GenomeNet

Database: PDB
Entry: 2E2I
LinkDB: 2E2I
Original site: 2E2I 
HEADER    TRANSCRIPTION,TRANSFERASE/DNA-RNA HYBRID14-NOV-06   2E2I              
TITLE     RNA POLYMERASE II ELONGATION COMPLEX IN 5 MM MG+2 WITH 2'-DGTP        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-R(*AP*UP*CP*GP*AP*GP*AP*GP*GP*A)-3';                    
COMPND   3 CHAIN: R;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: 28-MER DNA TEMPLATE STRAND;                                
COMPND   7 CHAIN: T;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: 5'-D(*CP*TP*GP*CP*TP*TP*AP*TP*CP*GP*GP*TP*AP*G)-3';        
COMPND  11 CHAIN: N;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT;            
COMPND  15 CHAIN: A;                                                            
COMPND  16 SYNONYM: RNA POLYMERASE II SUBUNIT 1, B220;                          
COMPND  17 EC: 2.7.7.6;                                                         
COMPND  18 MOL_ID: 5;                                                           
COMPND  19 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 140 KDA POLYPEPTIDE;        
COMPND  20 CHAIN: B;                                                            
COMPND  21 SYNONYM: B150, RNA POLYMERASE II SUBUNIT 2;                          
COMPND  22 EC: 2.7.7.6;                                                         
COMPND  23 MOL_ID: 6;                                                           
COMPND  24 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 45 KDA POLYPEPTIDE;         
COMPND  25 CHAIN: C;                                                            
COMPND  26 SYNONYM: B44.5;                                                      
COMPND  27 EC: 2.7.7.6;                                                         
COMPND  28 MOL_ID: 7;                                                           
COMPND  29 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 27 KDA         
COMPND  30 POLYPEPTIDE;                                                         
COMPND  31 CHAIN: E;                                                            
COMPND  32 SYNONYM: ABC27;                                                      
COMPND  33 EC: 2.7.7.6;                                                         
COMPND  34 MOL_ID: 8;                                                           
COMPND  35 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 23 KDA         
COMPND  36 POLYPEPTIDE;                                                         
COMPND  37 CHAIN: F;                                                            
COMPND  38 SYNONYM: ABC23;                                                      
COMPND  39 EC: 2.7.7.6;                                                         
COMPND  40 MOL_ID: 9;                                                           
COMPND  41 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 14.5 KDA       
COMPND  42 POLYPEPTIDE;                                                         
COMPND  43 CHAIN: H;                                                            
COMPND  44 SYNONYM: ABC14.4;                                                    
COMPND  45 EC: 2.7.7.6;                                                         
COMPND  46 MOL_ID: 10;                                                          
COMPND  47 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT 9;                  
COMPND  48 CHAIN: I;                                                            
COMPND  49 SYNONYM: DNA-DIRECTED RNA POLYMERASE II 14.2 KDA POLYPEPTIDE, B12.6; 
COMPND  50 EC: 2.7.7.6;                                                         
COMPND  51 MOL_ID: 11;                                                          
COMPND  52 MOLECULE: DNA-DIRECTED RNA POLYMERASES I/II/III SUBUNIT 10;          
COMPND  53 CHAIN: J;                                                            
COMPND  54 SYNONYM: DNA- DIRECTED RNA POLYMERASES I, II, AND III 8.3 KDA        
COMPND  55 POLYPEPTIDE, ABC10- BETA, ABC8;                                      
COMPND  56 EC: 2.7.7.6;                                                         
COMPND  57 MOL_ID: 12;                                                          
COMPND  58 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 13.6 KDA POLYPEPTIDE;       
COMPND  59 CHAIN: K;                                                            
COMPND  60 SYNONYM: B13.6;                                                      
COMPND  61 EC: 2.7.7.6;                                                         
COMPND  62 MOL_ID: 13;                                                          
COMPND  63 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 7.7 KDA        
COMPND  64 POLYPEPTIDE;                                                         
COMPND  65 CHAIN: L;                                                            
COMPND  66 SYNONYM: ABC10-ALPHA;                                                
COMPND  67 EC: 2.7.7.6                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 SYNTHETIC: YES;                                                      
SOURCE   5 MOL_ID: 3;                                                           
SOURCE   6 SYNTHETIC: YES;                                                      
SOURCE   7 MOL_ID: 4;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   9 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  10 ORGANISM_TAXID: 4932;                                                
SOURCE  11 STRAIN: DELTA-RPB4;                                                  
SOURCE  12 MOL_ID: 5;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  14 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  15 ORGANISM_TAXID: 4932;                                                
SOURCE  16 STRAIN: DELTA-RPB4;                                                  
SOURCE  17 MOL_ID: 6;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  19 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  20 ORGANISM_TAXID: 4932;                                                
SOURCE  21 STRAIN: DELTA-RPB4;                                                  
SOURCE  22 MOL_ID: 7;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  24 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  25 ORGANISM_TAXID: 4932;                                                
SOURCE  26 STRAIN: DELTA-RPB4;                                                  
SOURCE  27 MOL_ID: 8;                                                           
SOURCE  28 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  29 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  30 ORGANISM_TAXID: 4932;                                                
SOURCE  31 STRAIN: DELTA-RPB4;                                                  
SOURCE  32 MOL_ID: 9;                                                           
SOURCE  33 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  34 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  35 ORGANISM_TAXID: 4932;                                                
SOURCE  36 STRAIN: DELTA-RPB4;                                                  
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  39 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  40 ORGANISM_TAXID: 4932;                                                
SOURCE  41 STRAIN: DELTA-RPB4;                                                  
SOURCE  42 MOL_ID: 11;                                                          
SOURCE  43 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  44 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  45 ORGANISM_TAXID: 4932;                                                
SOURCE  46 STRAIN: DELTA-RPB4;                                                  
SOURCE  47 MOL_ID: 12;                                                          
SOURCE  48 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  49 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  50 ORGANISM_TAXID: 4932;                                                
SOURCE  51 STRAIN: DELTA-RPB4;                                                  
SOURCE  52 MOL_ID: 13;                                                          
SOURCE  53 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  54 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  55 ORGANISM_TAXID: 4932;                                                
SOURCE  56 STRAIN: DELTA-RPB4                                                   
KEYWDS    TRANSCRIPTION, MRNA, MULTIPROTEIN COMPLEX, MOLECULAR MACHINE, DNA,    
KEYWDS   2 TRANSFERASE-DNA-RNA HYBRID COMPLEX                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.WANG,D.A.BUSHNELL,K.D.WESTOVER,C.D.KAPLAN,R.D.KORNBERG              
REVDAT   3   25-OCT-23 2E2I    1       REMARK                                   
REVDAT   2   24-FEB-09 2E2I    1       VERSN                                    
REVDAT   1   19-DEC-06 2E2I    0                                                
JRNL        AUTH   D.WANG,D.A.BUSHNELL,K.D.WESTOVER,C.D.KAPLAN,R.D.KORNBERG     
JRNL        TITL   STRUCTURAL BASIS OF TRANSCRIPTION: ROLE OF THE TRIGGER LOOP  
JRNL        TITL 2 IN SUBSTRATE SPECIFICITY AND CATALYSIS                       
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 127   941 2006              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   17129781                                                     
JRNL        DOI    10.1016/J.CELL.2006.11.023                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 89433                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.269                           
REMARK   3   R VALUE            (WORKING SET) : 0.266                           
REMARK   3   FREE R VALUE                     : 0.316                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4732                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.41                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.50                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5822                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3860                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 303                          
REMARK   3   BIN FREE R VALUE                    : 0.3920                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 28587                                   
REMARK   3   NUCLEIC ACID ATOMS       : 1064                                    
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 116.8                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.42000                                              
REMARK   3    B22 (A**2) : -3.25000                                             
REMARK   3    B33 (A**2) : -3.81000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -7.20000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.637         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.899                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.867                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 30373 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 41254 ; 1.594 ; 2.017       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3576 ; 8.144 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1359 ;36.909 ;24.040       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5346 ;19.852 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   228 ;14.699 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4626 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 22366 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 13224 ; 0.259 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 20207 ; 0.316 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   699 ; 0.184 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    40 ; 0.276 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.334 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 17909 ; 1.898 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 29015 ; 2.332 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 12464 ; 1.429 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12239 ; 2.533 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2E2I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-NOV-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000026142.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 94186                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.56200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1R9T                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 390MM (NH4)2HPO4/NAH2PO4, PH 6.5, 50MM   
REMARK 280  DIOXANE, 10MM DTT, 9-11% PEG6000, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       84.34100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      111.76200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.34100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000      111.76200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
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: TRIDECAMERIC                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, T, N, A, B, C, E, F, H, I,         
REMARK 350                    AND CHAINS: J, K, L                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     GLY A   192                                                      
REMARK 465     ASP A   193                                                      
REMARK 465     ALA A   194                                                      
REMARK 465     ASP A   195                                                      
REMARK 465     GLU A   196                                                      
REMARK 465     PRO A   197                                                      
REMARK 465     ASN A  1082                                                      
REMARK 465     THR A  1083                                                      
REMARK 465     PHE A  1084                                                      
REMARK 465     HIS A  1085                                                      
REMARK 465     PHE A  1086                                                      
REMARK 465     ALA A  1087                                                      
REMARK 465     GLY A  1088                                                      
REMARK 465     VAL A  1089                                                      
REMARK 465     ALA A  1090                                                      
REMARK 465     SER A  1091                                                      
REMARK 465     LEU A  1177                                                      
REMARK 465     ASP A  1178                                                      
REMARK 465     GLU A  1179                                                      
REMARK 465     GLU A  1180                                                      
REMARK 465     ALA A  1181                                                      
REMARK 465     GLU A  1182                                                      
REMARK 465     GLN A  1183                                                      
REMARK 465     SER A  1184                                                      
REMARK 465     PHE A  1185                                                      
REMARK 465     ASP A  1186                                                      
REMARK 465     ARG A  1244                                                      
REMARK 465     PRO A  1245                                                      
REMARK 465     LYS A  1246                                                      
REMARK 465     SER A  1247                                                      
REMARK 465     LEU A  1248                                                      
REMARK 465     ASP A  1249                                                      
REMARK 465     ALA A  1250                                                      
REMARK 465     GLU A  1251                                                      
