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Database: PDB
Entry: 6R70
LinkDB: 6R70
Original site: 6R70 
HEADER    HYDROLASE                               28-MAR-19   6R70              
TITLE     ENDOGENEOUS NATIVE HUMAN 20S PROTEASOME                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;                            
COMPND   3 CHAIN: M, a;                                                         
COMPND   4 SYNONYM: 26 KDA PROSOMAL PROTEIN,PROS-26,MACROPAIN BETA CHAIN,       
COMPND   5 MULTICATALYTIC ENDOPEPTIDASE COMPLEX BETA CHAIN,PROTEASOME BETA      
COMPND   6 CHAIN,PROTEASOME CHAIN 3,HSN3;                                       
COMPND   7 EC: 3.4.25.1;                                                        
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;                           
COMPND  10 CHAIN: A, O;                                                         
COMPND  11 SYNONYM: MACROPAIN SUBUNIT C3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  12 SUBUNIT C3,PROTEASOME COMPONENT C3;                                  
COMPND  13 EC: 3.4.25.1;                                                        
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;                           
COMPND  16 CHAIN: B, P;                                                         
COMPND  17 SYNONYM: MACROPAIN SUBUNIT C9,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  18 SUBUNIT C9,PROTEASOME COMPONENT C9,PROTEASOME SUBUNIT L;             
COMPND  19 EC: 3.4.25.1;                                                        
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-7;                           
COMPND  22 CHAIN: C, Q;                                                         
COMPND  23 SYNONYM: PROTEASOME SUBUNIT RC6-1,PROTEASOME SUBUNIT XAPC7;          
COMPND  24 EC: 3.4.25.1;                                                        
COMPND  25 MOL_ID: 5;                                                           
COMPND  26 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;                           
COMPND  27 CHAIN: D, R;                                                         
COMPND  28 SYNONYM: MACROPAIN ZETA CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  29 ZETA CHAIN,PROTEASOME ZETA CHAIN;                                    
COMPND  30 EC: 3.4.25.1;                                                        
COMPND  31 MOL_ID: 6;                                                           
COMPND  32 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;                           
COMPND  33 CHAIN: E, S;                                                         
COMPND  34 SYNONYM: 30 KDA PROSOMAL PROTEIN,PROS-30,MACROPAIN SUBUNIT C2,       
COMPND  35 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C2,PROTEASOME COMPONENT 
COMPND  36 C2,PROTEASOME NU CHAIN;                                              
COMPND  37 EC: 3.4.25.1;                                                        
COMPND  38 MOL_ID: 7;                                                           
COMPND  39 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;                           
COMPND  40 CHAIN: F, T;                                                         
COMPND  41 SYNONYM: MACROPAIN SUBUNIT C8,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  42 SUBUNIT C8,PROTEASOME COMPONENT C8;                                  
COMPND  43 EC: 3.4.25.1;                                                        
COMPND  44 MOL_ID: 8;                                                           
COMPND  45 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;                           
COMPND  46 CHAIN: G, U;                                                         
COMPND  47 SYNONYM: 27 KDA PROSOMAL PROTEIN,P27K,MACROPAIN IOTA CHAIN,          
COMPND  48 MULTICATALYTIC ENDOPEPTIDASE COMPLEX IOTA CHAIN,PROTEASOME IOTA      
COMPND  49 CHAIN;                                                               
COMPND  50 EC: 3.4.25.1;                                                        
COMPND  51 MOL_ID: 9;                                                           
COMPND  52 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;                            
COMPND  53 CHAIN: H, V;                                                         
COMPND  54 SYNONYM: MACROPAIN CHAIN Z,MULTICATALYTIC ENDOPEPTIDASE COMPLEX CHAIN
COMPND  55 Z,PROTEASOME SUBUNIT Z;                                              
COMPND  56 EC: 3.4.25.1;                                                        
COMPND  57 MOL_ID: 10;                                                          
COMPND  58 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;                            
COMPND  59 CHAIN: I, W;                                                         
COMPND  60 SYNONYM: PROTEASOME CHAIN 13,PROTEASOME COMPONENT C10-II,PROTEASOME  
COMPND  61 THETA CHAIN;                                                         
COMPND  62 EC: 3.4.25.1;                                                        
COMPND  63 MOL_ID: 11;                                                          
COMPND  64 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;                            
COMPND  65 CHAIN: J, X;                                                         
COMPND  66 SYNONYM: MACROPAIN SUBUNIT C7-I,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  67 SUBUNIT C7-I,PROTEASOME COMPONENT C7-I;                              
COMPND  68 EC: 3.4.25.1;                                                        
COMPND  69 MOL_ID: 12;                                                          
COMPND  70 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;                            
COMPND  71 CHAIN: K, Y;                                                         
COMPND  72 SYNONYM: MACROPAIN EPSILON CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  73 EPSILON CHAIN,PROTEASOME CHAIN 6,PROTEASOME EPSILON CHAIN,PROTEASOME 
COMPND  74 SUBUNIT MB1,PROTEASOME SUBUNIT X;                                    
COMPND  75 EC: 3.4.25.1;                                                        
COMPND  76 MOL_ID: 13;                                                          
COMPND  77 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;                            
COMPND  78 CHAIN: L, Z;                                                         
COMPND  79 SYNONYM: MACROPAIN SUBUNIT C5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  80 SUBUNIT C5,PROTEASOME COMPONENT C5,PROTEASOME GAMMA CHAIN;           
COMPND  81 EC: 3.4.25.1;                                                        
COMPND  82 MOL_ID: 14;                                                          
COMPND  83 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;                            
COMPND  84 CHAIN: N, b;                                                         
COMPND  85 SYNONYM: MACROPAIN DELTA CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  86 DELTA CHAIN,PROTEASOME DELTA CHAIN,PROTEASOME SUBUNIT Y;             
COMPND  87 EC: 3.4.25.1                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: HELA;                                                     
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 CELL_LINE: HELA;                                                     
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 CELL_LINE: HELA;                                                     
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 CELL_LINE: HELA;                                                     
SOURCE  21 MOL_ID: 5;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 CELL_LINE: HELA;                                                     
SOURCE  26 MOL_ID: 6;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  28 ORGANISM_COMMON: HUMAN;                                              
SOURCE  29 ORGANISM_TAXID: 9606;                                                
SOURCE  30 CELL_LINE: HELA;                                                     
SOURCE  31 MOL_ID: 7;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  33 ORGANISM_COMMON: HUMAN;                                              
SOURCE  34 ORGANISM_TAXID: 9606;                                                
SOURCE  35 CELL_LINE: HELA;                                                     
SOURCE  36 MOL_ID: 8;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  38 ORGANISM_COMMON: HUMAN;                                              
SOURCE  39 ORGANISM_TAXID: 9606;                                                
SOURCE  40 CELL_LINE: HELA;                                                     
SOURCE  41 MOL_ID: 9;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  43 ORGANISM_COMMON: HUMAN;                                              
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 CELL_LINE: HELA;                                                     
SOURCE  46 MOL_ID: 10;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  48 ORGANISM_COMMON: HUMAN;                                              
SOURCE  49 ORGANISM_TAXID: 9606;                                                
SOURCE  50 CELL_LINE: HELA;                                                     
SOURCE  51 MOL_ID: 11;                                                          
SOURCE  52 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  53 ORGANISM_COMMON: HUMAN;                                              
SOURCE  54 ORGANISM_TAXID: 9606;                                                
SOURCE  55 CELL_LINE: HELA;                                                     
SOURCE  56 MOL_ID: 12;                                                          
SOURCE  57 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  58 ORGANISM_COMMON: HUMAN;                                              
SOURCE  59 ORGANISM_TAXID: 9606;                                                
SOURCE  60 CELL_LINE: HELA;                                                     
SOURCE  61 MOL_ID: 13;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  63 ORGANISM_COMMON: HUMAN;                                              
SOURCE  64 ORGANISM_TAXID: 9606;                                                
SOURCE  65 CELL_LINE: HELA;                                                     
SOURCE  66 MOL_ID: 14;                                                          
SOURCE  67 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  68 ORGANISM_COMMON: HUMAN;                                              
SOURCE  69 ORGANISM_TAXID: 9606;                                                
SOURCE  70 CELL_LINE: HELA                                                      
KEYWDS    NATIVE, HUMAN, 20S PROTEASOME, PROTEASOME, CRYO-EM, MICROFLUIDIC,     
KEYWDS   2 CRYOWRITER, PROTEIN ISOLATION, ENDOGENEOUS, HYDROLASE                
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    C.SCHMIDLI,S.ALBIEZ,L.RIMA,R.RIGHETTO,I.MOHAMMED,P.OLIVA,L.KOVACIK,   
AUTHOR   2 H.STAHLBERG,T.BRAUN                                                  
REVDAT   4   31-JUL-19 6R70    1       JRNL                                     
REVDAT   3   24-JUL-19 6R70    1       JRNL                                     
REVDAT   2   17-JUL-19 6R70    1       JRNL                                     
REVDAT   1   03-JUL-19 6R70    0                                                
JRNL        AUTH   C.SCHMIDLI,S.ALBIEZ,L.RIMA,R.RIGHETTO,I.MOHAMMED,P.OLIVA,    
JRNL        AUTH 2 L.KOVACIK,H.STAHLBERG,T.BRAUN                                
JRNL        TITL   MICROFLUIDIC PROTEIN ISOLATION AND SAMPLE PREPARATION FOR    
JRNL        TITL 2 HIGH-RESOLUTION CRYO-EM.                                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 116 15007 2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   31292253                                                     
JRNL        DOI    10.1073/PNAS.1907214116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : RELION, SERIALEM, CTFFIND, UCSF           
REMARK   3                            CHIMERA, PHENIX, RELION, RELION           
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 5LE5                                
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               : 16015                          
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 6R70 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292100800.                                   
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                 : NATIVE HUMAN 20S PROTEASOME       
REMARK 245                                    WITH BOUND FABS TO THE TWO        
REMARK 245                                    ALPHA-4 SUBUNITS                  
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : CRYOWRITER. (SEE                  
REMARK 245  HTTPS://DOI.ORG/10.1016/J.JSB.2016.11.002 FOR MORE INFORMATION)     
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.40                              
REMARK 245   SAMPLE DETAILS                 : FAB FRAGMENT GENERATED BY         
REMARK 245  PROTEOLYTIC CLEAVAGE OF MONOCLONAL IGG1 ANTIBODY.                   
