 19.96           C  
ATOM    396  CA  SER B  55     143.062 112.114 203.038  1.00 20.42           C  
ATOM    397  CA  GLY B  56     142.550 111.685 199.311  1.00 20.18           C  
ATOM    398  CA  CYS B  57     141.343 113.517 196.214  1.00 18.83           C  
ATOM    399  CA  THR B  58     139.128 110.773 194.877  1.00 19.57           C  
ATOM    400  CA  GLY B  59     142.235 110.299 192.805  1.00  2.90           C  
ATOM    401  CA  ASP B  60     141.869 106.599 193.446  1.00  3.10           C  
ATOM    402  CA  ALA B  61     138.113 106.563 192.831  1.00 -0.30           C  
ATOM    403  CA  MET B  62     138.414 108.157 189.392  1.00  0.40           C  
ATOM    404  CA  SER B  63     141.021 105.572 188.411  1.00  3.70           C  
ATOM    405  CA  LEU B  64     138.698 102.841 189.659  1.00  2.60           C  
ATOM    406  CA  THR B  65     135.776 104.121 187.602  1.00  1.20           C  
ATOM    407  CA  GLU B  66     137.607 104.017 184.291  1.00  1.30           C  
ATOM    408  CA  ASN B  67     136.381 102.277 182.437  1.00  0.30           C  
ATOM    409  CA  TYR B  68     135.310  98.962 180.834  1.00 -1.30           C  
ATOM    410  CA  ASP B  69     134.592  96.215 180.866  1.00  3.40           C  
ATOM    411  CA  ILE B  70     132.267  95.307 182.143  1.00 -0.80           C  
ATOM    412  CA  LEU B  71     133.641  97.595 184.850  1.00  1.60           C  
ATOM    413  CA  ALA B  72     130.081  98.758 185.438  1.00  1.70           C  
ATOM    414  CA  GLU B  73     128.421  95.617 184.092  1.00  1.20           C  
ATOM    415  CA  LEU B  74     131.599  93.988 185.319  1.00  1.90           C  
ATOM    416  CA  LEU B  75     131.074  95.874 188.582  1.00  1.10           C  
ATOM    417  CA  THR B  76     127.596  94.332 188.807  1.00  0.50           C  
ATOM    418  CA  ASN B  77     129.076  90.891 188.132  1.00  1.80           C  
ATOM    419  CA  MET B  78     132.042  91.822 190.285  1.00 -0.50           C  
ATOM    420  CA  VAL B  79     132.907  91.690 193.951  1.00 21.73           C  
ATOM    421  CA  ASP B  80     130.543  93.690 196.146  1.00 21.28           C  
ATOM    422  CA  ILE B  81     131.985  96.207 198.609  1.00 20.34           C  
ATOM    423  CA  VAL B  82     129.762  97.994 201.102  1.00 18.99           C  
ATOM    424  CA  TYR B  83     130.094 101.320 202.872  1.00 17.53           C  
ATOM    425  CA  GLY B  84     127.023 102.959 201.345  1.00 30.00           C  
ATOM    426  CA  GLN B  85     124.427 102.528 198.600  1.00 30.00           C  
ATOM    427  CA  THR B  86     126.311 105.328 196.872  1.00 30.00           C  
ATOM    428  CA  LEU B  87     129.928 104.524 196.053  1.00 30.00           C  
ATOM    429  CA  VAL B  88     131.102 106.167 199.280  1.00 30.00           C  
ATOM    430  CA  ASP B  89     129.117 106.535 202.503  1.00 30.00           C  
ATOM    431  CA  LEU B  90     129.424 106.206 206.280  1.00 30.00           C  
ATOM    432  CA  TRP B  91     127.057 104.173 208.407  1.00 30.00           C  
ATOM    433  CA  GLU B  92     129.785 101.746 209.358  1.00 30.00           C  
ATOM    434  CA  MET B  93     130.415  98.302 207.835  1.00 30.00           C  
ATOM    435  CA  PRO B  94     131.078  94.698 208.896  1.00 30.00           C  
ATOM    436  CA  GLU B  95     132.131  91.347 207.390  1.00 30.00           C  
ATOM    437  CA  MET B  96     134.013  92.833 204.421  1.00 30.00           C  
ATOM    438  CA  ASP B  97     137.310  91.084 205.190  1.00 16.58           C  
ATOM    439  CA  LEU B  98     138.708  93.909 203.061  1.00 23.76           C  
ATOM    440  CA  ALA B  99     139.280  97.607 203.694  1.00 22.27           C  
ATOM    441  CA  LEU B 100     140.237  99.950 200.862  1.00 20.58           C  
ATOM    442  CA  VAL B 101     141.741 103.260 201.924  1.00 17.65           C  
ATOM    443  CA  GLU B 102     141.806 106.348 199.685  1.00 18.55           C  
ATOM    444  CA  GLY B 103     143.581 109.423 201.035  1.00 21.03           C  
ATOM    445  CA  SER B 104     146.034 110.026 203.904  1.00 20.75           C  
ATOM    446  CA  VAL B 105     145.329 109.923 207.660  1.00 19.77           C  
ATOM    447  CA  CYS B 106     145.714 113.162 209.647  1.00 21.51           C  
ATOM    448  CA  LEU B 107     146.369 113.087 213.395  1.00 22.73           C  
ATOM    449  CA  GLN B 108     143.843 115.758 214.328  1.00 22.73           C  
ATOM    450  CA  ASP B 109     140.798 114.503 216.220  1.00 30.00           C  
ATOM    451  CA  GLU B 110     138.583 112.960 216.688  1.00 17.34           C  
ATOM    452  CA  HIS B 111     136.778 110.552 214.381  1.00 16.68           C  
ATOM    453  CA  SER B 112     138.975 109.721 211.390  1.00 18.16           C  
ATOM    454  CA  LEU B 113     141.556 107.950 213.552  1.00 16.74           C  
ATOM    455  CA  HIS B 114     139.181 106.071 215.854  1.00 19.16           C  
ATOM    456  CA  GLU B 115     136.930 105.220 212.910  1.00 18.74           C  
ATOM    457  CA  LEU B 116     139.996 104.033 211.004  1.00 19.79           C  
ATOM    458  CA  LYS B 117     141.204 101.658 213.770  1.00 19.48           C  
ATOM    459  CA  GLU B 118     137.631 100.390 213.965  1.00 18.33           C  
ATOM    460  CA  LEU B 119     137.155  99.623 210.272  1.00 30.00           C  
ATOM    461  CA  ARG B 120     140.567  97.972 210.555  1.00 18.34           C  
ATOM    462  CA  GLU B 121     139.273  95.919 213.476  1.00 19.36           C  
ATOM    463  CA  LYS B 122     136.734  94.007 211.349  1.00 18.45           C  
ATOM    464  CA  ALA B 123     138.247  93.647 207.847  1.00 17.05           C  
ATOM    465  CA  LYS B 124     139.794  90.514 206.292  1.00 18.06           C  
ATOM    466  CA  LEU B 125     142.233  92.812 204.475  1.00 17.72           C  
ATOM    467  CA  VAL B 126     143.531  96.345 204.934  1.00 18.81           C  
ATOM    468  CA  CYS B 127     144.409  98.214 201.752  1.00 19.31           C  
ATOM    469  CA  ALA B 128     145.417 101.714 200.700  1.00 19.28           C  
ATOM    470  CA  PHE B 129     144.366 103.106 197.330  1.00 17.92           C  
ATOM    471  CA  GLY B 130     146.742 105.457 195.551  1.00 15.98           C  
ATOM    472  CA  SER B 131     149.923 107.093 196.877  1.00 17.33           C  
ATOM    473  CA  CYS B 132     148.058 109.259 199.436  1.00 17.81           C  
ATOM    474  CA  ALA B 133     146.988 106.269 201.529  1.00 16.89           C  
ATOM    475  CA  ALA B 134     150.274 104.565 200.699  1.00 18.97           C  
ATOM    476  CA  THR B 135     152.011 107.813 201.663  1.00 18.23           C  
ATOM    477  CA  GLY B 136     150.404 109.158 199.843  1.00 17.83           C  
ATOM    478  CA  CYS B 137     151.618 111.660 200.193  1.00 17.32           C  
ATOM    479  CA  PHE B 138     150.667 115.012 198.690  1.00 18.33           C  
ATOM    480  CA  THR B 139     150.205 116.006 202.306  1.00 17.18           C  
ATOM    481  CA  ARG B 140     153.584 115.358 203.952  1.00 17.45           C  
ATOM    482  CA  TYR B 141     154.830 118.416 202.014  1.00 17.38           C  
