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Database: PDB
Entry: 5VFO
LinkDB: 5VFO
Original site: 5VFO 
HEADER    HYDROLASE                               08-APR-17   5VFO              
TITLE     NUCLEOTIDE-DRIVEN TRIPLE-STATE REMODELING OF THE AAA-ATPASE CHANNEL IN
TITLE    2 THE ACTIVATED HUMAN 26S PROTEASOME                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;                           
COMPND   3 CHAIN: G, g;                                                         
COMPND   4 SYNONYM: 27 KDA PROSOMAL PROTEIN, P27K, MACROPAIN IOTA CHAIN,        
COMPND   5 MULTICATALYTIC ENDOPEPTIDASE COMPLEX IOTA CHAIN, PROTEASOME IOTA     
COMPND   6 CHAIN, ALPHA1;                                                       
COMPND   7 EC: 3.4.25.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;                           
COMPND  11 CHAIN: H, h;                                                         
COMPND  12 SYNONYM: MACROPAIN SUBUNIT C3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  13 SUBUNIT C3, PROTEASOME COMPONENT C3, ALPHA2;                         
COMPND  14 EC: 3.4.25.1;                                                        
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;                           
COMPND  18 CHAIN: I, i;                                                         
COMPND  19 SYNONYM: MACROPAIN SUBUNIT C9, MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  20 SUBUNIT C9, PROTEASOME COMPONENT C9, PROTEASOME SUBUNIT L, ALPHA3;   
COMPND  21 EC: 3.4.25.1;                                                        
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 MOL_ID: 4;                                                           
COMPND  24 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-7;                           
COMPND  25 CHAIN: J, j;                                                         
COMPND  26 SYNONYM: PROTEASOME SUBUNIT RC6-1, PROTEASOME SUBUNIT XAPC7, ALPHA4; 
COMPND  27 EC: 3.4.25.1;                                                        
COMPND  28 ENGINEERED: YES;                                                     
COMPND  29 MOL_ID: 5;                                                           
COMPND  30 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;                           
COMPND  31 CHAIN: K, k;                                                         
COMPND  32 SYNONYM: MACROPAIN ZETA CHAIN, MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  33 ZETA CHAIN, PROTEASOME ZETA CHAIN, ALPHA5;                           
COMPND  34 EC: 3.4.25.1;                                                        
COMPND  35 ENGINEERED: YES;                                                     
COMPND  36 MOL_ID: 6;                                                           
COMPND  37 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;                           
COMPND  38 CHAIN: L, l;                                                         
COMPND  39 SYNONYM: 30 KDA PROSOMAL PROTEIN, PROS-30, MACROPAIN SUBUNIT C2,     
COMPND  40 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C2, PROTEASOME COMPONENT
COMPND  41 C2, PROTEASOME NU CHAIN, ALPHA6;                                     
COMPND  42 EC: 3.4.25.1;                                                        
COMPND  43 ENGINEERED: YES;                                                     
COMPND  44 MOL_ID: 7;                                                           
COMPND  45 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;                           
COMPND  46 CHAIN: M, m;                                                         
COMPND  47 SYNONYM: MACROPAIN SUBUNIT C8, MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  48 SUBUNIT C8, PROTEASOME COMPONENT C8, ALPHA7;                         
COMPND  49 EC: 3.4.25.1;                                                        
COMPND  50 ENGINEERED: YES;                                                     
COMPND  51 MOL_ID: 8;                                                           
COMPND  52 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;                            
COMPND  53 CHAIN: N, n;                                                         
COMPND  54 SYNONYM: MACROPAIN DELTA CHAIN, MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  55 DELTA CHAIN, PROTEASOME DELTA CHAIN, PROTEASOME SUBUNIT Y, BETA1;    
COMPND  56 EC: 3.4.25.1;                                                        
COMPND  57 ENGINEERED: YES;                                                     
COMPND  58 MOL_ID: 9;                                                           
COMPND  59 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;                            
COMPND  60 CHAIN: O, o;                                                         
COMPND  61 SYNONYM: MACROPAIN CHAIN Z, MULTICATALYTIC ENDOPEPTIDASE COMPLEX     
COMPND  62 CHAIN Z, PROTEASOME SUBUNIT Z, BETA2;                                
COMPND  63 EC: 3.4.25.1;                                                        
COMPND  64 ENGINEERED: YES;                                                     
COMPND  65 MOL_ID: 10;                                                          
COMPND  66 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;                            
COMPND  67 CHAIN: P, p;                                                         
COMPND  68 SYNONYM: PROTEASOME CHAIN 13, PROTEASOME COMPONENT C10-II, PROTEASOME
COMPND  69 THETA CHAIN, BETA3;                                                  
COMPND  70 EC: 3.4.25.1;                                                        
COMPND  71 ENGINEERED: YES;                                                     
COMPND  72 MOL_ID: 11;                                                          
COMPND  73 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;                            
COMPND  74 CHAIN: Q, q;                                                         
COMPND  75 SYNONYM: MACROPAIN SUBUNIT C7-I, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  76 SUBUNIT C7-I, PROTEASOME COMPONENT C7-I, BETA4;                      
COMPND  77 EC: 3.4.25.1;                                                        
COMPND  78 ENGINEERED: YES;                                                     
COMPND  79 MOL_ID: 12;                                                          
COMPND  80 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;                            
COMPND  81 CHAIN: R, r;                                                         
COMPND  82 SYNONYM: MACROPAIN EPSILON CHAIN, MULTICATALYTIC ENDOPEPTIDASE       
COMPND  83 COMPLEX EPSILON CHAIN, PROTEASOME CHAIN 6, PROTEASOME EPSILON CHAIN, 
COMPND  84 PROTEASOME SUBUNIT MB1, PROTEASOME SUBUNIT X, BETA5;                 
COMPND  85 EC: 3.4.25.1;                                                        
COMPND  86 ENGINEERED: YES;                                                     
COMPND  87 MOL_ID: 13;                                                          
COMPND  88 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;                            
COMPND  89 CHAIN: S, s;                                                         
COMPND  90 SYNONYM: MACROPAIN SUBUNIT C5, MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  91 SUBUNIT C5, PROTEASOME COMPONENT C5, PROTEASOME GAMMA CHAIN, BETA6;  
COMPND  92 EC: 3.4.25.1;                                                        
COMPND  93 ENGINEERED: YES;                                                     
COMPND  94 MOL_ID: 14;                                                          
COMPND  95 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;                            
COMPND  96 CHAIN: T, t;                                                         
COMPND  97 SYNONYM: 26 KDA PROSOMAL PROTEIN, PROS-26, MACROPAIN BETA CHAIN,     
COMPND  98 MULTICATALYTIC ENDOPEPTIDASE COMPLEX BETA CHAIN, PROTEASOME BETA     
COMPND  99 CHAIN, PROTEASOME CHAIN 3, HSN3, BETA7;                              
COMPND 100 EC: 3.4.25.1;                                                        
COMPND 101 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PSMA6, PROS27;                                                 
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: PSMA2, HC3, PSC3;                                              
SOURCE  14 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  15 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 GENE: PSMA4, HC9, PSC9;                                              
SOURCE  22 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  23 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  27 ORGANISM_COMMON: HUMAN;                                              
SOURCE  28 ORGANISM_TAXID: 9606;                                                
SOURCE  29 GENE: PSMA7, HSPC;                                                   
SOURCE  30 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  31 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  32 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  33 MOL_ID: 5;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  35 ORGANISM_COMMON: HUMAN;                                              
SOURCE  36 ORGANISM_TAXID: 9606;                                                
SOURCE  37 GENE: PSMA5;                                                         
SOURCE  38 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  39 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  40 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  41 MOL_ID: 6;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  43 ORGANISM_COMMON: HUMAN;                                              
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 GENE: PSMA1, HC2, NU, PROS30, PSC2;                                  
SOURCE  46 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  47 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  48 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  49 MOL_ID: 7;                                                           
SOURCE  50 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  51 ORGANISM_COMMON: HUMAN;                                              
SOURCE  52 ORGANISM_TAXID: 9606;                                                
SOURCE  53 GENE: PSMA3, HC8, PSC8;                                              
SOURCE  54 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  55 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  56 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  57 MOL_ID: 8;                                                           
SOURCE  58 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  59 ORGANISM_COMMON: HUMAN;                                              
SOURCE  60 ORGANISM_TAXID: 9606;                                                
SOURCE  61 GENE: PSMB6, LMPY, Y;                                                
SOURCE  62 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  63 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  64 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  65 MOL_ID: 9;                                                           
SOURCE  66 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  67 ORGANISM_COMMON: HUMAN;                                              
SOURCE  68 ORGANISM_TAXID: 9606;                                                
SOURCE  69 GENE: PSMB7, Z;                                                      
SOURCE  70 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  71 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  72 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  73 MOL_ID: 10;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  75 ORGANISM_COMMON: HUMAN;                                              
SOURCE  76 ORGANISM_TAXID: 9606;                                                
SOURCE  77 GENE: PSMB3;                                                         
SOURCE  78 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  79 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  80 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  81 MOL_ID: 11;                                                          
SOURCE  82 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  83 ORGANISM_COMMON: HUMAN;                                              
SOURCE  84 ORGANISM_TAXID: 9606;                                                
SOURCE  85 GENE: PSMB2;                                                         
SOURCE  86 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  87 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  88 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  89 MOL_ID: 12;                                                          
SOURCE  90 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  91 ORGANISM_COMMON: HUMAN;                                              
SOURCE  92 ORGANISM_TAXID: 9606;                                                
SOURCE  93 GENE: PSMB5, LMPX, MB1, X;                                           
SOURCE  94 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  95 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  96 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  97 MOL_ID: 13;                                                          
SOURCE  98 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  99 ORGANISM_COMMON: HUMAN;                                              
SOURCE 100 ORGANISM_TAXID: 9606;                                                
SOURCE 101 GENE: PSMB1, PSC5;                                                   
SOURCE 102 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE 103 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE 104 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE 105 MOL_ID: 14;                                                          
SOURCE 106 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 107 ORGANISM_COMMON: HUMAN;                                              
SOURCE 108 ORGANISM_TAXID: 9606;                                                
SOURCE 109 GENE: PSMB4, PROS26;                                                 
SOURCE 110 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE 111 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE 112 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    26S PROTEASOME, ATP-DEPENDENT PROTEASE, AAA-ATPASE, PEPTIDE-UNFOLDING 
KEYWDS   2 CHANNEL, 20S CORE PARTICLE, HYDROLASE                                
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    Y.ZHU,W.L.WANG,D.YU,Q.OUYANG,Y.LU,Y.MAO                               
REVDAT   1   18-JUL-18 5VFO    0                                                
JRNL        AUTH   Y.ZHU,W.L.WANG,D.YU,Q.OUYANG,Y.LU,Y.MAO                      
JRNL        TITL   STRUCTURAL MECHANISM FOR NUCLEOTIDE-DRIVEN REMODELING OF THE 
JRNL        TITL 2 AAA-ATPASE UNFOLDASE IN THE ACTIVATED HUMAN 26S PROTEASOME.  
JRNL        REF    NAT COMMUN                    V.   9  1360 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29636472                                                     
JRNL        DOI    10.1038/S41467-018-03785-W                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.500                          
REMARK   3   NUMBER OF PARTICLES               : 228086                         
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 5VFO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227359.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : 26S PROTEASOME BOUND TO ATP       
REMARK 245                                    -GAMMAS                           
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TECNAI ARCTICA             
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 30.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 200                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 28-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L, M, N, O, P,         
REMARK 350                    AND CHAINS: Q, R, S, T, g, h, i, j, k,            
REMARK 350                    AND CHAINS: l, m, n, o, p, q, r, s, t             