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 523                            
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 QUANTUM (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                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 72.00                          
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)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 28-MERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 28-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 111250 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 218180 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -401.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, A, B, C, D, E, F, G, H, I,         
REMARK 350                    AND CHAINS: J, K, L, N, O, P, Q, R, S,            
REMARK 350                    AND CHAINS: T, U, V, W, X, Y, Z, a, b             
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     CYS C    63                                                      
REMARK 465     PHE E     2                                                      
REMARK 465     ARG E     3                                                      
REMARK 465     CYS E   148                                                      
REMARK 465     GLU E   238                                                      
REMARK 465     ARG E   239                                                      
REMARK 465     THR F     5                                                      
REMARK 465     CYS G    47                                                      
REMARK 465     CYS G   137                                                      
REMARK 465     CYS G   161                                                      
REMARK 465     CYS J    91                                                      
REMARK 465     PRO N   203                                                      
REMARK 465     ARG P   249                                                      
REMARK 465     CYS Q    63                                                      
REMARK 465     GLN Q   200                                                      
REMARK 465     SER Q   201                                                      
REMARK 465     GLY Q   202                                                      
REMARK 465     GLY Q   203                                                      
REMARK 465     LYS Q   204                                                      
REMARK 465     CYS S   148                                                      
REMARK 465     CYS U    47                                                      
REMARK 465     CYS U   137                                                      
REMARK 465     CYS U   161                                                      
REMARK 465     LYS U   185                                                      
REMARK 465     LYS U   186                                                      
REMARK 465     PHE U   187                                                      
REMARK 465     ASP U   188                                                      
REMARK 465     TRP U   189                                                      
REMARK 465     THR U   190                                                      
REMARK 465     PHE U   191                                                      
REMARK 465     GLU U   192                                                      
REMARK 465     GLN U   193                                                      
REMARK 465     CYS X    91                                                      
REMARK 465     SER Y   200                                                      
REMARK 465     GLY Y   201                                                      
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   O    LEU P   236     O    LYS P   239              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLN P 235   CB    GLN P 235   CG     -0.174                       
REMARK 500    LYS P 239   CB    LYS P 239   CG      0.199                       
REMARK 500    LYS P 239   CG    LYS P 239   CD      0.233                       
REMARK 500    LYS P 239   CD    LYS P 239   CE      0.171                       
REMARK 500    LYS P 239   CE    LYS P 239   NZ      0.154                       
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 B 206   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    LYS C 204   N   -  CA  -  C   ANGL. DEV. =  16.4 DEGREES          
REMARK 500    ILE C 232   CG1 -  CB  -  CG2 ANGL. DEV. = -18.4 DEGREES          
REMARK 500    LEU H  65   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    LEU P 190   CA  -  CB  -  CG  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    GLU P 234   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    LEU P 236   CA  -  CB  -  CG  ANGL. DEV. =  24.3 DEGREES          
REMARK 500    LYS P 239   CB  -  CG  -  CD  ANGL. DEV. =  16.4 DEGREES          
REMARK 500    LYS P 239   CD  -  CE  -  NZ  ANGL. DEV. =  19.8 DEGREES          
REMARK 500    HIS P 240   C   -  N   -  CA  ANGL. DEV. =  31.8 DEGREES          
REMARK 500    HIS P 240   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    HIS P 240   N   -  CA  -  C   ANGL. DEV. =  18.0 DEGREES          
REMARK 500    ASP T 206   CB  -  CG  -  OD1 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    LEU V  65   CA  -  CB  -  CG  ANGL. DEV. =  16.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN M  38       49.07   -140.08                                   
REMARK 500    ASN M  46     -159.55   -148.15                                   
REMARK 500    SER A  53       77.32     56.74                                   
REMARK 500    THR A  68     -166.32   -125.12                                   
REMARK 500    HIS A  70       12.11   -140.01                                   
REMARK 500    GLU A 199       82.16     59.72                                   
REMARK 500    GLN A 201       74.75     65.00                                   
REMARK 500    ASN A 213     -158.08   -149.19                                   
REMARK 500    SER B 204       71.68     57.11                                   
REMARK 500    LYS B 210      -37.04     94.75                                   
REMARK 500    GLN C 200       63.91     33.58                                   
REMARK 500    LYS C 204      -41.54    -19.10                                   
REMARK 500    SER C 216       77.51     60.54                                   
REMARK 500    LEU C 217      127.44    -26.33                                   
REMARK 500    ILE C 232       -1.23    -55.88                                   
REMARK 500    GLU C 233       20.69    147.90                                   
REMARK 500    GLU C 237      -20.67   -140.19                                   
REMARK 500    ALA D 120      -74.91    -74.36                                   
REMARK 500    LEU D 121       15.96     50.12                                   
REMARK 500    LEU D 121       15.96    -66.70                                   
REMARK 500    ASP D 127      -28.09   -142.37                                   
REMARK 500    GLU D 175      -71.85    -66.00                                   
REMARK 500    THR E  11       30.55    -97.73                                   
REMARK 500    SER E  54      -41.88   -138.20                                   
REMARK 500    GLU E  55     -157.52    178.85                                   
REMARK 500    LEU E  56      -31.62    -11.19                                   
REMARK 500    HIS E  59       80.52     67.14                                   
REMARK 500    GLN E  60      128.92    -36.19                                   
REMARK 500    ALA E 151       -2.30     75.57                                   
REMARK 500    ASN E 209        1.67     82.64                                   
REMARK 500    ASP E 225     -166.88   -119.27                                   
REMARK 500    LEU E 236      -67.75    -97.90                                   
REMARK 500    THR G  73     -168.05   -129.42                                   
REMARK 500    LYS G 171       40.05    -97.67                                   
REMARK 500    GLU G 192      -50.80   -121.48                                   
REMARK 500    ASP G 209       72.64     58.08                                   
REMARK 500    GLU G 244       50.32    -92.68                                   
REMARK 500    ILE H  37      -54.91   -126.49                                   
REMARK 500    ASP H 104     -166.25   -124.79                                   
REMARK 500    SER H 171      -10.98     79.57                                   
REMARK 500    GLN I  30      -48.68    -26.40                                   
REMARK 500    ASN I 156       61.72     62.04                                   
REMARK 500    ASN J  24      -35.06     72.68                                   
REMARK 500    ILE J  25      -19.31   -143.72                                   
REMARK 500    THR J  96      108.55    -52.42                                   
REMARK 500    GLU J 109       38.16    -98.34                                   
REMARK 500    HIS J 110      -27.19   -144.40                                   
REMARK 500    THR J 150       42.19   -105.52                                   
REMARK 500    SER K  18       19.14   -140.24                                   
REMARK 500    PRO K  39        1.15    -60.73                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     109 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 LYS B  205     LEU B  206                 -138.42                    
REMARK 500 SER B  207     ALA B  208                 -131.87                    
REMARK 500 GLU B  209     LYS B  210                   85.53                    
