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Database: PDB
Entry: 3JC6
LinkDB: 3JC6
Original site: 3JC6 
HEADER    REPLICATION                             24-NOV-15   3JC6              
TITLE     STRUCTURE OF THE EUKARYOTIC REPLICATIVE CMG HELICASE AND PUMPJACK     
TITLE    2 MOTION                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA REPLICATION LICENSING FACTOR MCM2;                     
COMPND   3 CHAIN: 2;                                                            
COMPND   4 SYNONYM: MINICHROMOSOME MAINTENANCE PROTEIN 2;                       
COMPND   5 EC: 3.6.4.12;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA REPLICATION LICENSING FACTOR MCM3;                     
COMPND   9 CHAIN: 3;                                                            
COMPND  10 SYNONYM: MINICHROMOSOME MAINTENANCE PROTEIN 3;                       
COMPND  11 EC: 3.6.4.12;                                                        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA REPLICATION LICENSING FACTOR MCM4;                     
COMPND  15 CHAIN: 4;                                                            
COMPND  16 SYNONYM: CELL DIVISION CONTROL PROTEIN 54;                           
COMPND  17 EC: 3.6.4.12;                                                        
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: MINICHROMOSOME MAINTENANCE PROTEIN 5;                      
COMPND  21 CHAIN: 5;                                                            
COMPND  22 SYNONYM: CELL DIVISION CONTROL PROTEIN 46;                           
COMPND  23 EC: 3.6.4.12;                                                        
COMPND  24 ENGINEERED: YES;                                                     
COMPND  25 MOL_ID: 5;                                                           
COMPND  26 MOLECULE: DNA REPLICATION LICENSING FACTOR MCM6;                     
COMPND  27 CHAIN: 6;                                                            
COMPND  28 SYNONYM: MINICHROMOSOME MAINTENANCE PROTEIN 6;                       
COMPND  29 EC: 3.6.4.12;                                                        
COMPND  30 ENGINEERED: YES;                                                     
COMPND  31 MOL_ID: 6;                                                           
COMPND  32 MOLECULE: DNA REPLICATION LICENSING FACTOR MCM7;                     
COMPND  33 CHAIN: 7;                                                            
COMPND  34 SYNONYM: CELL DIVISION CONTROL PROTEIN 47, MINICHROMOSOME MAINTENANCE
COMPND  35 PROTEIN 7;                                                           
COMPND  36 EC: 3.6.4.12;                                                        
COMPND  37 ENGINEERED: YES;                                                     
COMPND  38 MOL_ID: 7;                                                           
COMPND  39 MOLECULE: CELL DIVISION CONTROL PROTEIN 45;                          
COMPND  40 CHAIN: E;                                                            
COMPND  41 ENGINEERED: YES;                                                     
COMPND  42 MOL_ID: 8;                                                           
COMPND  43 MOLECULE: DNA REPLICATION COMPLEX GINS PROTEIN SLD5;                 
COMPND  44 CHAIN: D;                                                            
COMPND  45 ENGINEERED: YES;                                                     
COMPND  46 MOL_ID: 9;                                                           
COMPND  47 MOLECULE: DNA REPLICATION COMPLEX GINS PROTEIN PSF2;                 
COMPND  48 CHAIN: B;                                                            
COMPND  49 SYNONYM: PARTNER OF SLD FIVE 2;                                      
COMPND  50 ENGINEERED: YES;                                                     
COMPND  51 MOL_ID: 10;                                                          
COMPND  52 MOLECULE: DNA REPLICATION COMPLEX GINS PROTEIN PSF1;                 
COMPND  53 CHAIN: A;                                                            
COMPND  54 SYNONYM: PARTNER OF SLD FIVE 1;                                      
COMPND  55 ENGINEERED: YES;                                                     
COMPND  56 MOL_ID: 11;                                                          
COMPND  57 MOLECULE: DNA REPLICATION COMPLEX GINS PROTEIN PSF3;                 
COMPND  58 CHAIN: C;                                                            
COMPND  59 SYNONYM: PARTNER OF SLD FIVE 3;                                      
COMPND  60 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: MCM2, YBL023C, YBL0438;                                        
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  11 ORGANISM_COMMON: YEAST;                                              
SOURCE  12 ORGANISM_TAXID: 4932;                                                
SOURCE  13 GENE: MCM3, YEL032W, SYGP-ORF23;                                     
SOURCE  14 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  15 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  19 ORGANISM_COMMON: YEAST;                                              
SOURCE  20 ORGANISM_TAXID: 4932;                                                
SOURCE  21 GENE: MCM4, CDC54, HCD21, YPR019W, YP9531.13;                        
SOURCE  22 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  23 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  27 ORGANISM_COMMON: YEAST;                                              
SOURCE  28 ORGANISM_TAXID: 4932;                                                
SOURCE  29 GENE: MCM5, CDC46, YLR274W, L9328.1;                                 
SOURCE  30 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  31 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE  32 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  33 MOL_ID: 5;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  35 ORGANISM_COMMON: YEAST;                                              
SOURCE  36 ORGANISM_TAXID: 4932;                                                
SOURCE  37 GENE: MCM6, YGL201C;                                                 
SOURCE  38 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  39 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE  40 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  41 MOL_ID: 6;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  43 ORGANISM_COMMON: YEAST;                                              
SOURCE  44 ORGANISM_TAXID: 4932;                                                
SOURCE  45 GENE: MCM7, CDC47, YBR202W, YBR1441;                                 
SOURCE  46 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  47 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE  48 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  49 MOL_ID: 7;                                                           
SOURCE  50 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  51 ORGANISM_COMMON: YEAST;                                              
SOURCE  52 ORGANISM_TAXID: 4932;                                                
SOURCE  53 GENE: CDC45, SLD4, YLR103C, L8004.11;                                
SOURCE  54 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  55 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE  56 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  57 MOL_ID: 8;                                                           
SOURCE  58 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  59 ORGANISM_COMMON: YEAST;                                              
SOURCE  60 ORGANISM_TAXID: 4932;                                                
SOURCE  61 GENE: SLD5, YDR489W;                                                 
SOURCE  62 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  63 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE  64 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  65 MOL_ID: 9;                                                           
SOURCE  66 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  67 ORGANISM_COMMON: YEAST;                                              
SOURCE  68 ORGANISM_TAXID: 4932;                                                
SOURCE  69 GENE: PSF2, YJL072C, HRF213, J1086;                                  
SOURCE  70 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  71 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE  72 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  73 MOL_ID: 10;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  75 ORGANISM_COMMON: YEAST;                                              
SOURCE  76 ORGANISM_TAXID: 4932;                                                
SOURCE  77 GENE: PSF1, YDR013W, PZA208, YD8119.18;                              
SOURCE  78 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  79 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE  80 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  81 MOL_ID: 11;                                                          
SOURCE  82 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  83 ORGANISM_COMMON: YEAST;                                              
SOURCE  84 ORGANISM_TAXID: 4932;                                                
SOURCE  85 GENE: PSF3, YOL146W;                                                 
SOURCE  86 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  87 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE  88 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    CMG HELICASE, CRYO-EM, REPLICATION                                    
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    H.LI,L.BAI,Z.YUAN,J.SUN,R.E.GEORGESCU,J.LIU,M.E.O'DONNELL             
REVDAT   5   18-JUL-18 3JC6    1       REMARK                                   
REVDAT   4   24-JAN-18 3JC6    1       AUTHOR REMARK                            
REVDAT   3   16-MAR-16 3JC6    1       JRNL                                     
REVDAT   2   24-FEB-16 3JC6    1       JRNL                                     
REVDAT   1   10-FEB-16 3JC6    0                                                
JRNL        AUTH   Z.YUAN,L.BAI,J.SUN,R.GEORGESCU,J.LIU,M.E.O'DONNELL,H.LI      
JRNL        TITL   STRUCTURE OF THE EUKARYOTIC REPLICATIVE CMG HELICASE         
JRNL        TITL 2 SUGGESTS A PUMPJACK MOTION FOR TRANSLOCATION.                
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  23   217 2016              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   26854665                                                     
JRNL        DOI    10.1038/NSMB.3170                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : UCSF CHIMERA, RELION                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 2Q9Q                                
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)    : 1.010                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.700                          
REMARK   3   NUMBER OF PARTICLES               : 469818                         
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: (SINGLE PARTICLE DETAILS: ALL STEPS, INCLUDING        
REMARK   3  AUTOMATIC PARTICLE PICKING, 2D CLASSIFICATION, 3D CLASSIFICATION,   
REMARK   3  AND 3D REFINEMENT WERE PERFORMED IN RELION 1.4.) (SINGLE            
REMARK   3  PARTICLE--APPLIED SYMMETRY: C1)                                     
REMARK   4                                                                      
REMARK   4 3JC6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000160516.                                   
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                 : SACCHAROMYCES CEREVISIAE CMG      
REMARK 245                                    COMPLEX                           
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.60                              
REMARK 245   SAMPLE SUPPORT DETAILS         : 400 MESH HOLEY CARBON C-FLAT      
REMARK 245                                    GRID, GLOW-DISCHARGED IN AIR      
REMARK 245   SAMPLE VITRIFICATION DETAILS   : BLOT FOR 3 SECONDS BEFORE         
REMARK 245                                    PLUNGING INTO LIQUID ETHANE       
REMARK 245                                    (FEI VITROBOT MARK IV).           
REMARK 245   SAMPLE BUFFER                  : 20 MM TRIS ACETATE, PH 7.5, 40    
REMARK 245                                    MM POTASSIUM GLUTAMATE, 2 MM      
REMARK 245                                    DTT, 0.1 MM EDTA                  