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     SER G     5                                                      
REMARK 465     GLU H     3                                                      
REMARK 465     ARG H     4                                                      
REMARK 465     SER I     2                                                      
REMARK 465     ARG I     3                                                      
REMARK 465     LYS J   241                                                      
REMARK 465     LYS J   242                                                      
REMARK 465     LYS J   243                                                      
REMARK 465     GLN J   244                                                      
REMARK 465     ALA K   128                                                      
REMARK 465     ASP K   129                                                      
REMARK 465     PRO K   130                                                      
REMARK 465     GLY K   131                                                      
REMARK 465     ALA K   132                                                      
REMARK 465     MET K   133                                                      
REMARK 465     SER M     1                                                      
REMARK 465     SER M     2                                                      
REMARK 465     ILE M     3                                                      
REMARK 465     GLY M     4                                                      
REMARK 465     GLU M   245                                                      
REMARK 465     LYS j   241                                                      
REMARK 465     LYS j   242                                                      
REMARK 465     LYS j   243                                                      
REMARK 465     GLN j   244                                                      
REMARK 465     ALA k   128                                                      
REMARK 465     ASP k   129                                                      
REMARK 465     PRO k   130                                                      
REMARK 465     GLY k   131                                                      
REMARK 465     ALA k   132                                                      
REMARK 465     MET k   133                                                      
REMARK 465     SER m     1                                                      
REMARK 465     SER m     2                                                      
REMARK 465     ILE m     3                                                      
REMARK 465     GLY m     4                                                      
REMARK 465     GLU m   245                                                      
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     LYS G  45    CG   CD   CE   NZ                                   
REMARK 470     ASP G  46    CG   OD1  OD2                                       
REMARK 470     LYS G  55    CG   CD   CE   NZ                                   
REMARK 470     LYS G  59    CG   CD   CE   NZ                                   
REMARK 470     SER G  63    OG                                                  
REMARK 470     GLU G 146    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 181    CG   CD   CE   NZ                                   
REMARK 470     LYS G 186    CG   CD   CE   NZ                                   
REMARK 470     PHE G 187    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP G 188    CG   OD1  OD2                                       
REMARK 470     GLU G 196    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 223    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  18    CG   CD   CE   NZ                                   
REMARK 470     VAL H  36    CG1  CG2                                            
REMARK 470     GLN H  52    CG   CD   OE1  NE2                                  
REMARK 470     LYS H  53    CG   CD   CE   NZ                                   
REMARK 470     SER H  54    OG                                                  
REMARK 470     ILE H  55    CG1  CG2  CD1                                       
REMARK 470     ARG H  60    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP H 139    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H 139    CZ3  CH2                                            
REMARK 470     ASN H 140    CG   OD1  ND2                                       
REMARK 470     GLU H 141    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 143    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET H 163    CG   SD   CE                                        
REMARK 470     LYS H 176    CG   CD   CE   NZ                                   
REMARK 470     ARG H 177    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR H 178    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU H 184    CG   CD1  CD2                                       
REMARK 470     LEU H 193    CG   CD1  CD2                                       
REMARK 470     LEU H 195    CG   CD1  CD2                                       
REMARK 470     LYS H 196    CG   CD   CE   NZ                                   
REMARK 470     PHE H 199    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU H 200    CG   CD   OE1  OE2                                  
REMARK 470     GLN H 202    CG   CD   OE1  NE2                                  
REMARK 470     VAL H 226    CG1  CG2                                            
REMARK 470     LYS H 227    CG   CD   CE   NZ                                   
REMARK 470     LEU H 230    CG   CD1  CD2                                       
REMARK 470     ILE H 233    CG1  CG2  CD1                                       
REMARK 470     SER I  13    OG                                                  
REMARK 470     ILE I  37    CG1  CG2  CD1                                       
REMARK 470     ASN I  51    CG   OD1  ND2                                       
REMARK 470     ILE I  52    CG1  CG2  CD1                                       
REMARK 470     LYS I  54    CG   CD   CE   NZ                                   
REMARK 470     GLN I 177    CG   CD   OE1  NE2                                  
REMARK 470     MET I 184    CG   SD   CE                                        
REMARK 470     ILE I 194    CG1  CG2  CD1                                       
REMARK 470     MET I 201    CG   SD   CE                                        
REMARK 470     LYS I 205    CG   CD   CE   NZ                                   
REMARK 470     LYS I 210    CG   CD   CE   NZ                                   
REMARK 470     LYS I 222    CG   CD   CE   NZ                                   
REMARK 470     LYS I 229    CG   CD   CE   NZ                                   
REMARK 470     GLN I 230    CG   CD   OE1  NE2                                  
REMARK 470     LYS I 231    CG   CD   CE   NZ                                   
REMARK 470     GLU I 250    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 251    CG   CD   CE   NZ                                   
REMARK 470     LYS J  27    CG   CD   CE   NZ                                   
REMARK 470     ILE J  40    CG1  CG2  CD1                                       
REMARK 470     VAL J  42    CG1  CG2                                            
REMARK 470     GLU J  46    CG   CD   OE1  OE2                                  
REMARK 470     LYS J  47    CG   CD   CE   NZ                                   
REMARK 470     LYS J  48    CG   CD   CE   NZ                                   
REMARK 470     SER J  49    OG                                                  
REMARK 470     VAL J  50    CG1  CG2                                            
REMARK 470     LEU J  53    CG   CD1  CD2                                       
REMARK 470     PHE J 136    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE J 138    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR J 141    OG1  CG2                                            
REMARK 470     LYS J 157    CG   CD   CE   NZ                                   
REMARK 470     ARG J 163    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS J 166    CG   CD   CE   NZ                                   
REMARK 470     ARG J 169    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU J 170    CG   CD   OE1  OE2                                  
REMARK 470     LYS J 174    CG   CD   CE   NZ                                   
REMARK 470     ILE J 181    CG1  CG2  CD1                                       
REMARK 470     GLU J 182    CG   CD   OE1  OE2                                  
REMARK 470     THR J 183    OG1  CG2                                            
REMARK 470     ASP J 185    CG   OD1  OD2                                       
REMARK 470     THR J 187    OG1  CG2                                            
REMARK 470     LYS J 189    CG   CD   CE   NZ                                   
REMARK 470     ILE J 192    CG1  CG2  CD1                                       
REMARK 470     LYS J 193    CG   CD   CE   NZ                                   
REMARK 470     LEU J 195    CG   CD1  CD2                                       
REMARK 470     LEU J 196    CG   CD1  CD2                                       
REMARK 470     GLU J 197    CG   CD   OE1  OE2                                  
REMARK 470     VAL J 198    CG1  CG2                                            
REMARK 470     VAL J 199    CG1  CG2                                            
REMARK 470     LYS J 204    CG   CD   CE   NZ                                   
REMARK 470     GLU J 207    CG   CD   OE1  OE2                                  
REMARK 470     LEU J 208    CG   CD1  CD2                                       
REMARK 470     ARG J 212    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG J 213    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER J 216    OG                                                  
REMARK 470     LYS J 218    CG   CD   CE   NZ                                   
REMARK 470     GLU J 223    CG   CD   OE1  OE2                                  
REMARK 470     ILE J 225    CG1  CG2  CD1                                       
REMARK 470     GLU J 226    CG   CD   OE1  OE2                                  
REMARK 470     LYS J 227    CG   CD   CE   NZ                                   
REMARK 470     VAL J 229    CG1  CG2                                            
REMARK 470     ILE J 232    CG1  CG2  CD1                                       
REMARK 470     GLU J 233    CG   CD   OE1  OE2                                  
REMARK 470     LYS J 234    CG   CD   CE   NZ                                   
REMARK 470     GLU J 235    CG   CD   OE1  OE2                                  
REMARK 470     LYS J 236    CG   CD   CE   NZ                                   
REMARK 470     GLU J 237    CG   CD   OE1  OE2                                  
REMARK 470     ASN J 239    CG   OD1  ND2                                       
REMARK 470     GLU J 240    CG   CD   OE1  OE2                                  
REMARK 470     LYS K  86    CG   CD   CE   NZ                                   
REMARK 470     LYS K 187    CG   CD   CE   NZ                                   
REMARK 470     LYS K 192    CG   CD   CE   NZ                                   
REMARK 470     GLU K 208    CG   CD   OE1  OE2                                  
REMARK 470     LYS K 209    CG   CD   CE   NZ                                   
REMARK 470     LYS K 231    CG   CD   CE   NZ                                   
REMARK 470     LYS L 208    CG   CD   CE   NZ                                   
REMARK 470     LYS L 217    CG   CD   CE   NZ                                   
REMARK 470     ASP L 218    CG   OD1  OD2                                       
REMARK 470     GLU L 237    CG   CD   OE1  OE2                                  
REMARK 470     GLU L 238    CG   CD   OE1  OE2                                  
REMARK 470     GLN L 241    CG   CD   OE1  NE2                                  
REMARK 470     LYS M 109    CG   CD   CE   NZ                                   
REMARK 470     ASN M 143    CG   OD1  ND2                                       
REMARK 470     GLU M 203    CG   CD   OE1  OE2                                  
REMARK 470     LYS M 205    CG   CD   CE   NZ                                   
REMARK 470     LYS M 207    CG   CD   CE   NZ                                   
REMARK 470     ARG M 223    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS O   9    CG   CD   CE   NZ                                   
REMARK 470     LYS O 180    CG   CD   CE   NZ                                   
REMARK 470     LYS O 206    CG   CD   CE   NZ                                   
REMARK 470     GLU O 214    CG   CD   OE1  OE2                                  
REMARK 470     ARG P  48    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS Q  41    CG   CD   CE   NZ                                   
REMARK 470     ARG Q  95    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU Q 109    CG   CD   OE1  OE2                                  
REMARK 470     LYS Q 185    CG   CD   CE   NZ                                   
REMARK 470     LYS Q 198    CG   CD   CE   NZ                                   
REMARK 470     GLN Q 199    CG   CD   OE1  NE2                                  
REMARK 470     LYS R 106    CG   CD   CE   NZ                                   
REMARK 470     GLU R 150    CG   CD   OE1  OE2                                  
REMARK 470     ILE R 185    CG1  CG2  CD1                                       
REMARK 470     LYS S  45    CG   CD   CE   NZ                                   
REMARK 470     VAL S 161    CG1  CG2                                            
REMARK 470     LEU S 166    CG   CD1  CD2                                       
REMARK 470     LYS S 200    CG   CD   CE   NZ                                   
REMARK 470     ARG T  44    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS T 156    CG   CD   CE   NZ                                   
REMARK 470     LYS T 195    CG   CD   CE   NZ                                   
REMARK 470     LYS g  45    CG   CD   CE   NZ                                   
REMARK 470     ASP g  46    CG   OD1  OD2                                       
REMARK 470     LYS g  55    CG   CD   CE   NZ                                   
REMARK 470     LYS g  59    CG   CD   CE   NZ                                   
REMARK 470     SER g  63    OG                                                  
REMARK 470     GLU g 146    CG   CD   OE1  OE2                                  
REMARK 470     LYS g 181    CG   CD   CE   NZ                                   
REMARK 470     LYS g 186    CG   CD   CE   NZ                                   
REMARK 470     PHE g 187    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP g 188    CG   OD1  OD2                                       
REMARK 470     GLU g 196    CG   CD   OE1  OE2                                  
REMARK 470     GLU g 223    CG   CD   OE1  OE2                                  
REMARK 470     LYS h  18    CG   CD   CE   NZ                                   
REMARK 470     VAL h  36    CG1  CG2                                            
REMARK 470     GLN h  52    CG   CD   OE1  NE2                                  
REMARK 470     LYS h  53    CG   CD   CE   NZ                                   
REMARK 470     SER h  54    OG                                                  
REMARK 470     ILE h  55    CG1  CG2  CD1                                       
REMARK 470     ARG h  60    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP h 139    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP h 139    CZ3  CH2                                            
REMARK 470     ASN h 140    CG   OD1  ND2                                       
REMARK 470     GLU h 141    CG   CD   OE1  OE2                                  