REMARK 500 VAL B  211     GLU B  212                  144.41                    
REMARK 500 VAL C  199     GLN C  200                  136.78                    
REMARK 500 GLY C  203     LYS C  204                   74.95                    
REMARK 500 ILE C  232     GLU C  233                 -130.70                    
REMARK 500 GLU C  233     LYS C  234                  117.91                    
REMARK 500 GLN E   53     SER E   54                  142.99                    
REMARK 500 GLU E   55     LEU E   56                 -130.68                    
REMARK 500 LEU E   56     ALA E   57                  148.47                    
REMARK 500 ILE I   29     GLN I   30                 -141.22                    
REMARK 500 ILE P   52     HIS P   53                 -145.70                    
REMARK 500 LYS P  205     LEU P  206                 -140.69                    
REMARK 500 GLU P  209     LYS P  210                  119.22                    
REMARK 500 LYS P  238     LYS P  239                  133.08                    
REMARK 500 HIS P  240     GLU P  241                  144.13                    
REMARK 500 SER Q   49     VAL Q   50                 -146.42                    
REMARK 500 LEU Q  220     ASN Q  221                   44.41                    
REMARK 500 ASP R  129     PRO R  130                 -126.41                    
REMARK 500 PHE S    2     ARG S    3                  139.53                    
REMARK 500 ALA S   52     GLN S   53                  138.66                    
REMARK 500 LYS U   55     VAL U   56                 -139.49                    
REMARK 500 ILE W   29     GLN W   30                 -143.93                    
REMARK 500 GLY W  100     PRO W  101                 -149.84                    
REMARK 500 ARG Z    1     PHE Z    2                  142.62                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LEU P 236        -13.06                                           
REMARK 500    LYS P 238         12.99                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-4628   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-4738   RELATED DB: EMDB                              
REMARK 900 ENDOGENEOUS NATIVE HUMAN 20S PROTEASOME                              
DBREF  6R70 M    1   216  UNP    P28070   PSB4_HUMAN      46    261             
DBREF  6R70 A    3   232  UNP    P25787   PSA2_HUMAN       4    233             
DBREF  6R70 B    2   249  UNP    P25789   PSA4_HUMAN       2    249             
DBREF  6R70 C    2   238  UNP    O14818   PSA7_HUMAN       2    238             
DBREF  6R70 D    9   241  UNP    P28066   PSA5_HUMAN       9    241             
DBREF  6R70 E    2   239  UNP    P25786   PSA1_HUMAN       2    239             
DBREF  6R70 F    5   244  UNP    P25788   PSA3_HUMAN       6    245             
DBREF  6R70 G    2   245  UNP    P60900   PSA6_HUMAN       2    245             
DBREF  6R70 H    1   220  UNP    Q99436   PSB7_HUMAN      44    263             
DBREF  6R70 I    1   204  UNP    P49720   PSB3_HUMAN       2    205             
DBREF  6R70 J    1   196  UNP    P49721   PSB2_HUMAN       1    196             
DBREF  6R70 K    1   201  UNP    P28074   PSB5_HUMAN      60    260             
DBREF  6R70 L    1   213  UNP    P20618   PSB1_HUMAN      29    241             
DBREF  6R70 N    1   203  UNP    P28072   PSB6_HUMAN      35    237             
DBREF  6R70 O    3   232  UNP    P25787   PSA2_HUMAN       4    233             
DBREF  6R70 P    2   249  UNP    P25789   PSA4_HUMAN       2    249             
DBREF  6R70 Q    2   238  UNP    O14818   PSA7_HUMAN       2    238             
DBREF  6R70 R    9   241  UNP    P28066   PSA5_HUMAN       9    241             
DBREF  6R70 S    2   239  UNP    P25786   PSA1_HUMAN       2    239             
DBREF  6R70 T    5   244  UNP    P25788   PSA3_HUMAN       6    245             
DBREF  6R70 U    2   245  UNP    P60900   PSA6_HUMAN       2    245             
DBREF  6R70 V    1   220  UNP    Q99436   PSB7_HUMAN      44    263             
DBREF  6R70 W    1   204  UNP    P49720   PSB3_HUMAN       2    205             
DBREF  6R70 X    1   196  UNP    P49721   PSB2_HUMAN       1    196             
DBREF  6R70 Y    1   201  UNP    P28074   PSB5_HUMAN      60    260             
DBREF  6R70 Z    1   213  UNP    P20618   PSB1_HUMAN      29    241             
DBREF  6R70 a    1   216  UNP    P28070   PSB4_HUMAN      46    261             
DBREF  6R70 b    1   203  UNP    P28072   PSB6_HUMAN      35    237             
SEQRES   1 M  216  THR GLN ASN PRO MET VAL THR GLY THR SER VAL LEU GLY          
SEQRES   2 M  216  VAL LYS PHE GLU GLY GLY VAL VAL ILE ALA ALA ASP MET          
SEQRES   3 M  216  LEU GLY SER TYR GLY SER LEU ALA ARG PHE ARG ASN ILE          
SEQRES   4 M  216  SER ARG ILE MET ARG VAL ASN ASN SER THR MET LEU GLY          
SEQRES   5 M  216  ALA SER GLY ASP TYR ALA ASP PHE GLN TYR LEU LYS GLN          
SEQRES   6 M  216  VAL LEU GLY GLN MET VAL ILE ASP GLU GLU LEU LEU GLY          
SEQRES   7 M  216  ASP GLY HIS SER TYR SER PRO ARG ALA ILE HIS SER TRP          
SEQRES   8 M  216  LEU THR ARG ALA MET TYR SER ARG ARG SER LYS MET ASN          
SEQRES   9 M  216  PRO LEU TRP ASN THR MET VAL ILE GLY GLY TYR ALA ASP          
SEQRES  10 M  216  GLY GLU SER PHE LEU GLY TYR VAL ASP MET LEU GLY VAL          
SEQRES  11 M  216  ALA TYR GLU ALA PRO SER LEU ALA THR GLY TYR GLY ALA          
SEQRES  12 M  216  TYR LEU ALA GLN PRO LEU LEU ARG GLU VAL LEU GLU LYS          
SEQRES  13 M  216  GLN PRO VAL LEU SER GLN THR GLU ALA ARG ASP LEU VAL          
SEQRES  14 M  216  GLU ARG CYS MET ARG VAL LEU TYR TYR ARG ASP ALA ARG          
SEQRES  15 M  216  SER TYR ASN ARG PHE GLN ILE ALA THR VAL THR GLU LYS          
SEQRES  16 M  216  GLY VAL GLU ILE GLU GLY PRO LEU SER THR GLU THR ASN          
SEQRES  17 M  216  TRP ASP ILE ALA HIS MET ILE SER                              
SEQRES   1 A  230  ARG GLY TYR SER PHE SER LEU THR THR PHE SER PRO SER          
SEQRES   2 A  230  GLY LYS LEU VAL GLN ILE GLU TYR ALA LEU ALA ALA VAL          
SEQRES   3 A  230  ALA GLY GLY ALA PRO SER VAL GLY ILE LYS ALA ALA ASN          
SEQRES   4 A  230  GLY VAL VAL LEU ALA THR GLU LYS LYS GLN LYS SER ILE          
SEQRES   5 A  230  LEU TYR ASP GLU ARG SER VAL HIS LYS VAL GLU PRO ILE          
SEQRES   6 A  230  THR LYS HIS ILE GLY LEU VAL TYR SER GLY MET GLY PRO          
SEQRES   7 A  230  ASP TYR ARG VAL LEU VAL HIS ARG ALA ARG LYS LEU ALA          
SEQRES   8 A  230  GLN GLN TYR TYR LEU VAL TYR GLN GLU PRO ILE PRO THR          
SEQRES   9 A  230  ALA GLN LEU VAL GLN ARG VAL ALA SER VAL MET GLN GLU          
SEQRES  10 A  230  TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY VAL SER          
SEQRES  11 A  230  LEU LEU ILE CYS GLY TRP ASN GLU GLY ARG PRO TYR LEU          
SEQRES  12 A  230  PHE GLN SER ASP PRO SER GLY ALA TYR PHE ALA TRP LYS          
SEQRES  13 A  230  ALA THR ALA MET GLY LYS ASN TYR VAL ASN GLY LYS THR          
SEQRES  14 A  230  PHE LEU GLU LYS ARG TYR ASN GLU ASP LEU GLU LEU GLU          
SEQRES  15 A  230  ASP ALA ILE HIS THR ALA ILE LEU THR LEU LYS GLU SER          
SEQRES  16 A  230  PHE GLU GLY GLN MET THR GLU ASP ASN ILE GLU VAL GLY          
SEQRES  17 A  230  ILE CYS ASN GLU ALA GLY PHE ARG ARG LEU THR PRO THR          
SEQRES  18 A  230  GLU VAL LYS ASP TYR LEU ALA ALA ILE                          
SEQRES   1 B  248  SER ARG ARG TYR ASP SER ARG THR THR ILE PHE SER PRO          
SEQRES   2 B  248  GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA MET GLU ALA          
SEQRES   3 B  248  ILE GLY HIS ALA GLY THR CYS LEU GLY ILE LEU ALA ASN          
SEQRES   4 B  248  ASP GLY VAL LEU LEU ALA ALA GLU ARG ARG ASN ILE HIS          
SEQRES   5 B  248  LYS LEU LEU ASP GLU VAL PHE PHE SER GLU LYS ILE TYR          
SEQRES   6 B  248  LYS LEU ASN GLU ASP MET ALA CYS SER VAL ALA GLY ILE          
SEQRES   7 B  248  THR SER ASP ALA ASN VAL LEU THR ASN GLU LEU ARG LEU          
SEQRES   8 B  248  ILE ALA GLN ARG TYR LEU LEU GLN TYR GLN GLU PRO ILE          
SEQRES   9 B  248  PRO CYS GLU GLN LEU VAL THR ALA LEU CYS ASP ILE LYS          
SEQRES  10 B  248  GLN ALA TYR THR GLN PHE GLY GLY LYS ARG PRO PHE GLY          
SEQRES  11 B  248  VAL SER LEU LEU TYR ILE GLY TRP ASP LYS HIS TYR GLY          
SEQRES  12 B  248  PHE GLN LEU TYR GLN SER ASP PRO SER GLY ASN TYR GLY          
SEQRES  13 B  248  GLY TRP LYS ALA THR CYS ILE GLY ASN ASN SER ALA ALA          
SEQRES  14 B  248  ALA VAL SER MET LEU LYS GLN ASP TYR LYS GLU GLY GLU          
SEQRES  15 B  248  MET THR LEU LYS SER ALA LEU ALA LEU ALA ILE LYS VAL          
SEQRES  16 B  248  LEU ASN LYS THR MET ASP VAL SER LYS LEU SER ALA GLU          
SEQRES  17 B  248  LYS VAL GLU ILE ALA THR LEU THR ARG GLU ASN GLY LYS          
SEQRES  18 B  248  THR VAL ILE ARG VAL LEU LYS GLN LYS GLU VAL GLU GLN          
SEQRES  19 B  248  LEU ILE LYS LYS HIS GLU GLU GLU GLU ALA LYS ALA GLU          
SEQRES  20 B  248  ARG                                                          
SEQRES   1 C  237  SER TYR ASP ARG ALA ILE THR VAL PHE SER PRO ASP GLY          
SEQRES   2 C  237  HIS LEU PHE GLN VAL GLU TYR ALA GLN GLU ALA VAL LYS          
SEQRES   3 C  237  LYS GLY SER THR ALA VAL GLY VAL ARG GLY ARG ASP ILE          
SEQRES   4 C  237  VAL VAL LEU GLY VAL GLU LYS LYS SER VAL ALA LYS LEU          
SEQRES   5 C  237  GLN ASP GLU ARG THR VAL ARG LYS ILE CYS ALA LEU ASP          
SEQRES   6 C  237  ASP ASN VAL CYS MET ALA PHE ALA GLY LEU THR ALA ASP          
SEQRES   7 C  237  ALA ARG ILE VAL ILE ASN ARG ALA ARG VAL GLU CYS GLN          
SEQRES   8 C  237  SER HIS ARG LEU THR VAL GLU ASP PRO VAL THR VAL GLU          
SEQRES   9 C  237  TYR ILE THR ARG TYR ILE ALA SER LEU LYS GLN ARG TYR          
SEQRES  10 C  237  THR GLN SER ASN GLY ARG ARG PRO PHE GLY ILE SER ALA          
SEQRES  11 C  237  LEU ILE VAL GLY PHE ASP PHE ASP GLY THR PRO ARG LEU          