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 01-AUG-15                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : 1500.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3500.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 50.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 29000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 49505                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: UNDECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 2, 3, 4, 5, 6, 7, E, D, B, A,         
REMARK 350                    AND CHAINS: 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN 2 353    CG   CD   OE1  NE2                                  
REMARK 470     ASP 2 354    CG   OD1  OD2                                       
REMARK 470     SER 2 355    OG                                                  
REMARK 470     ASN 2 356    CG   OD1  ND2                                       
REMARK 470     GLU 2 357    CG   CD   OE1  OE2                                  
REMARK 470     GLU 2 358    CG   CD   OE1  OE2                                  
REMARK 470     ILE 2 359    CG1  CG2  CD1                                       
REMARK 470     ARG 2 360    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS 4 204    CG   CD   CE   NZ                                   
REMARK 470     ILE 4 374    CG1  CG2  CD1                                       
REMARK 470     ASP 4 375    CG   OD1  OD2                                       
REMARK 470     CYS 4 376    SG                                                  
REMARK 470     ASN 4 377    CG   OD1  ND2                                       
REMARK 470     GLU 4 378    CG   CD   OE1  OE2                                  
REMARK 470     PRO 4 379    CG   CD                                             
REMARK 470     ASN 4 380    CG   OD1  ND2                                       
REMARK 470     SER 4 381    OG                                                  
REMARK 470     THR 5 325    CG2                                                 
REMARK 470     PRO 5 326    CD                                                  
REMARK 470     VAL 5 337    CG2                                                 
REMARK 470     THR 5 339    CG2                                                 
REMARK 470     SER 6 308    OG                                                  
REMARK 470     PHE 6 309    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR 6 310    OG1  CG2                                            
REMARK 470     CYS 6 311    SG                                                  
REMARK 470     ASP 6 312    CG   OD1  OD2                                       
REMARK 470     MET 6 313    CG   SD   CE                                        
REMARK 470     CYS 6 314    SG                                                  
REMARK 470     ARG 6 315    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE 6 317    CG1  CG2  CD1                                       
REMARK 470     VAL 6 318    CG1  CG2                                            
REMARK 470     ASP 6 319    CG   OD1  OD2                                       
REMARK 470     ASN 6 320    CG   OD1  ND2                                       
REMARK 470     VAL 6 321    CG1  CG2                                            
REMARK 470     GLU 6 322    CG   CD   OE1  OE2                                  
REMARK 470     GLN 6 323    CG   CD   OE1  NE2                                  
REMARK 470     SER 6 324    OG                                                  
REMARK 470     PHE 6 325    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS 6 326    CG   CD   CE   NZ                                   
REMARK 470     TYR 6 327    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR 6 328    OG1  CG2                                            
REMARK 470     GLU 6 329    CG   CD   OE1  OE2                                  
REMARK 470     PRO 6 330    CG   CD                                             
REMARK 470     THR 6 331    OG1  CG2                                            
REMARK 470     PHE 6 332    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     CYS 6 333    SG                                                  
REMARK 470     PRO 6 334    CG   CD                                             
REMARK 470     ASN 6 335    CG   OD1  ND2                                       
REMARK 470     PRO 6 336    CG   CD                                             
REMARK 470     SER 6 337    OG                                                  
REMARK 470     CYS 6 338    SG                                                  
REMARK 470     GLU 6 339    CG   CD   OE1  OE2                                  
REMARK 470     ASN 6 340    CG   OD1  ND2                                       
REMARK 470     ARG 6 341    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE 6 343    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TRP 6 344    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP 6 344    CZ3  CH2                                            
REMARK 470     THR 6 345    OG1  CG2                                            
REMARK 470     LEU 6 346    CG   CD1  CD2                                       
REMARK 470     LYS E 224    CD   CE   NZ                                        
REMARK 470     GLU C 119    CG   CD   OE1  OE2                                  
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   CG   LYS D   137     NH1  ARG D   141              1.20            
REMARK 500   ND2  ASN E   345     CZ2  TRP E   551              1.55            
REMARK 500   O    LYS C    83     OD1  ASN C    86              1.55            
REMARK 500   CG1  VAL A   165     CD2  LEU A   205              1.62            
REMARK 500   OE2  GLU B   187     CG2  ILE C   176              1.65            
REMARK 500   OE1  GLU 3   234     O    GLY 3   238              1.67            
REMARK 500   CD1  LEU E    34     CD1  LEU E   543              1.73            
REMARK 500   O    LEU D   161     CD1  ILE D   169              1.74            
REMARK 500   OG1  THR 2   325     OG1  THR 2   389              1.80            
REMARK 500   CG   LYS D   137     CZ   ARG D   141              1.82            
REMARK 500   NH2  ARG D   141     O    ASP A   148              1.83            
REMARK 500   CG1  ILE 4   433     O    VAL 4   469              1.85            
REMARK 500   CG2  ILE A   149     N    LEU A   151              1.85            
REMARK 500   NZ   LYS 3   195     OD2  ASP 3   216              1.86            
REMARK 500   NH2  ARG D   141     CG1  VAL A   147              1.91            
REMARK 500   O    LYS D   137     NH1  ARG D   141              1.94            
REMARK 500   CD   GLU B   187     CG2  ILE C   176              1.94            
REMARK 500   O    ASP A   108     NH1  ARG A   198              1.95            
REMARK 500   OE2  GLU 2   392     OG1  THR 2   396              1.95            
REMARK 500   O    GLU D    70     NZ   LYS D   150              1.97            
REMARK 500   CZ   PHE 5   197     NZ   LYS 5   329              2.01            
REMARK 500   CD1  LEU E    34     CG   LEU E   543              2.03            
REMARK 500   SG   CYS E    33     O    ILE E    61              2.04            
REMARK 500   CE2  PHE 5   197     CG   LYS 5   329              2.05            
REMARK 500   O    ILE E    15     OG   SER E    19              2.05            
REMARK 500   NE2  GLN E    57     OG   SER A   187              2.06            
REMARK 500   CD1  ILE 4   433     O    VAL 4   469              2.07            
REMARK 500   OD1  ASN 2   442     N    PHE 2   444              2.07            
REMARK 500   CD2  LEU E   326     OG   SER E   337              2.07            
REMARK 500   OE1  GLU 3   234     O    ASN 3   239              2.08            
REMARK 500   NH1  ARG 3   104     O    ASN C    86              2.09            
REMARK 500   O    PHE 2   300     OG1  THR 2   302              2.10            
REMARK 500   OG   SER 2   213     OE2  GLU 2   217              2.11            
REMARK 500   CD1  ILE 6   290     CZ   PHE 6   454              2.12            
REMARK 500   CD2  LEU A   168     CB   GLN A   206              2.12            
REMARK 500   O    THR 3   187     OG1  THR 3   257              2.12            
REMARK 500   CB   LYS D   137     NH1  ARG D   141              2.12            
REMARK 500   OD2  ASP A   170     CA   TYR A   204              2.13            
REMARK 500   CG   LYS D   137     NH2  ARG D   141              2.13            
REMARK 500   O    PRO 7   126     CG2  THR 7   129              2.14            
REMARK 500   CD   LYS A   169     NZ   LYS A   185              2.14            
REMARK 500   OE2  GLU 3   234     CA   LYS 3   240              2.15            
REMARK 500   CG2  ILE A   149     CB   LEU A   151              2.15            
REMARK 500   CZ   PHE 5   197     CE   LYS 5   329              2.16            
REMARK 500   NH2  ARG 5   175     OD1  ASN 5   196              2.16            
REMARK 500   O    CYS D   146     OG   SER D   149              2.16            
REMARK 500   N    PHE C   104     OE2  GLU C   170              2.16            
REMARK 500   OG   SER E    32     O    VAL E    84              2.17            
REMARK 500   O    ALA 3    53     NZ   LYS 7   217              2.17            
REMARK 500   CG2  ILE 3   122     CD1  LEU 3   221              2.18            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU 3 171   CA  -  CB  -  CG  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    PRO 4 379   C   -  N   -  CA  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    LEU 5 258   CA  -  CB  -  CG  ANGL. DEV. =  17.5 DEGREES          
REMARK 500    PRO 5 326   C   -  N   -  CA  ANGL. DEV. =  21.1 DEGREES          
REMARK 500    ASP 6 105   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    PRO 6 334   C   -  N   -  CA  ANGL. DEV. =  16.9 DEGREES          
REMARK 500    PRO 6 374   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    LEU E  27   CA  -  CB  -  CG  ANGL. DEV. =  18.3 DEGREES          
REMARK 500    PRO A 157   C   -  N   -  CA  ANGL. DEV. =  10.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR 2 222       71.17     60.38                                   
REMARK 500    ARG 2 224       74.65     59.84                                   
REMARK 500    PRO 2 284       56.86    -63.10                                   
REMARK 500    ASP 2 285     -162.83   -165.35                                   
REMARK 500    HIS 2 290      -24.42     66.93                                   
REMARK 500    SER 2 291       16.29     39.55                                   
REMARK 500    ILE 2 297       85.84     58.84                                   
REMARK 500    SER 2 298     -170.08    -63.46                                   
REMARK 500    THR 2 302     -115.71     53.78                                   
REMARK 500    SER 2 305      -85.14    -88.85                                   
REMARK 500    LEU 2 306      -68.18   -139.49                                   
REMARK 500    SER 2 315       -1.41     65.72                                   
REMARK 500    LYS 2 335     -126.72     47.28                                   
REMARK 500    CYS 2 341       76.10     59.38                                   
REMARK 500    GLU 2 357      -66.66   -133.39                                   
REMARK 500    ASN 2 376      -79.81   -113.49                                   
REMARK 500    GLU 2 378      -74.43   -137.21                                   
REMARK 500    ALA 2 412     -121.38     50.84                                   
REMARK 500    ASP 2 416       -4.47     78.48                                   
REMARK 500    ASN 2 432      -59.39   -121.35                                   
REMARK 500    ASP 2 435       58.00     20.79                                   
REMARK 500    LEU 2 438      -87.90   -127.60                                   
REMARK 500    ASN 2 439       -7.46     55.87                                   
REMARK 500    ASN 2 442      -63.87   -143.93                                   
REMARK 500    ASP 3  33      -20.25     76.73                                   
REMARK 500    PHE 3 106      -72.03    -83.99                                   
REMARK 500    ASP 3 138      -95.46   -129.21                                   
REMARK 500    TRP 3 153     -152.08     54.00                                   
REMARK 500    SER 3 156      -55.35   -125.93                                   
REMARK 500    PHE 3 157       79.94     70.89                                   
REMARK 500    LYS 3 158      -75.93    -54.46                                   