REMARK 470     ARG h 143    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET h 163    CG   SD   CE                                        
REMARK 470     LYS h 176    CG   CD   CE   NZ                                   
REMARK 470     ARG h 177    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR h 178    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU h 184    CG   CD1  CD2                                       
REMARK 470     LEU h 193    CG   CD1  CD2                                       
REMARK 470     LEU h 195    CG   CD1  CD2                                       
REMARK 470     LYS h 196    CG   CD   CE   NZ                                   
REMARK 470     PHE h 199    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU h 200    CG   CD   OE1  OE2                                  
REMARK 470     GLN h 202    CG   CD   OE1  NE2                                  
REMARK 470     VAL h 226    CG1  CG2                                            
REMARK 470     LYS h 227    CG   CD   CE   NZ                                   
REMARK 470     LEU h 230    CG   CD1  CD2                                       
REMARK 470     ILE h 233    CG1  CG2  CD1                                       
REMARK 470     SER i  13    OG                                                  
REMARK 470     ILE i  37    CG1  CG2  CD1                                       
REMARK 470     ASN i  51    CG   OD1  ND2                                       
REMARK 470     ILE i  52    CG1  CG2  CD1                                       
REMARK 470     LYS i  54    CG   CD   CE   NZ                                   
REMARK 470     GLN i 177    CG   CD   OE1  NE2                                  
REMARK 470     MET i 184    CG   SD   CE                                        
REMARK 470     ILE i 194    CG1  CG2  CD1                                       
REMARK 470     MET i 201    CG   SD   CE                                        
REMARK 470     LYS i 205    CG   CD   CE   NZ                                   
REMARK 470     LYS i 210    CG   CD   CE   NZ                                   
REMARK 470     LYS i 222    CG   CD   CE   NZ                                   
REMARK 470     LYS i 229    CG   CD   CE   NZ                                   
REMARK 470     GLN i 230    CG   CD   OE1  NE2                                  
REMARK 470     LYS i 231    CG   CD   CE   NZ                                   
REMARK 470     GLU i 250    CG   CD   OE1  OE2                                  
REMARK 470     LYS i 251    CG   CD   CE   NZ                                   
REMARK 470     LYS j  27    CG   CD   CE   NZ                                   
REMARK 470     ILE j  40    CG1  CG2  CD1                                       
REMARK 470     VAL j  42    CG1  CG2                                            
REMARK 470     GLU j  46    CG   CD   OE1  OE2                                  
REMARK 470     LYS j  47    CG   CD   CE   NZ                                   
REMARK 470     LYS j  48    CG   CD   CE   NZ                                   
REMARK 470     SER j  49    OG                                                  
REMARK 470     VAL j  50    CG1  CG2                                            
REMARK 470     LEU j  53    CG   CD1  CD2                                       
REMARK 470     PHE j 136    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE j 138    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR j 141    OG1  CG2                                            
REMARK 470     LYS j 157    CG   CD   CE   NZ                                   
REMARK 470     ARG j 163    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS j 166    CG   CD   CE   NZ                                   
REMARK 470     ARG j 169    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU j 170    CG   CD   OE1  OE2                                  
REMARK 470     LYS j 174    CG   CD   CE   NZ                                   
REMARK 470     ILE j 181    CG1  CG2  CD1                                       
REMARK 470     GLU j 182    CG   CD   OE1  OE2                                  
REMARK 470     THR j 183    OG1  CG2                                            
REMARK 470     ASP j 185    CG   OD1  OD2                                       
REMARK 470     THR j 187    OG1  CG2                                            
REMARK 470     LYS j 189    CG   CD   CE   NZ                                   
REMARK 470     ILE j 192    CG1  CG2  CD1                                       
REMARK 470     LYS j 193    CG   CD   CE   NZ                                   
REMARK 470     LEU j 195    CG   CD1  CD2                                       
REMARK 470     LEU j 196    CG   CD1  CD2                                       
REMARK 470     GLU j 197    CG   CD   OE1  OE2                                  
REMARK 470     VAL j 198    CG1  CG2                                            
REMARK 470     VAL j 199    CG1  CG2                                            
REMARK 470     LYS j 204    CG   CD   CE   NZ                                   
REMARK 470     GLU j 207    CG   CD   OE1  OE2                                  
REMARK 470     LEU j 208    CG   CD1  CD2                                       
REMARK 470     ARG j 212    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG j 213    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER j 216    OG                                                  
REMARK 470     LYS j 218    CG   CD   CE   NZ                                   
REMARK 470     GLU j 223    CG   CD   OE1  OE2                                  
REMARK 470     ILE j 225    CG1  CG2  CD1                                       
REMARK 470     GLU j 226    CG   CD   OE1  OE2                                  
REMARK 470     LYS j 227    CG   CD   CE   NZ                                   
REMARK 470     VAL j 229    CG1  CG2                                            
REMARK 470     ILE j 232    CG1  CG2  CD1                                       
REMARK 470     GLU j 233    CG   CD   OE1  OE2                                  
REMARK 470     LYS j 234    CG   CD   CE   NZ                                   
REMARK 470     GLU j 235    CG   CD   OE1  OE2                                  
REMARK 470     LYS j 236    CG   CD   CE   NZ                                   
REMARK 470     GLU j 237    CG   CD   OE1  OE2                                  
REMARK 470     ASN j 239    CG   OD1  ND2                                       
REMARK 470     GLU j 240    CG   CD   OE1  OE2                                  
REMARK 470     TYR k   8    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS k  86    CG   CD   CE   NZ                                   
REMARK 470     LYS k 187    CG   CD   CE   NZ                                   
REMARK 470     LYS k 192    CG   CD   CE   NZ                                   
REMARK 470     GLU k 208    CG   CD   OE1  OE2                                  
REMARK 470     LYS k 209    CG   CD   CE   NZ                                   
REMARK 470     LYS k 231    CG   CD   CE   NZ                                   
REMARK 470     LYS l 208    CG   CD   CE   NZ                                   
REMARK 470     LYS l 217    CG   CD   CE   NZ                                   
REMARK 470     ASP l 218    CG   OD1  OD2                                       
REMARK 470     GLU l 237    CG   CD   OE1  OE2                                  
REMARK 470     GLU l 238    CG   CD   OE1  OE2                                  
REMARK 470     GLN l 241    CG   CD   OE1  NE2                                  
REMARK 470     LYS m 109    CG   CD   CE   NZ                                   
REMARK 470     ASN m 143    CG   OD1  ND2                                       
REMARK 470     GLU m 203    CG   CD   OE1  OE2                                  
REMARK 470     LYS m 205    CG   CD   CE   NZ                                   
REMARK 470     LYS m 207    CG   CD   CE   NZ                                   
REMARK 470     ARG m 223    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS o   9    CG   CD   CE   NZ                                   
REMARK 470     LYS o 180    CG   CD   CE   NZ                                   
REMARK 470     LYS o 206    CG   CD   CE   NZ                                   
REMARK 470     GLU o 214    CG   CD   OE1  OE2                                  
REMARK 470     ARG p  48    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS q  41    CG   CD   CE   NZ                                   
REMARK 470     ARG q  95    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU q 109    CG   CD   OE1  OE2                                  
REMARK 470     LYS q 185    CG   CD   CE   NZ                                   
REMARK 470     LYS q 198    CG   CD   CE   NZ                                   
REMARK 470     GLN q 199    CG   CD   OE1  NE2                                  
REMARK 470     LYS r 106    CG   CD   CE   NZ                                   
REMARK 470     GLU r 150    CG   CD   OE1  OE2                                  
REMARK 470     ILE r 185    CG1  CG2  CD1                                       
REMARK 470     LYS s  45    CG   CD   CE   NZ                                   
REMARK 470     VAL s 161    CG1  CG2                                            
REMARK 470     LEU s 166    CG   CD1  CD2                                       
REMARK 470     LYS s 200    CG   CD   CE   NZ                                   
REMARK 470     ARG t  44    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS t 156    CG   CD   CE   NZ                                   
REMARK 470     LYS t 195    CG   CD   CE   NZ                                   
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   OG1  THR P    58     O    LEU Q   121              2.17            
REMARK 500   OG1  THR p    58     O    LEU q   121              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU I  38   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    PHE K  22   C   -  N   -  CA  ANGL. DEV. =  17.5 DEGREES          
REMARK 500    TYR M   7   C   -  N   -  CA  ANGL. DEV. =  16.2 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    ASP G  10       -2.52     66.18                                   
REMARK 500    GLU G  19       75.55     48.40                                   
REMARK 500    LYS G  45     -151.55   -140.75                                   
REMARK 500    ASP G  46       34.59    -78.57                                   
REMARK 500    PRO G 133       45.55    -84.43                                   
REMARK 500    LYS G 184      -32.69   -141.15                                   
REMARK 500    LYS G 186       34.37    -95.08                                   
REMARK 500    THR G 190       44.77    -90.82                                   
REMARK 500    PHE G 191      -31.18     71.20                                   
REMARK 500    GLU G 223      -32.73   -140.19                                   
REMARK 500    PHE H   8       71.03     46.55                                   
REMARK 500    SER H   9      -43.57   -134.36                                   
REMARK 500    LEU H  10      -30.99   -149.90                                   
REMARK 500    LYS H  18     -151.67   -146.74                                   
REMARK 500    SER H  61      -62.04   -103.16                                   
REMARK 500    ILE H 233       95.97    -60.95                                   
REMARK 500    ASP I   6      -83.20   -101.15                                   
REMARK 500    SER I   7      -24.59     62.94                                   
REMARK 500    ILE I  11     -162.63   -126.40                                   
REMARK 500    PHE I  12     -167.26    -69.09                                   
REMARK 500    GLU I  15      -13.25     87.26                                   
REMARK 500    HIS I  30       63.63   -100.94                                   
REMARK 500    ASN I  51       70.65     55.08                                   
REMARK 500    LEU I  56     -169.87   -103.97                                   
REMARK 500    SER I  62      109.15   -160.52                                   
REMARK 500    CYS I 107      -24.73     76.20                                   
REMARK 500    ASP I 178       41.24   -109.37                                   
REMARK 500    LYS I 205       -0.59     66.17                                   
REMARK 500    LEU I 206       74.07     56.41                                   
REMARK 500    ASN I 220      -21.15     70.10                                   
REMARK 500    GLU I 250       22.87    -78.19                                   
REMARK 500    TYR J   3      154.11    -44.29                                   
REMARK 500    ALA J   6     -168.87   -112.57                                   
REMARK 500    LYS J  52       -8.87     72.72                                   
REMARK 500    THR J  97     -146.53    -85.90                                   
REMARK 500    VAL J  98      119.33    -24.01                                   
REMARK 500    THR J 147     -168.82   -104.84                                   
REMARK 500    LYS J 174       42.33    -85.66                                   
REMARK 500    ASN J 175      -40.11   -135.40                                   
REMARK 500    ILE J 181      -56.10   -120.92                                   
REMARK 500    PRO J 222       44.62    -79.70                                   
REMARK 500    ASP K   9      -19.93     73.27                                   
REMARK 500    ARG K  10       61.29     20.46                                   
REMARK 500    ARG K  20      160.26    176.83                                   
REMARK 500    PHE K  22       -2.72     73.59                                   
REMARK 500    THR K  55      -60.67    -91.79                                   
REMARK 500    ILE K  70      -60.53   -100.67                                   
REMARK 500    TYR K 103       -2.80   -140.95                                   
REMARK 500    HIS K 227       72.88     58.06                                   
REMARK 500    GLU K 232       -4.39     66.97                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     169 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 THR I   10     ILE I   11                   38.43                    
REMARK 500 ASN I  220     GLY I  221                  142.47                    
REMARK 500 GLY I  221     LYS I  222                 -145.57                    
REMARK 500 ASP K    9     ARG K   10                  126.99                    
REMARK 500 GLY K   19     ARG K   20                  -31.95                    
REMARK 500 LEU K  121     GLN K  122                  149.41                    
REMARK 500 GLU K  232     GLU K  233                  149.28                    
REMARK 500 SER O  171     ASN O  172                 -143.06                    
REMARK 500 ASN O  172     ILE O  173                  140.84                    
REMARK 500 ASN i  220     GLY i  221                  147.96                    
REMARK 500 GLY i  221     LYS i  222                 -148.80                    
REMARK 500 ALA j  180     ILE j  181                 -118.00                    
REMARK 500 ASN o  172     ILE o  173                 -141.50                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-8662   RELATED DB: EMDB                              
REMARK 900 NUCLEOTIDE-DRIVEN TRIPLE-STATE REMODELING OF THE AAA-ATPASE CHANNEL  
REMARK 900 IN THE ACTIVATED HUMAN 26S PROTEASOME                                
REMARK 900 RELATED ID: EMD-8666   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8663   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8664   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8665   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8667   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8668   RELATED DB: EMDB                              