REMARK 465     THR A  1252                                                      
REMARK 465     GLU A  1253                                                      
REMARK 465     LEU A  1450                                                      
REMARK 465     VAL A  1451                                                      
REMARK 465     LYS A  1452                                                      
REMARK 465     TYR A  1453                                                      
REMARK 465     MET A  1454                                                      
REMARK 465     PRO A  1455                                                      
REMARK 465     GLU A  1456                                                      
REMARK 465     GLN A  1457                                                      
REMARK 465     LYS A  1458                                                      
REMARK 465     ILE A  1459                                                      
REMARK 465     THR A  1460                                                      
REMARK 465     GLU A  1461                                                      
REMARK 465     ILE A  1462                                                      
REMARK 465     GLU A  1463                                                      
REMARK 465     ASP A  1464                                                      
REMARK 465     GLY A  1465                                                      
REMARK 465     GLN A  1466                                                      
REMARK 465     ASP A  1467                                                      
REMARK 465     GLY A  1468                                                      
REMARK 465     GLY A  1469                                                      
REMARK 465     VAL A  1470                                                      
REMARK 465     THR A  1471                                                      
REMARK 465     PRO A  1472                                                      
REMARK 465     TYR A  1473                                                      
REMARK 465     SER A  1474                                                      
REMARK 465     ASN A  1475                                                      
REMARK 465     GLU A  1476                                                      
REMARK 465     SER A  1477                                                      
REMARK 465     GLY A  1478                                                      
REMARK 465     LEU A  1479                                                      
REMARK 465     VAL A  1480                                                      
REMARK 465     ASN A  1481                                                      
REMARK 465     ALA A  1482                                                      
REMARK 465     ASP A  1483                                                      
REMARK 465     LEU A  1484                                                      
REMARK 465     ASP A  1485                                                      
REMARK 465     VAL A  1486                                                      
REMARK 465     LYS A  1487                                                      
REMARK 465     ASP A  1488                                                      
REMARK 465     GLU A  1489                                                      
REMARK 465     LEU A  1490                                                      
REMARK 465     MET A  1491                                                      
REMARK 465     PHE A  1492                                                      
REMARK 465     SER A  1493                                                      
REMARK 465     PRO A  1494                                                      
REMARK 465     LEU A  1495                                                      
REMARK 465     VAL A  1496                                                      
REMARK 465     ASP A  1497                                                      
REMARK 465     SER A  1498                                                      
REMARK 465     GLY A  1499                                                      
REMARK 465     SER A  1500                                                      
REMARK 465     ASN A  1501                                                      
REMARK 465     ASP A  1502                                                      
REMARK 465     ALA A  1503                                                      
REMARK 465     MET A  1504                                                      
REMARK 465     ALA A  1505                                                      
REMARK 465     GLY A  1506                                                      
REMARK 465     GLY A  1507                                                      
REMARK 465     PHE A  1508                                                      
REMARK 465     THR A  1509                                                      
REMARK 465     ALA A  1510                                                      
REMARK 465     TYR A  1511                                                      
REMARK 465     GLY A  1512                                                      
REMARK 465     GLY A  1513                                                      
REMARK 465     ALA A  1514                                                      
REMARK 465     ASP A  1515                                                      
REMARK 465     TYR A  1516                                                      
REMARK 465     GLY A  1517                                                      
REMARK 465     GLU A  1518                                                      
REMARK 465     ALA A  1519                                                      
REMARK 465     THR A  1520                                                      
REMARK 465     SER A  1521                                                      
REMARK 465     PRO A  1522                                                      
REMARK 465     PHE A  1523                                                      
REMARK 465     GLY A  1524                                                      
REMARK 465     ALA A  1525                                                      
REMARK 465     TYR A  1526                                                      
REMARK 465     GLY A  1527                                                      
REMARK 465     GLU A  1528                                                      
REMARK 465     ALA A  1529                                                      
REMARK 465     PRO A  1530                                                      
REMARK 465     THR A  1531                                                      
REMARK 465     SER A  1532                                                      
REMARK 465     PRO A  1533                                                      
REMARK 465     GLY A  1534                                                      
REMARK 465     PHE A  1535                                                      
REMARK 465     GLY A  1536                                                      
REMARK 465     VAL A  1537                                                      
REMARK 465     SER A  1538                                                      
REMARK 465     SER A  1539                                                      
REMARK 465     PRO A  1540                                                      
REMARK 465     GLY A  1541                                                      
REMARK 465     PHE A  1542                                                      
REMARK 465     SER A  1543                                                      
REMARK 465     PRO A  1544                                                      
REMARK 465     THR A  1545                                                      
REMARK 465     SER A  1546                                                      
REMARK 465     PRO A  1547                                                      
REMARK 465     THR A  1548                                                      
REMARK 465     TYR A  1549                                                      
REMARK 465     SER A  1550                                                      
REMARK 465     PRO A  1551                                                      
REMARK 465     THR A  1552                                                      
REMARK 465     SER A  1553                                                      
REMARK 465     PRO A  1554                                                      
REMARK 465     ALA A  1555                                                      
REMARK 465     TYR A  1556                                                      
REMARK 465     SER A  1557                                                      
REMARK 465     PRO A  1558                                                      
REMARK 465     THR A  1559                                                      
REMARK 465     SER A  1560                                                      
REMARK 465     PRO A  1561                                                      
REMARK 465     SER A  1562                                                      
REMARK 465     TYR A  1563                                                      
REMARK 465     SER A  1564                                                      
REMARK 465     PRO A  1565                                                      
REMARK 465     THR A  1566                                                      
REMARK 465     SER A  1567                                                      
REMARK 465     PRO A  1568                                                      
REMARK 465     SER A  1569                                                      
REMARK 465     TYR A  1570                                                      
REMARK 465     SER A  1571                                                      
REMARK 465     PRO A  1572                                                      
REMARK 465     THR A  1573                                                      
REMARK 465     SER A  1574                                                      
REMARK 465     PRO A  1575                                                      
REMARK 465     SER A  1576                                                      
REMARK 465     TYR A  1577                                                      
REMARK 465     SER A  1578                                                      
REMARK 465     PRO A  1579                                                      
REMARK 465     THR A  1580                                                      
REMARK 465     SER A  1581                                                      
REMARK 465     PRO A  1582                                                      
REMARK 465     SER A  1583                                                      
REMARK 465     TYR A  1584                                                      
REMARK 465     SER A  1585                                                      
REMARK 465     PRO A  1586                                                      
REMARK 465     THR A  1587                                                      
REMARK 465     SER A  1588                                                      
REMARK 465     PRO A  1589                                                      
REMARK 465     SER A  1590                                                      
REMARK 465     TYR A  1591                                                      
REMARK 465     SER A  1592                                                      
REMARK 465     PRO A  1593                                                      
REMARK 465     THR A  1594                                                      
REMARK 465     SER A  1595                                                      
REMARK 465     PRO A  1596                                                      
REMARK 465     SER A  1597                                                      
REMARK 465     TYR A  1598                                                      
REMARK 465     SER A  1599                                                      
REMARK 465     PRO A  1600                                                      
REMARK 465     THR A  1601                                                      
REMARK 465     SER A  1602                                                      
REMARK 465     PRO A  1603                                                      
REMARK 465     SER A  1604                                                      
REMARK 465     TYR A  1605                                                      
REMARK 465     SER A  1606                                                      
REMARK 465     PRO A  1607                                                      
REMARK 465     THR A  1608                                                      
REMARK 465     SER A  1609                                                      
REMARK 465     PRO A  1610                                                      
REMARK 465     SER A  1611                                                      
REMARK 465     TYR A  1612                                                      
REMARK 465     SER A  1613                                                      
REMARK 465     PRO A  1614                                                      
REMARK 465     THR A  1615                                                      
REMARK 465     SER A  1616                                                      
REMARK 465     PRO A  1617                                                      
REMARK 465     SER A  1618                                                      
REMARK 465     TYR A  1619                                                      
REMARK 465     SER A  1620                                                      
REMARK 465     PRO A  1621                                                      
REMARK 465     THR A  1622                                                      
REMARK 465     SER A  1623                                                      
REMARK 465     PRO A  1624                                                      
REMARK 465     SER A  1625                                                      
REMARK 465     TYR A  1626                                                      
REMARK 465     SER A  1627                                                      
REMARK 465     PRO A  1628                                                      
REMARK 465     THR A  1629                                                      
REMARK 465     SER A  1630                                                      
REMARK 465     PRO A  1631                                                      
REMARK 465     SER A  1632                                                      
REMARK 465     TYR A  1633                                                      
REMARK 465     SER A  1634                                                      
REMARK 465     PRO A  1635                                                      
REMARK 465     THR A  1636                                                      
REMARK 465     SER A  1637                                                      
REMARK 465     PRO A  1638                                                      
REMARK 465     SER A  1639                                                      
REMARK 465     TYR A  1640                                                      
REMARK 465     SER A  1641                                                      
REMARK 465     PRO A  1642                                                      
REMARK 465     THR A  1643                                                      
REMARK 465     SER A  1644                                                      
REMARK 465     PRO A  1645                                                      