REMARK 500    ALA 3 163      -60.28   -121.95                                   
REMARK 500    HIS 3 164       17.84     59.34                                   
REMARK 500    THR 3 172      102.80     62.65                                   
REMARK 500    THR 3 189       75.94     67.14                                   
REMARK 500    ILE 3 197      -66.48   -128.08                                   
REMARK 500    ARG 3 208     -150.58     49.32                                   
REMARK 500    THR 3 220     -127.37     46.33                                   
REMARK 500    LEU 3 221      -63.82   -124.54                                   
REMARK 500    PRO 3 228      151.22    -47.83                                   
REMARK 500    ILE 3 230     -138.22     55.47                                   
REMARK 500    THR 3 233      112.24     64.62                                   
REMARK 500    GLU 3 237     -169.71    -78.20                                   
REMARK 500    ASP 3 280     -129.51     59.23                                   
REMARK 500    THR 3 313      153.45    172.63                                   
REMARK 500    ASN 3 324      -62.36   -131.65                                   
REMARK 500    THR 3 325      -60.52   -108.73                                   
REMARK 500    VAL 3 326       68.27     66.24                                   
REMARK 500    ARG 4 178       70.17     57.21                                   
REMARK 500    TRP 4 181     -129.26     40.23                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     254 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA 3  163     HIS 3  164                   30.98                    
REMARK 500 ALA 3  165     LEU 3  166                 -149.09                    
REMARK 500 LYS 4  202     TYR 4  203                   38.35                    
REMARK 500 ALA 4  245     ARG 4  246                   36.33                    
REMARK 500 GLU 4  372     ARG 4  373                  147.99                    
REMARK 500 ASN 4  377     GLU 4  378                  -45.18                    
REMARK 500 SER 4  448     ARG 4  449                   37.17                    
REMARK 500 VAL 6  103     ASP 6  104                  -39.76                    
REMARK 500 MET 6  313     CYS 6  314                  -33.11                    
REMARK 500 PRO 6  334     ASN 6  335                  -36.30                    
REMARK 500 SER 7  221     SER 7  222                  -40.18                    
REMARK 500 VAL 7  257     ILE 7  258                   43.85                    
REMARK 500 GLU 7  283     CYS 7  284                  148.31                    
REMARK 500 PRO 7  359     TYR 7  360                  -41.43                    
REMARK 500 GLU E   97     ILE E   98                   32.82                    
REMARK 500 LYS D  200     TYR D  201                   33.35                    
REMARK 500 VAL D  258     THR D  259                   43.40                    
REMARK 500 ASN A  104     ASN A  105                  122.45                    
REMARK 500 ASN A  105     GLY A  106                   36.05                    
REMARK 500 GLY A  106     LEU A  107                  -39.36                    
REMARK 500 ASP A  160     VAL A  161                  -35.75                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN 71001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 7 262   SG                                                     
REMARK 620 2 CYS 7 289   SG   96.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 7 1001                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-6534   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-6535   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-6536   RELATED DB: EMDB                              
REMARK 900 RELATED ID: 3JC5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3JC7   RELATED DB: PDB                                   
DBREF  3JC6 2    1   868  UNP    P29469   MCM2_YEAST       1    868             
DBREF  3JC6 3    1   971  UNP    P24279   MCM3_YEAST       1    971             
DBREF  3JC6 4    1   933  UNP    P30665   MCM4_YEAST       1    933             
DBREF  3JC6 5    1   775  UNP    P29496   MCM5_YEAST       1    775             
DBREF  3JC6 6    1  1017  UNP    P53091   MCM6_YEAST       1   1017             
DBREF  3JC6 7    1   845  UNP    P38132   MCM7_YEAST       1    845             
DBREF  3JC6 E    1   650  UNP    Q08032   CDC45_YEAST      1    650             
DBREF  3JC6 D    1   294  UNP    Q03406   SLD5_YEAST       1    294             
DBREF  3JC6 B    1   213  UNP    P40359   PSF2_YEAST       1    213             
DBREF  3JC6 A    1   208  UNP    Q12488   PSF1_YEAST       1    208             
DBREF  3JC6 C    1   194  UNP    Q12146   PSF3_YEAST       1    194             
SEQADV 3JC6 ASP E  651  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 TYR E  652  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 LYS E  653  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 ASP E  654  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 HIS E  655  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 ASP E  656  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 GLY E  657  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 ASP E  658  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 TYR E  659  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 LYS E  660  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 ASP E  661  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 HIS E  662  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 ASP E  663  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 ILE E  664  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 ASP E  665  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 TYR E  666  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 LYS E  667  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 ASP E  668  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 ASP E  669  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 ASP E  670  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 ASP E  671  UNP  Q08032              EXPRESSION TAG                 
SEQADV 3JC6 LYS E  672  UNP  Q08032              EXPRESSION TAG                 
SEQRES   1 2  868  MET SER ASP ASN ARG ARG ARG ARG ARG GLU GLU ASP ASP          
SEQRES   2 2  868  SER ASP SER GLU ASN GLU LEU PRO PRO SER SER PRO GLN          
SEQRES   3 2  868  GLN HIS PHE ARG GLY GLY MET ASN PRO VAL SER SER PRO          
SEQRES   4 2  868  ILE GLY SER PRO ASP MET ILE ASN PRO GLU GLY ASP ASP          
SEQRES   5 2  868  ASN GLU VAL ASP ASP VAL PRO ASP ILE ASP GLU VAL GLU          
SEQRES   6 2  868  GLU GLN MET ASN GLU VAL ASP LEU MET ASP ASP ASN MET          
SEQRES   7 2  868  TYR GLU ASP TYR ALA ALA ASP HIS ASN ARG ASP ARG TYR          
SEQRES   8 2  868  ASP PRO ASP GLN VAL ASP ASP ARG GLU GLN GLN GLU LEU          
SEQRES   9 2  868  SER LEU SER GLU ARG ARG ARG ILE ASP ALA GLN LEU ASN          
SEQRES  10 2  868  GLU ARG ASP ARG LEU LEU ARG ASN VAL ALA TYR ILE ASP          
SEQRES  11 2  868  ASP GLU ASP GLU GLU GLN GLU GLY ALA ALA GLN LEU ASP          
SEQRES  12 2  868  GLU MET GLY LEU PRO VAL GLN ARG ARG ARG ARG ARG ARG          
SEQRES  13 2  868  GLN TYR GLU ASP LEU GLU ASN SER ASP ASP ASP LEU LEU          
SEQRES  14 2  868  SER ASP MET ASP ILE ASP PRO LEU ARG GLU GLU LEU THR          
SEQRES  15 2  868  LEU GLU SER LEU SER ASN VAL LYS ALA ASN SER TYR SER          
SEQRES  16 2  868  GLU TRP ILE THR GLN PRO ASN VAL SER ARG THR ILE ALA          
SEQRES  17 2  868  ARG GLU LEU LYS SER PHE LEU LEU GLU TYR THR ASP GLU          
SEQRES  18 2  868  THR GLY ARG SER VAL TYR GLY ALA ARG ILE ARG THR LEU          
SEQRES  19 2  868  GLY GLU MET ASN SER GLU SER LEU GLU VAL ASN TYR ARG          
SEQRES  20 2  868  HIS LEU ALA GLU SER LYS ALA ILE LEU ALA LEU PHE LEU          
SEQRES  21 2  868  ALA LYS CYS PRO GLU GLU MET LEU LYS ILE PHE ASP LEU          
SEQRES  22 2  868  VAL ALA MET GLU ALA THR GLU LEU HIS TYR PRO ASP TYR          
SEQRES  23 2  868  ALA ARG ILE HIS SER GLU ILE HIS VAL ARG ILE SER ASP          
SEQRES  24 2  868  PHE PRO THR ILE TYR SER LEU ARG GLU LEU ARG GLU SER          
SEQRES  25 2  868  ASN LEU SER SER LEU VAL ARG VAL THR GLY VAL VAL THR          
SEQRES  26 2  868  ARG ARG THR GLY VAL PHE PRO GLN LEU LYS TYR VAL LYS          
SEQRES  27 2  868  PHE ASN CYS LEU LYS CYS GLY SER ILE LEU GLY PRO PHE          
SEQRES  28 2  868  PHE GLN ASP SER ASN GLU GLU ILE ARG ILE SER PHE CYS          
SEQRES  29 2  868  THR ASN CYS LYS SER LYS GLY PRO PHE ARG VAL ASN GLY          
SEQRES  30 2  868  GLU LYS THR VAL TYR ARG ASN TYR GLN ARG VAL THR LEU          
SEQRES  31 2  868  GLN GLU ALA PRO GLY THR VAL PRO PRO GLY ARG LEU PRO          
SEQRES  32 2  868  ARG HIS ARG GLU VAL ILE LEU LEU ALA ASP LEU VAL ASP          
SEQRES  33 2  868  VAL SER LYS PRO GLY GLU GLU VAL GLU VAL THR GLY ILE          
SEQRES  34 2  868  TYR LYS ASN ASN TYR ASP GLY ASN LEU ASN ALA LYS ASN          
SEQRES  35 2  868  GLY PHE PRO VAL PHE ALA THR ILE ILE GLU ALA ASN SER          
SEQRES  36 2  868  ILE LYS ARG ARG GLU GLY ASN THR ALA ASN GLU GLY GLU          
SEQRES  37 2  868  GLU GLY LEU ASP VAL PHE SER TRP THR GLU GLU GLU GLU          
SEQRES  38 2  868  ARG GLU PHE ARG LYS ILE SER ARG ASP ARG GLY ILE ILE          
SEQRES  39 2  868  ASP LYS ILE ILE SER SER MET ALA PRO SER ILE TYR GLY          
SEQRES  40 2  868  HIS ARG ASP ILE LYS THR ALA VAL ALA CYS SER LEU PHE          
SEQRES  41 2  868  GLY GLY VAL PRO LYS ASN VAL ASN GLY LYS HIS SER ILE          
SEQRES  42 2  868  ARG GLY ASP ILE ASN VAL LEU LEU LEU GLY ASP PRO GLY          
SEQRES  43 2  868  THR ALA LYS SER GLN ILE LEU LYS TYR VAL GLU LYS THR          
SEQRES  44 2  868  ALA HIS ARG ALA VAL PHE ALA THR GLY GLN GLY ALA SER          
SEQRES  45 2  868  ALA VAL GLY LEU THR ALA SER VAL ARG LYS ASP PRO ILE          
SEQRES  46 2  868  THR LYS GLU TRP THR LEU GLU GLY GLY ALA LEU VAL LEU          
SEQRES  47 2  868  ALA ASP LYS GLY VAL CYS LEU ILE ASP GLU PHE ASP LYS          
SEQRES  48 2  868  MET ASN ASP GLN ASP ARG THR SER ILE HIS GLU ALA MET          
SEQRES  49 2  868  GLU GLN GLN SER ILE SER ILE SER LYS ALA GLY ILE VAL          
SEQRES  50 2  868  THR THR LEU GLN ALA ARG CYS SER ILE ILE ALA ALA ALA          
SEQRES  51 2  868  ASN PRO ASN GLY GLY ARG TYR ASN SER THR LEU PRO LEU          
SEQRES  52 2  868  ALA GLN ASN VAL SER LEU THR GLU PRO ILE LEU SER ARG          
SEQRES  53 2  868  PHE ASP ILE LEU CYS VAL VAL ARG ASP LEU VAL ASP GLU          
SEQRES  54 2  868  GLU ALA ASP GLU ARG LEU ALA THR PHE VAL VAL ASP SER          
SEQRES  55 2  868  HIS VAL ARG SER HIS PRO GLU ASN ASP GLU ASP ARG GLU          
SEQRES  56 2  868  GLY GLU GLU LEU LYS ASN ASN GLY GLU SER ALA ILE GLU          
SEQRES  57 2  868  GLN GLY GLU ASP GLU ILE ASN GLU GLN LEU ASN ALA ARG          
SEQRES  58 2  868  GLN ARG ARG LEU GLN ARG GLN ARG LYS LYS GLU GLU GLU          
SEQRES  59 2  868  ILE SER PRO ILE PRO GLN GLU LEU LEU MET LYS TYR ILE          
SEQRES  60 2  868  HIS TYR ALA ARG THR LYS ILE TYR PRO LYS LEU HIS GLN          
SEQRES  61 2  868  MET ASP MET ASP LYS VAL SER ARG VAL TYR ALA ASP LEU          
SEQRES  62 2  868  ARG ARG GLU SER ILE SER THR GLY SER PHE PRO ILE THR          
SEQRES  63 2  868  VAL ARG HIS LEU GLU SER ILE LEU ARG ILE ALA GLU SER          
SEQRES  64 2  868  PHE ALA LYS MET ARG LEU SER GLU PHE VAL SER SER TYR          
SEQRES  65 2  868  ASP LEU ASP ARG ALA ILE LYS VAL VAL VAL ASP SER PHE          
SEQRES  66 2  868  VAL ASP ALA GLN LYS VAL SER VAL ARG ARG GLN LEU ARG          
SEQRES  67 2  868  ARG SER PHE ALA ILE TYR THR LEU GLY HIS                      
SEQRES   1 3  971  MET GLU GLY SER THR GLY PHE ASP GLY ASP ALA THR THR          
SEQRES   2 3  971  PHE PHE ALA PRO ASP ALA VAL PHE GLY ASP ARG VAL ARG          
SEQRES   3 3  971  ARG PHE GLN GLU PHE LEU ASP THR PHE THR SER TYR ARG          
SEQRES   4 3  971  ASP SER VAL ARG SER ILE GLN VAL TYR ASN SER ASN ASN          
SEQRES   5 3  971  ALA ALA ASN TYR ASN ASP ASP GLN ASP ASP ALA ASP GLU          
SEQRES   6 3  971  ARG ASP LEU LEU GLY ASP ASP ASP GLY ASP ASP LEU GLU          
SEQRES   7 3  971  LYS GLU LYS LYS ALA ALA SER SER THR SER LEU ASN ILE          
SEQRES   8 3  971  LEU PRO HIS ARG ILE ILE ILE SER LEU ASP ASP LEU ARG          
SEQRES   9 3  971  GLU PHE ASP ARG SER PHE TRP SER GLY ILE LEU VAL GLU          
SEQRES  10 3  971  PRO ALA TYR PHE ILE PRO PRO ALA GLU LYS ALA LEU THR          
SEQRES  11 3  971  ASP LEU ALA ASP SER MET ASP ASP VAL PRO HIS PRO ASN          
SEQRES  12 3  971  ALA SER ALA VAL SER SER ARG HIS PRO TRP LYS LEU SER          