REMARK 900 RELATED ID: 5VFS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VFP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VFQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VFR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VFT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VFU   RELATED DB: PDB                                   
DBREF  5VFO G    5   244  UNP    P60900   PSA6_HUMAN       5    244             
DBREF  5VFO H    3   234  UNP    P25787   PSA2_HUMAN       3    234             
DBREF  5VFO I    2   251  UNP    P25789   PSA4_HUMAN       2    251             
DBREF  5VFO J    2   244  UNP    O14818   PSA7_HUMAN       2    244             
DBREF  5VFO K    8   241  UNP    P28066   PSA5_HUMAN       8    241             
DBREF  5VFO L    4   241  UNP    P25786   PSA1_HUMAN       4    241             
DBREF  5VFO M    1   245  UNP    P25788   PSA3_HUMAN       2    246             
DBREF  5VFO N    1   191  UNP    P28072   PSB6_HUMAN      35    225             
DBREF  5VFO O    1   220  UNP    Q99436   PSB7_HUMAN      44    263             
DBREF  5VFO P    2   205  UNP    P49720   PSB3_HUMAN       2    205             
DBREF  5VFO Q    1   199  UNP    P49721   PSB2_HUMAN       1    199             
DBREF  5VFO R    1   201  UNP    P28074   PSB5_HUMAN      60    260             
DBREF  5VFO S    1   213  UNP    P20618   PSB1_HUMAN      29    241             
DBREF  5VFO T    1   215  UNP    P28070   PSB4_HUMAN      46    260             
DBREF  5VFO g    5   244  UNP    P60900   PSA6_HUMAN       5    244             
DBREF  5VFO h    3   234  UNP    P25787   PSA2_HUMAN       3    234             
DBREF  5VFO i    2   251  UNP    P25789   PSA4_HUMAN       2    251             
DBREF  5VFO j    2   244  UNP    O14818   PSA7_HUMAN       2    244             
DBREF  5VFO k    8   241  UNP    P28066   PSA5_HUMAN       8    241             
DBREF  5VFO l    4   241  UNP    P25786   PSA1_HUMAN       4    241             
DBREF  5VFO m    1   245  UNP    P25788   PSA3_HUMAN       2    246             
DBREF  5VFO n    1   191  UNP    P28072   PSB6_HUMAN      35    225             
DBREF  5VFO o    1   220  UNP    Q99436   PSB7_HUMAN      44    263             
DBREF  5VFO p    2   205  UNP    P49720   PSB3_HUMAN       2    205             
DBREF  5VFO q    1   199  UNP    P49721   PSB2_HUMAN       1    199             
DBREF  5VFO r    1   201  UNP    P28074   PSB5_HUMAN      60    260             
DBREF  5VFO s    1   213  UNP    P20618   PSB1_HUMAN      29    241             
DBREF  5VFO t    1   215  UNP    P28070   PSB4_HUMAN      46    260             
SEQRES   1 G  240  SER SER ALA GLY PHE ASP ARG HIS ILE THR ILE PHE SER          
SEQRES   2 G  240  PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA PHE LYS          
SEQRES   3 G  240  ALA ILE ASN GLN GLY GLY LEU THR SER VAL ALA VAL ARG          
SEQRES   4 G  240  GLY LYS ASP CYS ALA VAL ILE VAL THR GLN LYS LYS VAL          
SEQRES   5 G  240  PRO ASP LYS LEU LEU ASP SER SER THR VAL THR HIS LEU          
SEQRES   6 G  240  PHE LYS ILE THR GLU ASN ILE GLY CYS VAL MET THR GLY          
SEQRES   7 G  240  MET THR ALA ASP SER ARG SER GLN VAL GLN ARG ALA ARG          
SEQRES   8 G  240  TYR GLU ALA ALA ASN TRP LYS TYR LYS TYR GLY TYR GLU          
SEQRES   9 G  240  ILE PRO VAL ASP MET LEU CYS LYS ARG ILE ALA ASP ILE          
SEQRES  10 G  240  SER GLN VAL TYR THR GLN ASN ALA GLU MET ARG PRO LEU          
SEQRES  11 G  240  GLY CYS CYS MET ILE LEU ILE GLY ILE ASP GLU GLU GLN          
SEQRES  12 G  240  GLY PRO GLN VAL TYR LYS CYS ASP PRO ALA GLY TYR TYR          
SEQRES  13 G  240  CYS GLY PHE LYS ALA THR ALA ALA GLY VAL LYS GLN THR          
SEQRES  14 G  240  GLU SER THR SER PHE LEU GLU LYS LYS VAL LYS LYS LYS          
SEQRES  15 G  240  PHE ASP TRP THR PHE GLU GLN THR VAL GLU THR ALA ILE          
SEQRES  16 G  240  THR CYS LEU SER THR VAL LEU SER ILE ASP PHE LYS PRO          
SEQRES  17 G  240  SER GLU ILE GLU VAL GLY VAL VAL THR VAL GLU ASN PRO          
SEQRES  18 G  240  LYS PHE ARG ILE LEU THR GLU ALA GLU ILE ASP ALA HIS          
SEQRES  19 G  240  LEU VAL ALA LEU ALA GLU                                      
SEQRES   1 H  232  GLU ARG GLY TYR SER PHE SER LEU THR THR PHE SER PRO          
SEQRES   2 H  232  SER GLY LYS LEU VAL GLN ILE GLU TYR ALA LEU ALA ALA          
SEQRES   3 H  232  VAL ALA GLY GLY ALA PRO SER VAL GLY ILE LYS ALA ALA          
SEQRES   4 H  232  ASN GLY VAL VAL LEU ALA THR GLU LYS LYS GLN LYS SER          
SEQRES   5 H  232  ILE LEU TYR ASP GLU ARG SER VAL HIS LYS VAL GLU PRO          
SEQRES   6 H  232  ILE THR LYS HIS ILE GLY LEU VAL TYR SER GLY MET GLY          
SEQRES   7 H  232  PRO ASP TYR ARG VAL LEU VAL HIS ARG ALA ARG LYS LEU          
SEQRES   8 H  232  ALA GLN GLN TYR TYR LEU VAL TYR GLN GLU PRO ILE PRO          
SEQRES   9 H  232  THR ALA GLN LEU VAL GLN ARG VAL ALA SER VAL MET GLN          
SEQRES  10 H  232  GLU TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY VAL          
SEQRES  11 H  232  SER LEU LEU ILE CYS GLY TRP ASN GLU GLY ARG PRO TYR          
SEQRES  12 H  232  LEU PHE GLN SER ASP PRO SER GLY ALA TYR PHE ALA TRP          
SEQRES  13 H  232  LYS ALA THR ALA MET GLY LYS ASN TYR VAL ASN GLY LYS          
SEQRES  14 H  232  THR PHE LEU GLU LYS ARG TYR ASN GLU ASP LEU GLU LEU          
SEQRES  15 H  232  GLU ASP ALA ILE HIS THR ALA ILE LEU THR LEU LYS GLU          
SEQRES  16 H  232  SER PHE GLU GLY GLN MET THR GLU ASP ASN ILE GLU VAL          
SEQRES  17 H  232  GLY ILE CYS ASN GLU ALA GLY PHE ARG ARG LEU THR PRO          
SEQRES  18 H  232  THR GLU VAL LYS ASP TYR LEU ALA ALA ILE ALA                  
SEQRES   1 I  250  SER ARG ARG TYR ASP SER ARG THR THR ILE PHE SER PRO          
SEQRES   2 I  250  GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA MET GLU ALA          
SEQRES   3 I  250  ILE GLY HIS ALA GLY THR CYS LEU GLY ILE LEU ALA ASN          
SEQRES   4 I  250  ASP GLY VAL LEU LEU ALA ALA GLU ARG ARG ASN ILE HIS          
SEQRES   5 I  250  LYS LEU LEU ASP GLU VAL PHE PHE SER GLU LYS ILE TYR          
SEQRES   6 I  250  LYS LEU ASN GLU ASP MET ALA CYS SER VAL ALA GLY ILE          
SEQRES   7 I  250  THR SER ASP ALA ASN VAL LEU THR ASN GLU LEU ARG LEU          
SEQRES   8 I  250  ILE ALA GLN ARG TYR LEU LEU GLN TYR GLN GLU PRO ILE          
SEQRES   9 I  250  PRO CYS GLU GLN LEU VAL THR ALA LEU CYS ASP ILE LYS          
SEQRES  10 I  250  GLN ALA TYR THR GLN PHE GLY GLY LYS ARG PRO PHE GLY          
SEQRES  11 I  250  VAL SER LEU LEU TYR ILE GLY TRP ASP LYS HIS TYR GLY          
SEQRES  12 I  250  PHE GLN LEU TYR GLN SER ASP PRO SER GLY ASN TYR GLY          
SEQRES  13 I  250  GLY TRP LYS ALA THR CYS ILE GLY ASN ASN SER ALA ALA          
SEQRES  14 I  250  ALA VAL SER MET LEU LYS GLN ASP TYR LYS GLU GLY GLU          
SEQRES  15 I  250  MET THR LEU LYS SER ALA LEU ALA LEU ALA ILE LYS VAL          
SEQRES  16 I  250  LEU ASN LYS THR MET ASP VAL SER LYS LEU SER ALA GLU          
SEQRES  17 I  250  LYS VAL GLU ILE ALA THR LEU THR ARG GLU ASN GLY LYS          
SEQRES  18 I  250  THR VAL ILE ARG VAL LEU LYS GLN LYS GLU VAL GLU GLN          
SEQRES  19 I  250  LEU ILE LYS LYS HIS GLU GLU GLU GLU ALA LYS ALA GLU          
SEQRES  20 I  250  ARG GLU LYS                                                  
SEQRES   1 J  243  SER TYR ASP ARG ALA ILE THR VAL PHE SER PRO ASP GLY          
SEQRES   2 J  243  HIS LEU PHE GLN VAL GLU TYR ALA GLN GLU ALA VAL LYS          
SEQRES   3 J  243  LYS GLY SER THR ALA VAL GLY VAL ARG GLY ARG ASP ILE          
SEQRES   4 J  243  VAL VAL LEU GLY VAL GLU LYS LYS SER VAL ALA LYS LEU          
SEQRES   5 J  243  GLN ASP GLU ARG THR VAL ARG LYS ILE CYS ALA LEU ASP          
SEQRES   6 J  243  ASP ASN VAL CYS MET ALA PHE ALA GLY LEU THR ALA ASP          
SEQRES   7 J  243  ALA ARG ILE VAL ILE ASN ARG ALA ARG VAL GLU CYS GLN          
SEQRES   8 J  243  SER HIS ARG LEU THR VAL GLU ASP PRO VAL THR VAL GLU          
SEQRES   9 J  243  TYR ILE THR ARG TYR ILE ALA SER LEU LYS GLN ARG TYR          
SEQRES  10 J  243  THR GLN SER ASN GLY ARG ARG PRO PHE GLY ILE SER ALA          
SEQRES  11 J  243  LEU ILE VAL GLY PHE ASP PHE ASP GLY THR PRO ARG LEU          
SEQRES  12 J  243  TYR GLN THR ASP PRO SER GLY THR TYR HIS ALA TRP LYS          
SEQRES  13 J  243  ALA ASN ALA ILE GLY ARG GLY ALA LYS SER VAL ARG GLU          
SEQRES  14 J  243  PHE LEU GLU LYS ASN TYR THR ASP GLU ALA ILE GLU THR          
SEQRES  15 J  243  ASP ASP LEU THR ILE LYS LEU VAL ILE LYS ALA LEU LEU          
SEQRES  16 J  243  GLU VAL VAL GLN SER GLY GLY LYS ASN ILE GLU LEU ALA          
SEQRES  17 J  243  VAL MET ARG ARG ASP GLN SER LEU LYS ILE LEU ASN PRO          
SEQRES  18 J  243  GLU GLU ILE GLU LYS TYR VAL ALA GLU ILE GLU LYS GLU          
SEQRES  19 J  243  LYS GLU GLU ASN GLU LYS LYS LYS GLN                          
SEQRES   1 K  234  TYR ASP ARG GLY VAL ASN THR PHE SER PRO GLU GLY ARG          
SEQRES   2 K  234  LEU PHE GLN VAL GLU TYR ALA ILE GLU ALA ILE LYS LEU          
SEQRES   3 K  234  GLY SER THR ALA ILE GLY ILE GLN THR SER GLU GLY VAL          
SEQRES   4 K  234  CYS LEU ALA VAL GLU LYS ARG ILE THR SER PRO LEU MET          
SEQRES   5 K  234  GLU PRO SER SER ILE GLU LYS ILE VAL GLU ILE ASP ALA          
SEQRES   6 K  234  HIS ILE GLY CYS ALA MET SER GLY LEU ILE ALA ASP ALA          
SEQRES   7 K  234  LYS THR LEU ILE ASP LYS ALA ARG VAL GLU THR GLN ASN          
SEQRES   8 K  234  HIS TRP PHE THR TYR ASN GLU THR MET THR VAL GLU SER          
SEQRES   9 K  234  VAL THR GLN ALA VAL SER ASN LEU ALA LEU GLN PHE GLY          
SEQRES  10 K  234  GLU GLU ASP ALA ASP PRO GLY ALA MET SER ARG PRO PHE          
SEQRES  11 K  234  GLY VAL ALA LEU LEU PHE GLY GLY VAL ASP GLU LYS GLY          
SEQRES  12 K  234  PRO GLN LEU PHE HIS MET ASP PRO SER GLY THR PHE VAL          
SEQRES  13 K  234  GLN CYS ASP ALA ARG ALA ILE GLY SER ALA SER GLU GLY          
SEQRES  14 K  234  ALA GLN SER SER LEU GLN GLU VAL TYR HIS LYS SER MET          
SEQRES  15 K  234  THR LEU LYS GLU ALA ILE LYS SER SER LEU ILE ILE LEU          
SEQRES  16 K  234  LYS GLN VAL MET GLU GLU LYS LEU ASN ALA THR ASN ILE          
SEQRES  17 K  234  GLU LEU ALA THR VAL GLN PRO GLY GLN ASN PHE HIS MET          
SEQRES  18 K  234  PHE THR LYS GLU GLU LEU GLU GLU VAL ILE LYS ASP ILE          
SEQRES   1 L  238  ASN GLN TYR ASP ASN ASP VAL THR VAL TRP SER PRO GLN          
SEQRES   2 L  238  GLY ARG ILE HIS GLN ILE GLU TYR ALA MET GLU ALA VAL          
SEQRES   3 L  238  LYS GLN GLY SER ALA THR VAL GLY LEU LYS SER LYS THR          
SEQRES   4 L  238  HIS ALA VAL LEU VAL ALA LEU LYS ARG ALA GLN SER GLU          
SEQRES   5 L  238  LEU ALA ALA HIS GLN LYS LYS ILE LEU HIS VAL ASP ASN          
SEQRES   6 L  238  HIS ILE GLY ILE SER ILE ALA GLY LEU THR ALA ASP ALA          
SEQRES   7 L  238  ARG LEU LEU CYS ASN PHE MET ARG GLN GLU CYS LEU ASP          
SEQRES   8 L  238  SER ARG PHE VAL PHE ASP ARG PRO LEU PRO VAL SER ARG          
SEQRES   9 L  238  LEU VAL SER LEU ILE GLY SER LYS THR GLN ILE PRO THR          
SEQRES  10 L  238  GLN ARG TYR GLY ARG ARG PRO TYR GLY VAL GLY LEU LEU          
SEQRES  11 L  238  ILE ALA GLY TYR ASP ASP MET GLY PRO HIS ILE PHE GLN          
SEQRES  12 L  238  THR CYS PRO SER ALA ASN TYR PHE ASP CYS ARG ALA MET          
SEQRES  13 L  238  SER ILE GLY ALA ARG SER GLN SER ALA ARG THR TYR LEU          
SEQRES  14 L  238  GLU ARG HIS MET SER GLU PHE MET GLU CYS ASN LEU ASN          
SEQRES  15 L  238  GLU LEU VAL LYS HIS GLY LEU ARG ALA LEU ARG GLU THR          
SEQRES  16 L  238  LEU PRO ALA GLU GLN ASP LEU THR THR LYS ASN VAL SER          
SEQRES  17 L  238  ILE GLY ILE VAL GLY LYS ASP LEU GLU PHE THR ILE TYR          
SEQRES  18 L  238  ASP ASP ASP ASP VAL SER PRO PHE LEU GLU GLY LEU GLU          
SEQRES  19 L  238  GLU ARG PRO GLN                                              
SEQRES   1 M  245  SER SER ILE GLY THR GLY TYR ASP LEU SER ALA SER THR          
SEQRES   2 M  245  PHE SER PRO ASP GLY ARG VAL PHE GLN VAL GLU TYR ALA          
SEQRES   3 M  245  MET LYS ALA VAL GLU ASN SER SER THR ALA ILE GLY ILE          
SEQRES   4 M  245  ARG CYS LYS ASP GLY VAL VAL PHE GLY VAL GLU LYS LEU          
SEQRES   5 M  245  VAL LEU SER LYS LEU TYR GLU GLU GLY SER ASN LYS ARG          
SEQRES   6 M  245  LEU PHE ASN VAL ASP ARG HIS VAL GLY MET ALA VAL ALA          
SEQRES   7 M  245  GLY LEU LEU ALA ASP ALA ARG SER LEU ALA ASP ILE ALA          
SEQRES   8 M  245  ARG GLU GLU ALA SER ASN PHE ARG SER ASN PHE GLY TYR          
SEQRES   9 M  245  ASN ILE PRO LEU LYS HIS LEU ALA ASP ARG VAL ALA MET          
SEQRES  10 M  245  TYR VAL HIS ALA TYR THR LEU TYR SER ALA VAL ARG PRO          
SEQRES  11 M  245  PHE GLY CYS SER PHE MET LEU GLY SER TYR SER VAL ASN          
SEQRES  12 M  245  ASP GLY ALA GLN LEU TYR MET ILE ASP PRO SER GLY VAL          
SEQRES  13 M  245  SER TYR GLY TYR TRP GLY CYS ALA ILE GLY LYS ALA ARG          
SEQRES  14 M  245  GLN ALA ALA LYS THR GLU ILE GLU LYS LEU GLN MET LYS          
SEQRES  15 M  245  GLU MET THR CYS ARG ASP ILE VAL LYS GLU VAL ALA LYS          
SEQRES  16 M  245  ILE ILE TYR ILE VAL HIS ASP GLU VAL LYS ASP LYS ALA          
SEQRES  17 M  245  PHE GLU LEU GLU LEU SER TRP VAL GLY GLU LEU THR ASN          
SEQRES  18 M  245  GLY ARG HIS GLU ILE VAL PRO LYS ASP ILE ARG GLU GLU          
SEQRES  19 M  245  ALA GLU LYS TYR ALA LYS GLU SER LEU LYS GLU                  
SEQRES   1 N  191  THR THR ILE MET ALA VAL GLN PHE ASP GLY GLY VAL VAL          
SEQRES   2 N  191  LEU GLY ALA ASP SER ARG THR THR THR GLY SER TYR ILE          
SEQRES   3 N  191  ALA ASN ARG VAL THR ASP LYS LEU THR PRO ILE HIS ASP          
SEQRES   4 N  191  ARG ILE PHE CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 N  191  GLN ALA VAL ALA ASP ALA VAL THR TYR GLN LEU GLY PHE          
SEQRES   6 N  191  HIS SER ILE GLU LEU ASN GLU PRO PRO LEU VAL HIS THR          
SEQRES   7 N  191  ALA ALA SER LEU PHE LYS GLU MET CYS TYR ARG TYR ARG          
SEQRES   8 N  191  GLU ASP LEU MET ALA GLY ILE ILE ILE ALA GLY TRP ASP          
SEQRES   9 N  191  PRO GLN GLU GLY GLY GLN VAL TYR SER VAL PRO MET GLY          
SEQRES  10 N  191  GLY MET MET VAL ARG GLN SER PHE ALA ILE GLY GLY SER          
SEQRES  11 N  191  GLY SER SER TYR ILE TYR GLY TYR VAL ASP ALA THR TYR          
SEQRES  12 N  191  ARG GLU GLY MET THR LYS GLU GLU CYS LEU GLN PHE THR          
SEQRES  13 N  191  ALA ASN ALA LEU ALA LEU ALA MET GLU ARG ASP GLY SER          
SEQRES  14 N  191  SER GLY GLY VAL ILE ARG LEU ALA ALA ILE ALA GLU SER          
SEQRES  15 N  191  GLY VAL GLU ARG GLN VAL LEU LEU GLY                          
SEQRES   1 O  220  THR THR ILE ALA GLY VAL VAL TYR LYS ASP GLY ILE VAL          
SEQRES   2 O  220  LEU GLY ALA ASP THR ARG ALA THR GLU GLY MET VAL VAL          
SEQRES   3 O  220  ALA ASP LYS ASN CYS SER LYS ILE HIS PHE ILE SER PRO          
SEQRES   4 O  220  ASN ILE TYR CYS CYS GLY ALA GLY THR ALA ALA ASP THR          
SEQRES   5 O  220  ASP MET THR THR GLN LEU ILE SER SER ASN LEU GLU LEU          
SEQRES   6 O  220  HIS SER LEU SER THR GLY ARG LEU PRO ARG VAL VAL THR          
SEQRES   7 O  220  ALA ASN ARG MET LEU LYS GLN MET LEU PHE ARG TYR GLN          
SEQRES   8 O  220  GLY TYR ILE GLY ALA ALA LEU VAL LEU GLY GLY VAL ASP          
SEQRES   9 O  220  VAL THR GLY PRO HIS LEU TYR SER ILE TYR PRO HIS GLY          
SEQRES  10 O  220  SER THR ASP LYS LEU PRO TYR VAL THR MET GLY SER GLY          
SEQRES  11 O  220  SER LEU ALA ALA MET ALA VAL PHE GLU ASP LYS PHE ARG          
SEQRES  12 O  220  PRO ASP MET GLU GLU GLU GLU ALA LYS ASN LEU VAL SER          
SEQRES  13 O  220  GLU ALA ILE ALA ALA GLY ILE PHE ASN ASP LEU GLY SER          
SEQRES  14 O  220  GLY SER ASN ILE ASP LEU CYS VAL ILE SER LYS ASN LYS          
SEQRES  15 O  220  LEU ASP PHE LEU ARG PRO TYR THR VAL PRO ASN LYS LYS          
SEQRES  16 O  220  GLY THR ARG LEU GLY ARG TYR ARG CYS GLU LYS GLY THR          
SEQRES  17 O  220  THR ALA VAL LEU THR GLU LYS ILE THR PRO LEU GLU              
SEQRES   1 P  204  SER ILE MET SER TYR ASN GLY GLY ALA VAL MET ALA MET          
SEQRES   2 P  204  LYS GLY LYS ASN CYS VAL ALA ILE ALA ALA ASP ARG ARG          
SEQRES   3 P  204  PHE GLY ILE GLN ALA GLN MET VAL THR THR ASP PHE GLN          
SEQRES   4 P  204  LYS ILE PHE PRO MET GLY ASP ARG LEU TYR ILE GLY LEU          
SEQRES   5 P  204  ALA GLY LEU ALA THR ASP VAL GLN THR VAL ALA GLN ARG          