REMARK 465     SER A  1646                                                      
REMARK 465     TYR A  1647                                                      
REMARK 465     SER A  1648                                                      
REMARK 465     PRO A  1649                                                      
REMARK 465     THR A  1650                                                      
REMARK 465     SER A  1651                                                      
REMARK 465     PRO A  1652                                                      
REMARK 465     SER A  1653                                                      
REMARK 465     TYR A  1654                                                      
REMARK 465     SER A  1655                                                      
REMARK 465     PRO A  1656                                                      
REMARK 465     THR A  1657                                                      
REMARK 465     SER A  1658                                                      
REMARK 465     PRO A  1659                                                      
REMARK 465     ALA A  1660                                                      
REMARK 465     TYR A  1661                                                      
REMARK 465     SER A  1662                                                      
REMARK 465     PRO A  1663                                                      
REMARK 465     THR A  1664                                                      
REMARK 465     SER A  1665                                                      
REMARK 465     PRO A  1666                                                      
REMARK 465     SER A  1667                                                      
REMARK 465     TYR A  1668                                                      
REMARK 465     SER A  1669                                                      
REMARK 465     PRO A  1670                                                      
REMARK 465     THR A  1671                                                      
REMARK 465     SER A  1672                                                      
REMARK 465     PRO A  1673                                                      
REMARK 465     SER A  1674                                                      
REMARK 465     TYR A  1675                                                      
REMARK 465     SER A  1676                                                      
REMARK 465     PRO A  1677                                                      
REMARK 465     THR A  1678                                                      
REMARK 465     SER A  1679                                                      
REMARK 465     PRO A  1680                                                      
REMARK 465     SER A  1681                                                      
REMARK 465     TYR A  1682                                                      
REMARK 465     SER A  1683                                                      
REMARK 465     PRO A  1684                                                      
REMARK 465     THR A  1685                                                      
REMARK 465     SER A  1686                                                      
REMARK 465     PRO A  1687                                                      
REMARK 465     SER A  1688                                                      
REMARK 465     TYR A  1689                                                      
REMARK 465     SER A  1690                                                      
REMARK 465     PRO A  1691                                                      
REMARK 465     THR A  1692                                                      
REMARK 465     SER A  1693                                                      
REMARK 465     PRO A  1694                                                      
REMARK 465     ASN A  1695                                                      
REMARK 465     TYR A  1696                                                      
REMARK 465     SER A  1697                                                      
REMARK 465     PRO A  1698                                                      
REMARK 465     THR A  1699                                                      
REMARK 465     SER A  1700                                                      
REMARK 465     PRO A  1701                                                      
REMARK 465     SER A  1702                                                      
REMARK 465     TYR A  1703                                                      
REMARK 465     SER A  1704                                                      
REMARK 465     PRO A  1705                                                      
REMARK 465     THR A  1706                                                      
REMARK 465     SER A  1707                                                      
REMARK 465     PRO A  1708                                                      
REMARK 465     GLY A  1709                                                      
REMARK 465     TYR A  1710                                                      
REMARK 465     SER A  1711                                                      
REMARK 465     PRO A  1712                                                      
REMARK 465     GLY A  1713                                                      
REMARK 465     SER A  1714                                                      
REMARK 465     PRO A  1715                                                      
REMARK 465     ALA A  1716                                                      
REMARK 465     TYR A  1717                                                      
REMARK 465     SER A  1718                                                      
REMARK 465     PRO A  1719                                                      
REMARK 465     LYS A  1720                                                      
REMARK 465     GLN A  1721                                                      
REMARK 465     ASP A  1722                                                      
REMARK 465     GLU A  1723                                                      
REMARK 465     GLN A  1724                                                      
REMARK 465     LYS A  1725                                                      
REMARK 465     HIS A  1726                                                      
REMARK 465     ASN A  1727                                                      
REMARK 465     GLU A  1728                                                      
REMARK 465     ASN A  1729                                                      
REMARK 465     GLU A  1730                                                      
REMARK 465     ASN A  1731                                                      
REMARK 465     SER A  1732                                                      
REMARK 465     ARG A  1733                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ASN B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     TYR B    10                                                      
REMARK 465     TYR B    11                                                      
REMARK 465     ASP B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     ASP B    14                                                      
REMARK 465     PRO B    15                                                      
REMARK 465     TYR B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     PHE B    18                                                      
REMARK 465     GLU B    19                                                      
REMARK 465     LEU B    74                                                      
REMARK 465     ALA B    75                                                      
REMARK 465     GLN B    76                                                      
REMARK 465     HIS B    77                                                      
REMARK 465     THR B    78                                                      
REMARK 465     THR B    79                                                      
REMARK 465     GLU B    80                                                      
REMARK 465     SER B    81                                                      
REMARK 465     ASP B    82                                                      
REMARK 465     ASN B    83                                                      
REMARK 465     ILE B    84                                                      
REMARK 465     SER B    85                                                      
REMARK 465     ARG B    86                                                      
REMARK 465     LYS B    87                                                      
REMARK 465     LYS B   148                                                      
REMARK 465     TYR B   149                                                      
REMARK 465     GLU B   150                                                      
REMARK 465     LEU B   151                                                      
REMARK 465     ILE B   152                                                      
REMARK 465     ALA B   153                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     GLU B   155                                                      
REMARK 465     SER B   156                                                      
REMARK 465     GLU B   157                                                      
REMARK 465     ASP B   158                                                      
REMARK 465     ASP B   159                                                      
REMARK 465     SER B   160                                                      
REMARK 465     GLU B   161                                                      
REMARK 465     SER B   162                                                      
REMARK 465     GLY B   163                                                      
REMARK 465     GLU B   438                                                      
REMARK 465     ALA B   439                                                      
REMARK 465     HIS B   440                                                      
REMARK 465     ASP B   441                                                      
REMARK 465     PHE B   442                                                      
REMARK 465     ILE B   669                                                      
REMARK 465     GLU B   670                                                      
REMARK 465     GLY B   671                                                      
REMARK 465     GLY B   672                                                      
REMARK 465     PHE B   673                                                      
REMARK 465     GLU B   674                                                      
REMARK 465     ASP B   675                                                      
REMARK 465     ALA B   715                                                      
REMARK 465     ASN B   716                                                      
REMARK 465     GLU B   717                                                      
REMARK 465     GLU B   718                                                      
REMARK 465     ASN B   719                                                      
REMARK 465     ASP B   720                                                      
REMARK 465     LEU B   721                                                      
REMARK 465     PRO B   920                                                      
REMARK 465     ASP B   921                                                      
REMARK 465     GLU B   922                                                      
REMARK 465     GLU B   923                                                      
REMARK 465     GLU B   924                                                      
REMARK 465     LEU B   925                                                      
REMARK 465     GLY B   926                                                      
REMARK 465     GLN B   927                                                      
REMARK 465     ARG B   928                                                      
REMARK 465     THR B   929                                                      
REMARK 465     ALA B   930                                                      
REMARK 465     TYR B   931                                                      
REMARK 465     HIS B   932                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     LYS C   269                                                      
REMARK 465     VAL C   270                                                      
REMARK 465     ASN C   271                                                      
REMARK 465     PHE C   272                                                      
REMARK 465     ALA C   273                                                      
REMARK 465     SER C   274                                                      
REMARK 465     GLY C   275                                                      
REMARK 465     ASP C   276                                                      
REMARK 465     ASN C   277                                                      
REMARK 465     ASN C   278                                                      
REMARK 465     THR C   279                                                      
REMARK 465     ALA C   280                                                      
REMARK 465     SER C   281                                                      
REMARK 465     ASN C   282                                                      
REMARK 465     MET C   283                                                      
REMARK 465     LEU C   284                                                      
REMARK 465     GLY C   285                                                      
REMARK 465     SER C   286                                                      
REMARK 465     ASN C   287                                                      
REMARK 465     GLU C   288                                                      
REMARK 465     ASP C   289                                                      
REMARK 465     VAL C   290                                                      
REMARK 465     MET C   291                                                      
REMARK 465     MET C   292                                                      
REMARK 465     THR C   293                                                      
REMARK 465     GLY C   294                                                      
REMARK 465     ALA C   295                                                      
REMARK 465     GLU C   296                                                      
REMARK 465     GLN C   297                                                      
REMARK 465     ASP C   298                                                      
REMARK 465     PRO C   299                                                      
REMARK 465     TYR C   300                                                      
REMARK 465     SER C   301                                                      
REMARK 465     ASN C   302                                                      
REMARK 465     ALA C   303                                                      
REMARK 465     SER C   304                                                      
REMARK 465     GLN C   305                                                      
REMARK 465     MET C   306                                                      
REMARK 465     GLY C   307                                                      
REMARK 465     ASN C   308                                                      
REMARK 465     THR C   309                                                      