SEQRES  12 C  237  TYR GLN THR ASP PRO SER GLY THR TYR HIS ALA TRP LYS          
SEQRES  13 C  237  ALA ASN ALA ILE GLY ARG GLY ALA LYS SER VAL ARG GLU          
SEQRES  14 C  237  PHE LEU GLU LYS ASN TYR THR ASP GLU ALA ILE GLU THR          
SEQRES  15 C  237  ASP ASP LEU THR ILE LYS LEU VAL ILE LYS ALA LEU LEU          
SEQRES  16 C  237  GLU VAL VAL GLN SER GLY GLY LYS ASN ILE GLU LEU ALA          
SEQRES  17 C  237  VAL MET ARG ARG ASP GLN SER LEU LYS ILE LEU ASN PRO          
SEQRES  18 C  237  GLU GLU ILE GLU LYS TYR VAL ALA GLU ILE GLU LYS GLU          
SEQRES  19 C  237  LYS GLU GLU                                                  
SEQRES   1 D  233  ASP ARG GLY VAL ASN THR PHE SER PRO GLU GLY ARG LEU          
SEQRES   2 D  233  PHE GLN VAL GLU TYR ALA ILE GLU ALA ILE LYS LEU GLY          
SEQRES   3 D  233  SER THR ALA ILE GLY ILE GLN THR SER GLU GLY VAL CYS          
SEQRES   4 D  233  LEU ALA VAL GLU LYS ARG ILE THR SER PRO LEU MET GLU          
SEQRES   5 D  233  PRO SER SER ILE GLU LYS ILE VAL GLU ILE ASP ALA HIS          
SEQRES   6 D  233  ILE GLY CYS ALA MET SER GLY LEU ILE ALA ASP ALA LYS          
SEQRES   7 D  233  THR LEU ILE ASP LYS ALA ARG VAL GLU THR GLN ASN HIS          
SEQRES   8 D  233  TRP PHE THR TYR ASN GLU THR MET THR VAL GLU SER VAL          
SEQRES   9 D  233  THR GLN ALA VAL SER ASN LEU ALA LEU GLN PHE GLY GLU          
SEQRES  10 D  233  GLU ASP ALA ASP PRO GLY ALA MET SER ARG PRO PHE GLY          
SEQRES  11 D  233  VAL ALA LEU LEU PHE GLY GLY VAL ASP GLU LYS GLY PRO          
SEQRES  12 D  233  GLN LEU PHE HIS MET ASP PRO SER GLY THR PHE VAL GLN          
SEQRES  13 D  233  CYS ASP ALA ARG ALA ILE GLY SER ALA SER GLU GLY ALA          
SEQRES  14 D  233  GLN SER SER LEU GLN GLU VAL TYR HIS LYS SER MET THR          
SEQRES  15 D  233  LEU LYS GLU ALA ILE LYS SER SER LEU ILE ILE LEU LYS          
SEQRES  16 D  233  GLN VAL MET GLU GLU LYS LEU ASN ALA THR ASN ILE GLU          
SEQRES  17 D  233  LEU ALA THR VAL GLN PRO GLY GLN ASN PHE HIS MET PHE          
SEQRES  18 D  233  THR LYS GLU GLU LEU GLU GLU VAL ILE LYS ASP ILE              
SEQRES   1 E  238  PHE ARG ASN GLN TYR ASP ASN ASP VAL THR VAL TRP SER          
SEQRES   2 E  238  PRO GLN GLY ARG ILE HIS GLN ILE GLU TYR ALA MET GLU          
SEQRES   3 E  238  ALA VAL LYS GLN GLY SER ALA THR VAL GLY LEU LYS SER          
SEQRES   4 E  238  LYS THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ALA GLN          
SEQRES   5 E  238  SER GLU LEU ALA ALA HIS GLN LYS LYS ILE LEU HIS VAL          
SEQRES   6 E  238  ASP ASN HIS ILE GLY ILE SER ILE ALA GLY LEU THR ALA          
SEQRES   7 E  238  ASP ALA ARG LEU LEU CYS ASN PHE MET ARG GLN GLU CYS          
SEQRES   8 E  238  LEU ASP SER ARG PHE VAL PHE ASP ARG PRO LEU PRO VAL          
SEQRES   9 E  238  SER ARG LEU VAL SER LEU ILE GLY SER LYS THR GLN ILE          
SEQRES  10 E  238  PRO THR GLN ARG TYR GLY ARG ARG PRO TYR GLY VAL GLY          
SEQRES  11 E  238  LEU LEU ILE ALA GLY TYR ASP ASP MET GLY PRO HIS ILE          
SEQRES  12 E  238  PHE GLN THR CYS PRO SER ALA ASN TYR PHE ASP CYS ARG          
SEQRES  13 E  238  ALA MET SER ILE GLY ALA ARG SER GLN SER ALA ARG THR          
SEQRES  14 E  238  TYR LEU GLU ARG HIS MET SER GLU PHE MET GLU CYS ASN          
SEQRES  15 E  238  LEU ASN GLU LEU VAL LYS HIS GLY LEU ARG ALA LEU ARG          
SEQRES  16 E  238  GLU THR LEU PRO ALA GLU GLN ASP LEU THR THR LYS ASN          
SEQRES  17 E  238  VAL SER ILE GLY ILE VAL GLY LYS ASP LEU GLU PHE THR          
SEQRES  18 E  238  ILE TYR ASP ASP ASP ASP VAL SER PRO PHE LEU GLU GLY          
SEQRES  19 E  238  LEU GLU GLU ARG                                              
SEQRES   1 F  240  THR GLY TYR ASP LEU SER ALA SER THR PHE SER PRO ASP          
SEQRES   2 F  240  GLY ARG VAL PHE GLN VAL GLU TYR ALA MET LYS ALA VAL          
SEQRES   3 F  240  GLU ASN SER SER THR ALA ILE GLY ILE ARG CYS LYS ASP          
SEQRES   4 F  240  GLY VAL VAL PHE GLY VAL GLU LYS LEU VAL LEU SER LYS          
SEQRES   5 F  240  LEU TYR GLU GLU GLY SER ASN LYS ARG LEU PHE ASN VAL          
SEQRES   6 F  240  ASP ARG HIS VAL GLY MET ALA VAL ALA GLY LEU LEU ALA          
SEQRES   7 F  240  ASP ALA ARG SER LEU ALA ASP ILE ALA ARG GLU GLU ALA          
SEQRES   8 F  240  SER ASN PHE ARG SER ASN PHE GLY TYR ASN ILE PRO LEU          
SEQRES   9 F  240  LYS HIS LEU ALA ASP ARG VAL ALA MET TYR VAL HIS ALA          
SEQRES  10 F  240  TYR THR LEU TYR SER ALA VAL ARG PRO PHE GLY CYS SER          
SEQRES  11 F  240  PHE MET LEU GLY SER TYR SER VAL ASN ASP GLY ALA GLN          
SEQRES  12 F  240  LEU TYR MET ILE ASP PRO SER GLY VAL SER TYR GLY TYR          
SEQRES  13 F  240  TRP GLY CYS ALA ILE GLY LYS ALA ARG GLN ALA ALA LYS          
SEQRES  14 F  240  THR GLU ILE GLU LYS LEU GLN MET LYS GLU MET THR CYS          
SEQRES  15 F  240  ARG ASP ILE VAL LYS GLU VAL ALA LYS ILE ILE TYR ILE          
SEQRES  16 F  240  VAL HIS ASP GLU VAL LYS ASP LYS ALA PHE GLU LEU GLU          
SEQRES  17 F  240  LEU SER TRP VAL GLY GLU LEU THR ASN GLY ARG HIS GLU          
SEQRES  18 F  240  ILE VAL PRO LYS ASP ILE ARG GLU GLU ALA GLU LYS TYR          
SEQRES  19 F  240  ALA LYS GLU SER LEU LYS                                      
SEQRES   1 G  244  SER ARG GLY SER SER ALA GLY PHE ASP ARG HIS ILE THR          
SEQRES   2 G  244  ILE PHE SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR          
SEQRES   3 G  244  ALA PHE LYS ALA ILE ASN GLN GLY GLY LEU THR SER VAL          
SEQRES   4 G  244  ALA VAL ARG GLY LYS ASP CYS ALA VAL ILE VAL THR GLN          
SEQRES   5 G  244  LYS LYS VAL PRO ASP LYS LEU LEU ASP SER SER THR VAL          
SEQRES   6 G  244  THR HIS LEU PHE LYS ILE THR GLU ASN ILE GLY CYS VAL          
SEQRES   7 G  244  MET THR GLY MET THR ALA ASP SER ARG SER GLN VAL GLN          
SEQRES   8 G  244  ARG ALA ARG TYR GLU ALA ALA ASN TRP LYS TYR LYS TYR          
SEQRES   9 G  244  GLY TYR GLU ILE PRO VAL ASP MET LEU CYS LYS ARG ILE          
SEQRES  10 G  244  ALA ASP ILE SER GLN VAL TYR THR GLN ASN ALA GLU MET          
SEQRES  11 G  244  ARG PRO LEU GLY CYS CYS MET ILE LEU ILE GLY ILE ASP          
SEQRES  12 G  244  GLU GLU GLN GLY PRO GLN VAL TYR LYS CYS ASP PRO ALA          
SEQRES  13 G  244  GLY TYR TYR CYS GLY PHE LYS ALA THR ALA ALA GLY VAL          
SEQRES  14 G  244  LYS GLN THR GLU SER THR SER PHE LEU GLU LYS LYS VAL          
SEQRES  15 G  244  LYS LYS LYS PHE ASP TRP THR PHE GLU GLN THR VAL GLU          
SEQRES  16 G  244  THR ALA ILE THR CYS LEU SER THR VAL LEU SER ILE ASP          
SEQRES  17 G  244  PHE LYS PRO SER GLU ILE GLU VAL GLY VAL VAL THR VAL          
SEQRES  18 G  244  GLU ASN PRO LYS PHE ARG ILE LEU THR GLU ALA GLU ILE          
SEQRES  19 G  244  ASP ALA HIS LEU VAL ALA LEU ALA GLU ARG                      
SEQRES   1 H  220  THR THR ILE ALA GLY VAL VAL TYR LYS ASP GLY ILE VAL          
SEQRES   2 H  220  LEU GLY ALA ASP THR ARG ALA THR GLU GLY MET VAL VAL          
SEQRES   3 H  220  ALA ASP LYS ASN CYS SER LYS ILE HIS PHE ILE SER PRO          
SEQRES   4 H  220  ASN ILE TYR CYS CYS GLY ALA GLY THR ALA ALA ASP THR          
SEQRES   5 H  220  ASP MET THR THR GLN LEU ILE SER SER ASN LEU GLU LEU          
SEQRES   6 H  220  HIS SER LEU SER THR GLY ARG LEU PRO ARG VAL VAL THR          
SEQRES   7 H  220  ALA ASN ARG MET LEU LYS GLN MET LEU PHE ARG TYR GLN          
SEQRES   8 H  220  GLY TYR ILE GLY ALA ALA LEU VAL LEU GLY GLY VAL ASP          
SEQRES   9 H  220  VAL THR GLY PRO HIS LEU TYR SER ILE TYR PRO HIS GLY          
SEQRES  10 H  220  SER THR ASP LYS LEU PRO TYR VAL THR MET GLY SER GLY          
SEQRES  11 H  220  SER LEU ALA ALA MET ALA VAL PHE GLU ASP LYS PHE ARG          
SEQRES  12 H  220  PRO ASP MET GLU GLU GLU GLU ALA LYS ASN LEU VAL SER          
SEQRES  13 H  220  GLU ALA ILE ALA ALA GLY ILE PHE ASN ASP LEU GLY SER          
SEQRES  14 H  220  GLY SER ASN ILE ASP LEU CYS VAL ILE SER LYS ASN LYS          
SEQRES  15 H  220  LEU ASP PHE LEU ARG PRO TYR THR VAL PRO ASN LYS LYS          
SEQRES  16 H  220  GLY THR ARG LEU GLY ARG TYR ARG CYS GLU LYS GLY THR          
SEQRES  17 H  220  THR ALA VAL LEU THR GLU LYS ILE THR PRO LEU GLU              
SEQRES   1 I  204  SER ILE MET SER TYR ASN GLY GLY ALA VAL MET ALA MET          
SEQRES   2 I  204  LYS GLY LYS ASN CYS VAL ALA ILE ALA ALA ASP ARG ARG          
SEQRES   3 I  204  PHE GLY ILE GLN ALA GLN MET VAL THR THR ASP PHE GLN          
SEQRES   4 I  204  LYS ILE PHE PRO MET GLY ASP ARG LEU TYR ILE GLY LEU          
SEQRES   5 I  204  ALA GLY LEU ALA THR ASP VAL GLN THR VAL ALA GLN ARG          
SEQRES   6 I  204  LEU LYS PHE ARG LEU ASN LEU TYR GLU LEU LYS GLU GLY          
SEQRES   7 I  204  ARG GLN ILE LYS PRO TYR THR LEU MET SER MET VAL ALA          
SEQRES   8 I  204  ASN LEU LEU TYR GLU LYS ARG PHE GLY PRO TYR TYR THR          
SEQRES   9 I  204  GLU PRO VAL ILE ALA GLY LEU ASP PRO LYS THR PHE LYS          
SEQRES  10 I  204  PRO PHE ILE CYS SER LEU ASP LEU ILE GLY CYS PRO MET          
SEQRES  11 I  204  VAL THR ASP ASP PHE VAL VAL SER GLY THR CYS ALA GLU          
SEQRES  12 I  204  GLN MET TYR GLY MET CYS GLU SER LEU TRP GLU PRO ASN          
SEQRES  13 I  204  MET ASP PRO ASP HIS LEU PHE GLU THR ILE SER GLN ALA          
SEQRES  14 I  204  MET LEU ASN ALA VAL ASP ARG ASP ALA VAL SER GLY MET          
SEQRES  15 I  204  GLY VAL ILE VAL HIS ILE ILE GLU LYS ASP LYS ILE THR          
SEQRES  16 I  204  THR ARG THR LEU LYS ALA ARG MET ASP                          
SEQRES   1 J  196  MET GLU TYR LEU ILE GLY ILE GLN GLY PRO ASP TYR VAL          
SEQRES   2 J  196  LEU VAL ALA SER ASP ARG VAL ALA ALA SER ASN ILE VAL          
SEQRES   3 J  196  GLN MET LYS ASP ASP HIS ASP LYS MET PHE LYS MET SER          
SEQRES   4 J  196  GLU LYS ILE LEU LEU LEU CYS VAL GLY GLU ALA GLY ASP          
SEQRES   5 J  196  THR VAL GLN PHE ALA GLU TYR ILE GLN LYS ASN VAL GLN          
SEQRES   6 J  196  LEU TYR LYS MET ARG ASN GLY TYR GLU LEU SER PRO THR          