SEQRES   6 P  204  LEU LYS PHE ARG LEU ASN LEU TYR GLU LEU LYS GLU GLY          
SEQRES   7 P  204  ARG GLN ILE LYS PRO TYR THR LEU MET SER MET VAL ALA          
SEQRES   8 P  204  ASN LEU LEU TYR GLU LYS ARG PHE GLY PRO TYR TYR THR          
SEQRES   9 P  204  GLU PRO VAL ILE ALA GLY LEU ASP PRO LYS THR PHE LYS          
SEQRES  10 P  204  PRO PHE ILE CYS SER LEU ASP LEU ILE GLY CYS PRO MET          
SEQRES  11 P  204  VAL THR ASP ASP PHE VAL VAL SER GLY THR CYS ALA GLU          
SEQRES  12 P  204  GLN MET TYR GLY MET CYS GLU SER LEU TRP GLU PRO ASN          
SEQRES  13 P  204  MET ASP PRO ASP HIS LEU PHE GLU THR ILE SER GLN ALA          
SEQRES  14 P  204  MET LEU ASN ALA VAL ASP ARG ASP ALA VAL SER GLY MET          
SEQRES  15 P  204  GLY VAL ILE VAL HIS ILE ILE GLU LYS ASP LYS ILE THR          
SEQRES  16 P  204  THR ARG THR LEU LYS ALA ARG MET ASP                          
SEQRES   1 Q  199  MET GLU TYR LEU ILE GLY ILE GLN GLY PRO ASP TYR VAL          
SEQRES   2 Q  199  LEU VAL ALA SER ASP ARG VAL ALA ALA SER ASN ILE VAL          
SEQRES   3 Q  199  GLN MET LYS ASP ASP HIS ASP LYS MET PHE LYS MET SER          
SEQRES   4 Q  199  GLU LYS ILE LEU LEU LEU CYS VAL GLY GLU ALA GLY ASP          
SEQRES   5 Q  199  THR VAL GLN PHE ALA GLU TYR ILE GLN LYS ASN VAL GLN          
SEQRES   6 Q  199  LEU TYR LYS MET ARG ASN GLY TYR GLU LEU SER PRO THR          
SEQRES   7 Q  199  ALA ALA ALA ASN PHE THR ARG ARG ASN LEU ALA ASP CYS          
SEQRES   8 Q  199  LEU ARG SER ARG THR PRO TYR HIS VAL ASN LEU LEU LEU          
SEQRES   9 Q  199  ALA GLY TYR ASP GLU HIS GLU GLY PRO ALA LEU TYR TYR          
SEQRES  10 Q  199  MET ASP TYR LEU ALA ALA LEU ALA LYS ALA PRO PHE ALA          
SEQRES  11 Q  199  ALA HIS GLY TYR GLY ALA PHE LEU THR LEU SER ILE LEU          
SEQRES  12 Q  199  ASP ARG TYR TYR THR PRO THR ILE SER ARG GLU ARG ALA          
SEQRES  13 Q  199  VAL GLU LEU LEU ARG LYS CYS LEU GLU GLU LEU GLN LYS          
SEQRES  14 Q  199  ARG PHE ILE LEU ASN LEU PRO THR PHE SER VAL ARG ILE          
SEQRES  15 Q  199  ILE ASP LYS ASN GLY ILE HIS ASP LEU ASP ASN ILE SER          
SEQRES  16 Q  199  PHE PRO LYS GLN                                              
SEQRES   1 R  201  THR THR THR LEU ALA PHE LYS PHE ARG HIS GLY VAL ILE          
SEQRES   2 R  201  VAL ALA ALA ASP SER ARG ALA THR ALA GLY ALA TYR ILE          
SEQRES   3 R  201  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 R  201  TYR LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 R  201  SER PHE TRP GLU ARG LEU LEU ALA ARG GLN CYS ARG ILE          
SEQRES   6 R  201  TYR GLU LEU ARG ASN LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 R  201  ALA SER LYS LEU LEU ALA ASN MET VAL TYR GLN TYR LYS          
SEQRES   8 R  201  GLY MET GLY LEU SER MET GLY THR MET ILE CYS GLY TRP          
SEQRES   9 R  201  ASP LYS ARG GLY PRO GLY LEU TYR TYR VAL ASP SER GLU          
SEQRES  10 R  201  GLY ASN ARG ILE SER GLY ALA THR PHE SER VAL GLY SER          
SEQRES  11 R  201  GLY SER VAL TYR ALA TYR GLY VAL MET ASP ARG GLY TYR          
SEQRES  12 R  201  SER TYR ASP LEU GLU VAL GLU GLN ALA TYR ASP LEU ALA          
SEQRES  13 R  201  ARG ARG ALA ILE TYR GLN ALA THR TYR ARG ASP ALA TYR          
SEQRES  14 R  201  SER GLY GLY ALA VAL ASN LEU TYR HIS VAL ARG GLU ASP          
SEQRES  15 R  201  GLY TRP ILE ARG VAL SER SER ASP ASN VAL ALA ASP LEU          
SEQRES  16 R  201  HIS GLU LYS TYR SER GLY                                      
SEQRES   1 S  213  ARG PHE SER PRO TYR VAL PHE ASN GLY GLY THR ILE LEU          
SEQRES   2 S  213  ALA ILE ALA GLY GLU ASP PHE ALA ILE VAL ALA SER ASP          
SEQRES   3 S  213  THR ARG LEU SER GLU GLY PHE SER ILE HIS THR ARG ASP          
SEQRES   4 S  213  SER PRO LYS CYS TYR LYS LEU THR ASP LYS THR VAL ILE          
SEQRES   5 S  213  GLY CYS SER GLY PHE HIS GLY ASP CYS LEU THR LEU THR          
SEQRES   6 S  213  LYS ILE ILE GLU ALA ARG LEU LYS MET TYR LYS HIS SER          
SEQRES   7 S  213  ASN ASN LYS ALA MET THR THR GLY ALA ILE ALA ALA MET          
SEQRES   8 S  213  LEU SER THR ILE LEU TYR SER ARG ARG PHE PHE PRO TYR          
SEQRES   9 S  213  TYR VAL TYR ASN ILE ILE GLY GLY LEU ASP GLU GLU GLY          
SEQRES  10 S  213  LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER TYR          
SEQRES  11 S  213  GLN ARG ASP SER PHE LYS ALA GLY GLY SER ALA SER ALA          
SEQRES  12 S  213  MET LEU GLN PRO LEU LEU ASP ASN GLN VAL GLY PHE LYS          
SEQRES  13 S  213  ASN MET GLN ASN VAL GLU HIS VAL PRO LEU SER LEU ASP          
SEQRES  14 S  213  ARG ALA MET ARG LEU VAL LYS ASP VAL PHE ILE SER ALA          
SEQRES  15 S  213  ALA GLU ARG ASP VAL TYR THR GLY ASP ALA LEU ARG ILE          
SEQRES  16 S  213  CYS ILE VAL THR LYS GLU GLY ILE ARG GLU GLU THR VAL          
SEQRES  17 S  213  SER LEU ARG LYS ASP                                          
SEQRES   1 T  215  THR GLN ASN PRO MET VAL THR GLY THR SER VAL LEU GLY          
SEQRES   2 T  215  VAL LYS PHE GLU GLY GLY VAL VAL ILE ALA ALA ASP MET          
SEQRES   3 T  215  LEU GLY SER TYR GLY SER LEU ALA ARG PHE ARG ASN ILE          
SEQRES   4 T  215  SER ARG ILE MET ARG VAL ASN ASN SER THR MET LEU GLY          
SEQRES   5 T  215  ALA SER GLY ASP TYR ALA ASP PHE GLN TYR LEU LYS GLN          
SEQRES   6 T  215  VAL LEU GLY GLN MET VAL ILE ASP GLU GLU LEU LEU GLY          
SEQRES   7 T  215  ASP GLY HIS SER TYR SER PRO ARG ALA ILE HIS SER TRP          
SEQRES   8 T  215  LEU THR ARG ALA MET TYR SER ARG ARG SER LYS MET ASN          
SEQRES   9 T  215  PRO LEU TRP ASN THR MET VAL ILE GLY GLY TYR ALA ASP          
SEQRES  10 T  215  GLY GLU SER PHE LEU GLY TYR VAL ASP MET LEU GLY VAL          
SEQRES  11 T  215  ALA TYR GLU ALA PRO SER LEU ALA THR GLY TYR GLY ALA          
SEQRES  12 T  215  TYR LEU ALA GLN PRO LEU LEU ARG GLU VAL LEU GLU LYS          
SEQRES  13 T  215  GLN PRO VAL LEU SER GLN THR GLU ALA ARG ASP LEU VAL          
SEQRES  14 T  215  GLU ARG CYS MET ARG VAL LEU TYR TYR ARG ASP ALA ARG          
SEQRES  15 T  215  SER TYR ASN ARG PHE GLN ILE ALA THR VAL THR GLU LYS          
SEQRES  16 T  215  GLY VAL GLU ILE GLU GLY PRO LEU SER THR GLU THR ASN          
SEQRES  17 T  215  TRP ASP ILE ALA HIS MET ILE                                  
SEQRES   1 g  240  SER SER ALA GLY PHE ASP ARG HIS ILE THR ILE PHE SER          
SEQRES   2 g  240  PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA PHE LYS          
SEQRES   3 g  240  ALA ILE ASN GLN GLY GLY LEU THR SER VAL ALA VAL ARG          
SEQRES   4 g  240  GLY LYS ASP CYS ALA VAL ILE VAL THR GLN LYS LYS VAL          
SEQRES   5 g  240  PRO ASP LYS LEU LEU ASP SER SER THR VAL THR HIS LEU          
SEQRES   6 g  240  PHE LYS ILE THR GLU ASN ILE GLY CYS VAL MET THR GLY          
SEQRES   7 g  240  MET THR ALA ASP SER ARG SER GLN VAL GLN ARG ALA ARG          
SEQRES   8 g  240  TYR GLU ALA ALA ASN TRP LYS TYR LYS TYR GLY TYR GLU          
SEQRES   9 g  240  ILE PRO VAL ASP MET LEU CYS LYS ARG ILE ALA ASP ILE          
SEQRES  10 g  240  SER GLN VAL TYR THR GLN ASN ALA GLU MET ARG PRO LEU          
SEQRES  11 g  240  GLY CYS CYS MET ILE LEU ILE GLY ILE ASP GLU GLU GLN          
SEQRES  12 g  240  GLY PRO GLN VAL TYR LYS CYS ASP PRO ALA GLY TYR TYR          
SEQRES  13 g  240  CYS GLY PHE LYS ALA THR ALA ALA GLY VAL LYS GLN THR          
SEQRES  14 g  240  GLU SER THR SER PHE LEU GLU LYS LYS VAL LYS LYS LYS          
SEQRES  15 g  240  PHE ASP TRP THR PHE GLU GLN THR VAL GLU THR ALA ILE          
SEQRES  16 g  240  THR CYS LEU SER THR VAL LEU SER ILE ASP PHE LYS PRO          
SEQRES  17 g  240  SER GLU ILE GLU VAL GLY VAL VAL THR VAL GLU ASN PRO          
SEQRES  18 g  240  LYS PHE ARG ILE LEU THR GLU ALA GLU ILE ASP ALA HIS          
SEQRES  19 g  240  LEU VAL ALA LEU ALA GLU                                      
SEQRES   1 h  232  GLU ARG GLY TYR SER PHE SER LEU THR THR PHE SER PRO          
SEQRES   2 h  232  SER GLY LYS LEU VAL GLN ILE GLU TYR ALA LEU ALA ALA          
SEQRES   3 h  232  VAL ALA GLY GLY ALA PRO SER VAL GLY ILE LYS ALA ALA          
SEQRES   4 h  232  ASN GLY VAL VAL LEU ALA THR GLU LYS LYS GLN LYS SER          
SEQRES   5 h  232  ILE LEU TYR ASP GLU ARG SER VAL HIS LYS VAL GLU PRO          
SEQRES   6 h  232  ILE THR LYS HIS ILE GLY LEU VAL TYR SER GLY MET GLY          
SEQRES   7 h  232  PRO ASP TYR ARG VAL LEU VAL HIS ARG ALA ARG LYS LEU          
SEQRES   8 h  232  ALA GLN GLN TYR TYR LEU VAL TYR GLN GLU PRO ILE PRO          
SEQRES   9 h  232  THR ALA GLN LEU VAL GLN ARG VAL ALA SER VAL MET GLN          
SEQRES  10 h  232  GLU TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY VAL          
SEQRES  11 h  232  SER LEU LEU ILE CYS GLY TRP ASN GLU GLY ARG PRO TYR          
SEQRES  12 h  232  LEU PHE GLN SER ASP PRO SER GLY ALA TYR PHE ALA TRP          
SEQRES  13 h  232  LYS ALA THR ALA MET GLY LYS ASN TYR VAL ASN GLY LYS          
SEQRES  14 h  232  THR PHE LEU GLU LYS ARG TYR ASN GLU ASP LEU GLU LEU          
SEQRES  15 h  232  GLU ASP ALA ILE HIS THR ALA ILE LEU THR LEU LYS GLU          
SEQRES  16 h  232  SER PHE GLU GLY GLN MET THR GLU ASP ASN ILE GLU VAL          
SEQRES  17 h  232  GLY ILE CYS ASN GLU ALA GLY PHE ARG ARG LEU THR PRO          
SEQRES  18 h  232  THR GLU VAL LYS ASP TYR LEU ALA ALA ILE ALA                  
SEQRES   1 i  250  SER ARG ARG TYR ASP SER ARG THR THR ILE PHE SER PRO          
SEQRES   2 i  250  GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA MET GLU ALA          
SEQRES   3 i  250  ILE GLY HIS ALA GLY THR CYS LEU GLY ILE LEU ALA ASN          
SEQRES   4 i  250  ASP GLY VAL LEU LEU ALA ALA GLU ARG ARG ASN ILE HIS          
SEQRES   5 i  250  LYS LEU LEU ASP GLU VAL PHE PHE SER GLU LYS ILE TYR          
SEQRES   6 i  250  LYS LEU ASN GLU ASP MET ALA CYS SER VAL ALA GLY ILE          
SEQRES   7 i  250  THR SER ASP ALA ASN VAL LEU THR ASN GLU LEU ARG LEU          
SEQRES   8 i  250  ILE ALA GLN ARG TYR LEU LEU GLN TYR GLN GLU PRO ILE          
SEQRES   9 i  250  PRO CYS GLU GLN LEU VAL THR ALA LEU CYS ASP ILE LYS          
SEQRES  10 i  250  GLN ALA TYR THR GLN PHE GLY GLY LYS ARG PRO PHE GLY          
SEQRES  11 i  250  VAL SER LEU LEU TYR ILE GLY TRP ASP LYS HIS TYR GLY          
SEQRES  12 i  250  PHE GLN LEU TYR GLN SER ASP PRO SER GLY ASN TYR GLY          
SEQRES  13 i  250  GLY TRP LYS ALA THR CYS ILE GLY ASN ASN SER ALA ALA          
SEQRES  14 i  250  ALA VAL SER MET LEU LYS GLN ASP TYR LYS GLU GLY GLU          
SEQRES  15 i  250  MET THR LEU LYS SER ALA LEU ALA LEU ALA ILE LYS VAL          
SEQRES  16 i  250  LEU ASN LYS THR MET ASP VAL SER LYS LEU SER ALA GLU          
SEQRES  17 i  250  LYS VAL GLU ILE ALA THR LEU THR ARG GLU ASN GLY LYS          
SEQRES  18 i  250  THR VAL ILE ARG VAL LEU LYS GLN LYS GLU VAL GLU GLN          
SEQRES  19 i  250  LEU ILE LYS LYS HIS GLU GLU GLU GLU ALA LYS ALA GLU          
SEQRES  20 i  250  ARG GLU LYS                                                  
SEQRES   1 j  243  SER TYR ASP ARG ALA ILE THR VAL PHE SER PRO ASP GLY          
SEQRES   2 j  243  HIS LEU PHE GLN VAL GLU TYR ALA GLN GLU ALA VAL LYS          
SEQRES   3 j  243  LYS GLY SER THR ALA VAL GLY VAL ARG GLY ARG ASP ILE          
SEQRES   4 j  243  VAL VAL LEU GLY VAL GLU LYS LYS SER VAL ALA LYS LEU          
SEQRES   5 j  243  GLN ASP GLU ARG THR VAL ARG LYS ILE CYS ALA LEU ASP          
SEQRES   6 j  243  ASP ASN VAL CYS MET ALA PHE ALA GLY LEU THR ALA ASP          
SEQRES   7 j  243  ALA ARG ILE VAL ILE ASN ARG ALA ARG VAL GLU CYS GLN          
SEQRES   8 j  243  SER HIS ARG LEU THR VAL GLU ASP PRO VAL THR VAL GLU          
SEQRES   9 j  243  TYR ILE THR ARG TYR ILE ALA SER LEU LYS GLN ARG TYR          
SEQRES  10 j  243  THR GLN SER ASN GLY ARG ARG PRO PHE GLY ILE SER ALA          
SEQRES  11 j  243  LEU ILE VAL GLY PHE ASP PHE ASP GLY THR PRO ARG LEU          
SEQRES  12 j  243  TYR GLN THR ASP PRO SER GLY THR TYR HIS ALA TRP LYS          
SEQRES  13 j  243  ALA ASN ALA ILE GLY ARG GLY ALA LYS SER VAL ARG GLU          
SEQRES  14 j  243  PHE LEU GLU LYS ASN TYR THR ASP GLU ALA ILE GLU THR          
SEQRES  15 j  243  ASP ASP LEU THR ILE LYS LEU VAL ILE LYS ALA LEU LEU          
SEQRES  16 j  243  GLU VAL VAL GLN SER GLY GLY LYS ASN ILE GLU LEU ALA          
SEQRES  17 j  243  VAL MET ARG ARG ASP GLN SER LEU LYS ILE LEU ASN PRO          
SEQRES  18 j  243  GLU GLU ILE GLU LYS TYR VAL ALA GLU ILE GLU LYS GLU          
SEQRES  19 j  243  LYS GLU GLU ASN GLU LYS LYS LYS GLN                          
SEQRES   1 k  234  TYR ASP ARG GLY VAL ASN THR PHE SER PRO GLU GLY ARG          
SEQRES   2 k  234  LEU PHE GLN VAL GLU TYR ALA ILE GLU ALA ILE LYS LEU          
SEQRES   3 k  234  GLY SER THR ALA ILE GLY ILE GLN THR SER GLU GLY VAL          
SEQRES   4 k  234  CYS LEU ALA VAL GLU LYS ARG ILE THR SER PRO LEU MET          
SEQRES   5 k  234  GLU PRO SER SER ILE GLU LYS ILE VAL GLU ILE ASP ALA          
SEQRES   6 k  234  HIS ILE GLY CYS ALA MET SER GLY LEU ILE ALA ASP ALA          
SEQRES   7 k  234  LYS THR LEU ILE ASP LYS ALA ARG VAL GLU THR GLN ASN          
SEQRES   8 k  234  HIS TRP PHE THR TYR ASN GLU THR MET THR VAL GLU SER          
SEQRES   9 k  234  VAL THR GLN ALA VAL SER ASN LEU ALA LEU GLN PHE GLY          
SEQRES  10 k  234  GLU GLU ASP ALA ASP PRO GLY ALA MET SER ARG PRO PHE          
SEQRES  11 k  234  GLY VAL ALA LEU LEU PHE GLY GLY VAL ASP GLU LYS GLY          
SEQRES  12 k  234  PRO GLN LEU PHE HIS MET ASP PRO SER GLY THR PHE VAL          
SEQRES  13 k  234  GLN CYS ASP ALA ARG ALA ILE GLY SER ALA SER GLU GLY          
SEQRES  14 k  234  ALA GLN SER SER LEU GLN GLU VAL TYR HIS LYS SER MET          
SEQRES  15 k  234  THR LEU LYS GLU ALA ILE LYS SER SER LEU ILE ILE LEU          
SEQRES  16 k  234  LYS GLN VAL MET GLU GLU LYS LEU ASN ALA THR ASN ILE          
SEQRES  17 k  234  GLU LEU ALA THR VAL GLN PRO GLY GLN ASN PHE HIS MET          
SEQRES  18 k  234  PHE THR LYS GLU GLU LEU GLU GLU VAL ILE LYS ASP ILE          
SEQRES   1 l  238  ASN GLN TYR ASP ASN ASP VAL THR VAL TRP SER PRO GLN          
SEQRES   2 l  238  GLY ARG ILE HIS GLN ILE GLU TYR ALA MET GLU ALA VAL          
SEQRES   3 l  238  LYS GLN GLY SER ALA THR VAL GLY LEU LYS SER LYS THR          
SEQRES   4 l  238  HIS ALA VAL LEU VAL ALA LEU LYS ARG ALA GLN SER GLU          
SEQRES   5 l  238  LEU ALA ALA HIS GLN LYS LYS ILE LEU HIS VAL ASP ASN          
SEQRES   6 l  238  HIS ILE GLY ILE SER ILE ALA GLY LEU THR ALA ASP ALA          
SEQRES   7 l  238  ARG LEU LEU CYS ASN PHE MET ARG GLN GLU CYS LEU ASP          
SEQRES   8 l  238  SER ARG PHE VAL PHE ASP ARG PRO LEU PRO VAL SER ARG          
SEQRES   9 l  238  LEU VAL SER LEU ILE GLY SER LYS THR GLN ILE PRO THR          
SEQRES  10 l  238  GLN ARG TYR GLY ARG ARG PRO TYR GLY VAL GLY LEU LEU          
SEQRES  11 l  238  ILE ALA GLY TYR ASP ASP MET GLY PRO HIS ILE PHE GLN          
SEQRES  12 l  238  THR CYS PRO SER ALA ASN TYR PHE ASP CYS ARG ALA MET          
SEQRES  13 l  238  SER ILE GLY ALA ARG SER GLN SER ALA ARG THR TYR LEU          
SEQRES  14 l  238  GLU ARG HIS MET SER GLU PHE MET GLU CYS ASN LEU ASN          
SEQRES  15 l  238  GLU LEU VAL LYS HIS GLY LEU ARG ALA LEU ARG GLU THR          
SEQRES  16 l  238  LEU PRO ALA GLU GLN ASP LEU THR THR LYS ASN VAL SER          
SEQRES  17 l  238  ILE GLY ILE VAL GLY LYS ASP LEU GLU PHE THR ILE TYR          
SEQRES  18 l  238  ASP ASP ASP ASP VAL SER PRO PHE LEU GLU GLY LEU GLU          
SEQRES  19 l  238  GLU ARG PRO GLN                                              
SEQRES   1 m  245  SER SER ILE GLY THR GLY TYR ASP LEU SER ALA SER THR          
SEQRES   2 m  245  PHE SER PRO ASP GLY ARG VAL PHE GLN VAL GLU TYR ALA          
SEQRES   3 m  245  MET LYS ALA VAL GLU ASN SER SER THR ALA ILE GLY ILE          
SEQRES   4 m  245  ARG CYS LYS ASP GLY VAL VAL PHE GLY VAL GLU LYS LEU          
SEQRES   5 m  245  VAL LEU SER LYS LEU TYR GLU GLU GLY SER ASN LYS ARG          
SEQRES   6 m  245  LEU PHE ASN VAL ASP ARG HIS VAL GLY MET ALA VAL ALA          
SEQRES   7 m  245  GLY LEU LEU ALA ASP ALA ARG SER LEU ALA ASP ILE ALA          
SEQRES   8 m  245  ARG GLU GLU ALA SER ASN PHE ARG SER ASN PHE GLY TYR          
SEQRES   9 m  245  ASN ILE PRO LEU LYS HIS LEU ALA ASP ARG VAL ALA MET          
SEQRES  10 m  245  TYR VAL HIS ALA TYR THR LEU TYR SER ALA VAL ARG PRO          