REMARK 465     GLY C   310                                                      
REMARK 465     SER C   311                                                      
REMARK 465     GLY C   312                                                      
REMARK 465     GLY C   313                                                      
REMARK 465     TYR C   314                                                      
REMARK 465     ASP C   315                                                      
REMARK 465     ASN C   316                                                      
REMARK 465     ALA C   317                                                      
REMARK 465     TRP C   318                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ASP E     2                                                      
REMARK 465     MET F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     ASP F     3                                                      
REMARK 465     TYR F     4                                                      
REMARK 465     GLU F     5                                                      
REMARK 465     GLU F     6                                                      
REMARK 465     ALA F     7                                                      
REMARK 465     PHE F     8                                                      
REMARK 465     ASN F     9                                                      
REMARK 465     ASP F    10                                                      
REMARK 465     GLY F    11                                                      
REMARK 465     ASN F    12                                                      
REMARK 465     GLU F    13                                                      
REMARK 465     ASN F    14                                                      
REMARK 465     PHE F    15                                                      
REMARK 465     GLU F    16                                                      
REMARK 465     ASP F    17                                                      
REMARK 465     PHE F    18                                                      
REMARK 465     ASP F    19                                                      
REMARK 465     VAL F    20                                                      
REMARK 465     GLU F    21                                                      
REMARK 465     HIS F    22                                                      
REMARK 465     PHE F    23                                                      
REMARK 465     SER F    24                                                      
REMARK 465     ASP F    25                                                      
REMARK 465     GLU F    26                                                      
REMARK 465     GLU F    27                                                      
REMARK 465     THR F    28                                                      
REMARK 465     TYR F    29                                                      
REMARK 465     GLU F    30                                                      
REMARK 465     GLU F    31                                                      
REMARK 465     LYS F    32                                                      
REMARK 465     PRO F    33                                                      
REMARK 465     GLN F    34                                                      
REMARK 465     PHE F    35                                                      
REMARK 465     LYS F    36                                                      
REMARK 465     ASP F    37                                                      
REMARK 465     GLY F    38                                                      
REMARK 465     GLU F    39                                                      
REMARK 465     THR F    40                                                      
REMARK 465     THR F    41                                                      
REMARK 465     ASP F    42                                                      
REMARK 465     ALA F    43                                                      
REMARK 465     ASN F    44                                                      
REMARK 465     GLY F    45                                                      
REMARK 465     LYS F    46                                                      
REMARK 465     THR F    47                                                      
REMARK 465     ILE F    48                                                      
REMARK 465     VAL F    49                                                      
REMARK 465     THR F    50                                                      
REMARK 465     GLY F    51                                                      
REMARK 465     GLY F    52                                                      
REMARK 465     ASN F    53                                                      
REMARK 465     GLY F    54                                                      
REMARK 465     PRO F    55                                                      
REMARK 465     GLU F    56                                                      
REMARK 465     ASP F    57                                                      
REMARK 465     PHE F    58                                                      
REMARK 465     GLN F    59                                                      
REMARK 465     GLN F    60                                                      
REMARK 465     HIS F    61                                                      
REMARK 465     GLU F    62                                                      
REMARK 465     GLN F    63                                                      
REMARK 465     ILE F    64                                                      
REMARK 465     ARG F    65                                                      
REMARK 465     ARG F    66                                                      
REMARK 465     LYS F    67                                                      
REMARK 465     THR F    68                                                      
REMARK 465     LEU F    69                                                      
REMARK 465     ASN H    64                                                      
REMARK 465     LEU H    65                                                      
REMARK 465     GLU H    66                                                      
REMARK 465     ASP H    67                                                      
REMARK 465     THR H    68                                                      
REMARK 465     PRO H    69                                                      
REMARK 465     ALA H    70                                                      
REMARK 465     ASN H    71                                                      
REMARK 465     ASP H    72                                                      
REMARK 465     SER H    73                                                      
REMARK 465     SER H    74                                                      
REMARK 465     ALA H    75                                                      
REMARK 465     MET I     1                                                      
REMARK 465     PHE I   121                                                      
REMARK 465     SER I   122                                                      
REMARK 465     LEU J    66                                                      
REMARK 465     GLU J    67                                                      
REMARK 465     LYS J    68                                                      
REMARK 465     ARG J    69                                                      
REMARK 465     ASP J    70                                                      
REMARK 465     ALA K   115                                                      
REMARK 465     ALA K   116                                                      
REMARK 465     ASP K   117                                                      
REMARK 465     ASP K   118                                                      
REMARK 465     ALA K   119                                                      
REMARK 465     PHE K   120                                                      
REMARK 465     MET L     1                                                      
REMARK 465     SER L     2                                                      
REMARK 465     ARG L     3                                                      
REMARK 465     GLU L     4                                                      
REMARK 465     GLY L     5                                                      
REMARK 465     PHE L     6                                                      
REMARK 465     GLN L     7                                                      
REMARK 465     ILE L     8                                                      
REMARK 465     PRO L     9                                                      
REMARK 465     THR L    10                                                      
REMARK 465     ASN L    11                                                      
REMARK 465     LEU L    12                                                      
REMARK 465     ASP L    13                                                      
REMARK 465     ALA L    14                                                      
REMARK 465     ALA L    15                                                      
REMARK 465     ALA L    16                                                      
REMARK 465     ALA L    17                                                      
REMARK 465     GLY L    18                                                      
REMARK 465     THR L    19                                                      
REMARK 465     SER L    20                                                      
REMARK 465     GLN L    21                                                      
REMARK 465     ALA L    22                                                      
REMARK 465     ARG L    23                                                      
REMARK 465     THR L    24                                                      
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       A R  10    O3'                                                 
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   SG   CYS B  1166     SG   CYS B  1185              1.53            
REMARK 500   SG   CYS A   107     SG   CYS A   148              2.03            
REMARK 500   SG   CYS J    10     SG   CYS J    46              2.05            
REMARK 500   SG   CYS A    67     SG   CYS A    77              2.05            
REMARK 500   SG   CYS I    78     SG   CYS I   106              2.05            
REMARK 500   SG   CYS L    48     SG   CYS L    51              2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DC T  18   C5'    DC T  18   C4'     0.045                       
REMARK 500     DA T  27   O3'    DA T  27   C3'    -0.047                       
REMARK 500    CYS B 302   CB    CYS B 302   SG     -0.098                       
REMARK 500    CYS C  86   CB    CYS C  86   SG     -0.106                       
REMARK 500    CYS J  10   CB    CYS J  10   SG      0.123                       
REMARK 500    CYS K  91   CB    CYS K  91   SG     -0.096                       
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      G R   6   N1  -  C6  -  O6  ANGL. DEV. =  -3.8 DEGREES          
REMARK 500      G R   9   C5' -  C4' -  C3' ANGL. DEV. = -15.2 DEGREES          
REMARK 500      G R   9   N9  -  C1' -  C2' ANGL. DEV. =  -6.6 DEGREES          
REMARK 500      G R   9   C8  -  N9  -  C4  ANGL. DEV. =  -2.4 DEGREES          
REMARK 500      G R   9   C3' -  O3' -  P   ANGL. DEV. = -10.1 DEGREES          
REMARK 500     DC T   1   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES          
REMARK 500     DC T   4   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DA T  10   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DC T  12   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DA T  15   C3' -  O3' -  P   ANGL. DEV. =   8.9 DEGREES          
REMARK 500     DC T  16   O4' -  C1' -  N1  ANGL. DEV. =   4.0 DEGREES          
REMARK 500     DC T  18   O4' -  C4' -  C3' ANGL. DEV. =  -8.4 DEGREES          
REMARK 500     DC T  18   C5' -  C4' -  C3' ANGL. DEV. =   7.5 DEGREES          
REMARK 500     DC T  18   C5' -  C4' -  O4' ANGL. DEV. =   6.8 DEGREES          
REMARK 500     DC T  18   C1' -  O4' -  C4' ANGL. DEV. =  -8.7 DEGREES          
REMARK 500     DC T  18   C4' -  C3' -  O3' ANGL. DEV. =  12.6 DEGREES          
REMARK 500     DC T  18   C4' -  C3' -  C2' ANGL. DEV. = -10.1 DEGREES          
REMARK 500     DC T  18   O4' -  C1' -  N1  ANGL. DEV. =   5.0 DEGREES          
REMARK 500     DT T  28   C1' -  O4' -  C4' ANGL. DEV. = -12.8 DEGREES          
REMARK 500     DT T  28   O4' -  C1' -  N1  ANGL. DEV. =   5.7 DEGREES          
REMARK 500     DG N   3   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DT N   5   C1' -  O4' -  C4' ANGL. DEV. =  -8.3 DEGREES          
REMARK 500     DT N   5   O4' -  C1' -  N1  ANGL. DEV. =   4.0 DEGREES          
REMARK 500     DT N   6   C1' -  O4' -  C4' ANGL. DEV. =  -6.4 DEGREES          
REMARK 500     DT N   6   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DG N  10   C3' -  O3' -  P   ANGL. DEV. =   8.5 DEGREES          
REMARK 500     DT N  12   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 839   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    LEU B  69   CA  -  CB  -  CG  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    ARG B 485   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    LEU B 492   CA  -  CB  -  CG  ANGL. DEV. = -16.3 DEGREES          
REMARK 500    PRO B 636   C   -  N   -  CA  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    PRO B 799   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    CYS J  10   CA  -  CB  -  SG  ANGL. DEV. =   8.6 DEGREES          
REMARK 500    CYS J  45   CA  -  CB  -  SG  ANGL. DEV. =   6.8 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    VAL A  27      -58.12    -27.35                                   
REMARK 500    VAL A  32       -1.84   -148.18                                   
REMARK 500    ILE A  35       79.11     62.16                                   
REMARK 500    THR A  40      -83.31    -88.70                                   
REMARK 500    GLU A  43       74.99   -105.65                                   
REMARK 500    THR A  44       83.05     50.05                                   
REMARK 500    GLN A  45      -22.37     66.84                                   
REMARK 500    ARG A  47       44.09    -82.41                                   
REMARK 500    ALA A  48     -138.19    -87.03                                   
REMARK 500    LYS A  49      -43.60   -140.11                                   
REMARK 500    ILE A  50      155.55     57.52                                   
REMARK 500    ASP A  55      -54.17   -170.40                                   
REMARK 500    PRO A  56      -30.61    -23.28                                   
REMARK 500    ARG A  57       -4.25   -156.75                                   
REMARK 500    ASP A  62       48.92    -91.75                                   
REMARK 500    ARG A  63       13.83     51.67                                   
REMARK 500    GLN A  68       84.26     50.89                                   
REMARK 500    THR A  69      -43.53     66.73                                   
REMARK 500    GLN A  71     -149.22     48.71                                   
REMARK 500    ASN A  75       35.77    -93.12                                   
REMARK 500    GLU A  76      -41.62   -169.28                                   
REMARK 500    PRO A  89      135.43    -36.45                                   
REMARK 500    GLU A 117       -8.91    -55.95                                   