SEQRES  13 3  971  PHE LYS GLY SER PHE GLY ALA HIS ALA LEU SER PRO ARG          
SEQRES  14 3  971  THR LEU THR ALA GLN HIS LEU ASN LYS LEU VAL SER VAL          
SEQRES  15 3  971  GLU GLY ILE VAL THR LYS THR SER LEU VAL ARG PRO LYS          
SEQRES  16 3  971  LEU ILE ARG SER VAL HIS TYR ALA ALA LYS THR GLY ARG          
SEQRES  17 3  971  PHE HIS TYR ARG ASP TYR THR ASP ALA THR THR THR LEU          
SEQRES  18 3  971  THR THR ARG ILE PRO THR PRO ALA ILE TYR PRO THR GLU          
SEQRES  19 3  971  ASP THR GLU GLY ASN LYS LEU THR THR GLU TYR GLY TYR          
SEQRES  20 3  971  SER THR PHE ILE ASP HIS GLN ARG ILE THR VAL GLN GLU          
SEQRES  21 3  971  MET PRO GLU MET ALA PRO ALA GLY GLN LEU PRO ARG SER          
SEQRES  22 3  971  ILE ASP VAL ILE LEU ASP ASP ASP LEU VAL ASP LYS THR          
SEQRES  23 3  971  LYS PRO GLY ASP ARG VAL ASN VAL VAL GLY VAL PHE LYS          
SEQRES  24 3  971  SER LEU GLY ALA GLY GLY MET ASN GLN SER ASN SER ASN          
SEQRES  25 3  971  THR LEU ILE GLY PHE LYS THR LEU ILE LEU GLY ASN THR          
SEQRES  26 3  971  VAL TYR PRO LEU HIS ALA ARG SER THR GLY VAL ALA ALA          
SEQRES  27 3  971  ARG GLN MET LEU THR ASP PHE ASP ILE ARG ASN ILE ASN          
SEQRES  28 3  971  LYS LEU SER LYS LYS LYS ASP ILE PHE ASP ILE LEU SER          
SEQRES  29 3  971  GLN SER LEU ALA PRO SER ILE TYR GLY HIS ASP HIS ILE          
SEQRES  30 3  971  LYS LYS ALA ILE LEU LEU MET LEU MET GLY GLY VAL GLU          
SEQRES  31 3  971  LYS ASN LEU GLU ASN GLY SER HIS LEU ARG GLY ASP ILE          
SEQRES  32 3  971  ASN ILE LEU MET VAL GLY ASP PRO SER THR ALA LYS SER          
SEQRES  33 3  971  GLN LEU LEU ARG PHE VAL LEU ASN THR ALA SER LEU ALA          
SEQRES  34 3  971  ILE ALA THR THR GLY ARG GLY SER SER GLY VAL GLY LEU          
SEQRES  35 3  971  THR ALA ALA VAL THR THR ASP ARG GLU THR GLY GLU ARG          
SEQRES  36 3  971  ARG LEU GLU ALA GLY ALA MET VAL LEU ALA ASP ARG GLY          
SEQRES  37 3  971  VAL VAL CYS ILE ASP GLU PHE ASP LYS MET THR ASP VAL          
SEQRES  38 3  971  ASP ARG VAL ALA ILE HIS GLU VAL MET GLU GLN GLN THR          
SEQRES  39 3  971  VAL THR ILE ALA LYS ALA GLY ILE HIS THR THR LEU ASN          
SEQRES  40 3  971  ALA ARG CYS SER VAL ILE ALA ALA ALA ASN PRO VAL PHE          
SEQRES  41 3  971  GLY GLN TYR ASP VAL ASN ARG ASP PRO HIS GLN ASN ILE          
SEQRES  42 3  971  ALA LEU PRO ASP SER LEU LEU SER ARG PHE ASP LEU LEU          
SEQRES  43 3  971  PHE VAL VAL THR ASP ASP ILE ASN GLU ILE ARG ASP ARG          
SEQRES  44 3  971  SER ILE SER GLU HIS VAL LEU ARG THR HIS ARG TYR LEU          
SEQRES  45 3  971  PRO PRO GLY TYR LEU GLU GLY GLU PRO VAL ARG GLU ARG          
SEQRES  46 3  971  LEU ASN LEU SER LEU ALA VAL GLY GLU ASP ALA ASP ILE          
SEQRES  47 3  971  ASN PRO GLU GLU HIS SER ASN SER GLY ALA GLY VAL GLU          
SEQRES  48 3  971  ASN GLU GLY GLU ASP ASP GLU ASP HIS VAL PHE GLU LYS          
SEQRES  49 3  971  PHE ASN PRO LEU LEU GLN ALA GLY ALA LYS LEU ALA LYS          
SEQRES  50 3  971  ASN LYS GLY ASN TYR ASN GLY THR GLU ILE PRO LYS LEU          
SEQRES  51 3  971  VAL THR ILE PRO PHE LEU ARG LYS TYR VAL GLN TYR ALA          
SEQRES  52 3  971  LYS GLU ARG VAL ILE PRO GLN LEU THR GLN GLU ALA ILE          
SEQRES  53 3  971  ASN VAL ILE VAL LYS ASN TYR THR ASP LEU ARG ASN ASP          
SEQRES  54 3  971  ASP ASN THR LYS LYS SER PRO ILE THR ALA ARG THR LEU          
SEQRES  55 3  971  GLU THR LEU ILE ARG LEU ALA THR ALA HIS ALA LYS VAL          
SEQRES  56 3  971  ARG LEU SER LYS THR VAL ASN LYS VAL ASP ALA LYS VAL          
SEQRES  57 3  971  ALA ALA ASN LEU LEU ARG PHE ALA LEU LEU GLY GLU ASP          
SEQRES  58 3  971  ILE GLY ASN ASP ILE ASP GLU GLU GLU SER GLU TYR GLU          
SEQRES  59 3  971  GLU ALA LEU SER LYS ARG SER PRO GLN LYS SER PRO LYS          
SEQRES  60 3  971  LYS ARG GLN ARG VAL ARG GLN PRO ALA SER ASN SER GLY          
SEQRES  61 3  971  SER PRO ILE LYS SER THR PRO ARG ARG SER THR ALA SER          
SEQRES  62 3  971  SER VAL ASN ALA THR PRO SER SER ALA ARG ARG ILE LEU          
SEQRES  63 3  971  ARG PHE GLN ASP ASP GLU GLN ASN ALA GLY GLU ASP ASP          
SEQRES  64 3  971  ASN ASP ILE MET SER PRO LEU PRO ALA ASP GLU GLU ALA          
SEQRES  65 3  971  GLU LEU GLN ARG ARG LEU GLN LEU GLY LEU ARG VAL SER          
SEQRES  66 3  971  PRO ARG ARG ARG GLU HIS LEU HIS ALA PRO GLU GLU GLY          
SEQRES  67 3  971  SER SER GLY PRO LEU THR GLU VAL GLY THR PRO ARG LEU          
SEQRES  68 3  971  PRO ASN VAL SER SER ALA GLY GLN ASP ASP GLU GLN GLN          
SEQRES  69 3  971  GLN SER VAL ILE SER PHE ASP ASN VAL GLU PRO GLY THR          
SEQRES  70 3  971  ILE SER THR GLY ARG LEU SER LEU ILE SER GLY ILE ILE          
SEQRES  71 3  971  ALA ARG LEU MET GLN THR GLU ILE PHE GLU GLU GLU SER          
SEQRES  72 3  971  TYR PRO VAL ALA SER LEU PHE GLU ARG ILE ASN GLU GLU          
SEQRES  73 3  971  LEU PRO GLU GLU GLU LYS PHE SER ALA GLN GLU TYR LEU          
SEQRES  74 3  971  ALA GLY LEU LYS ILE MET SER ASP ARG ASN ASN LEU MET          
SEQRES  75 3  971  VAL ALA ASP ASP LYS VAL TRP ARG VAL                          
SEQRES   1 4  933  MET SER GLN GLN SER SER SER PRO THR LYS GLU ASP ASN          
SEQRES   2 4  933  ASN SER SER SER PRO VAL VAL PRO ASN PRO ASP SER VAL          
SEQRES   3 4  933  PRO PRO GLN LEU SER SER PRO ALA LEU PHE TYR SER SER          
SEQRES   4 4  933  SER SER SER GLN GLY ASP ILE TYR GLY ARG ASN ASN SER          
SEQRES   5 4  933  GLN ASN LEU SER GLN GLY GLU GLY ASN ILE ARG ALA ALA          
SEQRES   6 4  933  ILE GLY SER SER PRO LEU ASN PHE PRO SER SER SER GLN          
SEQRES   7 4  933  ARG GLN ASN SER ASP VAL PHE GLN SER GLN GLY ARG GLN          
SEQRES   8 4  933  GLY ARG ILE ARG SER SER ALA SER ALA SER GLY ARG SER          
SEQRES   9 4  933  ARG TYR HIS SER ASP LEU ARG SER ASP ARG ALA LEU PRO          
SEQRES  10 4  933  THR SER SER SER SER LEU GLY ARG ASN GLY GLN ASN ARG          
SEQRES  11 4  933  VAL HIS MET ARG ARG ASN ASP ILE HIS THR SER ASP LEU          
SEQRES  12 4  933  SER SER PRO ARG ARG ILE VAL ASP PHE ASP THR ARG SER          
SEQRES  13 4  933  GLY VAL ASN THR LEU ASP THR SER SER SER SER ALA PRO          
SEQRES  14 4  933  PRO SER GLU ALA SER GLU PRO LEU ARG ILE ILE TRP GLY          
SEQRES  15 4  933  THR ASN VAL SER ILE GLN GLU CYS THR THR ASN PHE ARG          
SEQRES  16 4  933  ASN PHE LEU MET SER PHE LYS TYR LYS PHE ARG LYS ILE          
SEQRES  17 4  933  LEU ASP GLU ARG GLU GLU PHE ILE ASN ASN THR THR ASP          
SEQRES  18 4  933  GLU GLU LEU TYR TYR ILE LYS GLN LEU ASN GLU MET ARG          
SEQRES  19 4  933  GLU LEU GLY THR SER ASN LEU ASN LEU ASP ALA ARG ASN          
SEQRES  20 4  933  LEU LEU ALA TYR LYS GLN THR GLU ASP LEU TYR HIS GLN          
SEQRES  21 4  933  LEU LEU ASN TYR PRO GLN GLU VAL ILE SER ILE MET ASP          
SEQRES  22 4  933  GLN THR ILE LYS ASP CYS MET VAL SER LEU ILE VAL ASP          
SEQRES  23 4  933  ASN ASN LEU ASP TYR ASP LEU ASP GLU ILE GLU THR LYS          
SEQRES  24 4  933  PHE TYR LYS VAL ARG PRO TYR ASN VAL GLY SER CYS LYS          
SEQRES  25 4  933  GLY MET ARG GLU LEU ASN PRO ASN ASP ILE ASP LYS LEU          
SEQRES  26 4  933  ILE ASN LEU LYS GLY LEU VAL LEU ARG SER THR PRO VAL          
SEQRES  27 4  933  ILE PRO ASP MET LYS VAL ALA PHE PHE LYS CYS ASN VAL          
SEQRES  28 4  933  CYS ASP HIS THR MET ALA VAL GLU ILE ASP ARG GLY VAL          
SEQRES  29 4  933  ILE GLN GLU PRO ALA ARG CYS GLU ARG ILE ASP CYS ASN          
SEQRES  30 4  933  GLU PRO ASN SER MET SER LEU ILE HIS ASN ARG CYS SER          
SEQRES  31 4  933  PHE ALA ASP LYS GLN VAL ILE LYS LEU GLN GLU THR PRO          
SEQRES  32 4  933  ASP PHE VAL PRO ASP GLY GLN THR PRO HIS SER ILE SER          
SEQRES  33 4  933  LEU CYS VAL TYR ASP GLU LEU VAL ASP SER CYS ARG ALA          
SEQRES  34 4  933  GLY ASP ARG ILE GLU VAL THR GLY THR PHE ARG SER ILE          
SEQRES  35 4  933  PRO ILE ARG ALA ASN SER ARG GLN ARG VAL LEU LYS SER          
SEQRES  36 4  933  LEU TYR LYS THR TYR VAL ASP VAL VAL HIS VAL LYS LYS          
SEQRES  37 4  933  VAL SER ASP LYS ARG LEU ASP VAL ASP THR SER THR ILE          
SEQRES  38 4  933  GLU GLN GLU LEU MET GLN ASN LYS VAL ASP HIS ASN GLU          
SEQRES  39 4  933  VAL GLU GLU VAL ARG GLN ILE THR ASP GLN ASP LEU ALA          
SEQRES  40 4  933  LYS ILE ARG GLU VAL ALA ALA ARG GLU ASP LEU TYR SER          
SEQRES  41 4  933  LEU LEU ALA ARG SER ILE ALA PRO SER ILE TYR GLU LEU          
SEQRES  42 4  933  GLU ASP VAL LYS LYS GLY ILE LEU LEU GLN LEU PHE GLY          
SEQRES  43 4  933  GLY THR ASN LYS THR PHE THR LYS GLY GLY ARG TYR ARG          
SEQRES  44 4  933  GLY ASP ILE ASN ILE LEU LEU CYS GLY ASP PRO SER THR          
SEQRES  45 4  933  SER LYS SER GLN ILE LEU GLN TYR VAL HIS LYS ILE THR          
SEQRES  46 4  933  PRO ARG GLY VAL TYR THR SER GLY LYS GLY SER SER ALA          
SEQRES  47 4  933  VAL GLY LEU THR ALA TYR ILE THR ARG ASP VAL ASP THR          
SEQRES  48 4  933  LYS GLN LEU VAL LEU GLU SER GLY ALA LEU VAL LEU SER          
SEQRES  49 4  933  ASP GLY GLY VAL CYS CYS ILE ASP GLU PHE ASP LYS MET          
SEQRES  50 4  933  SER ASP SER THR ARG SER VAL LEU HIS GLU VAL MET GLU          
SEQRES  51 4  933  GLN GLN THR ILE SER ILE ALA LYS ALA GLY ILE ILE THR          
SEQRES  52 4  933  THR LEU ASN ALA ARG SER SER ILE LEU ALA SER ALA ASN          
SEQRES  53 4  933  PRO ILE GLY SER ARG TYR ASN PRO ASN LEU PRO VAL THR          
SEQRES  54 4  933  GLU ASN ILE ASP LEU PRO PRO PRO LEU LEU SER ARG PHE          
SEQRES  55 4  933  ASP LEU VAL TYR LEU VAL LEU ASP LYS VAL ASP GLU LYS          
SEQRES  56 4  933  ASN ASP ARG GLU LEU ALA LYS HIS LEU THR ASN LEU TYR          
SEQRES  57 4  933  LEU GLU ASP LYS PRO GLU HIS ILE SER GLN ASP ASP VAL          
SEQRES  58 4  933  LEU PRO VAL GLU PHE LEU THR MET TYR ILE SER TYR ALA          
SEQRES  59 4  933  LYS GLU HIS ILE HIS PRO ILE ILE THR GLU ALA ALA LYS          
SEQRES  60 4  933  THR GLU LEU VAL ARG ALA TYR VAL GLY MET ARG LYS MET          
SEQRES  61 4  933  GLY ASP ASP SER ARG SER ASP GLU LYS ARG ILE THR ALA          
SEQRES  62 4  933  THR THR ARG GLN LEU GLU SER MET ILE ARG LEU ALA GLU          
SEQRES  63 4  933  ALA HIS ALA LYS MET LYS LEU LYS ASN VAL VAL GLU LEU          
SEQRES  64 4  933  GLU ASP VAL GLN GLU ALA VAL ARG LEU ILE ARG SER ALA          
SEQRES  65 4  933  ILE LYS ASP TYR ALA THR ASP PRO LYS THR GLY LYS ILE          
SEQRES  66 4  933  ASP MET ASN LEU VAL GLN THR GLY LYS SER VAL ILE GLN          
SEQRES  67 4  933  ARG LYS LEU GLN GLU ASP LEU SER ARG GLU ILE MET ASN          
SEQRES  68 4  933  VAL LEU LYS ASP GLN ALA SER ASP SER MET SER PHE ASN          
SEQRES  69 4  933  GLU LEU ILE LYS GLN ILE ASN GLU HIS SER GLN ASP ARG          
SEQRES  70 4  933  VAL GLU SER SER ASP ILE GLN GLU ALA LEU SER ARG LEU          
SEQRES  71 4  933  GLN GLN GLU ASP LYS VAL ILE VAL LEU GLY GLU GLY VAL          
SEQRES  72 4  933  ARG ARG SER VAL ARG LEU ASN ASN ARG VAL                      
SEQRES   1 5  775  MET SER PHE ASP ARG PRO GLU ILE TYR SER ALA PRO VAL          
SEQRES   2 5  775  LEU GLN GLY GLU SER PRO ASN ASP ASP ASP ASN THR GLU          
SEQRES   3 5  775  ILE ILE LYS SER PHE LYS ASN PHE ILE LEU GLU PHE ARG          
SEQRES   4 5  775  LEU ASP SER GLN PHE ILE TYR ARG ASP GLN LEU ARG ASN          
SEQRES   5 5  775  ASN ILE LEU VAL LYS ASN TYR SER LEU THR VAL ASN MET          
SEQRES   6 5  775  GLU HIS LEU ILE GLY TYR ASN GLU ASP ILE TYR LYS LYS          
SEQRES   7 5  775  LEU SER ASP GLU PRO SER ASP ILE ILE PRO LEU PHE GLU          
SEQRES   8 5  775  THR ALA ILE THR GLN VAL ALA LYS ARG ILE SER ILE LEU          
SEQRES   9 5  775  SER ARG ALA GLN SER ALA ASN ASN ASN ASP LYS ASP PRO          
SEQRES  10 5  775  GLU ASN THR SER MET ASP THR ASP SER LEU LEU LEU ASN          
SEQRES  11 5  775  SER LEU PRO THR PHE GLN LEU ILE LEU ASN SER ASN ALA          
SEQRES  12 5  775  ASN GLN ILE PRO LEU ARG ASP LEU ASP SER GLU HIS VAL          
SEQRES  13 5  775  SER LYS ILE VAL ARG LEU SER GLY ILE ILE ILE SER THR          
SEQRES  14 5  775  SER VAL LEU SER SER ARG ALA THR TYR LEU SER ILE MET          
SEQRES  15 5  775  CYS ARG ASN CYS ARG HIS THR THR SER ILE THR ILE ASN          
SEQRES  16 5  775  ASN PHE ASN SER ILE THR GLY ASN THR VAL SER LEU PRO          
SEQRES  17 5  775  ARG SER CYS LEU SER THR ILE GLU SER GLU SER SER MET          
SEQRES  18 5  775  ALA ASN GLU SER ASN ILE GLY ASP GLU SER THR LYS LYS          
SEQRES  19 5  775  ASN CYS GLY PRO ASP PRO TYR ILE ILE ILE HIS GLU SER          
SEQRES  20 5  775  SER LYS PHE ILE ASP GLN GLN PHE LEU LYS LEU GLN GLU          
SEQRES  21 5  775  ILE PRO GLU LEU VAL PRO VAL GLY GLU MET PRO ARG ASN          
SEQRES  22 5  775  LEU THR MET THR CYS ASP ARG TYR LEU THR ASN LYS VAL          