ATOM    483  CA  SER B 142     151.930 120.311 203.554  1.00 19.26           C  
ATOM    484  CA  ARG B 143     153.012 122.369 206.600  1.00 30.00           C  
ATOM    485  CA  GLY B 144     151.369 124.802 208.886  1.00 30.00           C  
ATOM    486  CA  GLY B 145     147.651 125.486 208.937  1.00 30.00           C  
ATOM    487  CA  GLN B 146     145.425 127.100 206.331  1.00 30.00           C  
ATOM    488  CA  GLN B 147     142.457 128.424 208.310  1.00 30.00           C  
ATOM    489  CA  ALA B 148     139.806 128.296 209.125  1.00 30.00           C  
ATOM    490  CA  GLN B 149     141.713 126.151 211.636  1.00 30.00           C  
ATOM    491  CA  PRO B 150     145.306 124.843 211.745  1.00 30.00           C  
ATOM    492  CA  SER B 151     146.553 121.299 211.005  1.00 30.00           C  
ATOM    493  CA  HIS B 152     149.441 119.170 209.764  1.00 30.00           C  
ATOM    494  CA  GLU B 153     147.765 115.838 209.156  1.00 30.00           C  
ATOM    495  CA  SER B 154     150.083 112.830 208.959  1.00 30.00           C  
ATOM    496  CA  PHE B 155     148.010 111.112 206.274  1.00 30.00           C  
ATOM    497  CA  VAL B 156     149.922 107.958 207.191  1.00 30.00           C  
ATOM    498  CA  PRO B 157     148.936 104.279 207.003  1.00 30.00           C  
ATOM    499  CA  ILE B 158     151.526 103.541 209.688  1.00 30.00           C  
ATOM    500  CA  ALA B 159     149.292 104.619 212.577  1.00 30.00           C  
ATOM    501  CA  ASP B 160     147.023 103.226 213.073  1.00 30.00           C  
ATOM    502  CA  LEU B 161     147.430 100.723 210.244  1.00 30.00           C  
ATOM    503  CA  ILE B 162     149.301  97.536 209.352  1.00 30.00           C  
ATOM    504  CA  ASP B 163     149.529  95.292 206.281  1.00 30.00           C  
ATOM    505  CA  VAL B 164     147.861  94.675 204.170  1.00 19.55           C  
ATOM    506  CA  ASP B 165     147.522  96.934 202.582  1.00 19.37           C  
ATOM    507  CA  LEU B 166     147.798  94.983 200.470  1.00 19.79           C  
ATOM    508  CA  ALA B 167     147.436  98.270 198.586  1.00 18.28           C  
ATOM    509  CA  LEU B 168     148.604  99.708 195.241  1.00 16.46           C  
ATOM    510  CA  PRO B 169     150.558 102.985 194.799  1.00 17.34           C  
ATOM    511  CA  GLY B 170     150.179 105.782 192.215  1.00 17.53           C  
ATOM    512  CA  CYS B 171     148.693 109.240 191.664  1.00 18.25           C  
ATOM    513  CA  PRO B 172     146.293 107.668 191.002  1.00 17.78           C  
ATOM    514  CA  PRO B 173     147.369 104.102 190.112  1.00 16.32           C  
ATOM    515  CA  SER B 174     146.406 102.716 186.727  1.00 17.17           C  
ATOM    516  CA  PRO B 175     143.132 100.880 187.059  1.00 17.00           C  
ATOM    517  CA  GLU B 176     144.689  97.589 185.951  1.00 19.86           C  
ATOM    518  CA  ILE B 177     146.895  97.779 189.039  1.00 19.11           C  
ATOM    519  CA  ILE B 178     143.772  97.871 191.244  1.00 20.40           C  
ATOM    520  CA  ALA B 179     141.467  95.676 189.166  1.00 21.08           C  
ATOM    521  CA  LYS B 180     144.302  93.235 188.508  1.00 19.05           C  
ATOM    522  CA  THR B 181     145.047  93.091 192.233  1.00 18.62           C  
ATOM    523  CA  VAL B 182     141.400  92.505 193.142  1.00 17.18           C  
ATOM    524  CA  VAL B 183     141.098  89.736 190.553  1.00 19.11           C  
ATOM    525  CA  ALA B 184     143.911  87.689 192.090  1.00 21.52           C  
ATOM    526  CA  LEU B 185     142.835  88.611 195.620  1.00 21.44           C  
ATOM    527  CA  LEU B 186     139.494  86.977 194.824  1.00 21.58           C  
ATOM    528  CA  ASN B 187     140.757  83.997 192.824  1.00 23.48           C  
ATOM    529  CA  ALA B 200     148.521  83.460 194.955  1.00 30.00           C  
ATOM    530  CA  GLY B 201     150.465  86.193 193.175  1.00 30.00           C  
ATOM    531  CA  TYR B 202     151.788  88.420 194.194  1.00 30.00           C  
ATOM    532  CA  THR B 203     153.793  89.729 197.150  1.00 30.00           C  
ATOM    533  CA  GLU B 204     153.643  93.342 198.134  1.00 30.00           C  
ATOM    534  CA  ALA B 205     156.500  95.030 199.922  1.00 30.00           C  
ATOM    535  CA  CYS B 206     154.272  96.696 200.196  1.00 30.00           C  
ATOM    536  CA  GLY B 207     154.740 100.061 201.899  1.00 30.00           C  
ATOM    537  CA  CYS B 208     157.404 102.736 201.527  1.00 30.00           C  
ATOM    538  CA  ASP B 209     157.747 106.400 202.508  1.00 30.00           C  
ATOM    539  CA  LEU B 210     160.583 107.516 200.250  1.00 30.00           C  
ATOM    540  CA  GLN B 211     162.560 108.791 198.663  1.00 30.00           C  
ATOM    541  CA  THR B 212     164.276 112.134 198.147  1.00 30.00           C  
ATOM    542  CA  LYS B 213     164.801 112.346 195.400  1.00  6.84           C  
ATOM    543  CA  VAL B 214     165.841 108.700 194.999  1.00  6.80           C  
ATOM    544  CA  VAL B 215     169.034 106.675 195.265  1.00  6.73           C  
ATOM    545  CA  ASN B 216     170.594 103.843 193.283  1.00  6.17           C  
ATOM    546  CA  GLN B 217     174.157 103.661 194.586  1.00  9.23           C  
ATOM    547  CA  GLY B 218     175.010 101.451 191.619  1.00 12.09           C  
ATOM    548  CA  LEU B 219     173.278  98.298 190.417  1.00 12.07           C  
ATOM    549  CA  CYS B 220     171.384 100.478 187.940  1.00  8.17           C  
ATOM    550  CA  ILE B 221     170.061  99.144 184.630  1.00  8.54           C  
ATOM    551  CA  GLY B 222     170.357 102.459 182.797  1.00  9.00           C  
ATOM    552  CA  CYS B 223     167.076 101.616 181.087  1.00 11.78           C  
ATOM    553  CA  GLY B 224     165.569 104.924 182.183  1.00 10.78           C  
ATOM    554  CA  THR B 225     162.375 103.149 183.193  1.00  9.21           C  
ATOM    555  CA  CYS B 226     162.316 105.629 186.082  1.00  8.05           C  
ATOM    556  CA  ALA B 227     161.776 108.660 183.846  1.00 10.97           C  
ATOM    557  CA  MET B 228     158.727 106.936 182.362  1.00 13.25           C  
ATOM    558  CA  ALA B 229     155.515 106.879 184.401  1.00 13.22           C  
ATOM    559  CA  CYS B 230     156.193 109.809 186.730  1.00 10.65           C  
ATOM    560  CA  GLN B 231     152.654 111.136 187.011  1.00 11.48           C  
ATOM    561  CA  THR B 232     154.144 114.621 187.303  1.00 12.79           C  
ATOM    562  CA  ARG B 233     156.122 114.133 184.092  1.00 15.89           C  
ATOM    563  CA  ALA B 234     158.634 116.542 185.634  1.00 12.93           C  
ATOM    564  CA  LEU B 235     161.478 114.034 185.822  1.00 10.85           C  
ATOM    565  CA  ASP B 236     164.535 114.722 183.669  1.00 10.83           C  
ATOM    566  CA  MET B 237     166.248 111.846 181.884  1.00 14.44           C  
ATOM    567  CA  THR B 238     170.010 112.025 181.465  1.00 12.63           C  
ATOM    568  CA  ASN B 239     172.985 109.726 181.249  1.00 12.87           C  
ATOM    569  CA  GLY B 240     172.784 107.843 184.539  1.00 11.39           C  
ATOM    570  CA  ARG B 241     170.468 109.543 187.068  1.00  8.66           C  