REMARK 500    ASP A 130      150.40     77.08                                   
REMARK 500    CYS A 142      -16.15   -151.77                                   
REMARK 500    GLU A 149      144.98     67.86                                   
REMARK 500    VAL A 152      133.29     92.31                                   
REMARK 500    SER A 154      -65.53   -100.31                                   
REMARK 500    GLU A 155      -39.06   -175.58                                   
REMARK 500    GLN A 160     -178.20     75.32                                   
REMARK 500    ARG A 164      -72.43   -155.70                                   
REMARK 500    CYS A 167      -78.66   -136.19                                   
REMARK 500    LYS A 186       44.90    -96.45                                   
REMARK 500    LYS A 187       64.20   -111.09                                   
REMARK 500    ARG A 189     -147.45   -111.29                                   
REMARK 500    LEU A 199       86.01     78.29                                   
REMARK 500    HIS A 213     -117.08    -90.64                                   
REMARK 500    ILE A 214      136.30     64.10                                   
REMARK 500    PRO A 245      -13.37    -40.97                                   
REMARK 500    ARG A 247       68.90   -155.17                                   
REMARK 500    PRO A 248     -143.92    -66.55                                   
REMARK 500    SER A 249     -159.11   -176.66                                   
REMARK 500    ILE A 250      147.95     42.72                                   
REMARK 500    SER A 251      -67.62   -169.80                                   
REMARK 500    ASN A 253      129.13    164.99                                   
REMARK 500    GLN A 256       41.10     89.09                                   
REMARK 500    ASN A 282     -153.06   -118.16                                   
REMARK 500    HIS A 286      -76.99    -80.00                                   
REMARK 500    HIS A 287       45.40    -94.64                                   
REMARK 500    ILE A 308      -85.26   -124.31                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     372 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 PRO A  248     SER A  249                 -147.83                    
REMARK 500 ILE A  250     SER A  251                  135.46                    
REMARK 500 SER A  251     PHE A  252                  131.16                    
REMARK 500 PHE A  252     ASN A  253                  -88.04                    
REMARK 500 GLU A  254     SER A  255                  -65.47                    
REMARK 500 VAL A  460     LYS A  461                  147.89                    
REMARK 500 SER A 1175     LEU A 1176                  110.49                    
REMARK 500 LEU B   71     GLU B   72                   93.73                    
REMARK 500 GLU B   89     ILE B   90                   55.03                    
REMARK 500 ASP B  141     VAL B  142                 -145.96                    
REMARK 500 PRO B  143     GLY B  144                   35.13                    
REMARK 500 ARG B  145     GLU B  146                   55.25                    
REMARK 500 ILE B  502     GLY B  503                 -126.52                    
REMARK 500 GLY B  503     ARG B  504                 -137.09                    
REMARK 500 ARG B  504     ASP B  505                 -131.07                    
REMARK 500 GLY B  506     LYS B  507                  121.95                    
REMARK 500 LEU B  508     ALA B  509                  103.23                    
REMARK 500 PRO B  636     LEU B  637                  -36.87                    
REMARK 500 SER E   70     LYS E   71                 -141.94                    
REMARK 500 VAL J    3     PRO J    4                  146.68                    
REMARK 500 PRO J    4     VAL J    5                  128.99                    
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 A1735  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  67   SG                                                     
REMARK 620 2 CYS A  70   SG  118.4                                              
REMARK 620 3 CYS A  77   SG   47.5 137.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1734  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 110   SG                                                     
REMARK 620 2 CYS A 167   SG  116.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1307  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1163   SG                                                     
REMARK 620 2 CYS B1185   SG  108.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 319  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  86   SG                                                     
REMARK 620 2 CYS C  88   SG   80.2                                              
REMARK 620 3 CYS C  92   SG  101.1 115.5                                        
REMARK 620 4 CYS C  95   SG   99.3 119.3 123.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 203  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS I  10   SG                                                     
REMARK 620 2 CYS I  29   SG   92.3                                              
REMARK 620 3 CYS I  32   SG  148.8 118.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 204  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS I  75   SG                                                     
REMARK 620 2 CYS I  78   SG  136.9                                              
REMARK 620 3 CYS I 103   SG  109.2 113.0                                        
REMARK 620 4 CYS I 106   SG  109.3  57.0 117.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J   7   SG                                                     
REMARK 620 2 CYS J  10   SG   98.2                                              
REMARK 620 3 CYS J  45   SG  152.1 105.2                                        
REMARK 620 4 CYS J  46   SG  127.0  55.4  79.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 105  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS L  34   SG                                                     
REMARK 620 2 CYS L  48   SG  128.6                                              
REMARK 620 3 CYS L  51   SG  100.8  51.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1734                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1735                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 319                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 105                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGT B 1308                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SFO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1R9S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1R9T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2E2H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2E2J   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2NVQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2NVS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2NVT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2NVX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2NVY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2NVZ   RELATED DB: PDB                                   
DBREF  2E2I A    1  1733  UNP    P04050   RPB1_YEAST       1   1733             
DBREF  2E2I B    1  1224  UNP    P08518   RPB2_YEAST       1   1224             
DBREF  2E2I C    1   318  UNP    P16370   RPB3_YEAST       1    318             
DBREF  2E2I E    1   215  UNP    P20434   RPB5_YEAST       1    215             
DBREF  2E2I F    1   155  UNP    P20435   RPB6_YEAST       1    155             
DBREF  2E2I H    1   146  UNP    P20436   RPB8_YEAST       1    146             
DBREF  2E2I I    1   122  UNP    P27999   RPB9_YEAST       1    122             
DBREF  2E2I J    1    70  UNP    P22139   RPAB5_YEAST      1     70             
DBREF  2E2I K    1   120  UNP    P38902   RPB11_YEAST      1    120             
DBREF  2E2I L    1    70  UNP    P40422   RPAB4_YEAST      1     70             
DBREF  2E2I R    1    10  PDB    2E2I     2E2I             1     10             
DBREF  2E2I T    1    28  PDB    2E2I     2E2I             1     28             
DBREF  2E2I N    1    14  PDB    2E2I     2E2I             1     14             
SEQRES   1 R   10    A   U   C   G   A   G   A   G   G   A                      
SEQRES   1 T   28   DC  DT  DA  DC  DC  DG  DA  DT  DA  DA  DG  DC  DA          
SEQRES   2 T   28   DG  DA  DC  DG  DC  DT  DC  DC  DT  DC  DT  DC  DG          
SEQRES   3 T   28   DA  DT                                                      
SEQRES   1 N   14   DC  DT  DG  DC  DT  DT  DA  DT  DC  DG  DG  DT  DA          
SEQRES   2 N   14   DG                                                          
SEQRES   1 A 1733  MET VAL GLY GLN GLN TYR SER SER ALA PRO LEU ARG THR          
SEQRES   2 A 1733  VAL LYS GLU VAL GLN PHE GLY LEU PHE SER PRO GLU GLU          
SEQRES   3 A 1733  VAL ARG ALA ILE SER VAL ALA LYS ILE ARG PHE PRO GLU          
SEQRES   4 A 1733  THR MET ASP GLU THR GLN THR ARG ALA LYS ILE GLY GLY          
SEQRES   5 A 1733  LEU ASN ASP PRO ARG LEU GLY SER ILE ASP ARG ASN LEU          
SEQRES   6 A 1733  LYS CYS GLN THR CYS GLN GLU GLY MET ASN GLU CYS PRO          
SEQRES   7 A 1733  GLY HIS PHE GLY HIS ILE ASP LEU ALA LYS PRO VAL PHE          
SEQRES   8 A 1733  HIS VAL GLY PHE ILE ALA LYS ILE LYS LYS VAL CYS GLU          
SEQRES   9 A 1733  CYS VAL CYS MET HIS CYS GLY LYS LEU LEU LEU ASP GLU          
SEQRES  10 A 1733  HIS ASN GLU LEU MET ARG GLN ALA LEU ALA ILE LYS ASP          
SEQRES  11 A 1733  SER LYS LYS ARG PHE ALA ALA ILE TRP THR LEU CYS LYS          
SEQRES  12 A 1733  THR LYS MET VAL CYS GLU THR ASP VAL PRO SER GLU ASP          
SEQRES  13 A 1733  ASP PRO THR GLN LEU VAL SER ARG GLY GLY CYS GLY ASN          
SEQRES  14 A 1733  THR GLN PRO THR ILE ARG LYS ASP GLY LEU LYS LEU VAL          
SEQRES  15 A 1733  GLY SER TRP LYS LYS ASP ARG ALA THR GLY ASP ALA ASP          
SEQRES  16 A 1733  GLU PRO GLU LEU ARG VAL LEU SER THR GLU GLU ILE LEU          
SEQRES  17 A 1733  ASN ILE PHE LYS HIS ILE SER VAL LYS ASP PHE THR SER          
SEQRES  18 A 1733  LEU GLY PHE ASN GLU VAL PHE SER ARG PRO GLU TRP MET          
SEQRES  19 A 1733  ILE LEU THR CYS LEU PRO VAL PRO PRO PRO PRO VAL ARG          
SEQRES  20 A 1733  PRO SER ILE SER PHE ASN GLU SER GLN ARG GLY GLU ASP          
SEQRES  21 A 1733  ASP LEU THR PHE LYS LEU ALA ASP ILE LEU LYS ALA ASN          
SEQRES  22 A 1733  ILE SER LEU GLU THR LEU GLU HIS ASN GLY ALA PRO HIS          
SEQRES  23 A 1733  HIS ALA ILE GLU GLU ALA GLU SER LEU LEU GLN PHE HIS          
SEQRES  24 A 1733  VAL ALA THR TYR MET ASP ASN ASP ILE ALA GLY GLN PRO          
SEQRES  25 A 1733  GLN ALA LEU GLN LYS SER GLY ARG PRO VAL LYS SER ILE          
SEQRES  26 A 1733  ARG ALA ARG LEU LYS GLY LYS GLU GLY ARG ILE ARG GLY          
SEQRES  27 A 1733  ASN LEU MET GLY LYS ARG VAL ASP PHE SER ALA ARG THR          
SEQRES  28 A 1733  VAL ILE SER GLY ASP PRO ASN LEU GLU LEU ASP GLN VAL          
SEQRES  29 A 1733  GLY VAL PRO LYS SER ILE ALA LYS THR LEU THR TYR PRO          
SEQRES  30 A 1733  GLU VAL VAL THR PRO TYR ASN ILE ASP ARG LEU THR GLN          
SEQRES  31 A 1733  LEU VAL ARG ASN GLY PRO ASN GLU HIS PRO GLY ALA LYS          
SEQRES  32 A 1733  TYR VAL ILE ARG ASP SER GLY ASP ARG ILE ASP LEU ARG          
SEQRES  33 A 1733  TYR SER LYS ARG ALA GLY ASP ILE GLN LEU GLN TYR GLY          
SEQRES  34 A 1733  TRP LYS VAL GLU ARG HIS ILE MET ASP ASN ASP PRO VAL          
SEQRES  35 A 1733  LEU PHE ASN ARG GLN PRO SER LEU HIS LYS MET SER MET          
SEQRES  36 A 1733  MET ALA HIS ARG VAL LYS VAL ILE PRO TYR SER THR PHE          
SEQRES  37 A 1733  ARG LEU ASN LEU SER VAL THR SER PRO TYR ASN ALA ASP          
SEQRES  38 A 1733  PHE ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN SER          
SEQRES  39 A 1733  GLU GLU THR ARG ALA GLU LEU SER GLN LEU CYS ALA VAL          
SEQRES  40 A 1733  PRO LEU GLN ILE VAL SER PRO GLN SER ASN LYS PRO CYS          
SEQRES  41 A 1733  MET GLY ILE VAL GLN ASP THR LEU CYS GLY ILE ARG LYS          
SEQRES  42 A 1733  LEU THR LEU ARG ASP THR PHE ILE GLU LEU ASP GLN VAL          
SEQRES  43 A 1733  LEU ASN MET LEU TYR TRP VAL PRO ASP TRP ASP GLY VAL          
SEQRES  44 A 1733  ILE PRO THR PRO ALA ILE ILE LYS PRO LYS PRO LEU TRP          
SEQRES  45 A 1733  SER GLY LYS GLN ILE LEU SER VAL ALA ILE PRO ASN GLY          
SEQRES  46 A 1733  ILE HIS LEU GLN ARG PHE ASP GLU GLY THR THR LEU LEU          
SEQRES  47 A 1733  SER PRO LYS ASP ASN GLY MET LEU ILE ILE ASP GLY GLN          
SEQRES  48 A 1733  ILE ILE PHE GLY VAL VAL GLU LYS LYS THR VAL GLY SER          
SEQRES  49 A 1733  SER ASN GLY GLY LEU ILE HIS VAL VAL THR ARG GLU LYS          
SEQRES  50 A 1733  GLY PRO GLN VAL CYS ALA LYS LEU PHE GLY ASN ILE GLN          
SEQRES  51 A 1733  LYS VAL VAL ASN PHE TRP LEU LEU HIS ASN GLY PHE SER          
SEQRES  52 A 1733  THR GLY ILE GLY ASP THR ILE ALA ASP GLY PRO THR MET          
SEQRES  53 A 1733  ARG GLU ILE THR GLU THR ILE ALA GLU ALA LYS LYS LYS          
SEQRES  54 A 1733  VAL LEU ASP VAL THR LYS GLU ALA GLN ALA ASN LEU LEU          
SEQRES  55 A 1733  THR ALA LYS HIS GLY MET THR LEU ARG GLU SER PHE GLU          
SEQRES  56 A 1733  ASP ASN VAL VAL ARG PHE LEU ASN GLU ALA ARG ASP LYS          
SEQRES  57 A 1733  ALA GLY ARG LEU ALA GLU VAL ASN LEU LYS ASP LEU ASN          
SEQRES  58 A 1733  ASN VAL LYS GLN MET VAL MET ALA GLY SER LYS GLY SER          
SEQRES  59 A 1733  PHE ILE ASN ILE ALA GLN MET SER ALA CYS VAL GLY GLN          
SEQRES  60 A 1733  GLN SER VAL GLU GLY LYS ARG ILE ALA PHE GLY PHE VAL          
SEQRES  61 A 1733  ASP ARG THR LEU PRO HIS PHE SER LYS ASP ASP TYR SER          
SEQRES  62 A 1733  PRO GLU SER LYS GLY PHE VAL GLU ASN SER TYR LEU ARG          
SEQRES  63 A 1733  GLY LEU THR PRO GLN GLU PHE PHE PHE HIS ALA MET GLY          
SEQRES  64 A 1733  GLY ARG GLU GLY LEU ILE ASP THR ALA VAL LYS THR ALA          
SEQRES  65 A 1733  GLU THR GLY TYR ILE GLN ARG ARG LEU VAL LYS ALA LEU          
SEQRES  66 A 1733  GLU ASP ILE MET VAL HIS TYR ASP ASN THR THR ARG ASN          
SEQRES  67 A 1733  SER LEU GLY ASN VAL ILE GLN PHE ILE TYR GLY GLU ASP          
SEQRES  68 A 1733  GLY MET ASP ALA ALA HIS ILE GLU LYS GLN SER LEU ASP          
SEQRES  69 A 1733  THR ILE GLY GLY SER ASP ALA ALA PHE GLU LYS ARG TYR          
SEQRES  70 A 1733  ARG VAL ASP LEU LEU ASN THR ASP HIS THR LEU ASP PRO          
SEQRES  71 A 1733  SER LEU LEU GLU SER GLY SER GLU ILE LEU GLY ASP LEU          
SEQRES  72 A 1733  LYS LEU GLN VAL LEU LEU ASP GLU GLU TYR LYS GLN LEU          
SEQRES  73 A 1733  VAL LYS ASP ARG LYS PHE LEU ARG GLU VAL PHE VAL ASP          
SEQRES  74 A 1733  GLY GLU ALA ASN TRP PRO LEU PRO VAL ASN ILE ARG ARG          
SEQRES  75 A 1733  ILE ILE GLN ASN ALA GLN GLN THR PHE HIS ILE ASP HIS          
SEQRES  76 A 1733  THR LYS PRO SER ASP LEU THR ILE LYS ASP ILE VAL LEU          
SEQRES  77 A 1733  GLY VAL LYS ASP LEU GLN GLU ASN LEU LEU VAL LEU ARG          
SEQRES  78 A 1733  GLY LYS ASN GLU ILE ILE GLN ASN ALA GLN ARG ASP ALA          
SEQRES  79 A 1733  VAL THR LEU PHE CYS CYS LEU LEU ARG SER ARG LEU ALA          
SEQRES  80 A 1733  THR ARG ARG VAL LEU GLN GLU TYR ARG LEU THR LYS GLN          
SEQRES  81 A 1733  ALA PHE ASP TRP VAL LEU SER ASN ILE GLU ALA GLN PHE          
SEQRES  82 A 1733  LEU ARG SER VAL VAL HIS PRO GLY GLU MET VAL GLY VAL          
SEQRES  83 A 1733  LEU ALA ALA GLN SER ILE GLY GLU PRO ALA THR GLN MET          
SEQRES  84 A 1733  THR LEU ASN THR PHE HIS PHE ALA GLY VAL ALA SER LYS          
SEQRES  85 A 1733  LYS VAL THR SER GLY VAL PRO ARG LEU LYS GLU ILE LEU          
SEQRES  86 A 1733  ASN VAL ALA LYS ASN MET LYS THR PRO SER LEU THR VAL          
SEQRES  87 A 1733  TYR LEU GLU PRO GLY HIS ALA ALA ASP GLN GLU GLN ALA          