SEQRES  11 m  245  PHE GLY CYS SER PHE MET LEU GLY SER TYR SER VAL ASN          
SEQRES  12 m  245  ASP GLY ALA GLN LEU TYR MET ILE ASP PRO SER GLY VAL          
SEQRES  13 m  245  SER TYR GLY TYR TRP GLY CYS ALA ILE GLY LYS ALA ARG          
SEQRES  14 m  245  GLN ALA ALA LYS THR GLU ILE GLU LYS LEU GLN MET LYS          
SEQRES  15 m  245  GLU MET THR CYS ARG ASP ILE VAL LYS GLU VAL ALA LYS          
SEQRES  16 m  245  ILE ILE TYR ILE VAL HIS ASP GLU VAL LYS ASP LYS ALA          
SEQRES  17 m  245  PHE GLU LEU GLU LEU SER TRP VAL GLY GLU LEU THR ASN          
SEQRES  18 m  245  GLY ARG HIS GLU ILE VAL PRO LYS ASP ILE ARG GLU GLU          
SEQRES  19 m  245  ALA GLU LYS TYR ALA LYS GLU SER LEU LYS GLU                  
SEQRES   1 n  191  THR THR ILE MET ALA VAL GLN PHE ASP GLY GLY VAL VAL          
SEQRES   2 n  191  LEU GLY ALA ASP SER ARG THR THR THR GLY SER TYR ILE          
SEQRES   3 n  191  ALA ASN ARG VAL THR ASP LYS LEU THR PRO ILE HIS ASP          
SEQRES   4 n  191  ARG ILE PHE CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 n  191  GLN ALA VAL ALA ASP ALA VAL THR TYR GLN LEU GLY PHE          
SEQRES   6 n  191  HIS SER ILE GLU LEU ASN GLU PRO PRO LEU VAL HIS THR          
SEQRES   7 n  191  ALA ALA SER LEU PHE LYS GLU MET CYS TYR ARG TYR ARG          
SEQRES   8 n  191  GLU ASP LEU MET ALA GLY ILE ILE ILE ALA GLY TRP ASP          
SEQRES   9 n  191  PRO GLN GLU GLY GLY GLN VAL TYR SER VAL PRO MET GLY          
SEQRES  10 n  191  GLY MET MET VAL ARG GLN SER PHE ALA ILE GLY GLY SER          
SEQRES  11 n  191  GLY SER SER TYR ILE TYR GLY TYR VAL ASP ALA THR TYR          
SEQRES  12 n  191  ARG GLU GLY MET THR LYS GLU GLU CYS LEU GLN PHE THR          
SEQRES  13 n  191  ALA ASN ALA LEU ALA LEU ALA MET GLU ARG ASP GLY SER          
SEQRES  14 n  191  SER GLY GLY VAL ILE ARG LEU ALA ALA ILE ALA GLU SER          
SEQRES  15 n  191  GLY VAL GLU ARG GLN VAL LEU LEU GLY                          
SEQRES   1 o  220  THR THR ILE ALA GLY VAL VAL TYR LYS ASP GLY ILE VAL          
SEQRES   2 o  220  LEU GLY ALA ASP THR ARG ALA THR GLU GLY MET VAL VAL          
SEQRES   3 o  220  ALA ASP LYS ASN CYS SER LYS ILE HIS PHE ILE SER PRO          
SEQRES   4 o  220  ASN ILE TYR CYS CYS GLY ALA GLY THR ALA ALA ASP THR          
SEQRES   5 o  220  ASP MET THR THR GLN LEU ILE SER SER ASN LEU GLU LEU          
SEQRES   6 o  220  HIS SER LEU SER THR GLY ARG LEU PRO ARG VAL VAL THR          
SEQRES   7 o  220  ALA ASN ARG MET LEU LYS GLN MET LEU PHE ARG TYR GLN          
SEQRES   8 o  220  GLY TYR ILE GLY ALA ALA LEU VAL LEU GLY GLY VAL ASP          
SEQRES   9 o  220  VAL THR GLY PRO HIS LEU TYR SER ILE TYR PRO HIS GLY          
SEQRES  10 o  220  SER THR ASP LYS LEU PRO TYR VAL THR MET GLY SER GLY          
SEQRES  11 o  220  SER LEU ALA ALA MET ALA VAL PHE GLU ASP LYS PHE ARG          
SEQRES  12 o  220  PRO ASP MET GLU GLU GLU GLU ALA LYS ASN LEU VAL SER          
SEQRES  13 o  220  GLU ALA ILE ALA ALA GLY ILE PHE ASN ASP LEU GLY SER          
SEQRES  14 o  220  GLY SER ASN ILE ASP LEU CYS VAL ILE SER LYS ASN LYS          
SEQRES  15 o  220  LEU ASP PHE LEU ARG PRO TYR THR VAL PRO ASN LYS LYS          
SEQRES  16 o  220  GLY THR ARG LEU GLY ARG TYR ARG CYS GLU LYS GLY THR          
SEQRES  17 o  220  THR ALA VAL LEU THR GLU LYS ILE THR PRO LEU GLU              
SEQRES   1 p  204  SER ILE MET SER TYR ASN GLY GLY ALA VAL MET ALA MET          
SEQRES   2 p  204  LYS GLY LYS ASN CYS VAL ALA ILE ALA ALA ASP ARG ARG          
SEQRES   3 p  204  PHE GLY ILE GLN ALA GLN MET VAL THR THR ASP PHE GLN          
SEQRES   4 p  204  LYS ILE PHE PRO MET GLY ASP ARG LEU TYR ILE GLY LEU          
SEQRES   5 p  204  ALA GLY LEU ALA THR ASP VAL GLN THR VAL ALA GLN ARG          
SEQRES   6 p  204  LEU LYS PHE ARG LEU ASN LEU TYR GLU LEU LYS GLU GLY          
SEQRES   7 p  204  ARG GLN ILE LYS PRO TYR THR LEU MET SER MET VAL ALA          
SEQRES   8 p  204  ASN LEU LEU TYR GLU LYS ARG PHE GLY PRO TYR TYR THR          
SEQRES   9 p  204  GLU PRO VAL ILE ALA GLY LEU ASP PRO LYS THR PHE LYS          
SEQRES  10 p  204  PRO PHE ILE CYS SER LEU ASP LEU ILE GLY CYS PRO MET          
SEQRES  11 p  204  VAL THR ASP ASP PHE VAL VAL SER GLY THR CYS ALA GLU          
SEQRES  12 p  204  GLN MET TYR GLY MET CYS GLU SER LEU TRP GLU PRO ASN          
SEQRES  13 p  204  MET ASP PRO ASP HIS LEU PHE GLU THR ILE SER GLN ALA          
SEQRES  14 p  204  MET LEU ASN ALA VAL ASP ARG ASP ALA VAL SER GLY MET          
SEQRES  15 p  204  GLY VAL ILE VAL HIS ILE ILE GLU LYS ASP LYS ILE THR          
SEQRES  16 p  204  THR ARG THR LEU LYS ALA ARG MET ASP                          
SEQRES   1 q  199  MET GLU TYR LEU ILE GLY ILE GLN GLY PRO ASP TYR VAL          
SEQRES   2 q  199  LEU VAL ALA SER ASP ARG VAL ALA ALA SER ASN ILE VAL          
SEQRES   3 q  199  GLN MET LYS ASP ASP HIS ASP LYS MET PHE LYS MET SER          
SEQRES   4 q  199  GLU LYS ILE LEU LEU LEU CYS VAL GLY GLU ALA GLY ASP          
SEQRES   5 q  199  THR VAL GLN PHE ALA GLU TYR ILE GLN LYS ASN VAL GLN          
SEQRES   6 q  199  LEU TYR LYS MET ARG ASN GLY TYR GLU LEU SER PRO THR          
SEQRES   7 q  199  ALA ALA ALA ASN PHE THR ARG ARG ASN LEU ALA ASP CYS          
SEQRES   8 q  199  LEU ARG SER ARG THR PRO TYR HIS VAL ASN LEU LEU LEU          
SEQRES   9 q  199  ALA GLY TYR ASP GLU HIS GLU GLY PRO ALA LEU TYR TYR          
SEQRES  10 q  199  MET ASP TYR LEU ALA ALA LEU ALA LYS ALA PRO PHE ALA          
SEQRES  11 q  199  ALA HIS GLY TYR GLY ALA PHE LEU THR LEU SER ILE LEU          
SEQRES  12 q  199  ASP ARG TYR TYR THR PRO THR ILE SER ARG GLU ARG ALA          
SEQRES  13 q  199  VAL GLU LEU LEU ARG LYS CYS LEU GLU GLU LEU GLN LYS          
SEQRES  14 q  199  ARG PHE ILE LEU ASN LEU PRO THR PHE SER VAL ARG ILE          
SEQRES  15 q  199  ILE ASP LYS ASN GLY ILE HIS ASP LEU ASP ASN ILE SER          
SEQRES  16 q  199  PHE PRO LYS GLN                                              
SEQRES   1 r  201  THR THR THR LEU ALA PHE LYS PHE ARG HIS GLY VAL ILE          
SEQRES   2 r  201  VAL ALA ALA ASP SER ARG ALA THR ALA GLY ALA TYR ILE          
SEQRES   3 r  201  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 r  201  TYR LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 r  201  SER PHE TRP GLU ARG LEU LEU ALA ARG GLN CYS ARG ILE          
SEQRES   6 r  201  TYR GLU LEU ARG ASN LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 r  201  ALA SER LYS LEU LEU ALA ASN MET VAL TYR GLN TYR LYS          
SEQRES   8 r  201  GLY MET GLY LEU SER MET GLY THR MET ILE CYS GLY TRP          
SEQRES   9 r  201  ASP LYS ARG GLY PRO GLY LEU TYR TYR VAL ASP SER GLU          
SEQRES  10 r  201  GLY ASN ARG ILE SER GLY ALA THR PHE SER VAL GLY SER          
SEQRES  11 r  201  GLY SER VAL TYR ALA TYR GLY VAL MET ASP ARG GLY TYR          
SEQRES  12 r  201  SER TYR ASP LEU GLU VAL GLU GLN ALA TYR ASP LEU ALA          
SEQRES  13 r  201  ARG ARG ALA ILE TYR GLN ALA THR TYR ARG ASP ALA TYR          
SEQRES  14 r  201  SER GLY GLY ALA VAL ASN LEU TYR HIS VAL ARG GLU ASP          
SEQRES  15 r  201  GLY TRP ILE ARG VAL SER SER ASP ASN VAL ALA ASP LEU          
SEQRES  16 r  201  HIS GLU LYS TYR SER GLY                                      
SEQRES   1 s  213  ARG PHE SER PRO TYR VAL PHE ASN GLY GLY THR ILE LEU          
SEQRES   2 s  213  ALA ILE ALA GLY GLU ASP PHE ALA ILE VAL ALA SER ASP          
SEQRES   3 s  213  THR ARG LEU SER GLU GLY PHE SER ILE HIS THR ARG ASP          
SEQRES   4 s  213  SER PRO LYS CYS TYR LYS LEU THR ASP LYS THR VAL ILE          
SEQRES   5 s  213  GLY CYS SER GLY PHE HIS GLY ASP CYS LEU THR LEU THR          
SEQRES   6 s  213  LYS ILE ILE GLU ALA ARG LEU LYS MET TYR LYS HIS SER          
SEQRES   7 s  213  ASN ASN LYS ALA MET THR THR GLY ALA ILE ALA ALA MET          
SEQRES   8 s  213  LEU SER THR ILE LEU TYR SER ARG ARG PHE PHE PRO TYR          
SEQRES   9 s  213  TYR VAL TYR ASN ILE ILE GLY GLY LEU ASP GLU GLU GLY          
SEQRES  10 s  213  LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER TYR          
SEQRES  11 s  213  GLN ARG ASP SER PHE LYS ALA GLY GLY SER ALA SER ALA          
SEQRES  12 s  213  MET LEU GLN PRO LEU LEU ASP ASN GLN VAL GLY PHE LYS          
SEQRES  13 s  213  ASN MET GLN ASN VAL GLU HIS VAL PRO LEU SER LEU ASP          
SEQRES  14 s  213  ARG ALA MET ARG LEU VAL LYS ASP VAL PHE ILE SER ALA          
SEQRES  15 s  213  ALA GLU ARG ASP VAL TYR THR GLY ASP ALA LEU ARG ILE          
SEQRES  16 s  213  CYS ILE VAL THR LYS GLU GLY ILE ARG GLU GLU THR VAL          
SEQRES  17 s  213  SER LEU ARG LYS ASP                                          
SEQRES   1 t  215  THR GLN ASN PRO MET VAL THR GLY THR SER VAL LEU GLY          
SEQRES   2 t  215  VAL LYS PHE GLU GLY GLY VAL VAL ILE ALA ALA ASP MET          
SEQRES   3 t  215  LEU GLY SER TYR GLY SER LEU ALA ARG PHE ARG ASN ILE          
SEQRES   4 t  215  SER ARG ILE MET ARG VAL ASN ASN SER THR MET LEU GLY          
SEQRES   5 t  215  ALA SER GLY ASP TYR ALA ASP PHE GLN TYR LEU LYS GLN          
SEQRES   6 t  215  VAL LEU GLY GLN MET VAL ILE ASP GLU GLU LEU LEU GLY          
SEQRES   7 t  215  ASP GLY HIS SER TYR SER PRO ARG ALA ILE HIS SER TRP          
SEQRES   8 t  215  LEU THR ARG ALA MET TYR SER ARG ARG SER LYS MET ASN          
SEQRES   9 t  215  PRO LEU TRP ASN THR MET VAL ILE GLY GLY TYR ALA ASP          
SEQRES  10 t  215  GLY GLU SER PHE LEU GLY TYR VAL ASP MET LEU GLY VAL          
SEQRES  11 t  215  ALA TYR GLU ALA PRO SER LEU ALA THR GLY TYR GLY ALA          
SEQRES  12 t  215  TYR LEU ALA GLN PRO LEU LEU ARG GLU VAL LEU GLU LYS          
SEQRES  13 t  215  GLN PRO VAL LEU SER GLN THR GLU ALA ARG ASP LEU VAL          
SEQRES  14 t  215  GLU ARG CYS MET ARG VAL LEU TYR TYR ARG ASP ALA ARG          
SEQRES  15 t  215  SER TYR ASN ARG PHE GLN ILE ALA THR VAL THR GLU LYS          
SEQRES  16 t  215  GLY VAL GLU ILE GLU GLY PRO LEU SER THR GLU THR ASN          
SEQRES  17 t  215  TRP ASP ILE ALA HIS MET ILE                                  
HELIX    1 AA1 GLN G   24  PHE G   29  1                                   6    
HELIX    2 AA2 SER G   63  THR G   67  5                                   5    
HELIX    3 AA3 MET G   83  GLY G  106  1                                  24    
HELIX    4 AA4 PRO G  110  ASN G  128  1                                  19    
HELIX    5 AA5 LYS G  171  LYS G  181  1                                  11    
HELIX    6 AA6 PHE G  191  SER G  207  1                                  17    
HELIX    7 AA7 THR G  231  LEU G  242  1                                  12    
HELIX    8 AA8 LEU H   19  GLY H   31  1                                  13    
HELIX    9 AA9 MET H   79  GLN H  102  1                                  24    
HELIX   10 AB1 PRO H  106  GLN H  123  1                                  18    
HELIX   11 AB2 ASN H  166  TYR H  178  1                                  13    
HELIX   12 AB3 GLU H  183  PHE H  199  1                                  17    
HELIX   13 AB4 THR H  222  LEU H  230  1                                   9    
HELIX   14 AB5 TYR I   19  HIS I   30  1                                  12    
HELIX   15 AB6 SER I   81  GLN I  102  1                                  22    
HELIX   16 AB7 CYS I  107  PHE I  124  1                                  18    
HELIX   17 AB8 SER I  168  ASP I  178  1                                  11    
HELIX   18 AB9 THR I  185  MET I  201  1                                  17    
HELIX   19 AC1 SER I  207  GLU I  209  5                                   3    
HELIX   20 AC2 LYS I  229  GLU I  248  1                                  20    
HELIX   21 AC3 ARG I  249  LYS I  251  5                                   3    
HELIX   22 AC4 LEU J   16  LYS J   28  1                                  13    
HELIX   23 AC5 LEU J   76  THR J   97  1                                  22    
HELIX   24 AC6 THR J  103  GLN J  120  1                                  18    
HELIX   25 AC7 PHE J  138  GLY J  140  5                                   3    
HELIX   26 AC8 GLY J  164  LYS J  174  1                                  11    
HELIX   27 AC9 THR J  183  GLU J  197  1                                  15    
HELIX   28 AD1 GLU J  223  GLU J  240  1                                  18    
HELIX   29 AD2 GLN K   23  LYS K   32  1                                  10    
HELIX   30 AD3 GLU K   60  ILE K   64  5                                   5    
HELIX   31 AD4 ALA K   83  ASN K  104  1                                  22    
HELIX   32 AD5 THR K  108  ASN K  118  1                                  11    
HELIX   33 AD6 ALA K  173  TYR K  185  1                                  13    
HELIX   34 AD7 THR K  190  MET K  206  1                                  17    
HELIX   35 AD8 GLU K  233  LYS K  239  1                                   7    
HELIX   36 AD9 ILE L   19  LYS L   30  1                                  12    
HELIX   37 AE1 THR L   78  PHE L   99  1                                  22    
HELIX   38 AE2 PRO L  104  ILE L  118  1                                  15    
HELIX   39 AE3 PRO L  119  GLN L  121  5                                   3    
HELIX   40 AE4 SER L  165  MET L  180  1                                  16    
HELIX   41 AE5 ASN L  183  ARG L  196  1                                  14    
HELIX   42 AE6 VAL L  229  GLU L  234  1                                   6    
HELIX   43 AE7 VAL M   20  LYS M   28  1                                   9    
HELIX   44 AE8 ALA M   29  SER M   33  5                                   5    
HELIX   45 AE9 LEU M   80  GLY M  103  1                                  24    
HELIX   46 AF1 PRO M  107  TYR M  125  1                                  19    
HELIX   47 AF2 ALA M  168  GLU M  177  1                                  10    
HELIX   48 AF3 THR M  185  VAL M  200  1                                  16    
HELIX   49 AF4 ALA M  235  LYS M  240  1                                   6    
HELIX   50 AF5 ALA N   49  ASN N   71  1                                  23    
HELIX   51 AF6 LEU N   75  ARG N   89  1                                  15    
HELIX   52 AF7 GLY N  129  SER N  133  5                                   5    
HELIX   53 AF8 TYR N  134  TYR N  143  1                                  10    
HELIX   54 AF9 THR N  148  ASP N  167  1                                  20    
HELIX   55 AG1 THR O   48  GLY O   71  1                                  24    
HELIX   56 AG2 ARG O   75  TYR O   90  1                                  16    
HELIX   57 AG3 GLY O  130  PHE O  142  1                                  13    
HELIX   58 AG4 GLU O  147  ASN O  165  1                                  19    
HELIX   59 AG5 LEU P   56  GLU P   78  1                                  23    
HELIX   60 AG6 LYS P   83  LYS P   98  1                                  16    
HELIX   61 AG7 ALA P  143  TRP P  154  1                                  12    
HELIX   62 AG8 ASP P  159  ASP P  178  1                                  20    
HELIX   63 AG9 GLY Q   51  GLY Q   72  1                                  22    
HELIX   64 AH1 SER Q   76  ARG Q   93  1                                  18    
HELIX   65 AH2 TYR Q  134  TYR Q  146  1                                  13    
HELIX   66 AH3 SER Q  152  GLN Q  168  1                                  17    
HELIX   67 AH4 GLY R   48  LYS R   71  1                                  24    
HELIX   68 AH5 SER R   75  GLN R   89  1                                  15    
HELIX   69 AH6 GLY R  131  TYR R  143  1                                  13    
HELIX   70 AH7 GLU R  148  ASP R  167  1                                  20    
HELIX   71 AH8 ASN R  191  SER R  200  1                                  10    
HELIX   72 AH9 PHE S   57  ASN S   80  1                                  24    
HELIX   73 AI1 THR S   84  ARG S   99  1                                  16    
HELIX   74 AI2 LEU S  145  VAL S  153  1                                   9    
HELIX   75 AI3 SER S  167  ASP S  186  1                                  20    
HELIX   76 AI4 ASP T   56  GLY T   78  1                                  23    
HELIX   77 AI5 SER T   84  LYS T  102  1                                  19    
HELIX   78 AI6 TYR T  141  ALA T  146  1                                   6    