SEQRES  23 5  775  ILE PRO GLY THR ARG VAL THR ILE VAL GLY ILE TYR SER          
SEQRES  24 5  775  ILE TYR ASN SER LYS ASN GLY ALA GLY SER GLY ARG SER          
SEQRES  25 5  775  GLY GLY GLY ASN GLY GLY SER GLY VAL ALA ILE ARG THR          
SEQRES  26 5  775  PRO TYR ILE LYS ILE LEU GLY ILE GLN SER ASP VAL GLU          
SEQRES  27 5  775  THR SER SER ILE TRP ASN SER VAL THR MET PHE THR GLU          
SEQRES  28 5  775  GLU GLU GLU GLU GLU PHE LEU GLN LEU SER ARG ASN PRO          
SEQRES  29 5  775  LYS LEU TYR GLU ILE LEU THR ASN SER ILE ALA PRO SER          
SEQRES  30 5  775  ILE PHE GLY ASN GLU ASP ILE LYS LYS ALA ILE VAL CYS          
SEQRES  31 5  775  LEU LEU MET GLY GLY SER LYS LYS ILE LEU PRO ASP GLY          
SEQRES  32 5  775  MET ARG LEU ARG GLY ASP ILE ASN VAL LEU LEU LEU GLY          
SEQRES  33 5  775  ASP PRO GLY THR ALA LYS SER GLN LEU LEU LYS PHE VAL          
SEQRES  34 5  775  GLU LYS VAL SER PRO ILE ALA VAL TYR THR SER GLY LYS          
SEQRES  35 5  775  GLY SER SER ALA ALA GLY LEU THR ALA SER VAL GLN ARG          
SEQRES  36 5  775  ASP PRO MET THR ARG GLU PHE TYR LEU GLU GLY GLY ALA          
SEQRES  37 5  775  MET VAL LEU ALA ASP GLY GLY VAL VAL CYS ILE ASP GLU          
SEQRES  38 5  775  PHE ASP LYS MET ARG ASP GLU ASP ARG VAL ALA ILE HIS          
SEQRES  39 5  775  GLU ALA MET GLU GLN GLN THR ILE SER ILE ALA LYS ALA          
SEQRES  40 5  775  GLY ILE THR THR VAL LEU ASN SER ARG THR SER VAL LEU          
SEQRES  41 5  775  ALA ALA ALA ASN PRO ILE TYR GLY ARG TYR ASP ASP LEU          
SEQRES  42 5  775  LYS SER PRO GLY ASP ASN ILE ASP PHE GLN THR THR ILE          
SEQRES  43 5  775  LEU SER ARG PHE ASP MET ILE PHE ILE VAL LYS ASP ASP          
SEQRES  44 5  775  HIS ASN GLU GLU ARG ASP ILE SER ILE ALA ASN HIS VAL          
SEQRES  45 5  775  ILE ASN ILE HIS THR GLY ASN ALA ASN ALA MET GLN ASN          
SEQRES  46 5  775  GLN GLN GLU GLU ASN GLY SER GLU ILE SER ILE GLU LYS          
SEQRES  47 5  775  MET LYS ARG TYR ILE THR TYR CYS ARG LEU LYS CYS ALA          
SEQRES  48 5  775  PRO ARG LEU SER PRO GLN ALA ALA GLU LYS LEU SER SER          
SEQRES  49 5  775  ASN PHE VAL THR ILE ARG LYS GLN LEU LEU ILE ASN GLU          
SEQRES  50 5  775  LEU GLU SER THR GLU ARG SER SER ILE PRO ILE THR ILE          
SEQRES  51 5  775  ARG GLN LEU GLU ALA ILE ILE ARG ILE THR GLU SER LEU          
SEQRES  52 5  775  ALA LYS LEU GLU LEU SER PRO ILE ALA GLN GLU ARG HIS          
SEQRES  53 5  775  VAL ASP GLU ALA ILE ARG LEU PHE GLN ALA SER THR MET          
SEQRES  54 5  775  ASP ALA ALA SER GLN ASP PRO ILE GLY GLY LEU ASN GLN          
SEQRES  55 5  775  ALA SER GLY THR SER LEU SER GLU ILE ARG ARG PHE GLU          
SEQRES  56 5  775  GLN GLU LEU LYS ARG ARG LEU PRO ILE GLY TRP SER THR          
SEQRES  57 5  775  SER TYR GLN THR LEU ARG ARG GLU PHE VAL ASP THR HIS          
SEQRES  58 5  775  ARG PHE SER GLN LEU ALA LEU ASP LYS ALA LEU TYR ALA          
SEQRES  59 5  775  LEU GLU LYS HIS GLU THR ILE GLN LEU ARG HIS GLN GLY          
SEQRES  60 5  775  GLN ASN ILE TYR ARG SER GLY VAL                              
SEQRES   1 6 1017  MET SER SER PRO PHE PRO ALA ASP THR PRO SER SER ASN          
SEQRES   2 6 1017  ARG PRO SER ASN SER SER PRO PRO PRO SER SER ILE GLY          
SEQRES   3 6 1017  ALA GLY PHE GLY SER SER SER GLY LEU ASP SER GLN ILE          
SEQRES   4 6 1017  GLY SER ARG LEU HIS PHE PRO SER SER SER GLN PRO HIS          
SEQRES   5 6 1017  VAL SER ASN SER GLN THR GLY PRO PHE VAL ASN ASP SER          
SEQRES   6 6 1017  THR GLN PHE SER SER GLN ARG LEU GLN THR ASP GLY SER          
SEQRES   7 6 1017  ALA THR ASN ASP MET GLU GLY ASN GLU PRO ALA ARG SER          
SEQRES   8 6 1017  PHE LYS SER ARG ALA LEU ASN HIS VAL LYS LYS VAL ASP          
SEQRES   9 6 1017  ASP VAL THR GLY GLU LYS VAL ARG GLU ALA PHE GLU GLN          
SEQRES  10 6 1017  PHE LEU GLU ASP PHE SER VAL GLN SER THR ASP THR GLY          
SEQRES  11 6 1017  GLU VAL GLU LYS VAL TYR ARG ALA GLN ILE GLU PHE MET          
SEQRES  12 6 1017  LYS ILE TYR ASP LEU ASN THR ILE TYR ILE ASP TYR GLN          
SEQRES  13 6 1017  HIS LEU SER MET ARG GLU ASN GLY ALA LEU ALA MET ALA          
SEQRES  14 6 1017  ILE SER GLU GLN TYR TYR ARG PHE LEU PRO PHE LEU GLN          
SEQRES  15 6 1017  LYS GLY LEU ARG ARG VAL VAL ARG LYS TYR ALA PRO GLU          
SEQRES  16 6 1017  LEU LEU ASN THR SER ASP SER LEU LYS ARG SER GLU GLY          
SEQRES  17 6 1017  ASP GLU GLY GLN ALA ASP GLU ASP GLU GLN GLN ASP ASP          
SEQRES  18 6 1017  ASP MET ASN GLY SER SER LEU PRO ARG ASP SER GLY SER          
SEQRES  19 6 1017  SER ALA ALA PRO GLY ASN GLY THR SER ALA MET ALA THR          
SEQRES  20 6 1017  ARG SER ILE THR THR SER THR SER PRO GLU GLN THR GLU          
SEQRES  21 6 1017  ARG VAL PHE GLN ILE SER PHE PHE ASN LEU PRO THR VAL          
SEQRES  22 6 1017  HIS ARG ILE ARG ASP ILE ARG SER GLU LYS ILE GLY SER          
SEQRES  23 6 1017  LEU LEU SER ILE SER GLY THR VAL THR ARG THR SER GLU          
SEQRES  24 6 1017  VAL ARG PRO GLU LEU TYR LYS ALA SER PHE THR CYS ASP          
SEQRES  25 6 1017  MET CYS ARG ALA ILE VAL ASP ASN VAL GLU GLN SER PHE          
SEQRES  26 6 1017  LYS TYR THR GLU PRO THR PHE CYS PRO ASN PRO SER CYS          
SEQRES  27 6 1017  GLU ASN ARG ALA PHE TRP THR LEU ASN VAL THR ARG SER          
SEQRES  28 6 1017  ARG PHE LEU ASP TRP GLN LYS VAL ARG ILE GLN GLU ASN          
SEQRES  29 6 1017  ALA ASN GLU ILE PRO THR GLY SER MET PRO ARG THR LEU          
SEQRES  30 6 1017  ASP VAL ILE LEU ARG GLY ASP SER VAL GLU ARG ALA LYS          
SEQRES  31 6 1017  PRO GLY ASP ARG CYS LYS PHE THR GLY VAL GLU ILE VAL          
SEQRES  32 6 1017  VAL PRO ASP VAL THR GLN LEU GLY LEU PRO GLY VAL LYS          
SEQRES  33 6 1017  PRO SER SER THR LEU ASP THR ARG GLY ILE SER LYS THR          
SEQRES  34 6 1017  THR GLU GLY LEU ASN SER GLY VAL THR GLY LEU ARG SER          
SEQRES  35 6 1017  LEU GLY VAL ARG ASP LEU THR TYR LYS ILE SER PHE LEU          
SEQRES  36 6 1017  ALA CYS HIS VAL ILE SER ILE GLY SER ASN ILE GLY ALA          
SEQRES  37 6 1017  SER SER PRO ASP ALA ASN SER ASN ASN ARG GLU THR GLU          
SEQRES  38 6 1017  LEU GLN MET ALA ALA ASN LEU GLN ALA ASN ASN VAL TYR          
SEQRES  39 6 1017  GLN ASP ASN GLU ARG ASP GLN GLU VAL PHE LEU ASN SER          
SEQRES  40 6 1017  LEU SER SER ASP GLU ILE ASN GLU LEU LYS GLU MET VAL          
SEQRES  41 6 1017  LYS ASP GLU HIS ILE TYR ASP LYS LEU VAL ARG SER ILE          
SEQRES  42 6 1017  ALA PRO ALA VAL PHE GLY HIS GLU ALA VAL LYS LYS GLY          
SEQRES  43 6 1017  ILE LEU LEU GLN MET LEU GLY GLY VAL HIS LYS SER THR          
SEQRES  44 6 1017  VAL GLU GLY ILE LYS LEU ARG GLY ASP ILE ASN ILE CYS          
SEQRES  45 6 1017  VAL VAL GLY ASP PRO SER THR SER LYS SER GLN PHE LEU          
SEQRES  46 6 1017  LYS TYR VAL VAL GLY PHE ALA PRO ARG SER VAL TYR THR          
SEQRES  47 6 1017  SER GLY LYS ALA SER SER ALA ALA GLY LEU THR ALA ALA          
SEQRES  48 6 1017  VAL VAL ARG ASP GLU GLU GLY GLY ASP TYR THR ILE GLU          
SEQRES  49 6 1017  ALA GLY ALA LEU MET LEU ALA ASP ASN GLY ILE CYS CYS          
SEQRES  50 6 1017  ILE ASP GLU PHE ASP LYS MET ASP ILE SER ASP GLN VAL          
SEQRES  51 6 1017  ALA ILE HIS GLU ALA MET GLU GLN GLN THR ILE SER ILE          
SEQRES  52 6 1017  ALA LYS ALA GLY ILE HIS ALA THR LEU ASN ALA ARG THR          
SEQRES  53 6 1017  SER ILE LEU ALA ALA ALA ASN PRO VAL GLY GLY ARG TYR          
SEQRES  54 6 1017  ASN ARG LYS LEU SER LEU ARG GLY ASN LEU ASN MET THR          
SEQRES  55 6 1017  ALA PRO ILE MET SER ARG PHE ASP LEU PHE PHE VAL ILE          
SEQRES  56 6 1017  LEU ASP ASP CYS ASN GLU LYS ILE ASP THR GLU LEU ALA          
SEQRES  57 6 1017  SER HIS ILE VAL ASP LEU HIS MET LYS ARG ASP GLU ALA          
SEQRES  58 6 1017  ILE GLU PRO PRO PHE SER ALA GLU GLN LEU ARG ARG TYR          
SEQRES  59 6 1017  ILE LYS TYR ALA ARG THR PHE LYS PRO ILE LEU THR LYS          
SEQRES  60 6 1017  GLU ALA ARG SER TYR LEU VAL GLU LYS TYR LYS GLU LEU          
SEQRES  61 6 1017  ARG LYS ASP ASP ALA GLN GLY PHE SER ARG SER SER TYR          
SEQRES  62 6 1017  ARG ILE THR VAL ARG GLN LEU GLU SER MET ILE ARG LEU          
SEQRES  63 6 1017  SER GLU ALA ILE ALA ARG ALA ASN CYS VAL ASP GLU ILE          
SEQRES  64 6 1017  THR PRO SER PHE ILE ALA GLU ALA TYR ASP LEU LEU ARG          
SEQRES  65 6 1017  GLN SER ILE ILE ARG VAL ASP VAL ASP ASP VAL GLU MET          
SEQRES  66 6 1017  ASP GLU GLU PHE ASP ASN ILE GLU SER GLN SER HIS ALA          
SEQRES  67 6 1017  ALA SER GLY ASN ASN ASP ASP ASN ASP ASP GLY THR GLY          
SEQRES  68 6 1017  SER GLY VAL ILE THR SER GLU PRO PRO ALA ASP ILE GLU          
SEQRES  69 6 1017  GLU GLY GLN SER GLU ALA THR ALA ARG PRO GLY THR SER          
SEQRES  70 6 1017  GLU LYS LYS LYS THR THR VAL THR TYR ASP LYS TYR VAL          
SEQRES  71 6 1017  SER MET MET ASN MET ILE VAL ARG LYS ILE ALA GLU VAL          
SEQRES  72 6 1017  ASP ARG GLU GLY ALA GLU GLU LEU THR ALA VAL ASP ILE          
SEQRES  73 6 1017  VAL ASP TRP TYR LEU LEU GLN LYS GLU ASN ASP LEU GLY          
SEQRES  74 6 1017  SER LEU ALA GLU TYR TRP GLU GLU ARG ARG LEU ALA PHE          
SEQRES  75 6 1017  LYS VAL ILE LYS ARG LEU VAL LYS ASP ARG ILE LEU MET          
SEQRES  76 6 1017  GLU ILE HIS GLY THR ARG HIS ASN LEU ARG ASP LEU GLU          
SEQRES  77 6 1017  ASN GLU GLU ASN GLU ASN ASN LYS THR VAL TYR VAL ILE          
SEQRES  78 6 1017  HIS PRO ASN CYS GLU VAL LEU ASP GLN LEU GLU PRO GLN          
SEQRES  79 6 1017  ASP SER SER                                                  
SEQRES   1 7  845  MET SER ALA ALA LEU PRO SER ILE GLN LEU PRO VAL ASP          
SEQRES   2 7  845  TYR ASN ASN LEU PHE ASN GLU ILE THR ASP PHE LEU VAL          
SEQRES   3 7  845  THR PHE LYS GLN ASP THR LEU SER SER ASP ALA THR ARG          
SEQRES   4 7  845  ASN GLU ASN GLU ASP GLU ASN LEU ASP ALA GLU ASN ILE          
SEQRES   5 7  845  GLU GLN HIS LEU LEU GLU LYS GLY PRO LYS TYR MET ALA          
SEQRES   6 7  845  MET LEU GLN LYS VAL ALA ASN ARG GLU LEU ASN SER VAL          
SEQRES   7 7  845  ILE ILE ASP LEU ASP ASP ILE LEU GLN TYR GLN ASN GLU          
SEQRES   8 7  845  LYS PHE LEU GLN GLY THR GLN ALA ASP ASP LEU VAL SER          
SEQRES   9 7  845  ALA ILE GLN GLN ASN ALA ASN HIS PHE THR GLU LEU PHE          
SEQRES  10 7  845  CYS ARG ALA ILE ASP ASN ASN MET PRO LEU PRO THR LYS          
SEQRES  11 7  845  GLU ILE ASP TYR LYS ASP ASP VAL LEU ASP VAL ILE LEU          
SEQRES  12 7  845  ASN GLN ARG ARG LEU ARG ASN GLU ARG MET LEU SER ASP          
SEQRES  13 7  845  ARG THR ASN GLU ILE ARG SER GLU ASN LEU MET ASP THR          
SEQRES  14 7  845  THR MET ASP PRO PRO SER SER MET ASN ASP ALA LEU ARG          
SEQRES  15 7  845  GLU VAL VAL GLU ASP GLU THR GLU LEU PHE PRO PRO ASN          
SEQRES  16 7  845  LEU THR ARG ARG TYR PHE LEU TYR PHE LYS PRO LEU SER          
SEQRES  17 7  845  GLN ASN CYS ALA ARG ARG TYR ARG LYS LYS ALA ILE SER          
SEQRES  18 7  845  SER LYS PRO LEU SER VAL ARG GLN ILE LYS GLY ASP PHE          
SEQRES  19 7  845  LEU GLY GLN LEU ILE THR VAL ARG GLY ILE ILE THR ARG          
SEQRES  20 7  845  VAL SER ASP VAL LYS PRO ALA VAL GLU VAL ILE ALA TYR          
SEQRES  21 7  845  THR CYS ASP GLN CYS GLY TYR GLU VAL PHE GLN GLU VAL          
SEQRES  22 7  845  ASN SER ARG THR PHE THR PRO LEU SER GLU CYS THR SER          
SEQRES  23 7  845  GLU GLU CYS SER GLN ASN GLN THR LYS GLY GLN LEU PHE          
SEQRES  24 7  845  MET SER THR ARG ALA SER LYS PHE SER ALA PHE GLN GLU          
SEQRES  25 7  845  CYS LYS ILE GLN GLU LEU SER GLN GLN VAL PRO VAL GLY          
SEQRES  26 7  845  HIS ILE PRO ARG SER LEU ASN ILE HIS VAL ASN GLY THR          
SEQRES  27 7  845  LEU VAL ARG SER LEU SER PRO GLY ASP ILE VAL ASP VAL          
SEQRES  28 7  845  THR GLY ILE PHE LEU PRO ALA PRO TYR THR GLY PHE LYS          
SEQRES  29 7  845  ALA LEU LYS ALA GLY LEU LEU THR GLU THR TYR LEU GLU          
SEQRES  30 7  845  ALA GLN PHE VAL ARG GLN HIS LYS LYS LYS PHE ALA SER          
SEQRES  31 7  845  PHE SER LEU THR SER ASP VAL GLU GLU ARG VAL MET GLU          
SEQRES  32 7  845  LEU ILE THR SER GLY ASP VAL TYR ASN ARG LEU ALA LYS          
SEQRES  33 7  845  SER ILE ALA PRO GLU ILE TYR GLY ASN LEU ASP VAL LYS          
SEQRES  34 7  845  LYS ALA LEU LEU LEU LEU LEU VAL GLY GLY VAL ASP LYS          
SEQRES  35 7  845  ARG VAL GLY ASP GLY MET LYS ILE ARG GLY ASP ILE ASN          
SEQRES  36 7  845  VAL CYS LEU MET GLY ASP PRO GLY VAL ALA LYS SER GLN          
SEQRES  37 7  845  LEU LEU LYS ALA ILE CYS LYS ILE SER PRO ARG GLY VAL          
SEQRES  38 7  845  TYR THR THR GLY LYS GLY SER SER GLY VAL GLY LEU THR          
SEQRES  39 7  845  ALA ALA VAL MET LYS ASP PRO VAL THR ASP GLU MET ILE          
SEQRES  40 7  845  LEU GLU GLY GLY ALA LEU VAL LEU ALA ASP ASN GLY ILE          