SEQRES  88 A 1733  LYS LEU ILE ARG SER ALA ILE GLU HIS THR THR LEU LYS          
SEQRES  89 A 1733  SER VAL THR ILE ALA SER GLU ILE TYR TYR ASP PRO ASP          
SEQRES  90 A 1733  PRO ARG SER THR VAL ILE PRO GLU ASP GLU GLU ILE ILE          
SEQRES  91 A 1733  GLN LEU HIS PHE SER LEU LEU ASP GLU GLU ALA GLU GLN          
SEQRES  92 A 1733  SER PHE ASP GLN GLN SER PRO TRP LEU LEU ARG LEU GLU          
SEQRES  93 A 1733  LEU ASP ARG ALA ALA MET ASN ASP LYS ASP LEU THR MET          
SEQRES  94 A 1733  GLY GLN VAL GLY GLU ARG ILE LYS GLN THR PHE LYS ASN          
SEQRES  95 A 1733  ASP LEU PHE VAL ILE TRP SER GLU ASP ASN ASP GLU LYS          
SEQRES  96 A 1733  LEU ILE ILE ARG CYS ARG VAL VAL ARG PRO LYS SER LEU          
SEQRES  97 A 1733  ASP ALA GLU THR GLU ALA GLU GLU ASP HIS MET LEU LYS          
SEQRES  98 A 1733  LYS ILE GLU ASN THR MET LEU GLU ASN ILE THR LEU ARG          
SEQRES  99 A 1733  GLY VAL GLU ASN ILE GLU ARG VAL VAL MET MET LYS TYR          
SEQRES 100 A 1733  ASP ARG LYS VAL PRO SER PRO THR GLY GLU TYR VAL LYS          
SEQRES 101 A 1733  GLU PRO GLU TRP VAL LEU GLU THR ASP GLY VAL ASN LEU          
SEQRES 102 A 1733  SER GLU VAL MET THR VAL PRO GLY ILE ASP PRO THR ARG          
SEQRES 103 A 1733  ILE TYR THR ASN SER PHE ILE ASP ILE MET GLU VAL LEU          
SEQRES 104 A 1733  GLY ILE GLU ALA GLY ARG ALA ALA LEU TYR LYS GLU VAL          
SEQRES 105 A 1733  TYR ASN VAL ILE ALA SER ASP GLY SER TYR VAL ASN TYR          
SEQRES 106 A 1733  ARG HIS MET ALA LEU LEU VAL ASP VAL MET THR THR GLN          
SEQRES 107 A 1733  GLY GLY LEU THR SER VAL THR ARG HIS GLY PHE ASN ARG          
SEQRES 108 A 1733  SER ASN THR GLY ALA LEU MET ARG CYS SER PHE GLU GLU          
SEQRES 109 A 1733  THR VAL GLU ILE LEU PHE GLU ALA GLY ALA SER ALA GLU          
SEQRES 110 A 1733  LEU ASP ASP CYS ARG GLY VAL SER GLU ASN VAL ILE LEU          
SEQRES 111 A 1733  GLY GLN MET ALA PRO ILE GLY THR GLY ALA PHE ASP VAL          
SEQRES 112 A 1733  MET ILE ASP GLU GLU SER LEU VAL LYS TYR MET PRO GLU          
SEQRES 113 A 1733  GLN LYS ILE THR GLU ILE GLU ASP GLY GLN ASP GLY GLY          
SEQRES 114 A 1733  VAL THR PRO TYR SER ASN GLU SER GLY LEU VAL ASN ALA          
SEQRES 115 A 1733  ASP LEU ASP VAL LYS ASP GLU LEU MET PHE SER PRO LEU          
SEQRES 116 A 1733  VAL ASP SER GLY SER ASN ASP ALA MET ALA GLY GLY PHE          
SEQRES 117 A 1733  THR ALA TYR GLY GLY ALA ASP TYR GLY GLU ALA THR SER          
SEQRES 118 A 1733  PRO PHE GLY ALA TYR GLY GLU ALA PRO THR SER PRO GLY          
SEQRES 119 A 1733  PHE GLY VAL SER SER PRO GLY PHE SER PRO THR SER PRO          
SEQRES 120 A 1733  THR TYR SER PRO THR SER PRO ALA TYR SER PRO THR SER          
SEQRES 121 A 1733  PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO THR          
SEQRES 122 A 1733  SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO          
SEQRES 123 A 1733  THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER          
SEQRES 124 A 1733  PRO THR SER PRO SER TYR SER PRO THR SER PRO SER TYR          
SEQRES 125 A 1733  SER PRO THR SER PRO SER TYR SER PRO THR SER PRO SER          
SEQRES 126 A 1733  TYR SER PRO THR SER PRO SER TYR SER PRO THR SER PRO          
SEQRES 127 A 1733  SER TYR SER PRO THR SER PRO SER TYR SER PRO THR SER          
SEQRES 128 A 1733  PRO SER TYR SER PRO THR SER PRO ALA TYR SER PRO THR          
SEQRES 129 A 1733  SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO          
SEQRES 130 A 1733  THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER          
SEQRES 131 A 1733  PRO THR SER PRO ASN TYR SER PRO THR SER PRO SER TYR          
SEQRES 132 A 1733  SER PRO THR SER PRO GLY TYR SER PRO GLY SER PRO ALA          
SEQRES 133 A 1733  TYR SER PRO LYS GLN ASP GLU GLN LYS HIS ASN GLU ASN          
SEQRES 134 A 1733  GLU ASN SER ARG                                              
SEQRES   1 B 1224  MET SER ASP LEU ALA ASN SER GLU LYS TYR TYR ASP GLU          
SEQRES   2 B 1224  ASP PRO TYR GLY PHE GLU ASP GLU SER ALA PRO ILE THR          
SEQRES   3 B 1224  ALA GLU ASP SER TRP ALA VAL ILE SER ALA PHE PHE ARG          
SEQRES   4 B 1224  GLU LYS GLY LEU VAL SER GLN GLN LEU ASP SER PHE ASN          
SEQRES   5 B 1224  GLN PHE VAL ASP TYR THR LEU GLN ASP ILE ILE CYS GLU          
SEQRES   6 B 1224  ASP SER THR LEU ILE LEU GLU GLN LEU ALA GLN HIS THR          
SEQRES   7 B 1224  THR GLU SER ASP ASN ILE SER ARG LYS TYR GLU ILE SER          
SEQRES   8 B 1224  PHE GLY LYS ILE TYR VAL THR LYS PRO MET VAL ASN GLU          
SEQRES   9 B 1224  SER ASP GLY VAL THR HIS ALA LEU TYR PRO GLN GLU ALA          
SEQRES  10 B 1224  ARG LEU ARG ASN LEU THR TYR SER SER GLY LEU PHE VAL          
SEQRES  11 B 1224  ASP VAL LYS LYS ARG THR TYR GLU ALA ILE ASP VAL PRO          
SEQRES  12 B 1224  GLY ARG GLU LEU LYS TYR GLU LEU ILE ALA GLU GLU SER          
SEQRES  13 B 1224  GLU ASP ASP SER GLU SER GLY LYS VAL PHE ILE GLY ARG          
SEQRES  14 B 1224  LEU PRO ILE MET LEU ARG SER LYS ASN CYS TYR LEU SER          
SEQRES  15 B 1224  GLU ALA THR GLU SER ASP LEU TYR LYS LEU LYS GLU CYS          
SEQRES  16 B 1224  PRO PHE ASP MET GLY GLY TYR PHE ILE ILE ASN GLY SER          
SEQRES  17 B 1224  GLU LYS VAL LEU ILE ALA GLN GLU ARG SER ALA GLY ASN          
SEQRES  18 B 1224  ILE VAL GLN VAL PHE LYS LYS ALA ALA PRO SER PRO ILE          
SEQRES  19 B 1224  SER HIS VAL ALA GLU ILE ARG SER ALA LEU GLU LYS GLY          
SEQRES  20 B 1224  SER ARG PHE ILE SER THR LEU GLN VAL LYS LEU TYR GLY          
SEQRES  21 B 1224  ARG GLU GLY SER SER ALA ARG THR ILE LYS ALA THR LEU          
SEQRES  22 B 1224  PRO TYR ILE LYS GLN ASP ILE PRO ILE VAL ILE ILE PHE          
SEQRES  23 B 1224  ARG ALA LEU GLY ILE ILE PRO ASP GLY GLU ILE LEU GLU          
SEQRES  24 B 1224  HIS ILE CYS TYR ASP VAL ASN ASP TRP GLN MET LEU GLU          
SEQRES  25 B 1224  MET LEU LYS PRO CYS VAL GLU ASP GLY PHE VAL ILE GLN          
SEQRES  26 B 1224  ASP ARG GLU THR ALA LEU ASP PHE ILE GLY ARG ARG GLY          
SEQRES  27 B 1224  THR ALA LEU GLY ILE LYS LYS GLU LYS ARG ILE GLN TYR          
SEQRES  28 B 1224  ALA LYS ASP ILE LEU GLN LYS GLU PHE LEU PRO HIS ILE          
SEQRES  29 B 1224  THR GLN LEU GLU GLY PHE GLU SER ARG LYS ALA PHE PHE          
SEQRES  30 B 1224  LEU GLY TYR MET ILE ASN ARG LEU LEU LEU CYS ALA LEU          
SEQRES  31 B 1224  ASP ARG LYS ASP GLN ASP ASP ARG ASP HIS PHE GLY LYS          
SEQRES  32 B 1224  LYS ARG LEU ASP LEU ALA GLY PRO LEU LEU ALA GLN LEU          
SEQRES  33 B 1224  PHE LYS THR LEU PHE LYS LYS LEU THR LYS ASP ILE PHE          
SEQRES  34 B 1224  ARG TYR MET GLN ARG THR VAL GLU GLU ALA HIS ASP PHE          
SEQRES  35 B 1224  ASN MET LYS LEU ALA ILE ASN ALA LYS THR ILE THR SER          
SEQRES  36 B 1224  GLY LEU LYS TYR ALA LEU ALA THR GLY ASN TRP GLY GLU          
SEQRES  37 B 1224  GLN LYS LYS ALA MET SER SER ARG ALA GLY VAL SER GLN          
SEQRES  38 B 1224  VAL LEU ASN ARG TYR THR TYR SER SER THR LEU SER HIS          
SEQRES  39 B 1224  LEU ARG ARG THR ASN THR PRO ILE GLY ARG ASP GLY LYS          
SEQRES  40 B 1224  LEU ALA LYS PRO ARG GLN LEU HIS ASN THR HIS TRP GLY          
SEQRES  41 B 1224  LEU VAL CYS PRO ALA GLU THR PRO GLU GLY GLN ALA CYS          
SEQRES  42 B 1224  GLY LEU VAL LYS ASN LEU SER LEU MET SER CYS ILE SER          
SEQRES  43 B 1224  VAL GLY THR ASP PRO MET PRO ILE ILE THR PHE LEU SER          
SEQRES  44 B 1224  GLU TRP GLY MET GLU PRO LEU GLU ASP TYR VAL PRO HIS          
SEQRES  45 B 1224  GLN SER PRO ASP ALA THR ARG VAL PHE VAL ASN GLY VAL          
SEQRES  46 B 1224  TRP HIS GLY VAL HIS ARG ASN PRO ALA ARG LEU MET GLU          
SEQRES  47 B 1224  THR LEU ARG THR LEU ARG ARG LYS GLY ASP ILE ASN PRO          
SEQRES  48 B 1224  GLU VAL SER MET ILE ARG ASP ILE ARG GLU LYS GLU LEU          
SEQRES  49 B 1224  LYS ILE PHE THR ASP ALA GLY ARG VAL TYR ARG PRO LEU          
SEQRES  50 B 1224  PHE ILE VAL GLU ASP ASP GLU SER LEU GLY HIS LYS GLU          
SEQRES  51 B 1224  LEU LYS VAL ARG LYS GLY HIS ILE ALA LYS LEU MET ALA          
SEQRES  52 B 1224  THR GLU TYR GLN ASP ILE GLU GLY GLY PHE GLU ASP VAL          
SEQRES  53 B 1224  GLU GLU TYR THR TRP SER SER LEU LEU ASN GLU GLY LEU          
SEQRES  54 B 1224  VAL GLU TYR ILE ASP ALA GLU GLU GLU GLU SER ILE LEU          
SEQRES  55 B 1224  ILE ALA MET GLN PRO GLU ASP LEU GLU PRO ALA GLU ALA          
SEQRES  56 B 1224  ASN GLU GLU ASN ASP LEU ASP VAL ASP PRO ALA LYS ARG          
SEQRES  57 B 1224  ILE ARG VAL SER HIS HIS ALA THR THR PHE THR HIS CYS          
SEQRES  58 B 1224  GLU ILE HIS PRO SER MET ILE LEU GLY VAL ALA ALA SER          
SEQRES  59 B 1224  ILE ILE PRO PHE PRO ASP HIS ASN GLN SER PRO ARG ASN          
SEQRES  60 B 1224  THR TYR GLN SER ALA MET GLY LYS GLN ALA MET GLY VAL          
SEQRES  61 B 1224  PHE LEU THR ASN TYR ASN VAL ARG MET ASP THR MET ALA          
SEQRES  62 B 1224  ASN ILE LEU TYR TYR PRO GLN LYS PRO LEU GLY THR THR          
SEQRES  63 B 1224  ARG ALA MET GLU TYR LEU LYS PHE ARG GLU LEU PRO ALA          
SEQRES  64 B 1224  GLY GLN ASN ALA ILE VAL ALA ILE ALA CYS TYR SER GLY          
SEQRES  65 B 1224  TYR ASN GLN GLU ASP SER MET ILE MET ASN GLN SER SER          
SEQRES  66 B 1224  ILE ASP ARG GLY LEU PHE ARG SER LEU PHE PHE ARG SER          
SEQRES  67 B 1224  TYR MET ASP GLN GLU LYS LYS TYR GLY MET SER ILE THR          
SEQRES  68 B 1224  GLU THR PHE GLU LYS PRO GLN ARG THR ASN THR LEU ARG          
SEQRES  69 B 1224  MET LYS HIS GLY THR TYR ASP LYS LEU ASP ASP ASP GLY          
SEQRES  70 B 1224  LEU ILE ALA PRO GLY VAL ARG VAL SER GLY GLU ASP VAL          
SEQRES  71 B 1224  ILE ILE GLY LYS THR THR PRO ILE SER PRO ASP GLU GLU          
SEQRES  72 B 1224  GLU LEU GLY GLN ARG THR ALA TYR HIS SER LYS ARG ASP          
SEQRES  73 B 1224  ALA SER THR PRO LEU ARG SER THR GLU ASN GLY ILE VAL          
SEQRES  74 B 1224  ASP GLN VAL LEU VAL THR THR ASN GLN ASP GLY LEU LYS          
SEQRES  75 B 1224  PHE VAL LYS VAL ARG VAL ARG THR THR LYS ILE PRO GLN          
SEQRES  76 B 1224  ILE GLY ASP LYS PHE ALA SER ARG HIS GLY GLN LYS GLY          
SEQRES  77 B 1224  THR ILE GLY ILE THR TYR ARG ARG GLU ASP MET PRO PHE          
SEQRES  78 B 1224  THR ALA GLU GLY ILE VAL PRO ASP LEU ILE ILE ASN PRO          
SEQRES  79 B 1224  HIS ALA ILE PRO SER ARG MET THR VAL ALA HIS LEU ILE          
SEQRES  80 B 1224  GLU CYS LEU LEU SER LYS VAL ALA ALA LEU SER GLY ASN          
SEQRES  81 B 1224  GLU GLY ASP ALA SER PRO PHE THR ASP ILE THR VAL GLU          
SEQRES  82 B 1224  GLY ILE SER LYS LEU LEU ARG GLU HIS GLY TYR GLN SER          
SEQRES  83 B 1224  ARG GLY PHE GLU VAL MET TYR ASN GLY HIS THR GLY LYS          
SEQRES  84 B 1224  LYS LEU MET ALA GLN ILE PHE PHE GLY PRO THR TYR TYR          
SEQRES  85 B 1224  GLN ARG LEU ARG HIS MET VAL ASP ASP LYS ILE HIS ALA          
SEQRES  86 B 1224  ARG ALA ARG GLY PRO MET GLN VAL LEU THR ARG GLN PRO          
SEQRES  87 B 1224  VAL GLU GLY ARG SER ARG ASP GLY GLY LEU ARG PHE GLY          
SEQRES  88 B 1224  GLU MET GLU ARG ASP CYS MET ILE ALA HIS GLY ALA ALA          
SEQRES  89 B 1224  SER PHE LEU LYS GLU ARG LEU MET GLU ALA SER ASP ALA          
SEQRES  90 B 1224  PHE ARG VAL HIS ILE CYS GLY ILE CYS GLY LEU MET THR          
SEQRES  91 B 1224  VAL ILE ALA LYS LEU ASN HIS ASN GLN PHE GLU CYS LYS          
SEQRES  92 B 1224  GLY CYS ASP ASN LYS ILE ASP ILE TYR GLN ILE HIS ILE          
SEQRES  93 B 1224  PRO TYR ALA ALA LYS LEU LEU PHE GLN GLU LEU MET ALA          
SEQRES  94 B 1224  MET ASN ILE THR PRO ARG LEU TYR THR ASP ARG SER ARG          
SEQRES  95 B 1224  ASP PHE                                                      
SEQRES   1 C  318  MET SER GLU GLU GLY PRO GLN VAL LYS ILE ARG GLU ALA          
SEQRES   2 C  318  SER LYS ASP ASN VAL ASP PHE ILE LEU SER ASN VAL ASP          
SEQRES   3 C  318  LEU ALA MET ALA ASN SER LEU ARG ARG VAL MET ILE ALA          
SEQRES   4 C  318  GLU ILE PRO THR LEU ALA ILE ASP SER VAL GLU VAL GLU          
SEQRES   5 C  318  THR ASN THR THR VAL LEU ALA ASP GLU PHE ILE ALA HIS          
SEQRES   6 C  318  ARG LEU GLY LEU ILE PRO LEU GLN SER MET ASP ILE GLU          
SEQRES   7 C  318  GLN LEU GLU TYR SER ARG ASP CYS PHE CYS GLU ASP HIS          
SEQRES   8 C  318  CYS ASP LYS CYS SER VAL VAL LEU THR LEU GLN ALA PHE          
SEQRES   9 C  318  GLY GLU SER GLU SER THR THR ASN VAL TYR SER LYS ASP          
SEQRES  10 C  318  LEU VAL ILE VAL SER ASN LEU MET GLY ARG ASN ILE GLY          
SEQRES  11 C  318  HIS PRO ILE ILE GLN ASP LYS GLU GLY ASN GLY VAL LEU          
SEQRES  12 C  318  ILE CYS LYS LEU ARG LYS GLY GLN GLU LEU LYS LEU THR          
SEQRES  13 C  318  CYS VAL ALA LYS LYS GLY ILE ALA LYS GLU HIS ALA LYS          
SEQRES  14 C  318  TRP GLY PRO ALA ALA ALA ILE GLU PHE GLU TYR ASP PRO          
SEQRES  15 C  318  TRP ASN LYS LEU LYS HIS THR ASP TYR TRP TYR GLU GLN          
SEQRES  16 C  318  ASP SER ALA LYS GLU TRP PRO GLN SER LYS ASN CYS GLU          
SEQRES  17 C  318  TYR GLU ASP PRO PRO ASN GLU GLY ASP PRO PHE ASP TYR          
SEQRES  18 C  318  LYS ALA GLN ALA ASP THR PHE TYR MET ASN VAL GLU SER          
SEQRES  19 C  318  VAL GLY SER ILE PRO VAL ASP GLN VAL VAL VAL ARG GLY          
SEQRES  20 C  318  ILE ASP THR LEU GLN LYS LYS VAL ALA SER ILE LEU LEU          
SEQRES  21 C  318  ALA LEU THR GLN MET ASP GLN ASP LYS VAL ASN PHE ALA          
SEQRES  22 C  318  SER GLY ASP ASN ASN THR ALA SER ASN MET LEU GLY SER          
SEQRES  23 C  318  ASN GLU ASP VAL MET MET THR GLY ALA GLU GLN ASP PRO          
SEQRES  24 C  318  TYR SER ASN ALA SER GLN MET GLY ASN THR GLY SER GLY          
SEQRES  25 C  318  GLY TYR ASP ASN ALA TRP                                      
SEQRES   1 E  215  MET ASP GLN GLU ASN GLU ARG ASN ILE SER ARG LEU TRP          
SEQRES   2 E  215  ARG ALA PHE ARG THR VAL LYS GLU MET VAL LYS ASP ARG          
SEQRES   3 E  215  GLY TYR PHE ILE THR GLN GLU GLU VAL GLU LEU PRO LEU          
SEQRES   4 E  215  GLU ASP PHE LYS ALA LYS TYR CYS ASP SER MET GLY ARG          
SEQRES   5 E  215  PRO GLN ARG LYS MET MET SER PHE GLN ALA ASN PRO THR          
SEQRES   6 E  215  GLU GLU SER ILE SER LYS PHE PRO ASP MET GLY SER LEU          
SEQRES   7 E  215  TRP VAL GLU PHE CYS ASP GLU PRO SER VAL GLY VAL LYS          
SEQRES   8 E  215  THR MET LYS THR PHE VAL ILE HIS ILE GLN GLU LYS ASN          
SEQRES   9 E  215  PHE GLN THR GLY ILE PHE VAL TYR GLN ASN ASN ILE THR          
SEQRES  10 E  215  PRO SER ALA MET LYS LEU VAL PRO SER ILE PRO PRO ALA          
SEQRES  11 E  215  THR ILE GLU THR PHE ASN GLU ALA ALA LEU VAL VAL ASN          
SEQRES  12 E  215  ILE THR HIS HIS GLU LEU VAL PRO LYS HIS ILE ARG LEU          
SEQRES  13 E  215  SER SER ASP GLU LYS ARG GLU LEU LEU LYS ARG TYR ARG          
SEQRES  14 E  215  LEU LYS GLU SER GLN LEU PRO ARG ILE GLN ARG ALA ASP          
SEQRES  15 E  215  PRO VAL ALA LEU TYR LEU GLY LEU LYS ARG GLY GLU VAL          
SEQRES  16 E  215  VAL LYS ILE ILE ARG LYS SER GLU THR SER GLY ARG TYR          
SEQRES  17 E  215  ALA SER TYR ARG ILE CYS MET                                  
SEQRES   1 F  155  MET SER ASP TYR GLU GLU ALA PHE ASN ASP GLY ASN GLU          
SEQRES   2 F  155  ASN PHE GLU ASP PHE ASP VAL GLU HIS PHE SER ASP GLU          
SEQRES   3 F  155  GLU THR TYR GLU GLU LYS PRO GLN PHE LYS ASP GLY GLU          
SEQRES   4 F  155  THR THR ASP ALA ASN GLY LYS THR ILE VAL THR GLY GLY          
SEQRES   5 F  155  ASN GLY PRO GLU ASP PHE GLN GLN HIS GLU GLN ILE ARG          
SEQRES   6 F  155  ARG LYS THR LEU LYS GLU LYS ALA ILE PRO LYS ASP GLN          
SEQRES   7 F  155  ARG ALA THR THR PRO TYR MET THR LYS TYR GLU ARG ALA          
SEQRES   8 F  155  ARG ILE LEU GLY THR ARG ALA LEU GLN ILE SER MET ASN          
SEQRES   9 F  155  ALA PRO VAL PHE VAL ASP LEU GLU GLY GLU THR ASP PRO          
SEQRES  10 F  155  LEU ARG ILE ALA MET LYS GLU LEU ALA GLU LYS LYS ILE          
SEQRES  11 F  155  PRO LEU VAL ILE ARG ARG TYR LEU PRO ASP GLY SER PHE          
SEQRES  12 F  155  GLU ASP TRP SER VAL GLU GLU LEU ILE VAL ASP LEU              
SEQRES   1 H  146  MET SER ASN THR LEU PHE ASP ASP ILE PHE GLN VAL SER          
SEQRES   2 H  146  GLU VAL ASP PRO GLY ARG TYR ASN LYS VAL CYS ARG ILE          
SEQRES   3 H  146  GLU ALA ALA SER THR THR GLN ASP GLN CYS LYS LEU THR          