ATOM    571  CA  PRO B 242     167.733 111.703 185.584  1.00  7.97           C  
ATOM    572  CA  GLU B 243     167.637 114.663 187.943  1.00  9.75           C  
ATOM    573  CA  LEU B 244     164.442 116.676 188.405  1.00 12.66           C  
ATOM    574  CA  ASN B 245     163.151 120.136 189.091  1.00 30.00           C  
ATOM    575  CA  SER B 246     162.612 120.181 192.856  1.00 13.80           C  
ATOM    576  CA  ASP B 247     158.872 120.932 193.085  1.00 17.19           C  
ATOM    577  CA  ARG B 248     157.614 118.907 190.097  1.00 12.31           C  
ATOM    578  CA  CYS B 249     156.921 115.585 191.866  1.00 10.76           C  
ATOM    579  CA  ILE B 250     154.549 114.740 194.723  1.00 11.00           C  
ATOM    580  CA  LYS B 251     156.847 113.083 195.074  1.00 11.46           C  
ATOM    581  CA  CYS B 252     154.657 110.201 193.876  1.00 10.84           C  
ATOM    582  CA  GLY B 253     156.601 107.081 194.838  1.00 11.60           C  
ATOM    583  CA  ILE B 254     155.885 106.283 191.188  1.00 12.52           C  
ATOM    584  CA  CYS B 255     159.534 106.323 190.073  1.00  9.14           C  
ATOM    585  CA  TYR B 256     160.660 103.245 191.987  1.00 10.61           C  
ATOM    586  CA  VAL B 257     159.164 100.465 189.938  1.00 13.65           C  
ATOM    587  CA  GLN B 258     162.373 100.047 187.990  1.00 10.96           C  
ATOM    588  CA  CYS B 259     164.853  97.401 186.878  1.00  8.71           C  
ATOM    589  CA  PRO B 260     165.816  97.009 190.534  1.00 11.16           C  
ATOM    590  CA  ARG B 261     162.972  96.310 192.927  1.00 12.20           C  
ATOM    591  CA  SER B 262     162.105  92.862 194.132  1.00 10.02           C  
ATOM    592  CA  TRP B 263     161.835  91.443 190.635  1.00  7.15           C  
ATOM    593  CA  TRP B 264     158.649  89.890 189.412  1.00  1.00           C  
ATOM    594  CA  PRO B 265     159.096  86.386 188.075  1.00  1.00           C  
ATOM    595  CA  GLU B 266     155.464  86.416 187.017  1.00  1.00           C  
ATOM    596  CA  GLU B 267     155.471  89.212 184.450  1.00  1.00           C  
ATOM    597  CA  GLN B 268     157.605  87.009 182.209  1.00  1.00           C  
ATOM    598  CA  ILE B 269     155.226  84.115 182.835  1.00  1.00           C  
ATOM    599  CA  LYS B 270     152.301  86.351 181.895  1.00  1.00           C  
ATOM    600  CA  LYS B 271     154.115  87.316 178.699  1.00  1.00           C  
ATOM    601  CA  GLU B 272     154.690  83.644 177.894  1.00 30.00           C  
TER     602      GLU B 272                                                      
ATOM    603  CA  LEU C   3     167.516  79.902 176.512  1.00 30.00           C  
ATOM    604  CA  GLY C   4     164.787  80.315 173.904  1.00 30.00           C  
ATOM    605  CA  THR C   5     164.869  78.484 170.575  1.00 30.00           C  
ATOM    606  CA  TYR C   6     161.420  79.617 169.433  1.00 30.00           C  
ATOM    607  CA  LYS C   7     162.876  81.440 166.424  1.00 20.00           C  
ATOM    608  CA  GLU C   8     166.238  80.733 164.778  1.00 30.00           C  
ATOM    609  CA  ILE C   9     167.336  82.325 161.493  1.00 30.00           C  
ATOM    610  CA  VAL C  10     169.967  84.417 159.734  1.00 30.00           C  
ATOM    611  CA  SER C  11     169.355  86.693 156.745  1.00 30.00           C  
ATOM    612  CA  ALA C  12     170.757  89.477 154.592  1.00 30.00           C  
ATOM    613  CA  ARG C  13     167.880  91.692 153.460  1.00 30.00           C  
ATOM    614  CA  SER C  14     166.940  92.989 150.003  1.00 30.00           C  
ATOM    615  CA  THR C  15     168.267  96.311 148.668  1.00 30.00           C  
ATOM    616  CA  ASP C  16     168.523  99.116 148.925  1.00  1.00           C  
ATOM    617  CA  ARG C  17     169.697 102.069 151.034  1.00  1.00           C  
ATOM    618  CA  GLU C  18     169.212  99.896 154.114  1.00  1.00           C  
ATOM    619  CA  ILE C  19     172.305  97.670 154.167  1.00  1.00           C  
ATOM    620  CA  GLN C  20     174.950 100.361 153.761  1.00  1.00           C  
ATOM    621  CA  LYS C  21     173.971 102.520 156.718  1.00  1.00           C  
ATOM    622  CA  LEU C  22     172.533  99.826 158.985  1.00  1.00           C  
ATOM    623  CA  ALA C  23     175.879  98.418 160.080  1.00 30.00           C  
ATOM    624  CA  GLN C  24     176.723  97.912 162.661  1.00  1.00           C  
ATOM    625  CA  ASP C  25     172.966  97.797 163.303  1.00  1.00           C  
ATOM    626  CA  GLY C  26     169.594  99.040 162.062  1.00  1.00           C  
ATOM    627  CA  GLY C  27     169.399  97.400 158.656  1.00  1.00           C  
ATOM    628  CA  ILE C  28     167.196  94.794 160.291  1.00  1.00           C  
ATOM    629  CA  VAL C  29     165.498  97.188 162.704  1.00  1.00           C  
ATOM    630  CA  THR C  30     164.619  99.509 159.823  1.00  1.00           C  
ATOM    631  CA  GLY C  31     163.074  96.955 157.473  1.00  1.00           C  
ATOM    632  CA  LEU C  32     161.162  95.558 160.431  1.00  1.00           C  
ATOM    633  CA  LEU C  33     159.900  99.039 161.292  1.00  1.00           C  
ATOM    634  CA  ALA C  34     158.720  99.585 157.717  1.00  1.00           C  
ATOM    635  CA  TYR C  35     156.484  96.513 157.869  1.00  1.00           C  
ATOM    636  CA  ALA C  36     154.992  97.696 161.158  1.00 30.00           C  
ATOM    637  CA  LEU C  37     154.294 101.084 159.585  1.00 30.00           C  
ATOM    638  CA  ASP C  38     152.565  99.226 156.773  1.00 30.00           C  
ATOM    639  CA  GLU C  39     151.536  96.964 159.636  1.00 30.00           C  
ATOM    640  CA  GLY C  40     150.442  99.417 162.320  1.00 30.00           C  
ATOM    641  CA  ILE C  41     151.408  98.486 164.741  1.00 30.00           C  
ATOM    642  CA  ILE C  42     151.620 102.168 163.810  1.00 30.00           C  
ATOM    643  CA  GLU C  43     153.486 104.066 163.030  1.00 30.00           C  
ATOM    644  CA  GLY C  44     154.797 102.146 164.489  1.00 30.00           C  
ATOM    645  CA  ALA C  45     158.002 102.164 166.503  1.00 30.00           C  
ATOM    646  CA  VAL C  46     160.744 104.377 167.915  1.00 30.00           C  
ATOM    647  CA  VAL C  47     164.330 105.018 166.827  1.00 30.00           C  
ATOM    648  CA  ALA C  48     167.253 106.510 168.780  1.00 30.00           C  
ATOM    649  CA  GLY C  49     168.627 108.830 168.151  1.00 30.00           C  
ATOM    650  CA  PRO C  50     169.424 112.113 166.340  1.00 30.00           C  
ATOM    651  CA  GLY C  51     172.955 113.162 167.146  1.00 30.00           C  
ATOM    652  CA  GLU C  52     175.614 113.712 164.491  1.00 30.00           C  
ATOM    653  CA  GLU C  53     178.929 115.367 165.464  1.00 30.00           C  
ATOM    654  CA  PHE C  54     178.020 114.534 169.050  1.00 30.00           C  
ATOM    655  CA  TRP C  55     177.174 110.885 169.659  1.00 30.00           C  
ATOM    656  CA  LYS C  56     173.823 110.236 169.422  1.00 30.00           C  
ATOM    657  CA  PRO C  57     172.124 110.543 172.807  1.00 30.00           C  