SEQRES  41 7  845  CYS CYS ILE ASP GLU PHE ASP LYS MET ASP GLU SER ASP          
SEQRES  42 7  845  ARG THR ALA ILE HIS GLU VAL MET GLU GLN GLN THR ILE          
SEQRES  43 7  845  SER ILE SER LYS ALA GLY ILE ASN THR THR LEU ASN ALA          
SEQRES  44 7  845  ARG THR SER ILE LEU ALA ALA ALA ASN PRO LEU TYR GLY          
SEQRES  45 7  845  ARG TYR ASN PRO ARG LEU SER PRO LEU ASP ASN ILE ASN          
SEQRES  46 7  845  LEU PRO ALA ALA LEU LEU SER ARG PHE ASP ILE LEU PHE          
SEQRES  47 7  845  LEU MET LEU ASP ILE PRO SER ARG ASP ASP ASP GLU LYS          
SEQRES  48 7  845  LEU ALA GLU HIS VAL THR TYR VAL HIS MET HIS ASN LYS          
SEQRES  49 7  845  GLN PRO ASP LEU ASP PHE THR PRO VAL GLU PRO SER LYS          
SEQRES  50 7  845  MET ARG GLU TYR ILE ALA TYR ALA LYS THR LYS ARG PRO          
SEQRES  51 7  845  VAL MET SER GLU ALA VAL ASN ASP TYR VAL VAL GLN ALA          
SEQRES  52 7  845  TYR ILE ARG LEU ARG GLN ASP SER LYS ARG GLU MET ASP          
SEQRES  53 7  845  SER LYS PHE SER PHE GLY GLN ALA THR PRO ARG THR LEU          
SEQRES  54 7  845  LEU GLY ILE ILE ARG LEU SER GLN ALA LEU ALA LYS LEU          
SEQRES  55 7  845  ARG LEU ALA ASP MET VAL ASP ILE ASP ASP VAL GLU GLU          
SEQRES  56 7  845  ALA LEU ARG LEU VAL ARG VAL SER LYS GLU SER LEU TYR          
SEQRES  57 7  845  GLN GLU THR ASN LYS SER LYS GLU ASP GLU SER PRO THR          
SEQRES  58 7  845  THR LYS ILE PHE THR ILE ILE LYS LYS MET LEU GLN GLU          
SEQRES  59 7  845  THR GLY LYS ASN THR LEU SER TYR GLU ASN ILE VAL LYS          
SEQRES  60 7  845  THR VAL ARG LEU ARG GLY PHE THR MET LEU GLN LEU SER          
SEQRES  61 7  845  ASN CYS ILE GLN GLU TYR SER TYR LEU ASN VAL TRP HIS          
SEQRES  62 7  845  LEU ILE ASN GLU GLY ASN THR LEU LYS PHE VAL ASP ASP          
SEQRES  63 7  845  GLY THR MET ASP THR ASP GLN GLU ASP SER LEU VAL SER          
SEQRES  64 7  845  THR PRO LYS LEU ALA PRO GLN THR THR ALA SER ALA ASN          
SEQRES  65 7  845  VAL SER ALA GLN ASP SER ASP ILE ASP LEU GLN ASP ALA          
SEQRES   1 E  672  MET TYR TYR GLY ILE SER GLN PHE SER GLU ALA TYR ASN          
SEQRES   2 E  672  LYS ILE LEU ARG ASN SER SER SER HIS SER SER CYS GLN          
SEQRES   3 E  672  LEU VAL ILE PHE VAL SER CYS LEU ASN ILE ASP ALA LEU          
SEQRES   4 E  672  CYS ALA THR LYS MET LEU SER LEU LEU PHE LYS LYS GLN          
SEQRES   5 E  672  LEU VAL GLN SER GLN ILE VAL PRO ILE PHE GLY TYR SER          
SEQRES   6 E  672  GLU LEU ARG ARG HIS TYR SER GLN LEU ASP ASP ASN ILE          
SEQRES   7 E  672  ASN SER LEU LEU LEU VAL GLY PHE GLY GLY VAL ILE ASP          
SEQRES   8 E  672  LEU GLU ALA PHE LEU GLU ILE ASP PRO GLN GLU TYR VAL          
SEQRES   9 E  672  ILE ASP THR ASP GLU LYS SER GLY GLU GLN SER PHE ARG          
SEQRES  10 E  672  ARG ASP ILE TYR VAL LEU ASP ALA HIS ARG PRO TRP ASN          
SEQRES  11 E  672  LEU ASP ASN ILE PHE GLY SER GLN ILE ILE GLN CYS PHE          
SEQRES  12 E  672  ASP ASP GLY THR VAL ASP ASP THR LEU GLY GLU GLN LYS          
SEQRES  13 E  672  GLU ALA TYR TYR LYS LEU LEU GLU LEU ASP GLU GLU SER          
SEQRES  14 E  672  GLY ASP ASP GLU LEU SER GLY ASP GLU ASN ASP ASN ASN          
SEQRES  15 E  672  GLY GLY ASP ASP GLU ALA THR ASP ALA ASP GLU VAL THR          
SEQRES  16 E  672  ASP GLU ASP GLU GLU ASP GLU ASP GLU THR ILE SER ASN          
SEQRES  17 E  672  LYS ARG GLY ASN SER SER ILE GLY PRO ASN ASP LEU SER          
SEQRES  18 E  672  LYS ARG LYS GLN ARG LYS LYS GLN ILE HIS GLU TYR GLU          
SEQRES  19 E  672  GLY VAL LEU GLU GLU TYR TYR SER GLN GLY THR THR VAL          
SEQRES  20 E  672  VAL ASN SER ILE SER ALA GLN ILE TYR SER LEU LEU SER          
SEQRES  21 E  672  ALA ILE GLY GLU THR ASN LEU SER ASN LEU TRP LEU ASN          
SEQRES  22 E  672  ILE LEU GLY THR THR SER LEU ASP ILE ALA TYR ALA GLN          
SEQRES  23 E  672  VAL TYR ASN ARG LEU TYR PRO LEU LEU GLN ASP GLU VAL          
SEQRES  24 E  672  LYS ARG LEU THR PRO SER SER ARG ASN SER VAL LYS THR          
SEQRES  25 E  672  PRO ASP THR LEU THR LEU ASN ILE GLN PRO ASP TYR TYR          
SEQRES  26 E  672  LEU PHE LEU LEU ARG HIS SER SER LEU TYR ASP SER PHE          
SEQRES  27 E  672  TYR TYR SER ASN TYR VAL ASN ALA LYS LEU SER LEU TRP          
SEQRES  28 E  672  ASN GLU ASN GLY LYS LYS ARG LEU HIS LYS MET PHE ALA          
SEQRES  29 E  672  ARG MET GLY ILE PRO LEU SER THR ALA GLN GLU THR TRP          
SEQRES  30 E  672  LEU TYR MET ASP HIS SER ILE LYS ARG GLU LEU GLY ILE          
SEQRES  31 E  672  ILE PHE ASP LYS ASN LEU ASP ARG TYR GLY LEU GLN ASP          
SEQRES  32 E  672  ILE ILE ARG ASP GLY PHE VAL ARG THR LEU GLY TYR ARG          
SEQRES  33 E  672  GLY SER ILE SER ALA SER GLU PHE VAL GLU ALA LEU THR          
SEQRES  34 E  672  ALA LEU LEU GLU VAL GLY ASN SER THR ASP LYS ASP SER          
SEQRES  35 E  672  VAL LYS ILE ASN ASN ASP ASN ASN ASP ASP THR ASP GLY          
SEQRES  36 E  672  GLU GLU GLU GLU ASP ASN SER ALA GLN LYS LEU THR ASN          
SEQRES  37 E  672  LEU ARG LYS ARG TRP VAL SER ASN PHE TRP LEU SER TRP          
SEQRES  38 E  672  ASP ALA LEU ASP ASP ARG LYS VAL GLU LEU LEU ASN ARG          
SEQRES  39 E  672  GLY ILE GLN LEU ALA GLN ASP LEU GLN ARG ALA ILE PHE          
SEQRES  40 E  672  ASN THR GLY VAL ALA ILE LEU GLU LYS LYS LEU ILE LYS          
SEQRES  41 E  672  HIS LEU ARG ILE TYR ARG LEU CYS VAL LEU GLN ASP GLY          
SEQRES  42 E  672  PRO ASP LEU ASP LEU TYR ARG ASN PRO LEU THR LEU LEU          
SEQRES  43 E  672  ARG LEU GLY ASN TRP LEU ILE GLU CYS CYS ALA GLU SER          
SEQRES  44 E  672  GLU ASP LYS GLN LEU LEU PRO MET VAL LEU ALA SER ILE          
SEQRES  45 E  672  ASP GLU ASN THR ASP THR TYR LEU VAL ALA GLY LEU THR          
SEQRES  46 E  672  PRO ARG TYR PRO ARG GLY LEU ASP THR ILE HIS THR LYS          
SEQRES  47 E  672  LYS PRO ILE LEU ASN ASN PHE SER MET ALA PHE GLN GLN          
SEQRES  48 E  672  ILE THR ALA GLU THR ASP ALA LYS VAL ARG ILE ASP ASN          
SEQRES  49 E  672  PHE GLU SER SER ILE ILE GLU ILE ARG ARG GLU ASP LEU          
SEQRES  50 E  672  SER PRO PHE LEU GLU LYS LEU THR LEU SER GLY LEU LEU          
SEQRES  51 E  672  ASP TYR LYS ASP HIS ASP GLY ASP TYR LYS ASP HIS ASP          
SEQRES  52 E  672  ILE ASP TYR LYS ASP ASP ASP ASP LYS                          
SEQRES   1 D  294  MET ASP ILE ASN ILE ASP ASP ILE LEU ALA GLU LEU ASP          
SEQRES   2 D  294  LYS GLU THR THR ALA VAL ASP SER THR LYS ILE THR GLN          
SEQRES   3 D  294  GLY SER SER SER THR THR HIS ARG ASP ALA ASN THR ILE          
SEQRES   4 D  294  VAL GLY SER SER LEU ASP LEU ASN ASP LYS THR GLN ILE          
SEQRES   5 D  294  TYR VAL SER PRO GLN GLN ASP PHE SER ASP LEU MET LYS          
SEQRES   6 D  294  SER TRP LYS ASN GLU ARG CYS SER PRO GLU LEU LEU PRO          
SEQRES   7 D  294  TYR PRO HIS GLN LEU MET LYS ARG LEU LEU ASN ARG ILE          
SEQRES   8 D  294  SER MET GLN SER GLN LEU ILE GLU ASN ILE SER MET GLY          
SEQRES   9 D  294  PHE LEU ASP MET GLN ASN ALA SER ASN ALA ASN PRO PRO          
SEQRES  10 D  294  MET PRO ASN GLU SER LYS LEU PRO LEU LEU CYS MET GLU          
SEQRES  11 D  294  THR GLU LEU GLU ARG LEU LYS PHE VAL ILE ARG SER TYR          
SEQRES  12 D  294  ILE ARG CYS ARG LEU SER LYS ILE ASP LYS PHE SER LEU          
SEQRES  13 D  294  TYR LEU ARG GLN LEU ASN GLU ASP GLU ASN SER LEU ILE          
SEQRES  14 D  294  SER LEU THR ASP LEU LEU SER LYS ASP GLU ILE LYS TYR          
SEQRES  15 D  294  HIS ASP THR HIS SER LEU ILE TRP LEU LYS LEU VAL ASN          
SEQRES  16 D  294  ASP SER ILE LEU LYS TYR MET PRO GLU GLU LEU GLN ALA          
SEQRES  17 D  294  ILE ASN ASP THR GLU GLY SER VAL ASN MET ILE ASP GLU          
SEQRES  18 D  294  PRO ASP TRP ASN LYS PHE VAL PHE ILE HIS VAL ASN GLY          
SEQRES  19 D  294  PRO PRO ASP GLY LYS TRP ASN GLU ASP PRO LEU LEU GLN          
SEQRES  20 D  294  GLU ASN GLU PHE GLY LYS PRO CYS TYR THR VAL THR ILE          
SEQRES  21 D  294  PRO ASP LEU LYS GLU GLU VAL GLU LEU THR ILE GLY SER          
SEQRES  22 D  294  ILE TYR VAL MET ARG TYR GLU VAL ILE ARG ASP LEU LEU          
SEQRES  23 D  294  ARG ASP ASP LYS VAL ALA LEU ILE                              
SEQRES   1 B  213  MET SER LEU PRO ALA HIS LEU GLN GLN THR PHE SER PRO          
SEQRES   2 B  213  GLU GLU ILE GLN PHE ILE VAL GLU ASN GLU PRO ILE LYS          
SEQRES   3 B  213  ILE PHE PRO ARG ILE THR THR ARG GLN LYS ILE ARG GLY          
SEQRES   4 B  213  ASP ASP ARG GLY THR GLY ASN HIS THR ARG TRP GLN LEU          
SEQRES   5 B  213  ILE THR THR ASP ASP LYS ALA LEU ASN ASN MET VAL ALA          
SEQRES   6 B  213  MET ARG SER THR GLU VAL VAL LEU TRP ILE ALA LEU LEU          
SEQRES   7 B  213  LEU LYS GLN GLN SER LYS CYS SER ILE VAL ALA PRO GLN          
SEQRES   8 B  213  TRP LEU THR THR LYS GLU LEU ASP ARG LYS ILE GLN TYR          
SEQRES   9 B  213  GLU LYS THR HIS PRO ASP ARG PHE SER GLU LEU PRO TRP          
SEQRES  10 B  213  ASN TRP LEU VAL LEU ALA ARG ILE LEU PHE ASN LYS ALA          
SEQRES  11 B  213  LYS ASP ASP PHE HIS ASP PRO ILE HIS GLU LEU ARG GLY          
SEQRES  12 B  213  LYS ILE GLN ASP LEU ARG GLU ILE ARG GLN ILE LYS VAL          
SEQRES  13 B  213  LEU LYS GLY LEU LYS TYR LEU ASN GLU SER HIS LEU GLN          
SEQRES  14 B  213  LEU ASP ASN LEU SER LEU LEU GLU ILE ASN GLU LEU ARG          
SEQRES  15 B  213  PRO PHE ILE THR GLU ILE MET ASP LYS LEU ARG GLU ILE          
SEQRES  16 B  213  HIS THR ALA SER LEU THR ALA GLY THR GLU ASN ASP GLU          
SEQRES  17 B  213  GLU GLU PHE ASN ILE                                          
SEQRES   1 A  208  MET TYR GLY ASP LEU GLY ASN LYS LEU VAL LEU GLU ALA          
SEQRES   2 A  208  LYS ARG THR LYS GLN LEU TYR ALA ARG SER ASN GLN ASP          
SEQRES   3 A  208  VAL ASN LEU PRO MET TYR HIS GLU ASP ILE ILE ARG ASN          
SEQRES   4 A  208  ILE LEU LYS GLU VAL SER ASN LEU ARG LYS ASN THR GLU          
SEQRES   5 A  208  TYR LEU LYS GLU GLN GLN GLN LEU GLY MET LEU ASP ASP          
SEQRES   6 A  208  LYS VAL ALA LYS CYS GLN TYR PHE VAL THR LEU LEU CYS          
SEQRES   7 A  208  MET GLU ARG ASN LYS ARG CYS LEU LEU ALA TYR GLN ARG          
SEQRES   8 A  208  LEU ARG THR ASP ILE LEU ASP SER MET ALA TRP ASN ASN          
SEQRES   9 A  208  ASN GLY LEU ASP LEU MET SER SER ILE THR PHE SER GLN          
SEQRES  10 A  208  GLN ASP THR ASN ASN LEU SER HIS GLN GLU GLN GLU TYR          
SEQRES  11 A  208  LEU LYS GLU TYR CYS ASP LEU ILE THR ASP LEU LYS SER          
SEQRES  12 A  208  GLY ASP LEU VAL ASP ILE ASP LEU SER GLY SER LEU VAL          
SEQRES  13 A  208  PRO PRO SER ASP VAL PHE ILE ASP VAL ARG VAL LEU LYS          
SEQRES  14 A  208  ASP ALA GLY GLU ILE GLN THR GLU TYR GLY VAL PHE ASN          
SEQRES  15 A  208  LEU ILE LYS ASP SER GLN PHE PHE VAL ARG GLN SER ASP          
SEQRES  16 A  208  VAL GLU ARG LEU ILE GLN GLN GLY TYR LEU GLN LYS ILE          
SEQRES   1 C  194  MET GLY TYR TYR ASP ILE ASP ASP VAL LEU ALA ASP GLY          
SEQRES   2 C  194  THR GLU PHE PRO CYS LYS PHE GLN TYR ASP ILE PRO GLY          
SEQRES   3 C  194  LEU GLY TYR LEU GLU ASN ASN PRO GLY ARG PRO ILE THR          
SEQRES   4 C  194  LYS ASN THR LYS LEU SER LEU PRO LEU TRP LEU ALA ARG          
SEQRES   5 C  194  ILE LEU ALA ILE VAL GLY GLY ASP GLU ALA LEU VAL ASP          
SEQRES   6 C  194  GLU GLU PRO VAL PRO PHE VAL GLU LEU LEU PRO PRO ASP          
SEQRES   7 C  194  MET PHE SER THR LYS VAL MET ASN ALA ILE LYS THR ASP          
SEQRES   8 C  194  PRO VAL ALA LEU ASP LEU HIS SER ILE ASN SER HIS PHE          
SEQRES   9 C  194  PHE SER LEU ALA ILE LYS TRP ILE MET LEU PHE SER GLU          
SEQRES  10 C  194  LYS GLU LEU ALA ASN VAL VAL SER GLU LEU LEU LEU GLN          
SEQRES  11 C  194  ARG ALA GLN GLU LEU ASN HIS HIS ALA SER SER LEU SER          
SEQRES  12 C  194  ILE ASP LEU ASN ALA ASP SER THR GLY LYS ASN SER ALA          
SEQRES  13 C  194  ASN THR ASN ILE ALA THR SER THR PHE LEU LEU LYS LEU          
SEQRES  14 C  194  GLU GLU MET GLU LYS GLU ILE TYR LYS LYS SER HIS GLU          
SEQRES  15 C  194  SER TYR LYS ASP THR LYS ARG TRP MET PHE LYS LYS              
HET     ZN  71001       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  12   ZN    ZN 2+                                                        
HELIX    1   1 ASN 2  202  LEU 2  216  1                                  15    
HELIX    2   2 SER 2  225  MET 2  237  1                                  13    
HELIX    3   3 ASN 2  245  LYS 2  253  1                                   9    
HELIX    4   4 LYS 2  253  ALA 2  261  1                                   9    
HELIX    5   5 CYS 2  263  TYR 2  283  1                                  21    
HELIX    6   6 ARG 2  310  LEU 2  314  5                                   5    
HELIX    7   7 ALA 2  393  VAL 2  397  5                                   5    