SEQRES   7 J  196  ALA ALA ALA ASN PHE THR ARG ARG ASN LEU ALA ASP CYS          
SEQRES   8 J  196  LEU ARG SER ARG THR PRO TYR HIS VAL ASN LEU LEU LEU          
SEQRES   9 J  196  ALA GLY TYR ASP GLU HIS GLU GLY PRO ALA LEU TYR TYR          
SEQRES  10 J  196  MET ASP TYR LEU ALA ALA LEU ALA LYS ALA PRO PHE ALA          
SEQRES  11 J  196  ALA HIS GLY TYR GLY ALA PHE LEU THR LEU SER ILE LEU          
SEQRES  12 J  196  ASP ARG TYR TYR THR PRO THR ILE SER ARG GLU ARG ALA          
SEQRES  13 J  196  VAL GLU LEU LEU ARG LYS CYS LEU GLU GLU LEU GLN LYS          
SEQRES  14 J  196  ARG PHE ILE LEU ASN LEU PRO THR PHE SER VAL ARG ILE          
SEQRES  15 J  196  ILE ASP LYS ASN GLY ILE HIS ASP LEU ASP ASN ILE SER          
SEQRES  16 J  196  PHE                                                          
SEQRES   1 K  201  THR THR THR LEU ALA PHE LYS PHE ARG HIS GLY VAL ILE          
SEQRES   2 K  201  VAL ALA ALA ASP SER ARG ALA THR ALA GLY ALA TYR ILE          
SEQRES   3 K  201  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 K  201  TYR LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 K  201  SER PHE TRP GLU ARG LEU LEU ALA ARG GLN CYS ARG ILE          
SEQRES   6 K  201  TYR GLU LEU ARG ASN LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 K  201  ALA SER LYS LEU LEU ALA ASN MET VAL TYR GLN TYR LYS          
SEQRES   8 K  201  GLY MET GLY LEU SER MET GLY THR MET ILE CYS GLY TRP          
SEQRES   9 K  201  ASP LYS ARG GLY PRO GLY LEU TYR TYR VAL ASP SER GLU          
SEQRES  10 K  201  GLY ASN ARG ILE SER GLY ALA THR PHE SER VAL GLY SER          
SEQRES  11 K  201  GLY SER VAL TYR ALA TYR GLY VAL MET ASP ARG GLY TYR          
SEQRES  12 K  201  SER TYR ASP LEU GLU VAL GLU GLN ALA TYR ASP LEU ALA          
SEQRES  13 K  201  ARG ARG ALA ILE TYR GLN ALA THR TYR ARG ASP ALA TYR          
SEQRES  14 K  201  SER GLY GLY ALA VAL ASN LEU TYR HIS VAL ARG GLU ASP          
SEQRES  15 K  201  GLY TRP ILE ARG VAL SER SER ASP ASN VAL ALA ASP LEU          
SEQRES  16 K  201  HIS GLU LYS TYR SER GLY                                      
SEQRES   1 L  213  ARG PHE SER PRO TYR VAL PHE ASN GLY GLY THR ILE LEU          
SEQRES   2 L  213  ALA ILE ALA GLY GLU ASP PHE ALA ILE VAL ALA SER ASP          
SEQRES   3 L  213  THR ARG LEU SER GLU GLY PHE SER ILE HIS THR ARG ASP          
SEQRES   4 L  213  SER PRO LYS CYS TYR LYS LEU THR ASP LYS THR VAL ILE          
SEQRES   5 L  213  GLY CYS SER GLY PHE HIS GLY ASP CYS LEU THR LEU THR          
SEQRES   6 L  213  LYS ILE ILE GLU ALA ARG LEU LYS MET TYR LYS HIS SER          
SEQRES   7 L  213  ASN ASN LYS ALA MET THR THR GLY ALA ILE ALA ALA MET          
SEQRES   8 L  213  LEU SER THR ILE LEU TYR SER ARG ARG PHE PHE PRO TYR          
SEQRES   9 L  213  TYR VAL TYR ASN ILE ILE GLY GLY LEU ASP GLU GLU GLY          
SEQRES  10 L  213  LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER TYR          
SEQRES  11 L  213  GLN ARG ASP SER PHE LYS ALA GLY GLY SER ALA SER ALA          
SEQRES  12 L  213  MET LEU GLN PRO LEU LEU ASP ASN GLN VAL GLY PHE LYS          
SEQRES  13 L  213  ASN MET GLN ASN VAL GLU HIS VAL PRO LEU SER LEU ASP          
SEQRES  14 L  213  ARG ALA MET ARG LEU VAL LYS ASP VAL PHE ILE SER ALA          
SEQRES  15 L  213  ALA GLU ARG ASP VAL TYR THR GLY ASP ALA LEU ARG ILE          
SEQRES  16 L  213  CYS ILE VAL THR LYS GLU GLY ILE ARG GLU GLU THR VAL          
SEQRES  17 L  213  SER LEU ARG LYS ASP                                          
SEQRES   1 N  203  THR THR ILE MET ALA VAL GLN PHE ASP GLY GLY VAL VAL          
SEQRES   2 N  203  LEU GLY ALA ASP SER ARG THR THR THR GLY SER TYR ILE          
SEQRES   3 N  203  ALA ASN ARG VAL THR ASP LYS LEU THR PRO ILE HIS ASP          
SEQRES   4 N  203  ARG ILE PHE CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 N  203  GLN ALA VAL ALA ASP ALA VAL THR TYR GLN LEU GLY PHE          
SEQRES   6 N  203  HIS SER ILE GLU LEU ASN GLU PRO PRO LEU VAL HIS THR          
SEQRES   7 N  203  ALA ALA SER LEU PHE LYS GLU MET CYS TYR ARG TYR ARG          
SEQRES   8 N  203  GLU ASP LEU MET ALA GLY ILE ILE ILE ALA GLY TRP ASP          
SEQRES   9 N  203  PRO GLN GLU GLY GLY GLN VAL TYR SER VAL PRO MET GLY          
SEQRES  10 N  203  GLY MET MET VAL ARG GLN SER PHE ALA ILE GLY GLY SER          
SEQRES  11 N  203  GLY SER SER TYR ILE TYR GLY TYR VAL ASP ALA THR TYR          
SEQRES  12 N  203  ARG GLU GLY MET THR LYS GLU GLU CYS LEU GLN PHE THR          
SEQRES  13 N  203  ALA ASN ALA LEU ALA LEU ALA MET GLU ARG ASP GLY SER          
SEQRES  14 N  203  SER GLY GLY VAL ILE ARG LEU ALA ALA ILE ALA GLU SER          
SEQRES  15 N  203  GLY VAL GLU ARG GLN VAL LEU LEU GLY ASP GLN ILE PRO          
SEQRES  16 N  203  LYS PHE ALA VAL ALA THR LEU PRO                              
SEQRES   1 O  230  ARG GLY TYR SER PHE SER LEU THR THR PHE SER PRO SER          
SEQRES   2 O  230  GLY LYS LEU VAL GLN ILE GLU TYR ALA LEU ALA ALA VAL          
SEQRES   3 O  230  ALA GLY GLY ALA PRO SER VAL GLY ILE LYS ALA ALA ASN          
SEQRES   4 O  230  GLY VAL VAL LEU ALA THR GLU LYS LYS GLN LYS SER ILE          
SEQRES   5 O  230  LEU TYR ASP GLU ARG SER VAL HIS LYS VAL GLU PRO ILE          
SEQRES   6 O  230  THR LYS HIS ILE GLY LEU VAL TYR SER GLY MET GLY PRO          
SEQRES   7 O  230  ASP TYR ARG VAL LEU VAL HIS ARG ALA ARG LYS LEU ALA          
SEQRES   8 O  230  GLN GLN TYR TYR LEU VAL TYR GLN GLU PRO ILE PRO THR          
SEQRES   9 O  230  ALA GLN LEU VAL GLN ARG VAL ALA SER VAL MET GLN GLU          
SEQRES  10 O  230  TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY VAL SER          
SEQRES  11 O  230  LEU LEU ILE CYS GLY TRP ASN GLU GLY ARG PRO TYR LEU          
SEQRES  12 O  230  PHE GLN SER ASP PRO SER GLY ALA TYR PHE ALA TRP LYS          
SEQRES  13 O  230  ALA THR ALA MET GLY LYS ASN TYR VAL ASN GLY LYS THR          
SEQRES  14 O  230  PHE LEU GLU LYS ARG TYR ASN GLU ASP LEU GLU LEU GLU          
SEQRES  15 O  230  ASP ALA ILE HIS THR ALA ILE LEU THR LEU LYS GLU SER          
SEQRES  16 O  230  PHE GLU GLY GLN MET THR GLU ASP ASN ILE GLU VAL GLY          
SEQRES  17 O  230  ILE CYS ASN GLU ALA GLY PHE ARG ARG LEU THR PRO THR          
SEQRES  18 O  230  GLU VAL LYS ASP TYR LEU ALA ALA ILE                          
SEQRES   1 P  248  SER ARG ARG TYR ASP SER ARG THR THR ILE PHE SER PRO          
SEQRES   2 P  248  GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA MET GLU ALA          
SEQRES   3 P  248  ILE GLY HIS ALA GLY THR CYS LEU GLY ILE LEU ALA ASN          
SEQRES   4 P  248  ASP GLY VAL LEU LEU ALA ALA GLU ARG ARG ASN ILE HIS          
SEQRES   5 P  248  LYS LEU LEU ASP GLU VAL PHE PHE SER GLU LYS ILE TYR          
SEQRES   6 P  248  LYS LEU ASN GLU ASP MET ALA CYS SER VAL ALA GLY ILE          
SEQRES   7 P  248  THR SER ASP ALA ASN VAL LEU THR ASN GLU LEU ARG LEU          
SEQRES   8 P  248  ILE ALA GLN ARG TYR LEU LEU GLN TYR GLN GLU PRO ILE          
SEQRES   9 P  248  PRO CYS GLU GLN LEU VAL THR ALA LEU CYS ASP ILE LYS          
SEQRES  10 P  248  GLN ALA TYR THR GLN PHE GLY GLY LYS ARG PRO PHE GLY          
SEQRES  11 P  248  VAL SER LEU LEU TYR ILE GLY TRP ASP LYS HIS TYR GLY          
SEQRES  12 P  248  PHE GLN LEU TYR GLN SER ASP PRO SER GLY ASN TYR GLY          
SEQRES  13 P  248  GLY TRP LYS ALA THR CYS ILE GLY ASN ASN SER ALA ALA          
SEQRES  14 P  248  ALA VAL SER MET LEU LYS GLN ASP TYR LYS GLU GLY GLU          
SEQRES  15 P  248  MET THR LEU LYS SER ALA LEU ALA LEU ALA ILE LYS VAL          
SEQRES  16 P  248  LEU ASN LYS THR MET ASP VAL SER LYS LEU SER ALA GLU          
SEQRES  17 P  248  LYS VAL GLU ILE ALA THR LEU THR ARG GLU ASN GLY LYS          
SEQRES  18 P  248  THR VAL ILE ARG VAL LEU LYS GLN LYS GLU VAL GLU GLN          
SEQRES  19 P  248  LEU ILE LYS LYS HIS GLU GLU GLU GLU ALA LYS ALA GLU          
SEQRES  20 P  248  ARG                                                          
SEQRES   1 Q  237  SER TYR ASP ARG ALA ILE THR VAL PHE SER PRO ASP GLY          
SEQRES   2 Q  237  HIS LEU PHE GLN VAL GLU TYR ALA GLN GLU ALA VAL LYS          
SEQRES   3 Q  237  LYS GLY SER THR ALA VAL GLY VAL ARG GLY ARG ASP ILE          
SEQRES   4 Q  237  VAL VAL LEU GLY VAL GLU LYS LYS SER VAL ALA LYS LEU          
SEQRES   5 Q  237  GLN ASP GLU ARG THR VAL ARG LYS ILE CYS ALA LEU ASP          
SEQRES   6 Q  237  ASP ASN VAL CYS MET ALA PHE ALA GLY LEU THR ALA ASP          
SEQRES   7 Q  237  ALA ARG ILE VAL ILE ASN ARG ALA ARG VAL GLU CYS GLN          
SEQRES   8 Q  237  SER HIS ARG LEU THR VAL GLU ASP PRO VAL THR VAL GLU          
SEQRES   9 Q  237  TYR ILE THR ARG TYR ILE ALA SER LEU LYS GLN ARG TYR          
SEQRES  10 Q  237  THR GLN SER ASN GLY ARG ARG PRO PHE GLY ILE SER ALA          
SEQRES  11 Q  237  LEU ILE VAL GLY PHE ASP PHE ASP GLY THR PRO ARG LEU          
SEQRES  12 Q  237  TYR GLN THR ASP PRO SER GLY THR TYR HIS ALA TRP LYS          
SEQRES  13 Q  237  ALA ASN ALA ILE GLY ARG GLY ALA LYS SER VAL ARG GLU          
SEQRES  14 Q  237  PHE LEU GLU LYS ASN TYR THR ASP GLU ALA ILE GLU THR          
SEQRES  15 Q  237  ASP ASP LEU THR ILE LYS LEU VAL ILE LYS ALA LEU LEU          
SEQRES  16 Q  237  GLU VAL VAL GLN SER GLY GLY LYS ASN ILE GLU LEU ALA          
SEQRES  17 Q  237  VAL MET ARG ARG ASP GLN SER LEU LYS ILE LEU ASN PRO          
SEQRES  18 Q  237  GLU GLU ILE GLU LYS TYR VAL ALA GLU ILE GLU LYS GLU          
SEQRES  19 Q  237  LYS GLU GLU                                                  
SEQRES   1 R  233  ASP ARG GLY VAL ASN THR PHE SER PRO GLU GLY ARG LEU          
SEQRES   2 R  233  PHE GLN VAL GLU TYR ALA ILE GLU ALA ILE LYS LEU GLY          
SEQRES   3 R  233  SER THR ALA ILE GLY ILE GLN THR SER GLU GLY VAL CYS          
SEQRES   4 R  233  LEU ALA VAL GLU LYS ARG ILE THR SER PRO LEU MET GLU          
SEQRES   5 R  233  PRO SER SER ILE GLU LYS ILE VAL GLU ILE ASP ALA HIS          
SEQRES   6 R  233  ILE GLY CYS ALA MET SER GLY LEU ILE ALA ASP ALA LYS          