ATOM    658  CA  GLN C  58     168.747 110.958 171.133  1.00 30.00           C  
ATOM    659  CA  PRO C  59     165.145 109.758 171.178  1.00 30.00           C  
ATOM    660  CA  MET C  60     162.957 109.786 168.062  1.00 30.00           C  
ATOM    661  CA  VAL C  61     159.692 108.320 166.733  1.00 30.00           C  
ATOM    662  CA  ALA C  62     159.896 107.070 163.158  1.00 30.00           C  
ATOM    663  CA  MET C  63     156.632 108.123 161.509  1.00 30.00           C  
ATOM    664  CA  SER C  64     158.141 108.379 158.031  1.00  1.00           C  
ATOM    665  CA  SER C  65     160.532 106.266 155.995  1.00  1.00           C  
ATOM    666  CA  ASP C  66     163.168 108.985 156.156  1.00  1.00           C  
ATOM    667  CA  GLU C  67     163.204 108.793 159.959  1.00  1.00           C  
ATOM    668  CA  LEU C  68     163.603 105.017 160.126  1.00  1.00           C  
ATOM    669  CA  LYS C  69     165.952 105.204 157.161  1.00  1.00           C  
ATOM    670  CA  ALA C  70     168.132 107.880 158.717  1.00  1.00           C  
ATOM    671  CA  ALA C  71     168.220 107.012 162.392  1.00  1.00           C  
ATOM    672  CA  ALA C  72     169.624 103.568 162.094  1.00  1.00           C  
ATOM    673  CA  GLY C  73     173.302 103.815 162.722  1.00  1.00           C  
ATOM    674  CA  THR C  74     173.944 101.577 165.701  1.00 30.00           C  
ATOM    675  CA  LYS C  75     175.746 104.325 167.599  1.00 30.00           C  
ATOM    676  CA  TYR C  76     176.248 103.235 171.209  1.00 30.00           C  
ATOM    677  CA  THR C  77     176.099 104.416 174.831  1.00 30.00           C  
ATOM    678  CA  PHE C  78     173.466 104.257 177.595  1.00 30.00           C  
ATOM    679  CA  SER C  79     171.621 107.460 176.665  1.00 30.00           C  
ATOM    680  CA  PRO C  80     168.107 106.545 175.472  1.00 30.00           C  
ATOM    681  CA  ASN C  81     165.463 107.421 178.090  1.00 30.00           C  
ATOM    682  CA  VAL C  82     162.756 104.860 177.230  1.00 30.00           C  
ATOM    683  CA  MET C  83     160.225 107.626 177.987  1.00  1.00           C  
ATOM    684  CA  MET C  84     159.701 108.849 174.414  1.00  1.00           C  
ATOM    685  CA  LEU C  85     157.036 106.071 174.186  1.00  1.00           C  
ATOM    686  CA  LYS C  86     155.078 108.164 176.706  1.00  1.00           C  
ATOM    687  CA  LYS C  87     156.187 111.031 174.477  1.00  1.00           C  
ATOM    688  CA  ALA C  88     154.762 109.091 171.541  1.00  1.00           C  
ATOM    689  CA  VAL C  89     151.352 108.927 173.221  1.00  1.00           C  
ATOM    690  CA  ARG C  90     151.259 112.708 173.461  1.00  1.00           C  
ATOM    691  CA  GLN C  91     151.934 112.439 169.740  1.00 30.00           C  
ATOM    692  CA  TYR C  92     149.884 109.205 169.681  1.00 30.00           C  
ATOM    693  CA  GLY C  93     148.902 106.520 169.348  1.00 30.00           C  
ATOM    694  CA  ILE C  94     146.418 105.403 170.101  1.00 30.00           C  
ATOM    695  CA  GLU C  95     147.787 102.050 168.724  1.00 30.00           C  
ATOM    696  CA  LYS C  96     151.410 101.988 169.742  1.00 30.00           C  
ATOM    697  CA  LEU C  97     154.637 100.196 168.809  1.00 30.00           C  
ATOM    698  CA  GLY C  98     157.941 100.526 170.684  1.00 30.00           C  
ATOM    699  CA  THR C  99     161.423  99.210 169.870  1.00 30.00           C  
ATOM    700  CA  VAL C 100     164.435  99.525 172.188  1.00 30.00           C  
ATOM    701  CA  ALA C 101     167.431  98.218 173.745  1.00 30.00           C  
ATOM    702  CA  ILE C 102     166.643  98.207 176.441  1.00 30.00           C  
ATOM    703  CA  PRO C 103     169.229  95.427 176.685  1.00 30.00           C  
ATOM    704  CA  CYS C 104     168.599  96.023 180.352  1.00 16.16           C  
ATOM    705  CA  GLN C 105     166.073  98.471 178.967  1.00 30.00           C  
ATOM    706  CA  THR C 106     163.796  95.703 177.704  1.00 20.67           C  
ATOM    707  CA  MET C 107     163.583  94.252 181.199  1.00 19.41           C  
ATOM    708  CA  GLY C 108     162.040  97.516 182.375  1.00 17.79           C  
ATOM    709  CA  ILE C 109     159.165  97.444 179.933  1.00 22.19           C  
ATOM    710  CA  ARG C 110     157.827  93.948 180.570  1.00 19.75           C  
ATOM    711  CA  LYS C 111     157.281  94.330 184.316  1.00 17.50           C  
ATOM    712  CA  MET C 112     155.424  97.600 183.806  1.00 22.09           C  
ATOM    713  CA  GLN C 113     153.302  95.922 181.153  1.00 15.77           C  
ATOM    714  CA  THR C 114     152.451  93.152 183.614  1.00 17.97           C  
ATOM    715  CA  TYR C 115     151.458  96.003 185.861  1.00 15.85           C  
ATOM    716  CA  PRO C 116     152.252  99.722 185.664  1.00 30.00           C  
ATOM    717  CA  PHE C 117     151.377  99.092 188.247  1.00 30.00           C  
ATOM    718  CA  GLY C 118     149.471 102.224 187.299  1.00 30.00           C  
ATOM    719  CA  VAL C 119     150.133 103.637 183.839  1.00 30.00           C  
ATOM    720  CA  ARG C 120     148.177 105.603 181.241  1.00 30.00           C  
ATOM    721  CA  PHE C 121     147.530 102.826 178.709  1.00 30.00           C  
ATOM    722  CA  LEU C 122     151.239 102.458 177.920  1.00 30.00           C  
ATOM    723  CA  ALA C 123     150.976  98.821 176.833  1.00 30.00           C  
ATOM    724  CA  ASP C 124     149.451  97.683 174.770  1.00 30.00           C  
ATOM    725  CA  LYS C 125     152.830  98.863 173.502  1.00 30.00           C  
ATOM    726  CA  ILE C 126     152.479  95.984 171.056  1.00 30.00           C  
ATOM    727  CA  LYS C 127     155.649  94.860 169.311  1.00 30.00           C  
ATOM    728  CA  LEU C 128     159.259  95.403 170.336  1.00 30.00           C  
ATOM    729  CA  LEU C 129     162.790  95.143 169.016  1.00 30.00           C  
ATOM    730  CA  VAL C 130     165.501  93.453 171.094  1.00 30.00           C  
ATOM    731  CA  GLY C 131     169.235  93.958 170.576  1.00 30.00           C  
ATOM    732  CA  ILE C 132     172.374  92.237 171.683  1.00 30.00           C  
ATOM    733  CA  TYR C 133     174.187  92.428 175.046  1.00 30.00           C  
ATOM    734  CA  CYS C 134     175.571  94.700 177.764  1.00 30.00           C  
ATOM    735  CA  MET C 135     177.434  96.527 178.714  1.00 30.00           C  
ATOM    736  CA  GLU C 136     177.381  99.789 176.758  1.00 30.00           C  
ATOM    737  CA  ASN C 137     180.848 101.321 176.780  1.00 30.00           C  
ATOM    738  CA  PHE C 138     179.988 104.843 177.924  1.00 30.00           C  
ATOM    739  CA  PRO C 139     177.100 107.295 177.749  1.00 30.00           C  
ATOM    740  CA  TYR C 140     179.461 109.894 176.265  1.00  1.00           C  
ATOM    741  CA  THR C 141     182.891 110.672 177.642  1.00  1.00           C  
ATOM    742  CA  SER C 142     184.395 107.210 178.211  1.00  1.00           C  
ATOM    743  CA  LEU C 143     183.826 106.306 174.567  1.00  1.00           C  
ATOM    744  CA  GLN C 144     185.574 109.524 173.615  1.00  1.00           C  