HELIX    8   8 ASP 2  413  VAL 2  415  5                                   3    
HELIX    9   9 ALA 3   19  LEU 3   32  1                                  14    
HELIX   10  10 TYR 3   38  ASN 3   55  1                                  18    
HELIX   11  11 SER 3   99  ASP 3  101  5                                   3    
HELIX   12  12 ASP 3  102  ASP 3  107  1                                   6    
HELIX   13  13 ASP 3  107  GLU 3  117  1                                  11    
HELIX   14  14 PRO 3  118  TYR 3  120  5                                   3    
HELIX   15  15 PHE 3  121  SER 3  135  1                                  15    
HELIX   16  16 MET 3  261  ALA 3  265  5                                   5    
HELIX   17  17 ASP 3  279  VAL 3  283  5                                   5    
HELIX   18  18 GLU 4  189  ASN 4  196  1                                   8    
HELIX   19  19 TYR 4  226  GLY 4  237  1                                  12    
HELIX   20  20 THR 4  254  TYR 4  264  1                                  11    
HELIX   21  21 TYR 4  264  VAL 4  285  1                                  22    
HELIX   22  22 ASP 4  294  LYS 4  299  1                                   6    
HELIX   23  23 TYR 4  420  VAL 4  424  5                                   5    
HELIX   24  24 ASP 5   22  GLU 5   37  1                                  16    
HELIX   25  25 PHE 5   44  VAL 5   56  1                                  13    
HELIX   26  26 ASN 5   64  ASN 5   72  1                                   9    
HELIX   27  27 ASN 5   72  SER 5   80  1                                   9    
HELIX   28  28 GLU 5   82  SER 5  102  1                                  21    
HELIX   29  29 PRO 5  147  LEU 5  151  5                                   5    
HELIX   30  30 ASP 5  279  THR 5  283  5                                   5    
HELIX   31  31 VAL 6  106  ASP 6  121  1                                  16    
HELIX   32  32 VAL 6  135  LYS 6  144  1                                  10    
HELIX   33  33 TYR 6  155  ARG 6  161  1                                   7    
HELIX   34  34 GLY 6  164  ILE 6  170  1                                   7    
HELIX   35  35 GLN 6  173  ARG 6  176  5                                   4    
HELIX   36  36 PHE 6  177  ALA 6  193  1                                  17    
HELIX   37  37 ASP 7   13  LEU 7   25  1                                  13    
HELIX   38  38 PRO 7   61  ASN 7   72  1                                  12    
HELIX   39  39 LEU 7   82  LYS 7   92  1                                  11    
HELIX   40  40 LEU 7  102  ALA 7  110  1                                   9    
HELIX   41  41 ASN 7  111  GLU 7  115  5                                   5    
HELIX   42  42 ARG 7  119  MET 7  125  1                                   7    
HELIX   43  43 LEU 7  139  THR 7  158  1                                  20    
HELIX   44  44 ARG 7  216  ILE 7  220  5                                   5    
HELIX   45  45 THR 7  338  VAL 7  340  5                                   3    
HELIX   46  46 GLN E    7  ASN E   18  1                                  12    
HELIX   47  47 ASN E   35  GLN E   52  1                                  18    
HELIX   48  48 GLY E   63  LEU E   74  1                                  12    
HELIX   49  49 ASP E   91  GLU E   97  1                                   7    
HELIX   50  50 ASN E  130  PHE E  135  1                                   6    
HELIX   51  51 LEU E  152  GLU E  157  1                                   6    
HELIX   52  52 ASP E  219  TYR E  240  1                                  22    
HELIX   53  53 SER E  250  GLY E  263  1                                  14    
HELIX   54  54 ASN E  266  THR E  278  1                                  13    
HELIX   55  55 VAL E  287  ASN E  289  5                                   3    
HELIX   56  56 ARG E  290  ARG E  301  1                                  12    
HELIX   57  57 SER E  333  TYR E  340  1                                   8    
HELIX   58  58 TYR E  343  LEU E  348  1                                   6    
HELIX   59  59 ASN E  352  GLY E  367  1                                  16    
HELIX   60  60 PRO E  369  GLU E  375  1                                   7    
HELIX   61  61 THR E  376  MET E  380  5                                   5    
HELIX   62  62 ASP E  381  GLU E  387  1                                   7    
HELIX   63  63 ILE E  390  LEU E  396  1                                   7    
HELIX   64  64 ASP E  397  GLY E  400  5                                   4    
HELIX   65  65 ALA E  421  VAL E  434  1                                  14    
HELIX   66  66 ALA E  463  ALA E  483  1                                  21    
HELIX   67  67 LEU E  491  GLU E  515  1                                  25    
HELIX   68  68 ASP E  537  ARG E  540  5                                   4    
HELIX   69  69 ASN E  541  ALA E  557  1                                  17    
HELIX   70  70 ASN E  604  ALA E  614  1                                  11    
HELIX   71  71 ARG E  633  LEU E  646  1                                  14    
HELIX   72  72 SER D   55  SER D   73  1                                  19    
HELIX   73  73 PRO D   80  PHE D  105  1                                  26    
HELIX   74  74 LYS D  123  ASP D  164  1                                  42    
HELIX   75  75 ASP D  178  ILE D  198  1                                  21    
HELIX   76  76 TYR D  279  ASP D  288  1                                  10    
HELIX   77  77 SER B   12  GLU B   21  1                                  10    
HELIX   78  78 LEU B   73  GLN B   82  1                                  10    
HELIX   79  79 THR B   94  THR B  107  1                                  14    
HELIX   80  80 ASN B  118  LYS B  129  1                                  12    
HELIX   81  81 ALA B  130  ASP B  133  5                                   4    
HELIX   82  82 GLU B  140  LEU B  160  1                                  21    
HELIX   83  83 LYS B  161  LEU B  163  5                                   3    
HELIX   84  84 SER B  174  SER B  199  1                                  26    
HELIX   85  85 GLY A    3  ARG A   22  1                                  20    
HELIX   86  86 GLU A   34  GLY A   61  1                                  28    
HELIX   87  87 VAL A   67  ASN A  104  1                                  38    
HELIX   88  88 SER A  124  ASP A  145  1                                  22    
HELIX   89  89 GLN A  193  GLN A  201  1                                   9    
HELIX   90  90 ASP C    5  ASP C   12  1                                   8    
HELIX   91  91 LEU C   48  ALA C   55  1                                   8    
HELIX   92  92 PRO C   77  PHE C   80  5                                   4    
HELIX   93  93 SER C   81  ILE C   88  1                                   8    
HELIX   94  94 PHE C  104  SER C  116  1                                  13    
HELIX   95  95 LYS C  118  ASN C  136  1                                  19    
HELIX   96  96 THR C  164  LEU C  169  5                                   6    
HELIX   97  97 GLU C  170  PHE C  192  1                                  23    
SHEET    1   A 5 PHE 2 331  GLN 2 333  0                                        
SHEET    2   A 5 ARG 2 383  GLN 2 391 -1  O  ARG 2 383   N  GLN 2 333           
SHEET    3   A 5 HIS 2 405  LEU 2 411 -1  O  VAL 2 408   N  VAL 2 388           
SHEET    4   A 5 ILE 2 450  GLU 2 452  1  O  ILE 2 451   N  GLU 2 407           
SHEET    5   A 5 ILE 2 429  LYS 2 431 -1  N  LYS 2 431   O  ILE 2 450           
SHEET    1   B 5 PHE 2 331  GLN 2 333  0                                        
SHEET    2   B 5 ARG 2 383  GLN 2 391 -1  O  ARG 2 383   N  GLN 2 333           
SHEET    3   B 5 VAL 2 320  THR 2 325 -1  N  VAL 2 323   O  GLN 2 391           
SHEET    4   B 5 GLU 2 423  VAL 2 426 -1  O  VAL 2 424   N  GLY 2 322           
SHEET    5   B 5 ILE 2 456  ARG 2 458 -1  O  LYS 2 457   N  GLU 2 425           
SHEET    1   C 8 LEU 3 179  VAL 3 180  0                                        
SHEET    2   C 8 GLY 3 296  SER 3 300 -1  O  GLY 3 296   N  VAL 3 180           
SHEET    3   C 8 THR 3 319  ILE 3 321 -1  O  LEU 3 320   N  LYS 3 299           
SHEET    4   C 8 ILE 3 274  ILE 3 277  1  N  ASP 3 275   O  ILE 3 321           
SHEET    5   C 8 ARG 3 255  GLN 3 259 -1  N  ILE 3 256   O  VAL 3 276           
SHEET    6   C 8 GLY 3 184  VAL 3 186 -1  N  ILE 3 185   O  GLN 3 259           
SHEET    7   C 8 ARG 3 291  ASN 3 293 -1  O  VAL 3 292   N  GLY 3 184           
SHEET    8   C 8 TYR 3 327  PRO 3 328 -1  O  TYR 3 327   N  ASN 3 293           
SHEET    1   D 3 HIS 3 210  ASP 3 213  0                                        
SHEET    2   D 3 ARG 3 198  ALA 3 203 -1  N  HIS 3 201   O  HIS 3 210           
SHEET    3   D 3 LEU 3 241  THR 3 243 -1  O  THR 3 242   N  TYR 3 202           
SHEET    1   E 3 VAL 4 332  SER 4 335  0                                        
SHEET    2   E 3 ILE 4 397  GLN 4 400 -1  O  LYS 4 398   N  ARG 4 334           
SHEET    3   E 3 SER 4 414  LEU 4 417 -1  O  LEU 4 417   N  ILE 4 397           
SHEET    1   F 2 ILE 4 339  MET 4 342  0                                        
SHEET    2   F 2 PHE 4 391  LYS 4 394 -1  O  LYS 4 394   N  ILE 4 339           
SHEET    1   G 2 VAL 4 344  ALA 4 345  0                                        
SHEET    2   G 2 VAL 4 358  GLU 4 359 -1  O  VAL 4 358   N  ALA 4 345           
SHEET    1   H 2 ILE 4 365  GLN 4 366  0                                        
SHEET    2   H 2 SER 6 419  THR 6 420  1  O  THR 6 420   N  ILE 4 365           
SHEET    1   I 2 VAL 4 435  THR 4 436  0                                        
SHEET    2   I 2 HIS 4 465  VAL 4 466 -1  O  HIS 4 465   N  THR 4 436           
SHEET    1   J 2 PHE 4 439  ILE 4 442  0                                        
SHEET    2   J 2 LYS 4 458  VAL 4 461 -1  O  TYR 4 460   N  ARG 4 440           
SHEET    1   K 2 SER 5  60  VAL 5  63  0                                        
SHEET    2   K 2 GLN 5 136  LEU 5 139  1  O  ILE 5 138   N  LEU 5  61           
SHEET    1   L 7 TYR 5 298  TYR 5 301  0                                        
SHEET    2   L 7 THR 5 325  LYS 5 329 -1  O  TYR 5 327   N  SER 5 299           
SHEET    3   L 7 ASN 5 273  THR 5 277  1  N  THR 5 275   O  ILE 5 328           
SHEET    4   L 7 LEU 5 256  GLU 5 260 -1  N  LEU 5 256   O  MET 5 276           
SHEET    5   L 7 LEU 5 162  THR 5 169 -1  N  ILE 5 167   O  LYS 5 257           
SHEET    6   L 7 ARG 5 291  ILE 5 294 -1  O  ILE 5 294   N  LEU 5 162           
SHEET    7   L 7 GLN 5 334  SER 5 335 -1  O  GLN 5 334   N  THR 5 293           
SHEET    1   M 3 THR 5 190  THR 5 193  0                                        
SHEET    2   M 3 ALA 5 176  CYS 5 183 -1  N  ILE 5 181   O  THR 5 190           
SHEET    3   M 3 TYR 5 241  PHE 5 250 -1  O  LYS 5 249   N  TYR 5 178           
SHEET    1   N 2 THR 6 150  ASP 6 154  0                                        
SHEET    2   N 2 GLN 6 264  PHE 6 268  1  O  GLN 6 264   N  ILE 6 151           
SHEET    1   O 2 VAL 6 273  HIS 6 274  0                                        
SHEET    2   O 2 SER 6 289  ILE 6 290  1  O  SER 6 289   N  HIS 6 274           
SHEET    1   P 6 PHE 6 454  ALA 6 456  0                                        
SHEET    2   P 6 LEU 6 377  LEU 6 381  1  N  ASP 6 378   O  PHE 6 454           
SHEET    3   P 6 GLN 6 357  GLN 6 362 -1  N  ILE 6 361   O  LEU 6 377           
SHEET    4   P 6 GLY 6 292  THR 6 295 -1  N  THR 6 293   O  GLN 6 362           
SHEET    5   P 6 ARG 6 394  PHE 6 397 -1  O  CYS 6 395   N  GLY 6 292           
SHEET    6   P 6 VAL 6 459  ILE 6 460 -1  O  ILE 6 460   N  LYS 6 396           
SHEET    1   Q 2 VAL 6 404  PRO 6 405  0                                        
SHEET    2   Q 2 TYR 6 450  LYS 6 451 -1  O  LYS 6 451   N  VAL 6 404           
SHEET    1   R 2 SER 7  77  ASP 7  81  0                                        
SHEET    2   R 2 PHE 7 201  LYS 7 205  1  O  PHE 7 201   N  VAL 7  78           
SHEET    1   S 4 LYS 7 252  PRO 7 253  0                                        
SHEET    2   S 4 ALA 7 309  GLN 7 316 -1  O  PHE 7 310   N  LYS 7 252           
SHEET    3   S 4 LEU 7 331  ASN 7 336 -1  O  ILE 7 333   N  CYS 7 313           
SHEET    4   S 4 LEU 7 376  GLU 7 377  1  O  LEU 7 376   N  ASN 7 332           
SHEET    1   T 5 LYS 7 252  PRO 7 253  0                                        
SHEET    2   T 5 ALA 7 309  GLN 7 316 -1  O  PHE 7 310   N  LYS 7 252           
SHEET    3   T 5 ILE 7 239  THR 7 246 -1  N  THR 7 246   O  LYS 7 314           