HELIX   79 AI7 ALA T  146  GLN T  157  1                                  12    
HELIX   80 AI8 SER T  161  ASP T  180  1                                  20    
HELIX   81 AI9 TRP T  209  MET T  214  5                                   6    
HELIX   82 AJ1 SER g   17  ARG g   21  5                                   5    
HELIX   83 AJ2 GLN g   24  PHE g   29  1                                   6    
HELIX   84 AJ3 SER g   63  THR g   67  5                                   5    
HELIX   85 AJ4 MET g   83  GLY g  106  1                                  24    
HELIX   86 AJ5 PRO g  110  ASN g  128  1                                  19    
HELIX   87 AJ6 LYS g  171  VAL g  183  1                                  13    
HELIX   88 AJ7 PHE g  191  SER g  207  1                                  17    
HELIX   89 AJ8 THR g  231  LEU g  242  1                                  12    
HELIX   90 AJ9 LEU h   19  GLY h   31  1                                  13    
HELIX   91 AK1 MET h   79  GLN h  102  1                                  24    
HELIX   92 AK2 PRO h  106  SER h  124  1                                  19    
HELIX   93 AK3 ASN h  166  TYR h  178  1                                  13    
HELIX   94 AK4 GLU h  183  PHE h  199  1                                  17    
HELIX   95 AK5 THR h  222  LEU h  230  1                                   9    
HELIX   96 AK6 LEU i   18  HIS i   30  1                                  13    
HELIX   97 AK7 ILE i   79  GLN i  102  1                                  24    
HELIX   98 AK8 CYS i  107  GLN i  123  1                                  17    
HELIX   99 AK9 SER i  168  ASP i  178  1                                  11    
HELIX  100 AL1 THR i  185  MET i  201  1                                  17    
HELIX  101 AL2 SER i  207  GLU i  209  5                                   3    
HELIX  102 AL3 GLN i  230  GLU i  248  1                                  19    
HELIX  103 AL4 ARG i  249  LYS i  251  5                                   3    
HELIX  104 AL5 GLN j   18  LYS j   28  1                                  11    
HELIX  105 AL6 LEU j   76  THR j   97  1                                  22    
HELIX  106 AL7 THR j  103  SER j  121  1                                  19    
HELIX  107 AL8 PHE j  138  GLY j  140  5                                   3    
HELIX  108 AL9 GLY j  164  ASN j  175  1                                  12    
HELIX  109 AM1 THR j  183  LEU j  196  1                                  14    
HELIX  110 AM2 GLU j  223  GLU j  240  1                                  18    
HELIX  111 AM3 LEU k   21  LYS k   32  1                                  12    
HELIX  112 AM4 GLU k   60  ILE k   64  5                                   5    
HELIX  113 AM5 ILE k   82  ASN k  104  1                                  23    
HELIX  114 AM6 THR k  108  ASN k  118  1                                  11    
HELIX  115 AM7 ALA k  173  TYR k  185  1                                  13    
HELIX  116 AM8 THR k  190  MET k  206  1                                  17    
HELIX  117 AM9 GLU k  233  ASP k  240  1                                   8    
HELIX  118 AN1 ILE l   19  GLN l   31  1                                  13    
HELIX  119 AN2 THR l   78  PHE l   99  1                                  22    
HELIX  120 AN3 PRO l  104  ILE l  118  1                                  15    
HELIX  121 AN4 PRO l  119  GLN l  121  5                                   3    
HELIX  122 AN5 SER l  165  MET l  176  1                                  12    
HELIX  123 AN6 ASN l  183  ARG l  196  1                                  14    
HELIX  124 AN7 VAL l  229  GLU l  234  1                                   6    
HELIX  125 AN8 VAL m   20  LYS m   28  1                                   9    
HELIX  126 AN9 ALA m   29  SER m   33  5                                   5    
HELIX  127 AO1 LEU m   80  GLY m  103  1                                  24    
HELIX  128 AO2 PRO m  107  TYR m  125  1                                  19    
HELIX  129 AO3 ALA m  168  GLU m  177  1                                  10    
HELIX  130 AO4 THR m  185  VAL m  200  1                                  16    
HELIX  131 AO5 LEU m  219  ASN m  221  5                                   3    
HELIX  132 AO6 ALA m  235  LYS m  240  1                                   6    
HELIX  133 AO7 SER n   48  ASN n   71  1                                  24    
HELIX  134 AO8 LEU n   75  TYR n   90  1                                  16    
HELIX  135 AO9 GLY n  129  SER n  133  5                                   5    
HELIX  136 AP1 TYR n  134  TYR n  143  1                                  10    
HELIX  137 AP2 THR n  148  ASP n  167  1                                  20    
HELIX  138 AP3 THR o   48  GLY o   71  1                                  24    
HELIX  139 AP4 ARG o   75  TYR o   90  1                                  16    
HELIX  140 AP5 GLY o  130  PHE o  142  1                                  13    
HELIX  141 AP6 GLU o  147  ASN o  165  1                                  19    
HELIX  142 AP7 ILE p    3  ASN p    7  5                                   5    
HELIX  143 AP8 LEU p   56  GLU p   78  1                                  23    
HELIX  144 AP9 LYS p   83  LYS p   98  1                                  16    
HELIX  145 AQ1 ALA p  143  TRP p  154  1                                  12    
HELIX  146 AQ2 ASP p  159  ASP p  178  1                                  20    
HELIX  147 AQ3 GLU q   49  GLY q   72  1                                  24    
HELIX  148 AQ4 SER q   76  ARG q   93  1                                  18    
HELIX  149 AQ5 TYR q  134  LEU q  138  5                                   5    
HELIX  150 AQ6 SER q  152  GLN q  168  1                                  17    
HELIX  151 AQ7 ALA r   49  LYS r   71  1                                  23    
HELIX  152 AQ8 SER r   75  GLN r   89  1                                  15    
HELIX  153 AQ9 GLY r  131  TYR r  143  1                                  13    
HELIX  154 AR1 GLU r  148  ASP r  167  1                                  20    
HELIX  155 AR2 ASN r  191  SER r  200  1                                  10    
HELIX  156 AR3 PHE s   57  ASN s   80  1                                  24    
HELIX  157 AR4 THR s   84  ARG s   99  1                                  16    
HELIX  158 AR5 LEU s  145  VAL s  153  1                                   9    
HELIX  159 AR6 SER s  167  ASP s  186  1                                  20    
HELIX  160 AR7 ASP t   56  LEU t   76  1                                  21    
HELIX  161 AR8 SER t   84  LYS t  102  1                                  19    
HELIX  162 AR9 TYR t  141  ALA t  146  1                                   6    
HELIX  163 AS1 ALA t  146  GLN t  157  1                                  12    
HELIX  164 AS2 SER t  161  ASP t  180  1                                  20    
HELIX  165 AS3 TRP t  209  MET t  214  5                                   6    
SHEET    1 AA1 5 ALA G 165  GLY G 169  0                                        
SHEET    2 AA1 5 THR G  38  VAL G  42 -1  N  ALA G  41   O  THR G 166           
SHEET    3 AA1 5 CYS G  47  GLN G  53 -1  O  VAL G  51   N  VAL G  40           
SHEET    4 AA1 5 ILE G 215  THR G 221 -1  O  GLY G 218   N  ILE G  50           
SHEET    5 AA1 5 ARG G 228  ILE G 229 -1  O  ARG G 228   N  VAL G 219           
SHEET    1 AA2 4 LEU G  69  THR G  73  0                                        
SHEET    2 AA2 4 ILE G  76  MET G  80 -1  O  ILE G  76   N  THR G  73           
SHEET    3 AA2 4 MET G 138  ASP G 144 -1  O  ILE G 139   N  VAL G  79           
SHEET    4 AA2 4 GLY G 148  CYS G 154 -1  O  GLY G 148   N  ASP G 144           
SHEET    1 AA3 5 ALA H 160  MET H 163  0                                        
SHEET    2 AA3 5 SER H  35  LYS H  39 -1  N  GLY H  37   O  THR H 161           
SHEET    3 AA3 5 VAL H  44  GLU H  49 -1  O  VAL H  45   N  ILE H  38           
SHEET    4 AA3 5 ILE H 208  ASN H 214 -1  O  GLY H 211   N  LEU H  46           
SHEET    5 AA3 5 GLY H 217  ARG H 220 -1  O  ARG H 219   N  ILE H 212           
SHEET    1 AA4 4 GLU H  66  THR H  69  0                                        
SHEET    2 AA4 4 ILE H  72  GLY H  78 -1  O  ILE H  72   N  ILE H  68           
SHEET    3 AA4 4 VAL H 132  TRP H 139 -1  O  CYS H 137   N  GLY H  73           
SHEET    4 AA4 4 PRO H 144  GLN H 148 -1  O  PHE H 147   N  ILE H 136           
SHEET    1 AA5 4 CYS I  34  GLY I  36  0                                        
SHEET    2 AA5 4 VAL I  43  GLU I  48 -1  O  ALA I  46   N  LEU I  35           
SHEET    3 AA5 4 VAL I 211  LEU I 216 -1  O  LEU I 216   N  VAL I  43           
SHEET    4 AA5 4 ILE I 225  VAL I 227 -1  O  ARG I 226   N  THR I 215           
SHEET    1 AA6 4 MET I  72  ALA I  73  0                                        
SHEET    2 AA6 4 LEU I 135  GLY I 138 -1  O  ILE I 137   N  ALA I  73           
SHEET    3 AA6 4 GLN I 146  SER I 150 -1  O  GLN I 146   N  GLY I 138           
SHEET    4 AA6 4 TYR I 156  GLY I 158 -1  O  GLY I 157   N  GLN I 149           
SHEET    1 AA7 2 ALA I  77  GLY I  78  0                                        
SHEET    2 AA7 2 VAL I 132  SER I 133 -1  O  SER I 133   N  ALA I  77           
SHEET    1 AA8 5 ALA J 158  ILE J 161  0                                        
SHEET    2 AA8 5 ALA J  32  ARG J  36 -1  N  GLY J  34   O  ASN J 159           
SHEET    3 AA8 5 VAL J  41  VAL J  45 -1  O  VAL J  42   N  VAL J  35           
SHEET    4 AA8 5 GLU J 207  MET J 211 -1  O  MET J 211   N  VAL J  41           
SHEET    5 AA8 5 LYS J 218  ILE J 219 -1  O  LYS J 218   N  VAL J 210           
SHEET    1 AA9 4 VAL J  69  CYS J  70  0                                        
SHEET    2 AA9 4 LEU J 132  PHE J 136 -1  O  VAL J 134   N  CYS J  70           
SHEET    3 AA9 4 PRO J 142  GLN J 146 -1  O  TYR J 145   N  ILE J 133           
SHEET    4 AA9 4 HIS J 154  TRP J 156 -1  O  TRP J 156   N  LEU J 144           
SHEET    1 AB1 4 ALA K 167  ILE K 170  0                                        
SHEET    2 AB1 4 ALA K  37  THR K  42 -1  N  GLY K  39   O  ARG K 168           
SHEET    3 AB1 4 GLY K  45  GLU K  51 -1  O  ALA K  49   N  ILE K  38           
SHEET    4 AB1 4 ILE K 215  VAL K 220 -1  O  VAL K 220   N  VAL K  46           
SHEET    1 AB2 3 LEU K 142  ASP K 147  0                                        
SHEET    2 AB2 3 GLY K 150  HIS K 155 -1  O  PHE K 154   N  PHE K 143           
SHEET    3 AB2 3 VAL K 163  GLN K 164 -1  O  VAL K 163   N  HIS K 155           
SHEET    1 AB3 5 ALA L 158  ILE L 161  0                                        
SHEET    2 AB3 5 THR L  35  LYS L  39 -1  N  GLY L  37   O  MET L 159           
SHEET    3 AB3 5 HIS L  43  LEU L  49 -1  O  VAL L  47   N  VAL L  36           
SHEET    4 AB3 5 VAL L 210  GLY L 216 -1  O  VAL L 215   N  ALA L  44           
SHEET    5 AB3 5 THR L 222  TYR L 224 -1  O  THR L 222   N  ILE L 214           
SHEET    1 AB4 2 ARG L  51  ALA L  52  0                                        
SHEET    2 AB4 2 HIS L  59  GLN L  60 -1  O  GLN L  60   N  ARG L  51           
SHEET    1 AB5 5 LEU L  64  HIS L  65  0                                        
SHEET    2 AB5 5 GLY L  71  SER L  73 -1  O  ILE L  72   N  LEU L  64           
SHEET    3 AB5 5 LEU L 133  ASP L 138 -1  O  ALA L 135   N  GLY L  71           
SHEET    4 AB5 5 GLY L 141  GLN L 146 -1  O  PHE L 145   N  ILE L 134           
SHEET    5 AB5 5 PHE L 154  ASP L 155 -1  O  PHE L 154   N  GLN L 146           
SHEET    1 AB6 4 GLY M 162  ILE M 165  0                                        
SHEET    2 AB6 4 ALA M  36  CYS M  41 -1  N  ALA M  36   O  ILE M 165           
SHEET    3 AB6 4 GLY M  44  LEU M  52 -1  O  GLY M  44   N  CYS M  41           
SHEET    4 AB6 4 PHE M 209  GLU M 212 -1  O  GLU M 210   N  LYS M  51           
SHEET    1 AB7 5 GLY M 162  ILE M 165  0                                        
SHEET    2 AB7 5 ALA M  36  CYS M  41 -1  N  ALA M  36   O  ILE M 165           
SHEET    3 AB7 5 GLY M  44  LEU M  52 -1  O  GLY M  44   N  CYS M  41           
SHEET    4 AB7 5 SER M 214  GLY M 217 -1  O  VAL M 216   N  VAL M  45           
SHEET    5 AB7 5 HIS M 224  ILE M 226 -1  O  GLU M 225   N  TRP M 215           
SHEET    1 AB8 4 GLY M  74  GLY M  79  0                                        
SHEET    2 AB8 4 CYS M 133  GLY M 138 -1  O  SER M 134   N  ALA M  78           
SHEET    3 AB8 4 LEU M 148  ILE M 151 -1  O  TYR M 149   N  LEU M 137           
SHEET    4 AB8 4 SER M 157  GLY M 159 -1  O  TYR M 158   N  MET M 150           
SHEET    1 AB9 5 PHE N 125  GLY N 128  0                                        
SHEET    2 AB9 5 ILE N   3  GLN N   7 -1  N  ILE N   3   O  GLY N 128           
SHEET    3 AB9 5 VAL N  12  ALA N  16 -1  O  VAL N  13   N  VAL N   6           
SHEET    4 AB9 5 ILE N 174  ILE N 179 -1  O  ARG N 175   N  ALA N  16           
SHEET    5 AB9 5 VAL N 184  LEU N 189 -1  O  GLU N 185   N  ALA N 178           
SHEET    1 AC1 2 THR N  20  THR N  22  0                                        
SHEET    2 AC1 2 TYR N  25  ASN N  28 -1  O  TYR N  25   N  THR N  22           
SHEET    1 AC2 5 LEU N  34  PRO N  36  0                                        
SHEET    2 AC2 5 ILE N  41  CYS N  44 -1  O  CYS N  43   N  THR N  35           
SHEET    3 AC2 5 ILE N  99  ASP N 104 -1  O  ILE N  99   N  CYS N  44           
SHEET    4 AC2 5 GLY N 108  SER N 113 -1  O  TYR N 112   N  ILE N 100           
SHEET    5 AC2 5 VAL N 121  ARG N 122 -1  O  VAL N 121   N  SER N 113           
SHEET    1 AC3 5 TYR O 124  GLY O 128  0                                        
SHEET    2 AC3 5 THR O   2  VAL O   7 -1  N  ILE O   3   O  MET O 127           
SHEET    3 AC3 5 ILE O  12  ALA O  16 -1  O  GLY O  15   N  ALA O   4           
SHEET    4 AC3 5 ASP O 174  ILE O 178 -1  O  CYS O 176   N  LEU O  14           
SHEET    5 AC3 5 LEU O 183  LEU O 186 -1  O  ASP O 184   N  VAL O 177           
SHEET    1 AC4 5 ILE O  34  PHE O  36  0                                        
SHEET    2 AC4 5 ILE O  41  GLY O  47 -1  O  CYS O  43   N  HIS O  35           
SHEET    3 AC4 5 ALA O  96  VAL O 103 -1  O  GLY O 101   N  TYR O  42           
SHEET    4 AC4 5 PRO O 108  TYR O 114 -1  O  TYR O 111   N  LEU O 100           
SHEET    5 AC4 5 SER O 118  LYS O 121 -1  O  SER O 118   N  TYR O 114           
SHEET    1 AC5 3 VAL O 211  THR O 213  0                                        
SHEET    2 AC5 3 LYS P 194  LEU P 200 -1  O  THR P 199   N  LEU O 212           
SHEET    3 AC5 3 ILE O 216  PRO O 218 -1  N  THR O 217   O  ILE P 195           
SHEET    1 AC6 6 VAL O 211  THR O 213  0                                        
SHEET    2 AC6 6 LYS P 194  LEU P 200 -1  O  THR P 199   N  LEU O 212           
SHEET    3 AC6 6 VAL P 185  ILE P 190 -1  N  VAL P 187   O  ARG P 198           
SHEET    4 AC6 6 VAL P  20  ASP P  25 -1  N  ILE P  22   O  HIS P 188           
SHEET    5 AC6 6 ALA P  10  LYS P  15 -1  N  MET P  12   O  ALA P  23           
SHEET    6 AC6 6 PHE P 136  GLY P 140 -1  O  VAL P 137   N  ALA P  13           
SHEET    1 AC7 2 PHE P  28  GLY P  29  0                                        
SHEET    2 AC7 2 MET P  34  THR P  36 -1  O  VAL P  35   N  PHE P  28           
SHEET    1 AC8 5 ILE P  42  PRO P  44  0                                        
SHEET    2 AC8 5 LEU P  49  GLY P  52 -1  O  ILE P  51   N  PHE P  43           
SHEET    3 AC8 5 VAL P 108  LEU P 112 -1  O  VAL P 108   N  GLY P  52           
SHEET    4 AC8 5 PRO P 119  LEU P 124 -1  O  CYS P 122   N  ILE P 109           
SHEET    5 AC8 5 PRO P 130  VAL P 132 -1  O  MET P 131   N  SER P 123           
SHEET    1 AC9 4 ILE Q   5  GLN Q   8  0                                        
SHEET    2 AC9 4 VAL Q  13  ALA Q  16 -1  O  LEU Q  14   N  ILE Q   7           
SHEET    3 AC9 4 VAL Q 180  ILE Q 183 -1  O  ARG Q 181   N  VAL Q  15           
SHEET    4 AC9 4 ILE Q 188  ASP Q 190 -1  O  HIS Q 189   N  ILE Q 182           
SHEET    1 AD1 3 ILE Q  42  GLY Q  48  0                                        
SHEET    2 AD1 3 VAL Q 100  ASP Q 108 -1  O  ALA Q 105   N  LEU Q  43           