ATOM    745  CA  THR C 145     188.514 108.577 175.828  1.00  1.00           C  
ATOM    746  CA  PHE C 146     188.633 105.164 174.153  1.00  1.00           C  
ATOM    747  CA  ILE C 147     188.697 106.809 170.723  1.00  1.00           C  
ATOM    748  CA  CYS C 148     191.507 109.037 171.971  1.00  1.00           C  
ATOM    749  CA  GLU C 149     193.507 105.970 173.006  1.00  1.00           C  
ATOM    750  CA  LYS C 150     193.471 104.308 169.596  1.00  1.00           C  
ATOM    751  CA  LEU C 151     193.336 107.072 168.629  1.00 30.00           C  
ATOM    752  CA  GLY C 152     190.802 108.136 168.723  1.00 30.00           C  
ATOM    753  CA  VAL C 153     190.769 111.208 166.478  1.00 30.00           C  
ATOM    754  CA  SER C 154     188.009 110.310 166.319  1.00  1.00           C  
ATOM    755  CA  MET C 155     185.052 112.352 165.056  1.00  1.00           C  
ATOM    756  CA  GLU C 156     185.357 111.943 161.277  1.00  1.00           C  
ATOM    757  CA  LEU C 157     185.603 108.196 161.680  1.00  1.00           C  
ATOM    758  CA  VAL C 158     182.146 106.793 161.048  1.00 30.00           C  
ATOM    759  CA  GLU C 159     179.510 106.015 160.285  1.00 30.00           C  
ATOM    760  CA  LYS C 160     180.527 102.613 161.610  1.00 30.00           C  
ATOM    761  CA  MET C 161     182.303 102.057 164.939  1.00 27.03           C  
ATOM    762  CA  ASP C 162     180.896  98.915 166.599  1.00 27.51           C  
ATOM    763  CA  ILE C 163     183.139  95.945 167.384  1.00 27.19           C  
ATOM    764  CA  GLY C 164     183.806  92.283 166.647  1.00 24.72           C  
ATOM    765  CA  LYS C 165     185.417  90.022 169.220  1.00 22.74           C  
ATOM    766  CA  GLY C 166     189.019  91.131 169.622  1.00 19.25           C  
ATOM    767  CA  LYS C 167     188.190  94.245 167.593  1.00 20.90           C  
ATOM    768  CA  PHE C 168     186.661  97.737 167.688  1.00 21.98           C  
ATOM    769  CA  TRP C 169     184.992  99.342 164.677  1.00 21.99           C  
ATOM    770  CA  VAL C 170     185.230 102.111 165.220  1.00 30.00           C  
ATOM    771  CA  TYR C 171     186.404 103.592 161.367  1.00 30.00           C  
ATOM    772  CA  THR C 172     187.022 106.719 159.220  1.00 30.00           C  
ATOM    773  CA  GLN C 173     186.833 107.527 155.517  1.00 30.00           C  
ATOM    774  CA  ASP C 174     189.969 106.236 153.804  1.00 30.00           C  
ATOM    775  CA  ASP C 175     191.540 105.763 157.233  1.00 30.00           C  
ATOM    776  CA  VAL C 176     190.836 102.026 157.281  1.00 30.00           C  
ATOM    777  CA  LEU C 177     189.690 100.024 160.305  1.00 30.00           C  
ATOM    778  CA  THR C 178     191.122 100.497 163.797  1.00 30.00           C  
ATOM    779  CA  LEU C 179     191.450  97.564 166.195  1.00 30.00           C  
ATOM    780  CA  PRO C 180     191.879  97.309 169.965  1.00 30.00           C  
ATOM    781  CA  LEU C 181     191.817  93.992 171.858  1.00 30.00           C  
ATOM    782  CA  LYS C 182     193.047  94.420 175.431  1.00  1.00           C  
ATOM    783  CA  GLU C 183     191.562  97.902 175.747  1.00  1.00           C  
ATOM    784  CA  THR C 184     188.262  96.722 174.311  1.00  1.00           C  
ATOM    785  CA  HIS C 185     188.263  93.830 176.745  1.00  1.00           C  
ATOM    786  CA  GLY C 186     188.861  96.332 179.473  1.00  1.00           C  
ATOM    787  CA  TYR C 187     186.957  98.451 179.663  1.00 30.00           C  
ATOM    788  CA  GLU C 188     184.188 100.620 180.758  1.00 30.00           C  
ATOM    789  CA  GLN C 189     180.566 100.139 181.815  1.00 30.00           C  
ATOM    790  CA  ALA C 190     178.215 100.938 184.695  1.00 30.00           C  
ATOM    791  CA  GLY C 191     179.841  98.790 185.337  1.00 30.00           C  
ATOM    792  CA  CYS C 192     176.818  96.489 185.195  1.00 30.00           C  
ATOM    793  CA  LYS C 193     177.434  93.636 187.637  1.00 30.00           C  
ATOM    794  CA  ILE C 194     174.169  91.736 187.171  1.00 30.00           C  
ATOM    795  CA  CYS C 195     173.406  92.061 183.496  1.00 30.00           C  
ATOM    796  CA  LYS C 196     171.211  89.021 183.310  1.00 30.00           C  
ATOM    797  CA  ASP C 197     170.803  86.360 180.659  1.00 30.00           C  
ATOM    798  CA  TYR C 198     171.218  86.829 176.914  1.00 30.00           C  
ATOM    799  CA  VAL C 199     169.171  88.392 174.116  1.00 30.00           C  
ATOM    800  CA  ALA C 200     166.479  88.298 173.223  1.00 30.00           C  
ATOM    801  CA  GLU C 201     164.074  86.479 175.549  1.00 30.00           C  
ATOM    802  CA  LEU C 202     162.874  89.447 177.622  1.00 30.00           C  
ATOM    803  CA  ALA C 203     161.931  91.185 174.369  1.00 30.00           C  
ATOM    804  CA  ASP C 204     160.914  89.315 171.202  1.00 30.00           C  
ATOM    805  CA  VAL C 205     161.056  88.874 168.416  1.00 30.00           C  
ATOM    806  CA  SER C 206     164.748  89.642 168.930  1.00 30.00           C  
ATOM    807  CA  THR C 207     168.235  89.502 167.583  1.00 30.00           C  
ATOM    808  CA  GLY C 208     171.586  90.412 168.890  1.00 30.00           C  
ATOM    809  CA  SER C 209     174.124  89.678 166.508  1.00 30.00           C  
ATOM    810  CA  VAL C 210     175.549  87.308 164.392  1.00 30.00           C  
ATOM    811  CA  GLY C 211     176.234  84.436 162.012  1.00 30.00           C  
ATOM    812  CA  SER C 212     178.093  86.215 159.247  1.00 30.00           C  
ATOM    813  CA  PRO C 213     177.500  89.706 157.865  1.00 30.00           C  
ATOM    814  CA  ASP C 214     174.504  88.497 155.865  1.00 30.00           C  
ATOM    815  CA  GLY C 215     172.616  88.602 157.900  1.00 30.00           C  
ATOM    816  CA  TRP C 216     173.977  90.910 158.195  1.00 20.00           C  
ATOM    817  CA  SER C 217     173.480  89.424 161.628  1.00 30.00           C  
ATOM    818  CA  THR C 218     170.739  86.968 162.597  1.00 30.00           C  
ATOM    819  CA  VAL C 219     167.389  87.409 164.357  1.00 30.00           C  
ATOM    820  CA  ILE C 220     165.544  85.001 166.650  1.00 30.00           C  
ATOM    821  CA  THR C 221     161.788  85.076 167.307  1.00 30.00           C  
ATOM    822  CA  ARG C 222     161.006  84.368 170.962  1.00 30.00           C  
ATOM    823  CA  THR C 223     157.338  85.183 170.412  1.00  1.00           C  
ATOM    824  CA  ASP C 224     154.759  84.270 167.769  1.00  1.00           C  
ATOM    825  CA  ALA C 225     154.122  87.886 166.776  1.00  1.00           C  
ATOM    826  CA  GLY C 226     157.730  88.289 165.659  1.00  1.00           C  
ATOM    827  CA  ASP C 227     157.866  84.912 163.946  1.00  1.00           C  
ATOM    828  CA  SER C 228     154.651  85.722 162.087  1.00  1.00           C  
ATOM    829  CA  ILE C 229     155.913  89.240 161.433  1.00  1.00           C  
ATOM    830  CA  PHE C 230     159.193  87.840 160.146  1.00  1.00           C  
ATOM    831  CA  LYS C 231     157.294  85.506 157.836  1.00  1.00           C  
ATOM    832  CA  GLN C 232     155.273  88.432 156.507  1.00  1.00           C  