SEQRES   7 R  233  THR LEU ILE ASP LYS ALA ARG VAL GLU THR GLN ASN HIS          
SEQRES   8 R  233  TRP PHE THR TYR ASN GLU THR MET THR VAL GLU SER VAL          
SEQRES   9 R  233  THR GLN ALA VAL SER ASN LEU ALA LEU GLN PHE GLY GLU          
SEQRES  10 R  233  GLU ASP ALA ASP PRO GLY ALA MET SER ARG PRO PHE GLY          
SEQRES  11 R  233  VAL ALA LEU LEU PHE GLY GLY VAL ASP GLU LYS GLY PRO          
SEQRES  12 R  233  GLN LEU PHE HIS MET ASP PRO SER GLY THR PHE VAL GLN          
SEQRES  13 R  233  CYS ASP ALA ARG ALA ILE GLY SER ALA SER GLU GLY ALA          
SEQRES  14 R  233  GLN SER SER LEU GLN GLU VAL TYR HIS LYS SER MET THR          
SEQRES  15 R  233  LEU LYS GLU ALA ILE LYS SER SER LEU ILE ILE LEU LYS          
SEQRES  16 R  233  GLN VAL MET GLU GLU LYS LEU ASN ALA THR ASN ILE GLU          
SEQRES  17 R  233  LEU ALA THR VAL GLN PRO GLY GLN ASN PHE HIS MET PHE          
SEQRES  18 R  233  THR LYS GLU GLU LEU GLU GLU VAL ILE LYS ASP ILE              
SEQRES   1 S  238  PHE ARG ASN GLN TYR ASP ASN ASP VAL THR VAL TRP SER          
SEQRES   2 S  238  PRO GLN GLY ARG ILE HIS GLN ILE GLU TYR ALA MET GLU          
SEQRES   3 S  238  ALA VAL LYS GLN GLY SER ALA THR VAL GLY LEU LYS SER          
SEQRES   4 S  238  LYS THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ALA GLN          
SEQRES   5 S  238  SER GLU LEU ALA ALA HIS GLN LYS LYS ILE LEU HIS VAL          
SEQRES   6 S  238  ASP ASN HIS ILE GLY ILE SER ILE ALA GLY LEU THR ALA          
SEQRES   7 S  238  ASP ALA ARG LEU LEU CYS ASN PHE MET ARG GLN GLU CYS          
SEQRES   8 S  238  LEU ASP SER ARG PHE VAL PHE ASP ARG PRO LEU PRO VAL          
SEQRES   9 S  238  SER ARG LEU VAL SER LEU ILE GLY SER LYS THR GLN ILE          
SEQRES  10 S  238  PRO THR GLN ARG TYR GLY ARG ARG PRO TYR GLY VAL GLY          
SEQRES  11 S  238  LEU LEU ILE ALA GLY TYR ASP ASP MET GLY PRO HIS ILE          
SEQRES  12 S  238  PHE GLN THR CYS PRO SER ALA ASN TYR PHE ASP CYS ARG          
SEQRES  13 S  238  ALA MET SER ILE GLY ALA ARG SER GLN SER ALA ARG THR          
SEQRES  14 S  238  TYR LEU GLU ARG HIS MET SER GLU PHE MET GLU CYS ASN          
SEQRES  15 S  238  LEU ASN GLU LEU VAL LYS HIS GLY LEU ARG ALA LEU ARG          
SEQRES  16 S  238  GLU THR LEU PRO ALA GLU GLN ASP LEU THR THR LYS ASN          
SEQRES  17 S  238  VAL SER ILE GLY ILE VAL GLY LYS ASP LEU GLU PHE THR          
SEQRES  18 S  238  ILE TYR ASP ASP ASP ASP VAL SER PRO PHE LEU GLU GLY          
SEQRES  19 S  238  LEU GLU GLU ARG                                              
SEQRES   1 T  240  THR GLY TYR ASP LEU SER ALA SER THR PHE SER PRO ASP          
SEQRES   2 T  240  GLY ARG VAL PHE GLN VAL GLU TYR ALA MET LYS ALA VAL          
SEQRES   3 T  240  GLU ASN SER SER THR ALA ILE GLY ILE ARG CYS LYS ASP          
SEQRES   4 T  240  GLY VAL VAL PHE GLY VAL GLU LYS LEU VAL LEU SER LYS          
SEQRES   5 T  240  LEU TYR GLU GLU GLY SER ASN LYS ARG LEU PHE ASN VAL          
SEQRES   6 T  240  ASP ARG HIS VAL GLY MET ALA VAL ALA GLY LEU LEU ALA          
SEQRES   7 T  240  ASP ALA ARG SER LEU ALA ASP ILE ALA ARG GLU GLU ALA          
SEQRES   8 T  240  SER ASN PHE ARG SER ASN PHE GLY TYR ASN ILE PRO LEU          
SEQRES   9 T  240  LYS HIS LEU ALA ASP ARG VAL ALA MET TYR VAL HIS ALA          
SEQRES  10 T  240  TYR THR LEU TYR SER ALA VAL ARG PRO PHE GLY CYS SER          
SEQRES  11 T  240  PHE MET LEU GLY SER TYR SER VAL ASN ASP GLY ALA GLN          
SEQRES  12 T  240  LEU TYR MET ILE ASP PRO SER GLY VAL SER TYR GLY TYR          
SEQRES  13 T  240  TRP GLY CYS ALA ILE GLY LYS ALA ARG GLN ALA ALA LYS          
SEQRES  14 T  240  THR GLU ILE GLU LYS LEU GLN MET LYS GLU MET THR CYS          
SEQRES  15 T  240  ARG ASP ILE VAL LYS GLU VAL ALA LYS ILE ILE TYR ILE          
SEQRES  16 T  240  VAL HIS ASP GLU VAL LYS ASP LYS ALA PHE GLU LEU GLU          
SEQRES  17 T  240  LEU SER TRP VAL GLY GLU LEU THR ASN GLY ARG HIS GLU          
SEQRES  18 T  240  ILE VAL PRO LYS ASP ILE ARG GLU GLU ALA GLU LYS TYR          
SEQRES  19 T  240  ALA LYS GLU SER LEU LYS                                      
SEQRES   1 U  244  SER ARG GLY SER SER ALA GLY PHE ASP ARG HIS ILE THR          
SEQRES   2 U  244  ILE PHE SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR          
SEQRES   3 U  244  ALA PHE LYS ALA ILE ASN GLN GLY GLY LEU THR SER VAL          
SEQRES   4 U  244  ALA VAL ARG GLY LYS ASP CYS ALA VAL ILE VAL THR GLN          
SEQRES   5 U  244  LYS LYS VAL PRO ASP LYS LEU LEU ASP SER SER THR VAL          
SEQRES   6 U  244  THR HIS LEU PHE LYS ILE THR GLU ASN ILE GLY CYS VAL          
SEQRES   7 U  244  MET THR GLY MET THR ALA ASP SER ARG SER GLN VAL GLN          
SEQRES   8 U  244  ARG ALA ARG TYR GLU ALA ALA ASN TRP LYS TYR LYS TYR          
SEQRES   9 U  244  GLY TYR GLU ILE PRO VAL ASP MET LEU CYS LYS ARG ILE          
SEQRES  10 U  244  ALA ASP ILE SER GLN VAL TYR THR GLN ASN ALA GLU MET          
SEQRES  11 U  244  ARG PRO LEU GLY CYS CYS MET ILE LEU ILE GLY ILE ASP          
SEQRES  12 U  244  GLU GLU GLN GLY PRO GLN VAL TYR LYS CYS ASP PRO ALA          
SEQRES  13 U  244  GLY TYR TYR CYS GLY PHE LYS ALA THR ALA ALA GLY VAL          
SEQRES  14 U  244  LYS GLN THR GLU SER THR SER PHE LEU GLU LYS LYS VAL          
SEQRES  15 U  244  LYS LYS LYS PHE ASP TRP THR PHE GLU GLN THR VAL GLU          
SEQRES  16 U  244  THR ALA ILE THR CYS LEU SER THR VAL LEU SER ILE ASP          
SEQRES  17 U  244  PHE LYS PRO SER GLU ILE GLU VAL GLY VAL VAL THR VAL          
SEQRES  18 U  244  GLU ASN PRO LYS PHE ARG ILE LEU THR GLU ALA GLU ILE          
SEQRES  19 U  244  ASP ALA HIS LEU VAL ALA LEU ALA GLU ARG                      
SEQRES   1 V  220  THR THR ILE ALA GLY VAL VAL TYR LYS ASP GLY ILE VAL          
SEQRES   2 V  220  LEU GLY ALA ASP THR ARG ALA THR GLU GLY MET VAL VAL          
SEQRES   3 V  220  ALA ASP LYS ASN CYS SER LYS ILE HIS PHE ILE SER PRO          
SEQRES   4 V  220  ASN ILE TYR CYS CYS GLY ALA GLY THR ALA ALA ASP THR          
SEQRES   5 V  220  ASP MET THR THR GLN LEU ILE SER SER ASN LEU GLU LEU          
SEQRES   6 V  220  HIS SER LEU SER THR GLY ARG LEU PRO ARG VAL VAL THR          
SEQRES   7 V  220  ALA ASN ARG MET LEU LYS GLN MET LEU PHE ARG TYR GLN          
SEQRES   8 V  220  GLY TYR ILE GLY ALA ALA LEU VAL LEU GLY GLY VAL ASP          
SEQRES   9 V  220  VAL THR GLY PRO HIS LEU TYR SER ILE TYR PRO HIS GLY          
SEQRES  10 V  220  SER THR ASP LYS LEU PRO TYR VAL THR MET GLY SER GLY          
SEQRES  11 V  220  SER LEU ALA ALA MET ALA VAL PHE GLU ASP LYS PHE ARG          
SEQRES  12 V  220  PRO ASP MET GLU GLU GLU GLU ALA LYS ASN LEU VAL SER          
SEQRES  13 V  220  GLU ALA ILE ALA ALA GLY ILE PHE ASN ASP LEU GLY SER          
SEQRES  14 V  220  GLY SER ASN ILE ASP LEU CYS VAL ILE SER LYS ASN LYS          
SEQRES  15 V  220  LEU ASP PHE LEU ARG PRO TYR THR VAL PRO ASN LYS LYS          
SEQRES  16 V  220  GLY THR ARG LEU GLY ARG TYR ARG CYS GLU LYS GLY THR          
SEQRES  17 V  220  THR ALA VAL LEU THR GLU LYS ILE THR PRO LEU GLU              
SEQRES   1 W  204  SER ILE MET SER TYR ASN GLY GLY ALA VAL MET ALA MET          
SEQRES   2 W  204  LYS GLY LYS ASN CYS VAL ALA ILE ALA ALA ASP ARG ARG          
SEQRES   3 W  204  PHE GLY ILE GLN ALA GLN MET VAL THR THR ASP PHE GLN          
SEQRES   4 W  204  LYS ILE PHE PRO MET GLY ASP ARG LEU TYR ILE GLY LEU          
SEQRES   5 W  204  ALA GLY LEU ALA THR ASP VAL GLN THR VAL ALA GLN ARG          
SEQRES   6 W  204  LEU LYS PHE ARG LEU ASN LEU TYR GLU LEU LYS GLU GLY          
SEQRES   7 W  204  ARG GLN ILE LYS PRO TYR THR LEU MET SER MET VAL ALA          
SEQRES   8 W  204  ASN LEU LEU TYR GLU LYS ARG PHE GLY PRO TYR TYR THR          
SEQRES   9 W  204  GLU PRO VAL ILE ALA GLY LEU ASP PRO LYS THR PHE LYS          
SEQRES  10 W  204  PRO PHE ILE CYS SER LEU ASP LEU ILE GLY CYS PRO MET          
SEQRES  11 W  204  VAL THR ASP ASP PHE VAL VAL SER GLY THR CYS ALA GLU          
SEQRES  12 W  204  GLN MET TYR GLY MET CYS GLU SER LEU TRP GLU PRO ASN          
SEQRES  13 W  204  MET ASP PRO ASP HIS LEU PHE GLU THR ILE SER GLN ALA          
SEQRES  14 W  204  MET LEU ASN ALA VAL ASP ARG ASP ALA VAL SER GLY MET          
SEQRES  15 W  204  GLY VAL ILE VAL HIS ILE ILE GLU LYS ASP LYS ILE THR          
SEQRES  16 W  204  THR ARG THR LEU LYS ALA ARG MET ASP                          
SEQRES   1 X  196  MET GLU TYR LEU ILE GLY ILE GLN GLY PRO ASP TYR VAL          
SEQRES   2 X  196  LEU VAL ALA SER ASP ARG VAL ALA ALA SER ASN ILE VAL          
SEQRES   3 X  196  GLN MET LYS ASP ASP HIS ASP LYS MET PHE LYS MET SER          
SEQRES   4 X  196  GLU LYS ILE LEU LEU LEU CYS VAL GLY GLU ALA GLY ASP          
SEQRES   5 X  196  THR VAL GLN PHE ALA GLU TYR ILE GLN LYS ASN VAL GLN          
SEQRES   6 X  196  LEU TYR LYS MET ARG ASN GLY TYR GLU LEU SER PRO THR          
SEQRES   7 X  196  ALA ALA ALA ASN PHE THR ARG ARG ASN LEU ALA ASP CYS          
SEQRES   8 X  196  LEU ARG SER ARG THR PRO TYR HIS VAL ASN LEU LEU LEU          
SEQRES   9 X  196  ALA GLY TYR ASP GLU HIS GLU GLY PRO ALA LEU TYR TYR          
SEQRES  10 X  196  MET ASP TYR LEU ALA ALA LEU ALA LYS ALA PRO PHE ALA          
SEQRES  11 X  196  ALA HIS GLY TYR GLY ALA PHE LEU THR LEU SER ILE LEU          
SEQRES  12 X  196  ASP ARG TYR TYR THR PRO THR ILE SER ARG GLU ARG ALA          
SEQRES  13 X  196  VAL GLU LEU LEU ARG LYS CYS LEU GLU GLU LEU GLN LYS          
SEQRES  14 X  196  ARG PHE ILE LEU ASN LEU PRO THR PHE SER VAL ARG ILE          
SEQRES  15 X  196  ILE ASP LYS ASN GLY ILE HIS ASP LEU ASP ASN ILE SER          
SEQRES  16 X  196  PHE                                                          
SEQRES   1 Y  201  THR THR THR LEU ALA PHE LYS PHE ARG HIS GLY VAL ILE          
SEQRES   2 Y  201  VAL ALA ALA ASP SER ARG ALA THR ALA GLY ALA TYR ILE          
SEQRES   3 Y  201  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 Y  201  TYR LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 Y  201  SER PHE TRP GLU ARG LEU LEU ALA ARG GLN CYS ARG ILE          