SHEET    3 AD1 3 GLY Q 112  LEU Q 115 -1  O  GLY Q 112   N  ASP Q 108           
SHEET    1 AD2 2 THR Q 177  PHE Q 178  0                                        
SHEET    2 AD2 2 ILE Q 194  SER Q 195 -1  O  ILE Q 194   N  PHE Q 178           
SHEET    1 AD3 5 THR R 125  GLY R 129  0                                        
SHEET    2 AD3 5 THR R   2  PHE R   8 -1  N  THR R   3   O  VAL R 128           
SHEET    3 AD3 5 GLY R  11  ALA R  16 -1  O  GLY R  11   N  PHE R   8           
SHEET    4 AD3 5 VAL R 174  VAL R 179 -1  O  TYR R 177   N  VAL R  14           
SHEET    5 AD3 5 ILE R 185  ASP R 190 -1  O  ASP R 190   N  VAL R 174           
SHEET    1 AD4 2 ALA R  20  ALA R  22  0                                        
SHEET    2 AD4 2 TYR R  25  SER R  28 -1  O  TYR R  25   N  ALA R  22           
SHEET    1 AD5 3 LEU R  41  GLY R  43  0                                        
SHEET    2 AD5 3 MET R 100  TRP R 104 -1  O  CYS R 102   N  LEU R  42           
SHEET    3 AD5 3 PRO R 109  TYR R 113 -1  O  TYR R 112   N  ILE R 101           
SHEET    1 AD6 5 PHE S 135  GLY S 139  0                                        
SHEET    2 AD6 5 THR S  11  ALA S  16 -1  N  ILE S  12   O  GLY S 138           
SHEET    3 AD6 5 ALA S  21  SER S  25 -1  O  ALA S  24   N  LEU S  13           
SHEET    4 AD6 5 ARG S 194  THR S 199 -1  O  ARG S 194   N  SER S  25           
SHEET    5 AD6 5 GLY S 202  THR S 207 -1  O  GLU S 206   N  ILE S 195           
SHEET    1 AD7 2 LEU S  29  GLU S  31  0                                        
SHEET    2 AD7 2 SER S  34  THR S  37 -1  O  HIS S  36   N  LEU S  29           
SHEET    1 AD8 5 CYS S  43  LYS S  45  0                                        
SHEET    2 AD8 5 THR S  50  GLY S  56 -1  O  ILE S  52   N  TYR S  44           
SHEET    3 AD8 5 VAL S 106  GLY S 112 -1  O  ILE S 109   N  GLY S  53           
SHEET    4 AD8 5 VAL S 121  SER S 123 -1  O  TYR S 122   N  ILE S 110           
SHEET    5 AD8 5 GLN S 131  ASP S 133 -1  O  ASP S 133   N  VAL S 121           
SHEET    1 AD9 5 SER T 136  ALA T 138  0                                        
SHEET    2 AD9 5 LEU T  12  PHE T  16 -1  N  GLY T  13   O  LEU T 137           
SHEET    3 AD9 5 GLY T  19  ASP T  25 -1  O  GLY T  19   N  PHE T  16           
SHEET    4 AD9 5 PHE T 187  THR T 193 -1  O  ALA T 190   N  ILE T  22           
SHEET    5 AD9 5 GLY T 196  LEU T 203 -1  O  GLU T 200   N  ILE T 189           
SHEET    1 AE1 5 ILE T  42  MET T  43  0                                        
SHEET    2 AE1 5 THR T  49  GLY T  55 -1  O  LEU T  51   N  MET T  43           
SHEET    3 AE1 5 ASN T 108  ALA T 116 -1  O  VAL T 111   N  GLY T  52           
SHEET    4 AE1 5 GLU T 119  VAL T 125 -1  O  GLY T 123   N  ILE T 112           
SHEET    5 AE1 5 ALA T 131  GLU T 133 -1  O  TYR T 132   N  TYR T 124           
SHEET    1 AE2 5 THR g 166  GLY g 169  0                                        
SHEET    2 AE2 5 THR g  38  VAL g  42 -1  N  ALA g  41   O  THR g 166           
SHEET    3 AE2 5 CYS g  47  GLN g  53 -1  O  VAL g  51   N  VAL g  40           
SHEET    4 AE2 5 ILE g 215  THR g 221 -1  O  GLY g 218   N  ILE g  50           
SHEET    5 AE2 5 ARG g 228  ILE g 229 -1  O  ARG g 228   N  VAL g 219           
SHEET    1 AE3 5 PHE g  70  LYS g  71  0                                        
SHEET    2 AE3 5 ILE g  76  MET g  80 -1  O  CYS g  78   N  PHE g  70           
SHEET    3 AE3 5 MET g 138  ASP g 144 -1  O  ILE g 141   N  GLY g  77           
SHEET    4 AE3 5 GLY g 148  CYS g 154 -1  O  GLY g 148   N  ASP g 144           
SHEET    5 AE3 5 TYR g 160  GLY g 162 -1  O  CYS g 161   N  LYS g 153           
SHEET    1 AE4 5 ALA h 160  MET h 163  0                                        
SHEET    2 AE4 5 SER h  35  LYS h  39 -1  N  GLY h  37   O  THR h 161           
SHEET    3 AE4 5 VAL h  44  GLU h  49 -1  O  VAL h  45   N  ILE h  38           
SHEET    4 AE4 5 ILE h 208  ASN h 214 -1  O  GLY h 211   N  LEU h  46           
SHEET    5 AE4 5 GLY h 217  ARG h 220 -1  O  ARG h 219   N  ILE h 212           
SHEET    1 AE5 4 GLU h  66  PRO h  67  0                                        
SHEET    2 AE5 4 ILE h  72  VAL h  75 -1  O  LEU h  74   N  GLU h  66           
SHEET    3 AE5 4 LEU h 135  TRP h 139 -1  O  LEU h 135   N  VAL h  75           
SHEET    4 AE5 4 PRO h 144  GLN h 148 -1  O  PHE h 147   N  ILE h 136           
SHEET    1 AE6 4 CYS i  34  GLY i  36  0                                        
SHEET    2 AE6 4 VAL i  43  GLU i  48 -1  O  ALA i  46   N  LEU i  35           
SHEET    3 AE6 4 VAL i 211  THR i 217 -1  O  ALA i 214   N  LEU i  45           
SHEET    4 AE6 4 VAL i 224  ARG i 226 -1  O  ARG i 226   N  THR i 215           
SHEET    1 AE7 4 MET i  72  ALA i  73  0                                        
SHEET    2 AE7 4 LEU i 135  GLY i 138 -1  O  ILE i 137   N  ALA i  73           
SHEET    3 AE7 4 GLN i 146  SER i 150 -1  O  GLN i 146   N  GLY i 138           
SHEET    4 AE7 4 TYR i 156  GLY i 157 -1  O  GLY i 157   N  GLN i 149           
SHEET    1 AE8 5 ALA j 158  ALA j 160  0                                        
SHEET    2 AE8 5 ALA j  32  ARG j  36 -1  N  GLY j  34   O  ASN j 159           
SHEET    3 AE8 5 VAL j  41  VAL j  45 -1  O  VAL j  42   N  VAL j  35           
SHEET    4 AE8 5 GLU j 207  MET j 211 -1  O  MET j 211   N  VAL j  41           
SHEET    5 AE8 5 LYS j 218  ILE j 219 -1  O  LYS j 218   N  VAL j 210           
SHEET    1 AE9 4 VAL j  69  CYS j  70  0                                        
SHEET    2 AE9 4 LEU j 132  PHE j 136 -1  O  VAL j 134   N  CYS j  70           
SHEET    3 AE9 4 PRO j 142  GLN j 146 -1  O  TYR j 145   N  ILE j 133           
SHEET    4 AE9 4 HIS j 154  TRP j 156 -1  O  HIS j 154   N  GLN j 146           
SHEET    1 AF1 4 ALA k 169  ILE k 170  0                                        
SHEET    2 AF1 4 ALA k  37  THR k  42 -1  N  ALA k  37   O  ILE k 170           
SHEET    3 AF1 4 GLY k  45  GLU k  51 -1  O  ALA k  49   N  ILE k  38           
SHEET    4 AF1 4 ILE k 215  LEU k 217 -1  O  GLU k 216   N  VAL k  50           
SHEET    1 AF2 3 LEU k 142  ASP k 147  0                                        
SHEET    2 AF2 3 GLY k 150  HIS k 155 -1  O  PHE k 154   N  PHE k 143           
SHEET    3 AF2 3 VAL k 163  GLN k 164 -1  O  VAL k 163   N  HIS k 155           
SHEET    1 AF3 5 ALA l 158  ILE l 161  0                                        
SHEET    2 AF3 5 THR l  35  LYS l  39 -1  N  GLY l  37   O  MET l 159           
SHEET    3 AF3 5 HIS l  43  LEU l  49 -1  O  VAL l  47   N  VAL l  36           
SHEET    4 AF3 5 VAL l 210  GLY l 216 -1  O  GLY l 213   N  LEU l  46           
SHEET    5 AF3 5 THR l 222  TYR l 224 -1  O  THR l 222   N  ILE l 214           
SHEET    1 AF4 5 LEU l  64  HIS l  65  0                                        
SHEET    2 AF4 5 GLY l  71  SER l  73 -1  O  ILE l  72   N  LEU l  64           
SHEET    3 AF4 5 LEU l 133  ASP l 138 -1  O  LEU l 133   N  SER l  73           
SHEET    4 AF4 5 GLY l 141  GLN l 146 -1  O  PHE l 145   N  ILE l 134           
SHEET    5 AF4 5 PHE l 154  ASP l 155 -1  O  PHE l 154   N  GLN l 146           
SHEET    1 AF5 4 GLY m 162  ILE m 165  0                                        
SHEET    2 AF5 4 ALA m  36  CYS m  41 -1  N  ALA m  36   O  ILE m 165           
SHEET    3 AF5 4 GLY m  44  LEU m  52 -1  O  VAL m  46   N  ILE m  39           
SHEET    4 AF5 4 PHE m 209  GLU m 212 -1  O  GLU m 210   N  LYS m  51           
SHEET    1 AF6 5 GLY m 162  ILE m 165  0                                        
SHEET    2 AF6 5 ALA m  36  CYS m  41 -1  N  ALA m  36   O  ILE m 165           
SHEET    3 AF6 5 GLY m  44  LEU m  52 -1  O  VAL m  46   N  ILE m  39           
SHEET    4 AF6 5 SER m 214  GLY m 217 -1  O  VAL m 216   N  VAL m  45           
SHEET    5 AF6 5 HIS m 224  ILE m 226 -1  O  GLU m 225   N  TRP m 215           
SHEET    1 AF7 3 GLY m  74  MET m  75  0                                        
SHEET    2 AF7 3 CYS m 133  SER m 141 -1  O  GLY m 138   N  GLY m  74           
SHEET    3 AF7 3 ALA m  78  GLY m  79 -1  N  ALA m  78   O  SER m 134           
SHEET    1 AF8 4 GLY m  74  MET m  75  0                                        
SHEET    2 AF8 4 CYS m 133  SER m 141 -1  O  GLY m 138   N  GLY m  74           
SHEET    3 AF8 4 GLY m 145  ILE m 151 -1  O  GLY m 145   N  SER m 141           
SHEET    4 AF8 4 SER m 157  GLY m 159 -1  O  TYR m 158   N  MET m 150           
SHEET    1 AF9 5 PHE n 125  GLY n 128  0                                        
SHEET    2 AF9 5 ILE n   3  GLN n   7 -1  N  ILE n   3   O  GLY n 128           
SHEET    3 AF9 5 VAL n  12  ALA n  16 -1  O  VAL n  13   N  VAL n   6           
SHEET    4 AF9 5 ILE n 174  ILE n 179 -1  O  ALA n 177   N  LEU n  14           
SHEET    5 AF9 5 VAL n 184  LEU n 189 -1  O  GLN n 187   N  LEU n 176           
SHEET    1 AG1 2 THR n  20  THR n  22  0                                        
SHEET    2 AG1 2 TYR n  25  ASN n  28 -1  O  TYR n  25   N  THR n  22           
SHEET    1 AG2 5 LEU n  34  PRO n  36  0                                        
SHEET    2 AG2 5 ILE n  41  CYS n  44 -1  O  CYS n  43   N  THR n  35           
SHEET    3 AG2 5 ILE n  99  ASP n 104 -1  O  ILE n  99   N  CYS n  44           
SHEET    4 AG2 5 GLY n 108  SER n 113 -1  O  TYR n 112   N  ILE n 100           
SHEET    5 AG2 5 VAL n 121  GLN n 123 -1  O  GLN n 123   N  VAL n 111           
SHEET    1 AG3 5 TYR o 124  GLY o 128  0                                        
SHEET    2 AG3 5 THR o   2  VAL o   7 -1  N  GLY o   5   O  VAL o 125           
SHEET    3 AG3 5 ILE o  12  ALA o  16 -1  O  GLY o  15   N  ALA o   4           
SHEET    4 AG3 5 ASP o 174  ILE o 178 -1  O  ILE o 178   N  ILE o  12           
SHEET    5 AG3 5 ASP o 184  LEU o 186 -1  O  ASP o 184   N  VAL o 177           
SHEET    1 AG4 5 ILE o  34  PHE o  36  0                                        
SHEET    2 AG4 5 ILE o  41  GLY o  47 -1  O  CYS o  43   N  HIS o  35           
SHEET    3 AG4 5 ALA o  96  VAL o 103 -1  O  ALA o  97   N  ALA o  46           
SHEET    4 AG4 5 PRO o 108  TYR o 114 -1  O  TYR o 111   N  LEU o 100           
SHEET    5 AG4 5 SER o 118  LYS o 121 -1  O  SER o 118   N  TYR o 114           
SHEET    1 AG5 6 ILE o 216  PRO o 218  0                                        
SHEET    2 AG5 6 LYS p 194  LEU p 200 -1  O  ILE p 195   N  THR o 217           
SHEET    3 AG5 6 VAL p 185  ILE p 190 -1  N  ILE p 189   O  THR p 196           
SHEET    4 AG5 6 VAL p  20  ASP p  25 -1  N  ILE p  22   O  HIS p 188           
SHEET    5 AG5 6 ALA p  10  LYS p  15 -1  N  MET p  12   O  ALA p  23           
SHEET    6 AG5 6 PHE p 136  GLY p 140 -1  O  VAL p 137   N  ALA p  13           
SHEET    1 AG6 2 PHE p  28  GLY p  29  0                                        
SHEET    2 AG6 2 MET p  34  THR p  36 -1  O  VAL p  35   N  PHE p  28           
SHEET    1 AG7 5 ILE p  42  PRO p  44  0                                        
SHEET    2 AG7 5 LEU p  49  GLY p  52 -1  O  ILE p  51   N  PHE p  43           
SHEET    3 AG7 5 VAL p 108  LEU p 112 -1  O  VAL p 108   N  GLY p  52           
SHEET    4 AG7 5 PRO p 119  SER p 123 -1  O  CYS p 122   N  ILE p 109           
SHEET    5 AG7 5 MET p 131  VAL p 132 -1  O  MET p 131   N  SER p 123           
SHEET    1 AG8 5 PHE q 129  HIS q 132  0                                        
SHEET    2 AG8 5 LEU q   4  GLN q   8 -1  N  GLY q   6   O  ALA q 130           
SHEET    3 AG8 5 VAL q  13  SER q  17 -1  O  LEU q  14   N  ILE q   7           
SHEET    4 AG8 5 VAL q 180  ILE q 183 -1  O  ARG q 181   N  VAL q  15           
SHEET    5 AG8 5 ILE q 188  ASP q 190 -1  O  HIS q 189   N  ILE q 182           
SHEET    1 AG9 3 LEU q  43  GLY q  48  0                                        
SHEET    2 AG9 3 VAL q 100  TYR q 107 -1  O  ALA q 105   N  LEU q  43           
SHEET    3 AG9 3 PRO q 113  LEU q 115 -1  O  ALA q 114   N  GLY q 106           
SHEET    1 AH1 2 THR q 177  PHE q 178  0                                        
SHEET    2 AH1 2 ILE q 194  SER q 195 -1  O  ILE q 194   N  PHE q 178           
SHEET    1 AH2 5 THR r 125  GLY r 129  0                                        
SHEET    2 AH2 5 THR r   2  PHE r   8 -1  N  THR r   3   O  VAL r 128           
SHEET    3 AH2 5 GLY r  11  ALA r  16 -1  O  GLY r  11   N  PHE r   8           
SHEET    4 AH2 5 VAL r 174  VAL r 179 -1  O  TYR r 177   N  VAL r  14           
SHEET    5 AH2 5 TRP r 184  ASP r 190 -1  O  ASP r 190   N  VAL r 174           
SHEET    1 AH3 2 ALA r  20  ALA r  22  0                                        
SHEET    2 AH3 2 TYR r  25  SER r  28 -1  O  TYR r  25   N  ALA r  22           
SHEET    1 AH4 4 LEU r  41  GLY r  43  0                                        
SHEET    2 AH4 4 MET r 100  TRP r 104 -1  O  CYS r 102   N  LEU r  42           
SHEET    3 AH4 4 PRO r 109  TYR r 113 -1  O  TYR r 112   N  ILE r 101           
SHEET    4 AH4 4 ILE r 121  SER r 122 -1  O  ILE r 121   N  TYR r 113           
SHEET    1 AH5 5 PHE s 135  GLY s 139  0                                        
SHEET    2 AH5 5 THR s  11  ALA s  16 -1  N  ILE s  12   O  GLY s 138           
SHEET    3 AH5 5 ALA s  21  SER s  25 -1  O  ALA s  24   N  LEU s  13           
SHEET    4 AH5 5 ARG s 194  VAL s 198 -1  O  ARG s 194   N  SER s  25           
SHEET    5 AH5 5 ILE s 203  THR s 207 -1  O  GLU s 206   N  ILE s 195           
SHEET    1 AH6 2 LEU s  29  GLU s  31  0                                        
SHEET    2 AH6 2 SER s  34  THR s  37 -1  O  HIS s  36   N  LEU s  29           
SHEET    1 AH7 5 CYS s  43  THR s  47  0                                        
SHEET    2 AH7 5 THR s  50  GLY s  56 -1  O  ILE s  52   N  TYR s  44           
SHEET    3 AH7 5 VAL s 106  GLY s 112 -1  O  GLY s 111   N  VAL s  51           
SHEET    4 AH7 5 VAL s 121  SER s 123 -1  O  TYR s 122   N  ILE s 110           
SHEET    5 AH7 5 GLN s 131  ASP s 133 -1  O  ASP s 133   N  VAL s 121           
SHEET    1 AH8 5 SER t 136  ALA t 138  0                                        
SHEET    2 AH8 5 LEU t  12  PHE t  16 -1  N  GLY t  13   O  LEU t 137           
SHEET    3 AH8 5 GLY t  19  ASP t  25 -1  O  ALA t  23   N  LEU t  12           
SHEET    4 AH8 5 PHE t 187  THR t 193 -1  O  ALA t 190   N  ILE t  22           
SHEET    5 AH8 5 GLY t 196  LEU t 203 -1  O  GLU t 200   N  ILE t 189           
SHEET    1 AH9 5 ILE t  42  MET t  43  0                                        
SHEET    2 AH9 5 THR t  49  GLY t  52 -1  O  LEU t  51   N  MET t  43           
SHEET    3 AH9 5 MET t 110  ALA t 116 -1  O  VAL t 111   N  GLY t  52           
SHEET    4 AH9 5 GLU t 119  VAL t 125 -1  O  GLY t 123   N  ILE t 112           
SHEET    5 AH9 5 ALA t 131  GLU t 133 -1  O  TYR t 132   N  TYR t 124           
SSBOND   1 CYS M   41    CYS M  186                          1555   1555  2.03  
SSBOND   2 CYS m   41    CYS m  186                          1555   1555  2.03  
CISPEP   1 ALA G    7    GLY G    8          0        -6.18                     
CISPEP   2 GLU G   19    GLY G   20          0       -24.81                     
CISPEP   3 SER H    7    PHE H    8          0         4.81                     
CISPEP   4 PHE H    8    SER H    9          0        -0.54                     
CISPEP   5 SER H  124    GLY H  125          0       -11.26                     
CISPEP   6 GLU I   15    GLY I   16          0       -25.20                     
CISPEP   7 GLY I  125    GLY I  126          0         1.01                     
CISPEP   8 ARG J    5    ALA J    6          0         2.80                     
CISPEP   9 GLU J  179    ALA J  180          0       -12.32                     
CISPEP  10 ALA J  180    ILE J  181          0       -19.58                     
CISPEP  11 ILE J  181    GLU J  182          0        27.37                     
CISPEP  12 GLU J  182    THR J  183          0        -9.08                     
CISPEP  13 LEU K   21    PHE K   22          0        26.53                     
CISPEP  14 GLY M    6    TYR M    7          0         7.52                     
CISPEP  15 GLY o  200    ARG o  201          0         0.62                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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