ATOM    833  CA  ALA C 233     158.344  90.434 155.450  1.00  1.00           C  
ATOM    834  CA  VAL C 234     160.340  87.506 154.067  1.00  1.00           C  
ATOM    835  CA  GLU C 235     157.250  86.068 152.378  1.00  1.00           C  
ATOM    836  CA  ALA C 236     156.281  89.339 150.713  1.00  1.00           C  
ATOM    837  CA  GLY C 237     159.106  89.292 150.689  1.00 30.00           C  
ATOM    838  CA  LEU C 238     160.578  92.119 152.746  1.00  1.00           C  
ATOM    839  CA  PHE C 239     164.103  90.868 152.193  1.00 30.00           C  
ATOM    840  CA  GLU C 240     165.222  87.292 151.722  1.00 30.00           C  
ATOM    841  CA  THR C 241     166.122  85.193 154.751  1.00 30.00           C  
ATOM    842  CA  LYS C 242     168.616  82.383 154.429  1.00 30.00           C  
ATOM    843  CA  PRO C 243     168.379  79.371 156.697  1.00 30.00           C  
ATOM    844  CA  ILE C 244     171.329  80.119 157.462  1.00 30.00           C  
ATOM    845  CA  GLU C 245     171.896  78.775 160.968  1.00 30.00           C  
ATOM    846  CA  GLU C 246     174.517  76.563 159.330  1.00 30.00           C  
ATOM    847  CA  VAL C 247     177.574  78.828 159.231  1.00 30.00           C  
ATOM    848  CA  LYS C 248     177.671  78.406 162.037  1.00  1.00           C  
ATOM    849  CA  PRO C 249     176.946  82.086 162.772  1.00 30.00           C  
ATOM    850  CA  GLY C 250     177.381  80.437 164.971  1.00  1.00           C  
ATOM    851  CA  LEU C 251     174.453  79.367 167.175  1.00  1.00           C  
ATOM    852  CA  GLY C 252     176.626  77.461 169.658  1.00  1.00           C  
ATOM    853  CA  LEU C 253     179.229  80.189 170.044  1.00  1.00           C  
ATOM    854  CA  LEU C 254     176.339  82.494 170.996  1.00  1.00           C  
ATOM    855  CA  GLU C 255     175.185  79.902 173.531  1.00  1.00           C  
ATOM    856  CA  LYS C 256     178.717  79.861 174.958  1.00  1.00           C  
ATOM    857  CA  LEU C 257     178.528  83.651 175.146  1.00  1.00           C  
ATOM    858  CA  ALA C 258     175.331  83.323 177.176  1.00  1.00           C  
ATOM    859  CA  ALA C 259     177.488  81.096 179.366  1.00  1.00           C  
ATOM    860  CA  GLN C 260     179.641  84.216 179.621  1.00  1.00           C  
ATOM    861  CA  LYS C 261     176.659  86.201 180.870  1.00  1.00           C  
ATOM    862  CA  LYS C 262     176.008  83.526 183.482  1.00  1.00           C  
ATOM    863  CA  GLU C 263     179.647  83.735 184.574  1.00  1.00           C  
ATOM    864  CA  LYS C 264     179.439  87.516 184.887  1.00  1.00           C  
ATOM    865  CA  ALA C 265     176.351  87.152 187.101  1.00  1.00           C  
ATOM    866  CA  GLU C 266     178.091  84.887 189.615  1.00  1.00           C  
ATOM    867  CA  LYS C 267     180.679  87.524 190.511  1.00  1.00           C  
ATOM    868  CA  ASN C 268     177.898  90.005 191.314  1.00 30.00           C  
ATOM    869  CA  ILE C 269     176.171  87.393 193.442  1.00 30.00           C  
ATOM    870  CA  ALA C 270     179.452  86.849 195.294  1.00 30.00           C  
ATOM    871  CA  ALA C 271     179.760  90.598 195.804  1.00 30.00           C  
ATOM    872  CA  ARG C 272     176.327  90.683 197.445  1.00 30.00           C  
ATOM    873  CA  LYS C 273     177.485  87.785 199.603  1.00 30.00           C  
ATOM    874  CA  GLU C 274     180.611  89.803 200.356  1.00 30.00           C  
ATOM    875  CA  MET C 275     178.417  92.891 200.769  1.00 30.00           C  
ATOM    876  CA  GLY C 276     174.679  93.505 201.086  1.00 30.00           C  
ATOM    877  CA  LEU C 277     172.512  93.616 197.957  1.00 30.00           C  
ATOM    878  CA  PRO C 278     172.241  95.736 196.074  1.00 30.00           C  
ATOM    879  CA  THR C 279     169.900  93.624 193.910  1.00 30.00           C  
ATOM    880  CA  PRO C 280     169.542  90.075 192.552  1.00 30.00           C  
TER     881      PRO C 280                                                      
HETATM  882 FE   FCO A2989     136.498 121.869 191.534  1.00 23.77          FE  
HETATM  883 NI    NI A2990     136.959 119.611 192.450  1.00 24.92          NI  
HETATM  884 FE   FE2 A2991     140.924 129.204 199.198  1.00 27.13          FE  
HETATM  885 FE1  SF4 B 300     144.795 112.307 195.112  1.00 20.00          FE  
HETATM  886 FE2  SF4 B 300     146.248 111.036 197.025  1.00 20.00          FE  
HETATM  887 FE3  SF4 B 300     146.999 110.886 194.419  1.00 20.00          FE  
HETATM  888 FE4  SF4 B 300     144.761 109.596 195.264  1.00 20.00          FE  
HETATM  889  S1  SF4 B 300     146.920 109.139 195.912  1.00 20.00           S  
HETATM  890  S2  SF4 B 300     144.966 110.846 193.343  1.00 20.00           S  
HETATM  891  S3  SF4 B 300     143.953 111.055 196.850  1.00 20.00           S  
HETATM  892  S4  SF4 B 300     146.962 112.787 195.714  1.00 20.00           S  
HETATM  893 FE1  SF4 B 301     157.267 109.722 191.364  1.00 20.00          FE  
HETATM  894 FE2  SF4 B 301     157.739 112.207 192.356  1.00 20.00          FE  
HETATM  895 FE3  SF4 B 301     158.422 111.610 189.796  1.00 20.00          FE  
HETATM  896 FE4  SF4 B 301     159.813 110.522 191.864  1.00 20.00          FE  
HETATM  897  S1  SF4 B 301     159.716 112.756 191.316  1.00 20.00           S  
HETATM  898  S2  SF4 B 301     159.082 109.414 189.983  1.00 20.00           S  
HETATM  899  S3  SF4 B 301     158.155 110.214 193.429  1.00 20.00           S  
HETATM  900  S4  SF4 B 301     156.287 111.678 190.651  1.00 20.00           S  
HETATM  901 FE1  SF4 B 302     166.622 101.803 186.353  1.00 20.00          FE  
HETATM  902 FE2  SF4 B 302     165.945 103.360 184.231  1.00 20.00          FE  
HETATM  903 FE3  SF4 B 302     168.404 103.590 185.361  1.00 20.00          FE  
HETATM  904 FE4  SF4 B 302     166.205 104.463 186.700  1.00 20.00          FE  
HETATM  905  S1  SF4 B 302     167.030 105.325 184.732  1.00 20.00           S  
HETATM  906  S2  SF4 B 302     167.937 103.233 187.585  1.00 20.00           S  
HETATM  907  S3  SF4 B 302     164.627 102.914 186.063  1.00 20.00           S  
HETATM  908  S4  SF4 B 302     167.582 101.743 184.263  1.00 20.00           S  
HETATM  909  N1  F42 C 285     179.520  89.197 168.146  1.00 31.86           N  
HETATM  910  C2  F42 C 285     179.562  87.946 168.682  1.00 31.64           C  
HETATM  911  O2  F42 C 285     180.507  87.667 169.447  1.00 28.39           O  
HETATM  912  N3  F42 C 285     178.917  86.934 168.051  1.00 29.66           N  
HETATM  913  C4  F42 C 285     177.902  87.215 167.183  1.00 32.98           C  
HETATM  914  O4  F42 C 285     177.057  86.321 166.888  1.00 30.69           O  
HETATM  915  C4A F42 C 285     177.609  88.559 166.943  1.00 31.19           C  
HETATM  916  C5  F42 C 285     176.472  88.964 166.224  1.00 32.54           C  
HETATM  917  C5A F42 C 285     176.626  90.081 165.400  1.00 32.60           C  
HETATM  918  C6  F42 C 285     175.745  90.294 164.333  1.00 33.69           C  
HETATM  919  C7  F42 C 285     175.912  91.401 163.511  1.00 31.39           C  