SEQRES   4 H  146  LEU ASP ILE ASN VAL GLU LEU PHE PRO VAL ALA ALA GLN          
SEQRES   5 H  146  ASP SER LEU THR VAL THR ILE ALA SER SER LEU ASN LEU          
SEQRES   6 H  146  GLU ASP THR PRO ALA ASN ASP SER SER ALA THR ARG SER          
SEQRES   7 H  146  TRP ARG PRO PRO GLN ALA GLY ASP ARG SER LEU ALA ASP          
SEQRES   8 H  146  ASP TYR ASP TYR VAL MET TYR GLY THR ALA TYR LYS PHE          
SEQRES   9 H  146  GLU GLU VAL SER LYS ASP LEU ILE ALA VAL TYR TYR SER          
SEQRES  10 H  146  PHE GLY GLY LEU LEU MET ARG LEU GLU GLY ASN TYR ARG          
SEQRES  11 H  146  ASN LEU ASN ASN LEU LYS GLN GLU ASN ALA TYR LEU LEU          
SEQRES  12 H  146  ILE ARG ARG                                                  
SEQRES   1 I  122  MET THR THR PHE ARG PHE CYS ARG ASP CYS ASN ASN MET          
SEQRES   2 I  122  LEU TYR PRO ARG GLU ASP LYS GLU ASN ASN ARG LEU LEU          
SEQRES   3 I  122  PHE GLU CYS ARG THR CYS SER TYR VAL GLU GLU ALA GLY          
SEQRES   4 I  122  SER PRO LEU VAL TYR ARG HIS GLU LEU ILE THR ASN ILE          
SEQRES   5 I  122  GLY GLU THR ALA GLY VAL VAL GLN ASP ILE GLY SER ASP          
SEQRES   6 I  122  PRO THR LEU PRO ARG SER ASP ARG GLU CYS PRO LYS CYS          
SEQRES   7 I  122  HIS SER ARG GLU ASN VAL PHE PHE GLN SER GLN GLN ARG          
SEQRES   8 I  122  ARG LYS ASP THR SER MET VAL LEU PHE PHE VAL CYS LEU          
SEQRES   9 I  122  SER CYS SER HIS ILE PHE THR SER ASP GLN LYS ASN LYS          
SEQRES  10 I  122  ARG THR GLN PHE SER                                          
SEQRES   1 J   70  MET ILE VAL PRO VAL ARG CYS PHE SER CYS GLY LYS VAL          
SEQRES   2 J   70  VAL GLY ASP LYS TRP GLU SER TYR LEU ASN LEU LEU GLN          
SEQRES   3 J   70  GLU ASP GLU LEU ASP GLU GLY THR ALA LEU SER ARG LEU          
SEQRES   4 J   70  GLY LEU LYS ARG TYR CYS CYS ARG ARG MET ILE LEU THR          
SEQRES   5 J   70  HIS VAL ASP LEU ILE GLU LYS PHE LEU ARG TYR ASN PRO          
SEQRES   6 J   70  LEU GLU LYS ARG ASP                                          
SEQRES   1 K  120  MET ASN ALA PRO ASP ARG PHE GLU LEU PHE LEU LEU GLY          
SEQRES   2 K  120  GLU GLY GLU SER LYS LEU LYS ILE ASP PRO ASP THR LYS          
SEQRES   3 K  120  ALA PRO ASN ALA VAL VAL ILE THR PHE GLU LYS GLU ASP          
SEQRES   4 K  120  HIS THR LEU GLY ASN LEU ILE ARG ALA GLU LEU LEU ASN          
SEQRES   5 K  120  ASP ARG LYS VAL LEU PHE ALA ALA TYR LYS VAL GLU HIS          
SEQRES   6 K  120  PRO PHE PHE ALA ARG PHE LYS LEU ARG ILE GLN THR THR          
SEQRES   7 K  120  GLU GLY TYR ASP PRO LYS ASP ALA LEU LYS ASN ALA CYS          
SEQRES   8 K  120  ASN SER ILE ILE ASN LYS LEU GLY ALA LEU LYS THR ASN          
SEQRES   9 K  120  PHE GLU THR GLU TRP ASN LEU GLN THR LEU ALA ALA ASP          
SEQRES  10 K  120  ASP ALA PHE                                                  
SEQRES   1 L   70  MET SER ARG GLU GLY PHE GLN ILE PRO THR ASN LEU ASP          
SEQRES   2 L   70  ALA ALA ALA ALA GLY THR SER GLN ALA ARG THR ALA THR          
SEQRES   3 L   70  LEU LYS TYR ILE CYS ALA GLU CYS SER SER LYS LEU SER          
SEQRES   4 L   70  LEU SER ARG THR ASP ALA VAL ARG CYS LYS ASP CYS GLY          
SEQRES   5 L   70  HIS ARG ILE LEU LEU LYS ALA ARG THR LYS ARG LEU VAL          
SEQRES   6 L   70  GLN PHE GLU ALA ARG                                          
HET     ZN  A1734       1                                                       
HET     ZN  A1735       1                                                       
HET     MG  A2001       1                                                       
HET     ZN  B1307       1                                                       
HET    DGT  B1308      62                                                       
HET     ZN  C 319       1                                                       
HET     ZN  I 203       1                                                       
HET     ZN  I 204       1                                                       
HET     ZN  J 101       1                                                       
HET     ZN  L 105       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     DGT 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE                                
FORMUL  14   ZN    8(ZN 2+)                                                     
FORMUL  16   MG    MG 2+                                                        
FORMUL  18  DGT    C10 H16 N5 O13 P3                                            
HELIX    1   1 SER A   23  SER A   31  1                                   9    
HELIX    2   2 HIS A   92  PHE A   95  5                                   4    
HELIX    3   3 ILE A   96  GLU A  104  1                                   9    
HELIX    4   4 MET A  122  ALA A  127  1                                   6    
HELIX    5   5 SER A  131  LEU A  141  1                                  11    
HELIX    6   6 SER A  203  LYS A  212  1                                  10    
HELIX    7   7 SER A  215  LEU A  222  1                                   8    
HELIX    8   8 PRO A  243  ARG A  247  5                                   5    
HELIX    9   9 ASP A  261  ILE A  274  1                                  14    
HELIX   10  10 LEU A  276  HIS A  281  1                                   6    
HELIX   11  11 ILE A  289  TYR A  303  1                                  15    
HELIX   12  12 SER A  324  LYS A  330  1                                   7    
HELIX   13  13 GLY A  334  LEU A  340  1                                   7    
HELIX   14  14 LYS A  368  LEU A  374  1                                   7    
HELIX   15  15 ASN A  384  GLY A  395  1                                  12    
HELIX   16  16 VAL A  474  ASN A  479  1                                   6    
HELIX   17  17 SER A  494  GLN A  503  1                                  10    
HELIX   18  18 VAL A  507  GLN A  510  5                                   4    
HELIX   19  19 GLN A  525  LEU A  536  1                                  12    
HELIX   20  20 LEU A  543  VAL A  553  1                                  11    
HELIX   21  21 GLY A  574  SER A  579  1                                   6    
HELIX   22  22 GLU A  618  GLY A  623  1                                   6    
HELIX   23  23 GLY A  628  GLY A  638  1                                  11    
HELIX   24  24 GLY A  638  GLY A  661  1                                  24    
HELIX   25  25 ASP A  672  ALA A  699  1                                  28    
HELIX   26  26 THR A  709  LEU A  737  1                                  29    
HELIX   27  27 ASN A  741  GLY A  750  1                                  10    
HELIX   28  28 SER A  754  ALA A  763  1                                  10    
HELIX   29  29 THR A  809  THR A  827  1                                  19    
HELIX   30  30 VAL A  829  GLU A  846  1                                  18    
HELIX   31  31 ILE A  867  ASP A  871  5                                   5    
HELIX   32  32 SER A  889  ARG A  898  1                                  10    
HELIX   33  33 LYS A  924  PHE A  947  1                                  24    
HELIX   34  34 ASN A  959  GLN A  969  1                                  11    
HELIX   35  35 THR A  982  ASN A  996  1                                  15    
HELIX   36  36 ASN A 1004  ALA A 1014  1                                  11    
HELIX   37  37 VAL A 1015  LEU A 1026  1                                  12    
HELIX   38  38 ALA A 1027  GLU A 1034  1                                   8    
HELIX   39  39 THR A 1038  VAL A 1057  1                                  20    
HELIX   40  40 MET A 1063  THR A 1077  1                                  15    
HELIX   41  41 GLY A 1097  VAL A 1107  1                                  11    
HELIX   42  42 ASP A 1127  SER A 1136  1                                  10    
HELIX   43  43 ILE A 1163  GLU A 1165  5                                   3    
HELIX   44  44 ASP A 1166  LEU A 1172  1                                   7    
HELIX   45  45 ALA A 1200  LYS A 1205  1                                   6    
HELIX   46  46 THR A 1208  LYS A 1221  1                                  14    
HELIX   47  47 LEU A 1260  ASN A 1270  1                                  11    
HELIX   48  48 ASN A 1312  MET A 1317  1                                   6    
HELIX   49  49 SER A 1331  GLY A 1340  1                                  10    
HELIX   50  50 GLY A 1340  SER A 1358  1                                  19    
HELIX   51  51 ASN A 1364  THR A 1377  1                                  14    
HELIX   52  52 LEU A 1397  SER A 1401  5                                   5    
HELIX   53  53 GLU A 1404  SER A 1415  1                                  12    
HELIX   54  54 GLY A 1423  GLY A 1431  1                                   9    
HELIX   55  55 ILE A 1436  ALA A 1440  5                                   5    
HELIX   56  56 ASP B   29  GLU B   40  1                                  12    
HELIX   57  57 VAL B   44  TYR B   57  1                                  14    
HELIX   58  58 TYR B   57  CYS B   64  1                                   8    
HELIX   59  59 TYR B  113  ARG B  120  1                                   8    
HELIX   60  60 TYR B  180  ALA B  184  5                                   5    
HELIX   61  61 THR B  185  LEU B  192  1                                   8    
HELIX   62  62 ILE B  282  LEU B  289  1                                   8    
HELIX   63  63 ILE B  297  ILE B  301  5                                   5    
HELIX   64  64 ASP B  307  ASP B  320  1                                  14    
HELIX   65  65 ASP B  326  LEU B  331  1                                   6    
HELIX   66  66 GLU B  346  GLU B  359  1                                  14    
HELIX   67  67 PHE B  370  LEU B  390  1                                  21    
HELIX   68  68 HIS B  400  GLY B  402  5                                   3    
HELIX   69  69 LEU B  408  GLN B  433  1                                  26    
HELIX   70  70 ASN B  449  GLY B  464  1                                  16    
HELIX   71  71 MET B  473  GLY B  478  5                                   6    
HELIX   72  72 THR B  487  ARG B  496  1                                  10    
HELIX   73  73 HIS B  515  TRP B  519  5                                   5    
HELIX   74  74 PRO B  551  GLU B  560  1                                  10    
HELIX   75  75 ASN B  592  GLY B  607  1                                  16    
HELIX   76  76 ARG B  654  GLN B  667  1                                  14    
HELIX   77  77 THR B  680  GLY B  688  1                                   9    
HELIX   78  78 GLU B  696  SER B  700  5                                   5    
HELIX   79  79 GLN B  706  GLU B  711  1                                   6    
HELIX   80  80 HIS B  744  LEU B  749  5                                   6    
HELIX   81  81 VAL B  751  ILE B  756  5                                   6    
HELIX   82  82 GLN B  763  GLY B  774  1                                  12    
HELIX   83  83 LYS B  775  ALA B  777  5                                   3    
HELIX   84  84 THR B  806  TYR B  811  5                                   6    
HELIX   85  85 LYS B  813  LEU B  817  5                                   5    
HELIX   86  86 ASN B  842  GLY B  849  1                                   8    
HELIX   87  87 PRO B 1014  ILE B 1017  5                                   4    
HELIX   88  88 THR B 1022  GLY B 1039  1                                  18    
HELIX   89  89 THR B 1051  GLY B 1063  1                                  13    
HELIX   90  90 MET B 1098  ILE B 1103  1                                   6    
HELIX   91  91 GLY B 1131  GLY B 1142  1                                  12    
HELIX   92  92 ALA B 1143  ARG B 1150  1                                   8    
HELIX   93  93 PRO B 1197  ALA B 1209  1                                  13    
HELIX   94  94 ASP C   26  ILE C   41  1                                  16    
HELIX   95  95 ALA C   59  ILE C   70  1                                  12    
HELIX   96  96 ASP C   76  LEU C   80  5                                   5    
HELIX   97  97 HIS C  167  GLY C  171  5                                   5    
HELIX   98  98 ASP C  196  TRP C  201  1                                   6    
HELIX   99  99 SER C  204  GLU C  208  5                                   5    
HELIX  100 100 PRO C  239  GLN C  264  1                                  26    
HELIX  101 101 GLU E    6  ASP E   25  1                                  20    
HELIX  102 102 THR E   31  GLU E   36  1                                   6    
HELIX  103 103 PRO E   38  TYR E   46  1                                   9    
HELIX  104 104 GLY E   89  ASN E  104  1                                  16    
HELIX  105 105 THR E  117  LYS E  122  1                                   6    
HELIX  106 106 ASN E  143  HIS E  147  5                                   5    
HELIX  107 107 SER E  157  TYR E  168  1                                  12    
HELIX  108 108 LYS E  171  LEU E  175  5                                   5    
HELIX  109 109 ASP E  182  GLY E  189  1                                   8    
HELIX  110 110 THR F   86  SER F  102  1                                  17    
HELIX  111 111 LEU F  118  GLU F  127  1                                  10    
HELIX  112 112 VAL I   59  ASP I   65  5                                   7    
HELIX  113 113 VAL J   14  ASP J   16  5                                   3    
HELIX  114 114 LYS J   17  GLU J   27  1                                  11    
HELIX  115 115 ASP J   31  LEU J   39  1                                   9    
HELIX  116 116 ARG J   43  CYS J   46  5                                   4    
HELIX  117 117 ARG J   47  THR J   52  1                                   6    
HELIX  118 118 LEU J   56  ARG J   62  1                                   7    
HELIX  119 119 ASP K    5  PHE K   10  5                                   6    
HELIX  120 120 ASP K   39  ASP K   53  1                                  15    
HELIX  121 121 ASP K   82  ASN K  110  1                                  29    
SHEET    1   A 3 LEU A1418  ASP A1419  0                                        
SHEET    2   A 3 GLU A  16  GLN A  18 -1  N  VAL A  17   O  ASP A1419           
SHEET    3   A 3 ARG B1215  TYR B1217 -1  O  TYR B1217   N  GLU A  16           
SHEET    1   B 2 GLY A  82  HIS A  83  0                                        
SHEET    2   B 2 PRO A 240  VAL A 241 -1  O  VAL A 241   N  GLY A  82           
SHEET    1   C 3 ARG A 175  ASP A 177  0                                        
SHEET    2   C 3 LYS A 180  GLY A 183 -1  O  VAL A 182   N  ARG A 175           
SHEET    3   C 3 ARG A 200  LEU A 202 -1  O  LEU A 202   N  LEU A 181           
SHEET    1   D 2 LYS A 343  ARG A 344  0                                        
SHEET    2   D 2 ARG B1129  PHE B1130 -1  O  PHE B1130   N  LYS A 343           
SHEET    1   E 8 HIS B1104  ARG B1106  0                                        
SHEET    2   E 8 SER A 348  GLY A 355 -1  N  SER A 348   O  ARG B1106           
SHEET    3   E 8 GLU A 486  HIS A 490 -1  O  MET A 487   N  THR A 351           
SHEET    4   E 8 PRO A 441  ASN A 445 -1  N  LEU A 443   O  HIS A 490           
SHEET    5   E 8 MET A 455  ILE A 463 -1  O  HIS A 458   N  VAL A 442           
SHEET    6   E 8 GLN A 363  PRO A 367  1  N  VAL A 366   O  ILE A 463           
SHEET    7   E 8 PHE A 468  LEU A 470 -1  O  ARG A 469   N  GLY A 365           
SHEET    8   E 8 SER A 348  GLY A 355  1  N  VAL A 352   O  PHE A 468           
SHEET    1   F 3 ARG A 412  ILE A 413  0                                        
SHEET    2   F 3 ALA A 402  ILE A 406 -1  N  VAL A 405   O  ILE A 413           
SHEET    3   F 3 LYS A 431  ARG A 434 -1  O  LYS A 431   N  ILE A 406           
SHEET    1   G 2 VAL A 512  SER A 513  0                                        