SHEET    4   T 5 ILE 7 348  GLY 7 353 -1  O  VAL 7 351   N  VAL 7 241           
SHEET    5   T 5 PHE 7 380  GLN 7 383 -1  O  ARG 7 382   N  ASP 7 350           
SHEET    1   U 3 VAL 7 269  PHE 7 270  0                                        
SHEET    2   U 3 ALA 7 259  CYS 7 262 -1  N  TYR 7 260   O  VAL 7 269           
SHEET    3   U 3 LEU 7 298  MET 7 300 -1  O  PHE 7 299   N  THR 7 261           
SHEET    1   V 6 ASP E 119  LEU E 123  0                                        
SHEET    2   V 6 SER E  80  VAL E  84  1  N  LEU E  81   O  TYR E 121           
SHEET    3   V 6 VAL E  28  VAL E  31  1  N  PHE E  30   O  LEU E  82           
SHEET    4   V 6 SER E  56  PRO E  60  1  O  GLN E  57   N  ILE E  29           
SHEET    5   V 6 GLN A 188  ARG A 192 -1  O  PHE A 190   N  SER E  56           
SHEET    6   V 6 PHE A 162  ARG A 166 -1  N  ILE A 163   O  VAL A 191           
SHEET    1   W 3 LEU E 318  GLN E 321  0                                        
SHEET    2   W 3 GLY E 408  GLY E 414 -1  O  VAL E 410   N  ASN E 319           
SHEET    3   W 3 GLY E 417  SER E 420 -1  O  GLY E 417   N  GLY E 414           
SHEET    1   X 3 LEU E 569  SER E 571  0                                        
SHEET    2   X 3 LEU E 580  ALA E 582 -1  O  LEU E 580   N  SER E 571           
SHEET    3   X 3 ILE E 629  ILE E 630 -1  O  ILE E 630   N  VAL E 581           
SHEET    1   Y 2 PHE D 227  VAL D 228  0                                        
SHEET    2   Y 2 MET D 277  ARG D 278 -1  O  MET D 277   N  VAL D 228           
SHEET    1   Z 3 THR B  69  VAL B  72  0                                        
SHEET    2   Z 3 PRO B  24  PRO B  29 -1  N  ILE B  25   O  VAL B  71           
SHEET    3   Z 3 CYS B  85  ILE B  87 -1  O  SER B  86   N  PHE B  28           
SHEET    1  AA 2 GLU C  15  LYS C  19  0                                        
SHEET    2  AA 2 LYS C  43  PRO C  47 -1  O  LEU C  46   N  PHE C  16           
SSBOND   1 CYS 5  186    CYS 5  211                          1555   1555  2.04  
LINK         SG  CYS 7 262                ZN    ZN 71001     1555   1555  2.29  
LINK         SG  CYS 7 289                ZN    ZN 71001     1555   1555  2.45  
CISPEP   1 LEU 2  234    GLY 2  235          0       -28.63                     
CISPEP   2 PRO 2  301    THR 2  302          0       -13.72                     
CISPEP   3 CYS 2  341    LEU 2  342          0        23.52                     
CISPEP   4 GLN 2  353    ASP 2  354          0        -6.00                     
CISPEP   5 SER 2  355    ASN 2  356          0       -28.75                     
CISPEP   6 ILE 2  359    ARG 2  360          0        -1.45                     
CISPEP   7 ASN 2  433    TYR 2  434          0       -14.75                     
CISPEP   8 ASP 2  435    GLY 2  436          0         4.20                     
CISPEP   9 GLY 2  436    ASN 2  437          0        -9.52                     
CISPEP  10 ARG 2  459    GLU 2  460          0        -0.58                     
CISPEP  11 THR 3   34    PHE 3   35          0       -14.87                     
CISPEP  12 ASP 3  137    ASP 3  138          0       -26.20                     
CISPEP  13 GLY 3  159    SER 3  160          0         5.73                     
CISPEP  14 PHE 3  161    GLY 3  162          0         2.10                     
CISPEP  15 THR 3  172    ALA 3  173          0        10.43                     
CISPEP  16 THR 3  187    LYS 3  188          0        -9.74                     
CISPEP  17 ALA 3  204    LYS 3  205          0         0.95                     
CISPEP  18 PRO 3  228    ALA 3  229          0        18.61                     
CISPEP  19 THR 3  236    GLU 3  237          0         0.05                     
CISPEP  20 ASN 3  310    SER 3  311          0        -0.02                     
CISPEP  21 GLY 3  323    ASN 3  324          0       -13.45                     
CISPEP  22 PHE 4  201    LYS 4  202          0        -5.34                     
CISPEP  23 LYS 4  204    PHE 4  205          0        21.04                     
CISPEP  24 TYR 4  225    TYR 4  226          0       -11.11                     
CISPEP  25 LEU 4  249    ALA 4  250          0         6.41                     
CISPEP  26 LYS 4  252    GLN 4  253          0         9.60                     
CISPEP  27 ASP 4  292    LEU 4  293          0        -7.76                     
CISPEP  28 VAL 4  351    CYS 4  352          0        -2.99                     
CISPEP  29 CYS 4  352    ASP 4  353          0        -0.31                     
CISPEP  30 ARG 4  370    CYS 4  371          0       -18.28                     
CISPEP  31 ARG 4  373    ILE 4  374          0       -23.38                     
CISPEP  32 ILE 4  374    ASP 4  375          0       -28.37                     
CISPEP  33 ASP 4  375    CYS 4  376          0        -1.80                     
CISPEP  34 CYS 4  376    ASN 4  377          0        20.15                     
CISPEP  35 ASP 4  408    GLY 4  409          0        28.21                     
CISPEP  36 ASN 4  447    SER 4  448          0        -4.00                     
CISPEP  37 LYS 4  467    LYS 4  468          0        -0.02                     
CISPEP  38 ASP 5   41    SER 5   42          0        -9.07                     
CISPEP  39 ASN 5  130    SER 5  131          0        -6.14                     
CISPEP  40 ASN 5  196    PHE 5  197          0         7.31                     
CISPEP  41 ASN 5  235    CYS 5  236          0        -2.78                     
CISPEP  42 GLY 5  237    PRO 5  238          0       -10.23                     
CISPEP  43 LEU 5  264    VAL 5  265          0        -7.65                     
CISPEP  44 GLY 5  320    VAL 5  321          0         1.16                     
CISPEP  45 VAL 5  321    ALA 5  322          0        -8.00                     
CISPEP  46 LEU 5  331    GLY 5  332          0       -27.72                     
CISPEP  47 VAL 5  337    GLU 5  338          0        -0.54                     
CISPEP  48 GLU 5  338    THR 5  339          0       -14.62                     
CISPEP  49 VAL 6  100    LYS 6  101          0       -14.49                     
CISPEP  50 PHE 6  122    SER 6  123          0        -0.73                     
CISPEP  51 GLY 6  130    GLU 6  131          0       -14.84                     
CISPEP  52 GLU 6  133    LYS 6  134          0        29.84                     
CISPEP  53 LYS 6  134    VAL 6  135          0        10.75                     
CISPEP  54 THR 6  310    CYS 6  311          0       -13.59                     
CISPEP  55 CYS 6  311    ASP 6  312          0         5.77                     
CISPEP  56 LYS 6  326    TYR 6  327          0         7.59                     
CISPEP  57 THR 6  328    GLU 6  329          0        -1.55                     
CISPEP  58 ASN 6  335    PRO 6  336          0         5.06                     
CISPEP  59 PRO 6  336    SER 6  337          0       -20.29                     
CISPEP  60 ASN 6  340    ARG 6  341          0        -0.82                     
CISPEP  61 TRP 6  344    THR 6  345          0        -7.13                     
CISPEP  62 ASP 6  355    TRP 6  356          0       -20.34                     
CISPEP  63 THR 6  370    GLY 6  371          0         2.59                     
CISPEP  64 LEU 7   94    GLN 7   95          0        14.23                     
CISPEP  65 GLY 7   96    THR 7   97          0        -2.45                     
CISPEP  66 PRO 7  128    THR 7  129          0       -22.61                     
CISPEP  67 LYS 7  135    ASP 7  136          0       -15.32                     
CISPEP  68 SER 7  208    GLN 7  209          0       -11.55                     
CISPEP  69 ARG 7  214    TYR 7  215          0         5.08                     
CISPEP  70 ASN 7  292    GLN 7  293          0       -20.10                     
CISPEP  71 GLN 7  293    THR 7  294          0        -3.52                     
CISPEP  72 GLY 7  362    PHE 7  363          0       -28.47                     
CISPEP  73 LYS 7  367    ALA 7  368          0        -1.06                     
CISPEP  74 ALA 7  368    GLY 7  369          0        -9.38                     
CISPEP  75 GLY 7  369    LEU 7  370          0       -15.66                     
CISPEP  76 HIS E   22    SER E   23          0         0.00                     
CISPEP  77 SER E   24    CYS E   25          0         0.08                     
CISPEP  78 CYS E   25    GLN E   26          0         6.61                     
CISPEP  79 SER E   32    CYS E   33          0        -5.78                     
CISPEP  80 ILE E   98    ASP E   99          0        13.01                     
CISPEP  81 ARG E  127    PRO E  128          0        -6.82                     
CISPEP  82 ILE E  140    GLN E  141          0         4.03                     
CISPEP  83 ASP E  145    GLY E  146          0        -8.90                     
CISPEP  84 ASP E  149    ASP E  150          0        -5.07                     
CISPEP  85 ASP E  150    THR E  151          0         9.50                     
CISPEP  86 THR E  151    LEU E  152          0        11.11                     
CISPEP  87 LEU E  163    GLU E  164          0        -4.39                     
CISPEP  88 ALA E  285    GLN E  286          0       -20.96                     
CISPEP  89 ASN E  308    SER E  309          0        11.97                     
CISPEP  90 VAL E  310    LYS E  311          0        -2.14                     
CISPEP  91 LYS E  311    THR E  312          0        -6.61                     
CISPEP  92 THR E  315    LEU E  316          0         4.53                     
CISPEP  93 GLU E  558    SER E  559          0         2.75                     
CISPEP  94 SER E  559    GLU E  560          0        17.83                     
CISPEP  95 ASP E  561    LYS E  562          0         1.24                     
CISPEP  96 LEU E  646    SER E  647          0         0.35                     
CISPEP  97 ASN D  166    SER D  167          0        -0.07                     
CISPEP  98 THR D  212    GLU D  213          0         2.12                     
CISPEP  99 GLY D  214    SER D  215          0       -20.15                     
CISPEP 100 SER D  215    VAL D  216          0       -15.00                     
CISPEP 101 VAL D  216    ASN D  217          0        11.59                     
CISPEP 102 MET D  218    ILE D  219          0        15.18                     
CISPEP 103 ASP D  220    GLU D  221          0        11.56                     
CISPEP 104 GLY D  252    LYS D  253          0        -3.68                     
CISPEP 105 TYR D  256    THR D  257          0         9.00                     
CISPEP 106 VAL D  267    GLU D  268          0         1.82                     
CISPEP 107 HIS B    6    LEU B    7          0        -2.49                     
CISPEP 108 LEU B    7    GLN B    8          0       -13.21                     
CISPEP 109 TRP B   50    GLN B   51          0       -11.30                     
CISPEP 110 GLN B   51    LEU B   52          0         8.63                     
CISPEP 111 ALA B   59    LEU B   60          0         4.69                     
CISPEP 112 GLU B  165    SER B  166          0        -9.14                     
CISPEP 113 ARG A   22    SER A   23          0        -6.93                     
CISPEP 114 SER A   23    ASN A   24          0        18.95                     
CISPEP 115 ASP A  108    LEU A  109          0         8.67                     
CISPEP 116 MET A  110    SER A  111          0       -22.34                     
CISPEP 117 ASP A  145    LEU A  146          0        11.69                     
CISPEP 118 VAL A  147    ASP A  148          0        -1.08                     
CISPEP 119 ILE A  149    ASP A  150          0         0.09                     
CISPEP 120 SER A  159    ASP A  160          0       -24.46                     
CISPEP 121 ALA A  171    GLY A  172          0         0.12                     
CISPEP 122 GLY A  172    GLU A  173          0        -0.12                     
CISPEP 123 GLY C   35    ARG C   36          0       -12.31                     
CISPEP 124 ASN C  101    SER C  102          0         4.41                     
CISPEP 125 THR C  162    SER C  163          0        -5.71                     
SITE     1 AC1  5 CYS 7 262  CYS 7 265  GLY 7 266  SER 7 286                    
SITE     2 AC1  5 CYS 7 289                                                     
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 LINES ARE NOT SHOWN.)
END                                                                             
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