HETATM  920  C8  F42 C 285     176.961  92.295 163.753  1.00 33.16           C  
HETATM  921  O8M F42 C 285     177.106  93.386 162.943  1.00 34.10           O  
HETATM  922  C9  F42 C 285     177.843  92.080 164.824  1.00 33.62           C  
HETATM  923  C9A F42 C 285     177.672  90.970 165.656  1.00 33.04           C  
HETATM  924  N10 F42 C 285     178.515  90.736 166.696  1.00 34.20           N  
HETATM  925  C10 F42 C 285     178.607  89.491 167.196  1.00 32.79           C  
HETATM  926  C1' F42 C 285     179.318  91.824 167.301  1.00 34.57           C  
HETATM  927  C2' F42 C 285     180.728  91.864 166.711  1.00 35.28           C  
HETATM  928 FE1  SF4 C 303     172.199  95.152 181.005  1.00 20.00          FE  
HETATM  929 FE2  SF4 C 303     172.181  94.848 178.304  1.00 20.00          FE  
HETATM  930 FE3  SF4 C 303     174.340  95.939 179.539  1.00 20.00          FE  
HETATM  931 FE4  SF4 C 303     172.008  97.330 179.395  1.00 20.00          FE  
HETATM  932  S1  SF4 C 303     173.336  96.715 177.620  1.00 20.00           S  
HETATM  933  S2  SF4 C 303     173.357  97.124 181.248  1.00 20.00           S  
HETATM  934  S3  SF4 C 303     170.450  95.647 179.592  1.00 20.00           S  
HETATM  935  S4  SF4 C 303     173.584  93.780 179.783  1.00 20.00           S  
HETATM  936  PA  FAD C 304     169.139  98.185 163.983  1.00 20.00           P  
HETATM  937  O1A FAD C 304     168.360  97.696 165.180  1.00 20.00           O  
HETATM  938  O2A FAD C 304     168.449  98.349 162.650  1.00 20.00           O  
HETATM  939  O5B FAD C 304     169.828  99.588 164.370  1.00 20.00           O  
HETATM  940  C5B FAD C 304     169.376 100.804 163.778  1.00 20.00           C  
HETATM  941  C4B FAD C 304     168.157 101.315 164.535  1.00 20.00           C  
HETATM  942  O4B FAD C 304     168.204 100.860 165.890  1.00 20.00           O  
HETATM  943  C3B FAD C 304     168.119 102.835 164.556  1.00 20.00           C  
HETATM  944  O3B FAD C 304     166.913 103.304 163.945  1.00 20.00           O  
HETATM  945  C2B FAD C 304     168.153 103.241 166.016  1.00 20.00           C  
HETATM  946  O2B FAD C 304     166.970 103.972 166.349  1.00 20.00           O  
HETATM  947  C1B FAD C 304     168.210 101.949 166.816  1.00 20.00           C  
HETATM  948  N9A FAD C 304     169.457 101.915 167.621  1.00 20.00           N  
HETATM  949  C8A FAD C 304     170.691 101.652 167.150  1.00 20.00           C  
HETATM  950  N7A FAD C 304     171.615 101.697 168.144  1.00 20.00           N  
HETATM  951  C5A FAD C 304     170.966 101.997 169.285  1.00 20.00           C  
HETATM  952  C6A FAD C 304     171.340 102.199 170.704  1.00 20.00           C  
HETATM  953  N6A FAD C 304     172.628 102.087 171.113  1.00 20.00           N  
HETATM  954  N1A FAD C 304     170.354 102.499 171.578  1.00 20.00           N  
HETATM  955  C2A FAD C 304     169.071 102.613 171.185  1.00 20.00           C  
HETATM  956  N3A FAD C 304     168.661 102.444 169.915  1.00 20.00           N  
HETATM  957  C4A FAD C 304     169.545 102.139 168.935  1.00 20.00           C  
HETATM  958  N1  FAD C 304     174.615  92.290 168.756  1.00 20.00           N  
HETATM  959  C2  FAD C 304     175.207  91.191 169.289  1.00 20.00           C  
HETATM  960  O2  FAD C 304     174.812  90.062 168.926  1.00 20.00           O  
HETATM  961  N3  FAD C 304     176.202  91.266 170.192  1.00 20.00           N  
HETATM  962  C4  FAD C 304     176.681  92.436 170.631  1.00 20.00           C  
HETATM  963  O4  FAD C 304     177.606  92.473 171.471  1.00 20.00           O  
HETATM  964  C4X FAD C 304     176.089  93.687 170.099  1.00 20.00           C  
HETATM  965  N5  FAD C 304     176.516  94.908 170.491  1.00 20.00           N  
HETATM  966  C5X FAD C 304     175.955  96.031 169.987  1.00 20.00           C  
HETATM  967  C6  FAD C 304     176.410  97.276 170.405  1.00 20.00           C  
HETATM  968  C7  FAD C 304     175.840  98.436 169.892  1.00 20.00           C  
HETATM  969  C7M FAD C 304     176.336  99.783 170.348  1.00 20.00           C  
HETATM  970  C8  FAD C 304     174.741  98.347 168.895  1.00 20.00           C  
HETATM  971  C8M FAD C 304     174.124  99.605 168.340  1.00 20.00           C  
HETATM  972  C9  FAD C 304     174.282  97.105 168.473  1.00 20.00           C  
HETATM  973  C9A FAD C 304     174.852  95.946 168.986  1.00 20.00           C  
HETATM  974  N10 FAD C 304     174.393  94.682 168.565  1.00 20.00           N  
HETATM  975  C10 FAD C 304     174.999  93.535 169.109  1.00 20.00           C  
HETATM  976  C1' FAD C 304     173.312  94.566 167.583  1.00 20.00           C  
HETATM  977  C2' FAD C 304     173.499  95.616 166.495  1.00 20.00           C  
HETATM  978  O2' FAD C 304     172.564  96.682 166.695  1.00 20.00           O  
HETATM  979  C3' FAD C 304     173.291  95.012 165.111  1.00 20.00           C  
HETATM  980  O3' FAD C 304     174.028  93.788 165.009  1.00 20.00           O  
HETATM  981  C4' FAD C 304     173.749  95.973 164.021  1.00 20.00           C  
HETATM  982  O4' FAD C 304     173.970  97.269 164.589  1.00 20.00           O  
HETATM  983  C5' FAD C 304     172.709  96.076 162.912  1.00 20.00           C  
HETATM  984  O5' FAD C 304     171.666  95.132 163.149  1.00 20.00           O  
HETATM  985  P   FAD C 304     170.203  95.628 163.604  1.00 20.00           P  
HETATM  986  O1P FAD C 304     169.907  95.039 164.962  1.00 20.00           O  
HETATM  987  O2P FAD C 304     169.248  95.397 162.458  1.00 20.00           O  
HETATM  988  O3P FAD C 304     170.408  97.216 163.778  1.00 20.00           O  
CONECT  885  890  891  892                                                      
CONECT  886  889  891  892                                                      
CONECT  887  889  890  892                                                      
CONECT  888  889  890  891                                                      
CONECT  889  886  887  888                                                      
CONECT  890  885  887  888                                                      
CONECT  891  885  886  888                                                      
CONECT  892  885  886  887                                                      
CONECT  893  898  899  900                                                      
CONECT  894  897  899  900                                                      
CONECT  895  897  898  900                                                      
CONECT  896  897  898  899                                                      
CONECT  897  894  895  896                                                      
CONECT  898  893  895  896                                                      
CONECT  899  893  894  896                                                      
CONECT  900  893  894  895                                                      
CONECT  901  906  907  908                                                      
CONECT  902  905  907  908                                                      
CONECT  903  905  906  908                                                      