SEQRES   6 Y  201  TYR GLU LEU ARG ASN LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 Y  201  ALA SER LYS LEU LEU ALA ASN MET VAL TYR GLN TYR LYS          
SEQRES   8 Y  201  GLY MET GLY LEU SER MET GLY THR MET ILE CYS GLY TRP          
SEQRES   9 Y  201  ASP LYS ARG GLY PRO GLY LEU TYR TYR VAL ASP SER GLU          
SEQRES  10 Y  201  GLY ASN ARG ILE SER GLY ALA THR PHE SER VAL GLY SER          
SEQRES  11 Y  201  GLY SER VAL TYR ALA TYR GLY VAL MET ASP ARG GLY TYR          
SEQRES  12 Y  201  SER TYR ASP LEU GLU VAL GLU GLN ALA TYR ASP LEU ALA          
SEQRES  13 Y  201  ARG ARG ALA ILE TYR GLN ALA THR TYR ARG ASP ALA TYR          
SEQRES  14 Y  201  SER GLY GLY ALA VAL ASN LEU TYR HIS VAL ARG GLU ASP          
SEQRES  15 Y  201  GLY TRP ILE ARG VAL SER SER ASP ASN VAL ALA ASP LEU          
SEQRES  16 Y  201  HIS GLU LYS TYR SER GLY                                      
SEQRES   1 Z  213  ARG PHE SER PRO TYR VAL PHE ASN GLY GLY THR ILE LEU          
SEQRES   2 Z  213  ALA ILE ALA GLY GLU ASP PHE ALA ILE VAL ALA SER ASP          
SEQRES   3 Z  213  THR ARG LEU SER GLU GLY PHE SER ILE HIS THR ARG ASP          
SEQRES   4 Z  213  SER PRO LYS CYS TYR LYS LEU THR ASP LYS THR VAL ILE          
SEQRES   5 Z  213  GLY CYS SER GLY PHE HIS GLY ASP CYS LEU THR LEU THR          
SEQRES   6 Z  213  LYS ILE ILE GLU ALA ARG LEU LYS MET TYR LYS HIS SER          
SEQRES   7 Z  213  ASN ASN LYS ALA MET THR THR GLY ALA ILE ALA ALA MET          
SEQRES   8 Z  213  LEU SER THR ILE LEU TYR SER ARG ARG PHE PHE PRO TYR          
SEQRES   9 Z  213  TYR VAL TYR ASN ILE ILE GLY GLY LEU ASP GLU GLU GLY          
SEQRES  10 Z  213  LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER TYR          
SEQRES  11 Z  213  GLN ARG ASP SER PHE LYS ALA GLY GLY SER ALA SER ALA          
SEQRES  12 Z  213  MET LEU GLN PRO LEU LEU ASP ASN GLN VAL GLY PHE LYS          
SEQRES  13 Z  213  ASN MET GLN ASN VAL GLU HIS VAL PRO LEU SER LEU ASP          
SEQRES  14 Z  213  ARG ALA MET ARG LEU VAL LYS ASP VAL PHE ILE SER ALA          
SEQRES  15 Z  213  ALA GLU ARG ASP VAL TYR THR GLY ASP ALA LEU ARG ILE          
SEQRES  16 Z  213  CYS ILE VAL THR LYS GLU GLY ILE ARG GLU GLU THR VAL          
SEQRES  17 Z  213  SER LEU ARG LYS ASP                                          
SEQRES   1 a  216  THR GLN ASN PRO MET VAL THR GLY THR SER VAL LEU GLY          
SEQRES   2 a  216  VAL LYS PHE GLU GLY GLY VAL VAL ILE ALA ALA ASP MET          
SEQRES   3 a  216  LEU GLY SER TYR GLY SER LEU ALA ARG PHE ARG ASN ILE          
SEQRES   4 a  216  SER ARG ILE MET ARG VAL ASN ASN SER THR MET LEU GLY          
SEQRES   5 a  216  ALA SER GLY ASP TYR ALA ASP PHE GLN TYR LEU LYS GLN          
SEQRES   6 a  216  VAL LEU GLY GLN MET VAL ILE ASP GLU GLU LEU LEU GLY          
SEQRES   7 a  216  ASP GLY HIS SER TYR SER PRO ARG ALA ILE HIS SER TRP          
SEQRES   8 a  216  LEU THR ARG ALA MET TYR SER ARG ARG SER LYS MET ASN          
SEQRES   9 a  216  PRO LEU TRP ASN THR MET VAL ILE GLY GLY TYR ALA ASP          
SEQRES  10 a  216  GLY GLU SER PHE LEU GLY TYR VAL ASP MET LEU GLY VAL          
SEQRES  11 a  216  ALA TYR GLU ALA PRO SER LEU ALA THR GLY TYR GLY ALA          
SEQRES  12 a  216  TYR LEU ALA GLN PRO LEU LEU ARG GLU VAL LEU GLU LYS          
SEQRES  13 a  216  GLN PRO VAL LEU SER GLN THR GLU ALA ARG ASP LEU VAL          
SEQRES  14 a  216  GLU ARG CYS MET ARG VAL LEU TYR TYR ARG ASP ALA ARG          
SEQRES  15 a  216  SER TYR ASN ARG PHE GLN ILE ALA THR VAL THR GLU LYS          
SEQRES  16 a  216  GLY VAL GLU ILE GLU GLY PRO LEU SER THR GLU THR ASN          
SEQRES  17 a  216  TRP ASP ILE ALA HIS MET ILE SER                              
SEQRES   1 b  203  THR THR ILE MET ALA VAL GLN PHE ASP GLY GLY VAL VAL          
SEQRES   2 b  203  LEU GLY ALA ASP SER ARG THR THR THR GLY SER TYR ILE          
SEQRES   3 b  203  ALA ASN ARG VAL THR ASP LYS LEU THR PRO ILE HIS ASP          
SEQRES   4 b  203  ARG ILE PHE CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 b  203  GLN ALA VAL ALA ASP ALA VAL THR TYR GLN LEU GLY PHE          
SEQRES   6 b  203  HIS SER ILE GLU LEU ASN GLU PRO PRO LEU VAL HIS THR          
SEQRES   7 b  203  ALA ALA SER LEU PHE LYS GLU MET CYS TYR ARG TYR ARG          
SEQRES   8 b  203  GLU ASP LEU MET ALA GLY ILE ILE ILE ALA GLY TRP ASP          
SEQRES   9 b  203  PRO GLN GLU GLY GLY GLN VAL TYR SER VAL PRO MET GLY          
SEQRES  10 b  203  GLY MET MET VAL ARG GLN SER PHE ALA ILE GLY GLY SER          
SEQRES  11 b  203  GLY SER SER TYR ILE TYR GLY TYR VAL ASP ALA THR TYR          
SEQRES  12 b  203  ARG GLU GLY MET THR LYS GLU GLU CYS LEU GLN PHE THR          
SEQRES  13 b  203  ALA ASN ALA LEU ALA LEU ALA MET GLU ARG ASP GLY SER          
SEQRES  14 b  203  SER GLY GLY VAL ILE ARG LEU ALA ALA ILE ALA GLU SER          
SEQRES  15 b  203  GLY VAL GLU ARG GLN VAL LEU LEU GLY ASP GLN ILE PRO          
SEQRES  16 b  203  LYS PHE ALA VAL ALA THR LEU PRO                              
HELIX    1 AA1 TYR M   57  LEU M   76  1                                  20    
HELIX    2 AA2 SER M   84  LYS M  102  1                                  19    
HELIX    3 AA3 GLY M  140  TYR M  144  5                                   5    
HELIX    4 AA4 LEU M  145  GLN M  157  1                                  13    
HELIX    5 AA5 SER M  161  ASP M  180  1                                  20    
HELIX    6 AA6 TRP M  209  MET M  214  5                                   6    
HELIX    7 AA7 LEU A   18  GLY A   30  1                                  13    
HELIX    8 AA8 MET A   78  GLN A  101  1                                  24    
HELIX    9 AA9 PRO A  105  TYR A  120  1                                  16    
HELIX   10 AB1 ASN A  165  TYR A  177  1                                  13    
HELIX   11 AB2 GLU A  182  LYS A  195  1                                  14    
HELIX   12 AB3 GLU A  196  PHE A  198  5                                   3    
HELIX   13 AB4 THR A  221  ALA A  231  1                                  11    
HELIX   14 AB5 LEU B   18  GLY B   29  1                                  12    
HELIX   15 AB6 ILE B   79  GLN B  102  1                                  24    
HELIX   16 AB7 PRO B  106  PHE B  124  1                                  19    
HELIX   17 AB8 ASN B  167  TYR B  179  1                                  13    
HELIX   18 AB9 THR B  185  MET B  201  1                                  17    
HELIX   19 AC1 LYS B  229  LYS B  246  1                                  18    
HELIX   20 AC2 SER C   11  HIS C   15  5                                   5    
HELIX   21 AC3 LEU C   16  LYS C   28  1                                  13    
HELIX   22 AC4 GLU C   56  ARG C   60  5                                   5    
HELIX   23 AC5 LEU C   76  GLU C   99  1                                  24    
HELIX   24 AC6 THR C  103  TYR C  118  1                                  16    
HELIX   25 AC7 GLY C  164  TYR C  176  1                                  13    
HELIX   26 AC8 THR C  183  LEU C  196  1                                  14    
HELIX   27 AC9 ASN C  221  GLU C  233  1                                  13    
HELIX   28 AD1 LEU D   21  LYS D   32  1                                  12    
HELIX   29 AD2 LEU D   81  ASN D  104  1                                  24    
HELIX   30 AD3 THR D  108  LEU D  119  1                                  12    
HELIX   31 AD4 ALA D  173  TYR D  185  1                                  13    
HELIX   32 AD5 THR D  190  MET D  206  1                                  17    
HELIX   33 AD6 THR D  230  LYS D  239  1                                  10    
HELIX   34 AD7 ILE E   19  TYR E   24  1                                   6    
HELIX   35 AD8 MET E   26  GLY E   32  1                                   7    
HELIX   36 AD9 LEU E   77  ASP E  100  1                                  24    
HELIX   37 AE1 PRO E  104  ILE E  118  1                                  15    
HELIX   38 AE2 PRO E  119  GLN E  121  5                                   3    
HELIX   39 AE3 SER E  165  MET E  176  1                                  12    
HELIX   40 AE4 ASN E  183  LEU E  199  1                                  17    
HELIX   41 AE5 VAL E  229  GLU E  234  1                                   6    
HELIX   42 AE6 VAL F   20  GLU F   31  1                                  12    
HELIX   43 AE7 LEU F   80  GLY F  103  1                                  24    
HELIX   44 AE8 PRO F  107  ALA F  121  1                                  15    
HELIX   45 AE9 ALA F  168  LYS F  178  1                                  11    
HELIX   46 AF1 GLN F  180  MET F  184  5                                   5    
HELIX   47 AF2 THR F  185  HIS F  201  1                                  17    
HELIX   48 AF3 LEU F  219  ASN F  221  5                                   3    
HELIX   49 AF4 PRO F  228  LYS F  244  1                                  17    
HELIX   50 AF5 LEU G   22  ALA G   28  1                                   7    
HELIX   51 AF6 PHE G   29  GLN G   34  1                                   6    
HELIX   52 AF7 MET G   83  GLY G  106  1                                  24    
HELIX   53 AF8 VAL G  111  THR G  126  1                                  16    
HELIX   54 AF9 LYS G  171  LYS G  186  1                                  16    
HELIX   55 AG1 PHE G  187  THR G  190  5                                   4    
HELIX   56 AG2 GLN G  193  SER G  207  1                                  15    
HELIX   57 AG3 THR G  231  GLU G  244  1                                  14    
HELIX   58 AG4 THR H   48  GLY H   71  1                                  24    
HELIX   59 AG5 ARG H   75  TYR H   90  1                                  16    
HELIX   60 AG6 GLY H  130  PHE H  142  1                                  13    