SHEET    2   G 2 LYS A 518  PRO A 519 -1  O  LYS A 518   N  SER A 513           
SHEET    1   H 2 PHE A 540  GLU A 542  0                                        
SHEET    2   H 2 LEU A 571  SER A 573 -1  O  TRP A 572   N  ILE A 541           
SHEET    1   I 3 LEU A 588  GLN A 589  0                                        
SHEET    2   I 3 LEU A 606  ILE A 608 -1  O  ILE A 607   N  LEU A 588           
SHEET    3   I 3 GLN A 611  PHE A 614 -1  O  ILE A 613   N  LEU A 606           
SHEET    1   J 2 GLY A 766  GLN A 767  0                                        
SHEET    2   J 2 PHE A 799  VAL A 800 -1  O  VAL A 800   N  GLY A 766           
SHEET    1   K 3 MET A 849  VAL A 850  0                                        
SHEET    2   K 3 THR A 856  ARG A 857 -1  O  ARG A 857   N  MET A 849           
SHEET    3   K 3 VAL A 863  GLN A 865 -1  O  GLN A 865   N  THR A 856           
SHEET    1   L 2 GLU A 879  SER A 882  0                                        
SHEET    2   L 2 ASN A 953  LEU A 956 -1  O  TRP A 954   N  GLN A 881           
SHEET    1   M 4 VAL A1283  PRO A1292  0                                        
SHEET    2   M 4 TYR A1298  GLU A1307 -1  O  VAL A1305   N  MET A1285           
SHEET    3   M 4 LEU A1116  TYR A1119 -1  N  VAL A1118   O  LEU A1306           
SHEET    4   M 4 TYR A1328  THR A1329 -1  O  TYR A1328   N  THR A1117           
SHEET    1   N 2 THR A1141  THR A1142  0                                        
SHEET    2   N 2 THR A1272  ARG A1274 -1  O  LEU A1273   N  THR A1141           
SHEET    1   O 5 LEU A1224  TRP A1228  0                                        
SHEET    2   O 5 ILE A1237  VAL A1242 -1  O  ARG A1239   N  ILE A1227           
SHEET    3   O 5 TRP A1191  LEU A1197 -1  N  LEU A1193   O  CYS A1240           
SHEET    4   O 5 THR A1147  TYR A1154 -1  N  GLU A1151   O  ARG A1194           
SHEET    5   O 5 LEU I  42  ARG I  45 -1  O  VAL I  43   N  ILE A1152           
SHEET    1   P 3 ASP A1442  MET A1444  0                                        
SHEET    2   P 3 VAL F 133  TYR F 137 -1  O  VAL F 133   N  MET A1444           
SHEET    3   P 3 PHE F 143  SER F 147 -1  O  TRP F 146   N  ILE F 134           
SHEET    1   Q 3 SER B  91  VAL B  97  0                                        
SHEET    2   Q 3 SER B 125  LYS B 133 -1  O  PHE B 129   N  TYR B  96           
SHEET    3   Q 3 VAL B 165  PRO B 171 -1  O  ILE B 167   N  LEU B 128           
SHEET    1   R 2 MET B 101  ASN B 103  0                                        
SHEET    2   R 2 THR B 109  ALA B 111 -1  O  HIS B 110   N  VAL B 102           
SHEET    1   S 2 PHE B 203  ILE B 205  0                                        
SHEET    2   S 2 SER B 208  LYS B 210 -1  O  LYS B 210   N  PHE B 203           
SHEET    1   T 4 LYS B 404  ASP B 407  0                                        
SHEET    2   T 4 ALA B 214  SER B 218 -1  N  GLN B 215   O  ASP B 407           
SHEET    3   T 4 ARG B 497  ASN B 499  1  O  ASN B 499   N  ALA B 214           
SHEET    4   T 4 VAL B 536  ASN B 538 -1  O  LYS B 537   N  THR B 498           
SHEET    1   U 5 VAL B 223  LYS B 227  0                                        
SHEET    2   U 5 ILE B 234  SER B 242 -1  O  GLU B 239   N  GLN B 224           
SHEET    3   U 5 SER B 252  TYR B 259 -1  O  VAL B 256   N  ALA B 238           
SHEET    4   U 5 ILE B 269  THR B 272 -1  O  THR B 272   N  GLN B 255           
SHEET    5   U 5 ILE B 280  PRO B 281 -1  O  ILE B 280   N  ALA B 271           
SHEET    1   V 3 CYS B 544  ILE B 545  0                                        
SHEET    2   V 3 VAL B 633  ARG B 635 -1  O  TYR B 634   N  CYS B 544           
SHEET    3   V 3 ILE B 693  ASP B 694 -1  O  ILE B 693   N  ARG B 635           
SHEET    1   W 5 MET B 563  PRO B 565  0                                        
SHEET    2   W 5 TRP B 586  HIS B 590 -1  O  VAL B 589   N  GLU B 564           
SHEET    3   W 5 THR B 578  VAL B 582 -1  N  THR B 578   O  HIS B 590           
SHEET    4   W 5 GLU B 623  PHE B 627  1  O  LEU B 624   N  PHE B 581           
SHEET    5   W 5 SER B 614  ASP B 618 -1  N  ILE B 616   O  LYS B 625           
SHEET    1   X 4 GLU B 650  LEU B 651  0                                        
SHEET    2   X 4 PHE B 638  GLU B 641 -1  N  GLU B 641   O  GLU B 650           
SHEET    3   X 4 HIS B 740  CYS B 741 -1  O  CYS B 741   N  PHE B 638           
SHEET    4   X 4 ILE B 703  ALA B 704  1  N  ALA B 704   O  HIS B 740           
SHEET    1   Y 5 ALA B 793  LEU B 796  0                                        
SHEET    2   Y 5 SER B 853  ASP B 861 -1  O  PHE B 856   N  ALA B 793           
SHEET    3   Y 5 LYS B 962  LYS B 972 -1  O  VAL B 968   N  ARG B 857           
SHEET    4   Y 5 ASN B 946  THR B 956 -1  N  ILE B 948   O  ARG B 969           
SHEET    5   Y 5 ARG B 904  SER B 906 -1  N  VAL B 905   O  GLY B 947           
SHEET    1   Z 2 GLY B 804  THR B 805  0                                        
SHEET    2   Z 2 GLY B1042  ASP B1043  1  O  GLY B1042   N  THR B 805           
SHEET    1  AA 3 VAL B 825  ILE B 827  0                                        
SHEET    2  AA 3 LEU B1010  ILE B1012  1  O  LEU B1010   N  ALA B 826           
SHEET    3  AA 3 MET B 839  MET B 841 -1  N  ILE B 840   O  ILE B1011           
SHEET    1  AB 2 THR B 873  PHE B 874  0                                        
SHEET    2  AB 2 LYS B 914  THR B 915 -1  O  THR B 915   N  THR B 873           
SHEET    1  AC 2 VAL B 910  ILE B 912  0                                        
SHEET    2  AC 2 THR B 939  PRO B 940 -1  O  THR B 939   N  ILE B 911           
SHEET    1  AD 3 LYS B 987  THR B 989  0                                        
SHEET    2  AD 3 LYS B 979  ALA B 981 -1  N  PHE B 980   O  GLY B 988           
SHEET    3  AD 3 GLN B1093  ARG B1094 -1  O  GLN B1093   N  ALA B 981           
SHEET    1  AE 2 PHE B1001  THR B1002  0                                        
SHEET    2  AE 2 MET B1072  TYR B1073 -1  O  TYR B1073   N  PHE B1001           
SHEET    1  AF 2 PHE B1069  GLU B1070  0                                        
SHEET    2  AF 2 ILE B1085  PHE B1086 -1  O  ILE B1085   N  GLU B1070           
SHEET    1  AG 2 PHE B1158  CYS B1163  0                                        
SHEET    2  AG 2 ILE B1191  ILE B1196 -1  O  TYR B1192   N  ILE B1162           
SHEET    1  AH 4 GLN C   7  ALA C  13  0                                        
SHEET    2  AH 4 ASN C  17  SER C  23 -1  O  ASP C  19   N  ARG C  11           
SHEET    3  AH 4 TYR C 229  GLU C 233 -1  O  MET C 230   N  PHE C  20           
SHEET    4  AH 4 ILE C 176  GLU C 179 -1  N  GLU C 179   O  TYR C 229           
SHEET    1  AI 5 LEU C 118  ILE C 120  0                                        
SHEET    2  AI 5 VAL C  97  PHE C 104 -1  N  THR C 100   O  VAL C 119           
SHEET    3  AI 5 GLU C 152  GLY C 162 -1  O  CYS C 157   N  LEU C  99           
SHEET    4  AI 5 THR C  43  ASN C  54 -1  N  SER C  48   O  VAL C 158           
SHEET    5  AI 5 VAL L  65  GLU L  68 -1  O  PHE L  67   N  VAL C  49           
SHEET    1  AJ 2 THR C 111  TYR C 114  0                                        
SHEET    2  AJ 2 LEU C 143  LEU C 147 -1  O  ILE C 144   N  VAL C 113           
SHEET    1  AK 4 PHE E  60  ALA E  62  0                                        
SHEET    2  AK 4 LEU E  78  GLU E  81 -1  O  LEU E  78   N  ALA E  62           
SHEET    3  AK 4 THR E 107  TYR E 112  1  O  VAL E 111   N  GLU E  81           
SHEET    4  AK 4 THR E 131  ASN E 136  1  O  PHE E 135   N  PHE E 110           
SHEET    1  AL 2 SER E  87  VAL E  88  0                                        
SHEET    2  AL 2 ASN E 115  ILE E 116  1  O  ASN E 115   N  VAL E  88           
SHEET    1  AM 4 HIS E 153  ARG E 155  0                                        
SHEET    2  AM 4 VAL E 195  LYS E 201 -1  O  LYS E 197   N  ILE E 154           
SHEET    3  AM 4 ARG E 207  CYS E 214 -1  O  SER E 210   N  ILE E 198           
SHEET    4  AM 4 ARG E 177  ILE E 178  1  N  ILE E 178   O  ILE E 213           
SHEET    1  AN 9 TYR H  95  TYR H  98  0                                        
SHEET    2  AN 9 TYR H 141  ARG H 145 -1  O  ILE H 144   N  TYR H  95           
SHEET    3  AN 9 SER H  54  THR H  58 -1  N  THR H  58   O  LEU H 143           
SHEET    4  AN 9 ASP H   7  ASP H  16 -1  N  PHE H  10   O  LEU H  55           
SHEET    5  AN 9 VAL H  23  SER H  30 -1  O  ALA H  29   N  GLN H  11           
SHEET    6  AN 9 LYS H  37  ASN H  43 -1  O  LEU H  40   N  ILE H  26           
SHEET    7  AN 9 LEU H 121  GLU H 126 -1  O  ARG H 124   N  THR H  39           
SHEET    8  AN 9 ILE H 112  PHE H 118 -1  N  PHE H 118   O  LEU H 121           
SHEET    9  AN 9 THR H 100  GLU H 106 -1  N  GLU H 105   O  ALA H 113           
SHEET    1  AO 3 TYR I  15  ASP I  19  0                                        
SHEET    2  AO 3 ARG I  24  GLU I  28 -1  O  GLU I  28   N  TYR I  15           
SHEET    3  AO 3 VAL I  35  GLU I  37 -1  O  GLU I  36   N  PHE I  27           
SHEET    1  AP 3 ASN I  83  GLN I  87  0                                        
SHEET    2  AP 3 LEU I  99  CYS I 103 -1  O  VAL I 102   N  VAL I  84           
SHEET    3  AP 3 ILE I 109  THR I 111 -1  O  PHE I 110   N  PHE I 101           
SHEET    1  AQ 4 LEU K  19  LYS K  20  0                                        
SHEET    2  AQ 4 ALA K  30  GLU K  36 -1  O  THR K  34   N  LYS K  20           
SHEET    3  AQ 4 ARG K  70  THR K  77 -1  O  ILE K  75   N  VAL K  31           
SHEET    4  AQ 4 VAL K  56  LYS K  62 -1  N  LEU K  57   O  GLN K  76           
SHEET    1  AR 2 TYR L  29  ILE L  30  0                                        
SHEET    2  AR 2 LYS L  37  LEU L  38 -1  O  LEU L  38   N  TYR L  29           
LINK         SG  CYS A  67                ZN    ZN A1735     1555   1555  2.77  
LINK         SG  CYS A  70                ZN    ZN A1735     1555   1555  2.29  
LINK         SG  CYS A  77                ZN    ZN A1735     1555   1555  2.02  
LINK         SG  CYS A 110                ZN    ZN A1734     1555   1555  2.32  
LINK         SG  CYS A 167                ZN    ZN A1734     1555   1555  2.98  
LINK         OD1 ASP A 483                MG    MG A2001     1555   1555  2.49  
LINK         SG  CYS B1163                ZN    ZN B1307     1555   1555  2.53  
LINK         SG  CYS B1185                ZN    ZN B1307     1555   1555  2.48  
LINK         SG  CYS C  86                ZN    ZN C 319     1555   1555  2.55  
LINK         SG  CYS C  88                ZN    ZN C 319     1555   1555  2.36  
LINK         SG  CYS C  92                ZN    ZN C 319     1555   1555  2.23  
LINK         SG  CYS C  95                ZN    ZN C 319     1555   1555  2.33  
LINK         SG  CYS I  10                ZN    ZN I 203     1555   1555  1.97  
LINK         SG  CYS I  29                ZN    ZN I 203     1555   1555  2.12  
LINK         SG  CYS I  32                ZN    ZN I 203     1555   1555  2.33  
LINK         SG  CYS I  75                ZN    ZN I 204     1555   1555  2.46  
LINK         SG  CYS I  78                ZN    ZN I 204     1555   1555  2.24  
LINK         SG  CYS I 103                ZN    ZN I 204     1555   1555  2.31  
LINK         SG  CYS I 106                ZN    ZN I 204     1555   1555  2.04  
LINK         SG  CYS J   7                ZN    ZN J 101     1555   1555  1.99  
LINK         SG  CYS J  10                ZN    ZN J 101     1555   1555  2.35  
LINK         SG  CYS J  45                ZN    ZN J 101     1555   1555  2.37  
LINK         SG  CYS J  46                ZN    ZN J 101     1555   1555  2.00  
LINK         SG  CYS L  34                ZN    ZN L 105     1555   1555  1.91  
LINK         SG  CYS L  48                ZN    ZN L 105     1555   1555  2.23  
LINK         SG  CYS L  51                ZN    ZN L 105     1555   1555  2.51  
CISPEP   1 VAL A  152    PRO A  153          0       -22.77                     
CISPEP   2 PRO A  153    SER A  154          0         5.86                     
CISPEP   3 ASP A  156    ASP A  157          0         0.29                     
CISPEP   4 THR A  159    GLN A  160          0        -1.28                     
CISPEP   5 ARG A  164    GLY A  165          0        -0.41                     
CISPEP   6 GLY A  165    GLY A  166          0        -0.59                     
CISPEP   7 ASN A  253    GLU A  254          0         8.61                     
CISPEP   8 SER A  255    GLN A  256          0       -15.68                     
CISPEP   9 GLN A  256    ARG A  257          0       -28.26                     
CISPEP  10 LEU A  315    GLN A  316          0        10.82                     
CISPEP  11 GLN A  316    LYS A  317          0        22.25                     
CISPEP  12 ARG A  320    PRO A  321          0       -22.70                     
CISPEP  13 GLN A  447    PRO A  448          0         8.79                     
CISPEP  14 PHE A 1174    SER A 1175          0         6.44                     
CISPEP  15 GLU A 1448    SER A 1449          0        -9.94                     
CISPEP  16 LEU B   69    ILE B   70          0         4.99                     
CISPEP  17 THR B  136    TYR B  137          0        -1.18                     
CISPEP  18 ALA B  139    ILE B  140          0        10.63                     
CISPEP  19 GLY B  144    ARG B  145          0        10.33                     
CISPEP  20 PHE B  333    ILE B  334          0         7.99                     
CISPEP  21 ILE B  334    GLY B  335          0        -4.70                     
CISPEP  22 GLY B  335    ARG B  336          0       -13.50                     
CISPEP  23 GLY B  338    THR B  339          0         2.98                     
CISPEP  24 LEU B  341    GLY B  342          0        -0.85                     
CISPEP  25 GLY B  342    ILE B  343          0       -10.95                     
CISPEP  26 LYS B  344    LYS B  345          0         3.27                     
CISPEP  27 LYS B  345    GLU B  346          0        22.00                     
CISPEP  28 THR E   65    GLU E   66          0         5.99                     
CISPEP  29 GLU E   67    SER E   68          0       -12.39                     
CISPEP  30 SER E   68    ILE E   69          0       -19.27                     
CISPEP  31 PHE E   72    PRO E   73          0        16.88                     
CISPEP  32 MET E   75    GLY E   76          0        -7.36                     
CISPEP  33 PRO E  128    PRO E  129          0        -1.65                     
SITE     1 AC1  4 CYS A 107  CYS A 110  CYS A 148  CYS A 167                    
SITE     1 AC2  4 CYS A  67  CYS A  70  CYS A  77  HIS A  80                    
SITE     1 AC3  4 CYS B1163  CYS B1166  CYS B1182  CYS B1185                    
SITE     1 AC4  5 CYS C  86  CYS C  88  HIS C  91  CYS C  92                    
SITE     2 AC4  5 CYS C  95                                                     
SITE     1 AC5  4 CYS I   7  CYS I  10  CYS I  29  CYS I  32                    
SITE     1 AC6  5 CYS I  75  CYS I  78  SER I  80  CYS I 103                    
SITE     2 AC6  5 CYS I 106                                                     
SITE     1 AC7  5 CYS J   7  SER J   9  CYS J  10  CYS J  45                    
SITE     2 AC7  5 CYS J  46                                                     
SITE     1 AC8  4 CYS L  31  CYS L  34  CYS L  48  CYS L  51                    
SITE     1 AC9  5 ASP A 481  ASP A 483  ASP A 485  DGT B1308                    
SITE     2 AC9  5   A R  10                                                     
SITE     1 BC1  7 ASP A 481   MG A2001  ARG B 766  SER B1019                    
SITE     2 BC1  7 ARG B1020    A R  10   DC T  18                               
CRYST1  168.682  223.524  193.938  90.00 100.54  90.00 C 1 2 1       4          
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      0.005928  0.000000  0.001103        0.00000                         
SCALE2      0.000000  0.004474  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005245        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system