CONECT  904  905  906  907                                                      
CONECT  905  902  903  904                                                      
CONECT  906  901  903  904                                                      
CONECT  907  901  902  904                                                      
CONECT  908  901  902  903                                                      
CONECT  909  910  925                                                           
CONECT  910  909  911  912                                                      
CONECT  911  910                                                                
CONECT  912  910  913                                                           
CONECT  913  912  914  915                                                      
CONECT  914  913                                                                
CONECT  915  913  916  925                                                      
CONECT  916  915  917                                                           
CONECT  917  916  918  923                                                      
CONECT  918  917  919                                                           
CONECT  919  918  920                                                           
CONECT  920  919  921  922                                                      
CONECT  921  920                                                                
CONECT  922  920  923                                                           
CONECT  923  917  922  924                                                      
CONECT  924  923  925  926                                                      
CONECT  925  909  915  924                                                      
CONECT  926  924  927                                                           
CONECT  927  926                                                                
CONECT  928  933  934  935                                                      
CONECT  929  932  934  935                                                      
CONECT  930  932  933  935                                                      
CONECT  931  932  933  934                                                      
CONECT  932  929  930  931                                                      
CONECT  933  928  930  931                                                      
CONECT  934  928  929  931                                                      
CONECT  935  928  929  930                                                      
CONECT  936  937  938  939  988                                                 
CONECT  937  936                                                                
CONECT  938  936                                                                
CONECT  939  936  940                                                           
CONECT  940  939  941                                                           
CONECT  941  940  942  943                                                      
CONECT  942  941  947                                                           
CONECT  943  941  944  945                                                      
CONECT  944  943                                                                
CONECT  945  943  946  947                                                      
CONECT  946  945                                                                
CONECT  947  942  945  948                                                      
CONECT  948  947  949  957                                                      
CONECT  949  948  950                                                           
CONECT  950  949  951                                                           
CONECT  951  950  952  957                                                      
CONECT  952  951  953  954                                                      
CONECT  953  952                                                                
CONECT  954  952  955                                                           
CONECT  955  954  956                                                           
CONECT  956  955  957                                                           
CONECT  957  948  951  956                                                      
CONECT  958  959  975                                                           
CONECT  959  958  960  961                                                      
CONECT  960  959                                                                
CONECT  961  959  962                                                           
CONECT  962  961  963  964                                                      
CONECT  963  962                                                                
CONECT  964  962  965  975                                                      
CONECT  965  964  966                                                           
CONECT  966  965  967  973                                                      
CONECT  967  966  968                                                           
CONECT  968  967  969  970                                                      
CONECT  969  968                                                                
CONECT  970  968  971  972                                                      
CONECT  971  970                                                                
CONECT  972  970  973                                                           
CONECT  973  966  972  974                                                      
CONECT  974  973  975  976                                                      
CONECT  975  958  964  974                                                      
CONECT  976  974  977                                                           
CONECT  977  976  978  979                                                      
CONECT  978  977                                                                
CONECT  979  977  980  981                                                      
CONECT  980  979                                                                
CONECT  981  979  982  983                                                      
CONECT  982  981                                                                
CONECT  983  981  984                                                           
CONECT  984  983  985                                                           
CONECT  985  984  986  987  988                                                 
CONECT  986  985                                                                
CONECT  987  985                                                                
CONECT  988  936  985                                                           
MASTER      256    0    9   31   24    0   14    6  985    3  104   76          
END                                                                             