HELIX   61 AG7 GLU H  147  ASN H  165  1                                  19    
HELIX   62 AG8 LEU I   55  GLY I   78  1                                  24    
HELIX   63 AG9 LYS I   82  LYS I   97  1                                  16    
HELIX   64 AH1 CYS I  141  TRP I  153  1                                  13    
HELIX   65 AH2 ASP I  158  ASP I  175  1                                  18    
HELIX   66 AH3 GLY J   51  GLY J   72  1                                  22    
HELIX   67 AH4 SER J   76  ASP J   90  1                                  15    
HELIX   68 AH5 LEU J   92  SER J   94  5                                   3    
HELIX   69 AH6 TYR J  134  TYR J  147  1                                  14    
HELIX   70 AH7 SER J  152  ARG J  170  1                                  19    
HELIX   71 AH8 GLY K   48  ASN K   70  1                                  23    
HELIX   72 AH9 SER K   75  GLN K   89  1                                  15    
HELIX   73 AI1 GLY K  131  ARG K  141  1                                  11    
HELIX   74 AI2 GLU K  148  ASP K  167  1                                  20    
HELIX   75 AI3 VAL K  192  SER K  200  1                                   9    
HELIX   76 AI4 PHE L   57  ASN L   80  1                                  24    
HELIX   77 AI5 THR L   84  ARG L   99  1                                  16    
HELIX   78 AI6 ALA L  141  VAL L  153  1                                  13    
HELIX   79 AI7 SER L  167  ASP L  186  1                                  20    
HELIX   80 AI8 ALA N   50  ASN N   71  1                                  22    
HELIX   81 AI9 LEU N   75  TYR N   90  1                                  16    
HELIX   82 AJ1 GLY N  131  TYR N  134  5                                   4    
HELIX   83 AJ2 ILE N  135  TYR N  143  1                                   9    
HELIX   84 AJ3 THR N  148  ASP N  167  1                                  20    
HELIX   85 AJ4 LEU N  190  ILE N  194  5                                   5    
HELIX   86 AJ5 LEU O   18  GLY O   30  1                                  13    
HELIX   87 AJ6 ASP O   57  VAL O   61  5                                   5    
HELIX   88 AJ7 MET O   78  GLN O  101  1                                  24    
HELIX   89 AJ8 PRO O  105  TYR O  120  1                                  16    
HELIX   90 AJ9 ASN O  165  TYR O  177  1                                  13    
HELIX   91 AK1 GLU O  182  LYS O  195  1                                  14    
HELIX   92 AK2 GLU O  196  PHE O  198  5                                   3    
HELIX   93 AK3 THR O  221  ALA O  230  1                                  10    
HELIX   94 AK4 LEU P   18  GLY P   29  1                                  12    
HELIX   95 AK5 ILE P   79  GLN P  102  1                                  24    
HELIX   96 AK6 PRO P  106  PHE P  124  1                                  19    
HELIX   97 AK7 ASN P  167  TYR P  179  1                                  13    
HELIX   98 AK8 THR P  185  MET P  201  1                                  17    
HELIX   99 AK9 LYS P  229  LYS P  246  1                                  18    
HELIX  100 AL1 LEU Q   16  LYS Q   28  1                                  13    
HELIX  101 AL2 LEU Q   76  GLU Q   99  1                                  24    
HELIX  102 AL3 THR Q  103  TYR Q  118  1                                  16    
HELIX  103 AL4 GLY Q  164  TYR Q  176  1                                  13    
HELIX  104 AL5 THR Q  183  LEU Q  196  1                                  14    
HELIX  105 AL6 ASN Q  221  GLU Q  238  1                                  18    
HELIX  106 AL7 LEU R   21  LYS R   32  1                                  12    
HELIX  107 AL8 PRO R   61  ILE R   64  5                                   4    
HELIX  108 AL9 LEU R   81  ASN R  104  1                                  24    
HELIX  109 AM1 THR R  108  ASN R  118  1                                  11    
HELIX  110 AM2 ALA R  173  TYR R  185  1                                  13    
HELIX  111 AM3 THR R  190  MET R  206  1                                  17    
HELIX  112 AM4 THR R  230  LYS R  239  1                                  10    
HELIX  113 AM5 ILE S   19  GLY S   32  1                                  14    
HELIX  114 AM6 LEU S   77  ASP S  100  1                                  24    
HELIX  115 AM7 PRO S  104  ILE S  118  1                                  15    
HELIX  116 AM8 PRO S  119  GLN S  121  5                                   3    
HELIX  117 AM9 SER S  165  MET S  176  1                                  12    
HELIX  118 AN1 ASN S  183  LEU S  199  1                                  17    
HELIX  119 AN2 VAL S  229  GLU S  234  1                                   6    
HELIX  120 AN3 VAL T   20  GLU T   31  1                                  12    
HELIX  121 AN4 LEU T   80  GLY T  103  1                                  24    
HELIX  122 AN5 PRO T  107  ALA T  121  1                                  15    
HELIX  123 AN6 ALA T  168  LYS T  178  1                                  11    
HELIX  124 AN7 GLN T  180  MET T  184  5                                   5    
HELIX  125 AN8 THR T  185  ASP T  188  5                                   4    
HELIX  126 AN9 ILE T  189  HIS T  201  1                                  13    
HELIX  127 AO1 LEU T  219  ASN T  221  5                                   3    
HELIX  128 AO2 PRO T  228  LYS T  244  1                                  17    
HELIX  129 AO3 LEU U   22  ALA U   28  1                                   7    
HELIX  130 AO4 PHE U   29  GLN U   34  1                                   6    
HELIX  131 AO5 MET U   83  GLY U  106  1                                  24    
HELIX  132 AO6 VAL U  111  GLN U  123  1                                  13    
HELIX  133 AO7 VAL U  124  GLN U  127  5                                   4    
HELIX  134 AO8 LYS U  171  LYS U  184  1                                  14    
HELIX  135 AO9 VAL U  195  SER U  207  1                                  13    
HELIX  136 AP1 THR U  231  GLU U  244  1                                  14    
HELIX  137 AP2 THR V   48  GLY V   71  1                                  24    
HELIX  138 AP3 ARG V   75  TYR V   90  1                                  16    
HELIX  139 AP4 GLY V  130  PHE V  142  1                                  13    
HELIX  140 AP5 GLU V  147  ASN V  165  1                                  19    
HELIX  141 AP6 LEU W   55  GLY W   78  1                                  24    
HELIX  142 AP7 LYS W   82  LYS W   97  1                                  16    
HELIX  143 AP8 CYS W  141  TRP W  153  1                                  13    
HELIX  144 AP9 ASP W  158  ASP W  175  1                                  18    
HELIX  145 AQ1 GLY X   51  GLY X   72  1                                  22    
HELIX  146 AQ2 SER X   76  ASP X   90  1                                  15    
HELIX  147 AQ3 LEU X   92  SER X   94  5                                   3    
HELIX  148 AQ4 GLY X  135  TYR X  147  1                                  13    
HELIX  149 AQ5 SER X  152  ARG X  170  1                                  19    
HELIX  150 AQ6 GLY Y   48  LYS Y   71  1                                  24    
HELIX  151 AQ7 SER Y   75  GLN Y   89  1                                  15    
HELIX  152 AQ8 GLY Y  131  ARG Y  141  1                                  11    
HELIX  153 AQ9 GLU Y  148  ASP Y  167  1                                  20    
HELIX  154 AR1 VAL Y  192  TYR Y  199  1                                   8    
HELIX  155 AR2 PHE Z   57  ASN Z   80  1                                  24    
HELIX  156 AR3 THR Z   84  ARG Z   99  1                                  16    
HELIX  157 AR4 ALA Z  141  VAL Z  153  1                                  13    
HELIX  158 AR5 SER Z  167  ASP Z  186  1                                  20    
HELIX  159 AR6 TYR a   57  LEU a   76  1                                  20    
HELIX  160 AR7 SER a   84  LYS a  102  1                                  19    
HELIX  161 AR8 TYR a  141  ALA a  146  1                                   6    
HELIX  162 AR9 ALA a  146  GLN a  157  1                                  12    
HELIX  163 AS1 SER a  161  ASP a  180  1                                  20    
HELIX  164 AS2 TRP a  209  MET a  214  5                                   6    
HELIX  165 AS3 ALA b   50  ASN b   71  1                                  22    
HELIX  166 AS4 LEU b   75  TYR b   90  1                                  16    
HELIX  167 AS5 GLY b  131  TYR b  134  5                                   4    
HELIX  168 AS6 ILE b  135  TYR b  143  1                                   9    
HELIX  169 AS7 THR b  148  ASP b  167  1                                  20    
HELIX  170 AS8 LEU b  190  ILE b  194  5                                   5    
SHEET    1 AA1 5 LEU M  33  PHE M  36  0                                        
SHEET    2 AA1 5 GLY M  28  TYR M  30 -1  N  GLY M  28   O  PHE M  36           
SHEET    3 AA1 5 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4 AA1 5 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5 AA1 5 ILE M  42  ASN M  46 -1  N  MET M  43   O  LEU M  51           
SHEET    1 AA2 7 LEU M  33  PHE M  36  0                                        
SHEET    2 AA2 7 GLY M  28  TYR M  30 -1  N  GLY M  28   O  PHE M  36           
SHEET    3 AA2 7 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4 AA2 7 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5 AA2 7 ASN M 108  ALA M 116 -1  O  GLY M 113   N  MET M  50           
SHEET    6 AA2 7 GLU M 119  ASP M 126 -1  O  VAL M 125   N  MET M 110           
SHEET    7 AA2 7 ALA M 131  GLU M 133 -1  O  TYR M 132   N  TYR M 124           
SHEET    1 AA3 5 SER M 136  ALA M 138  0                                        
SHEET    2 AA3 5 VAL M  11  PHE M  16 -1  N  GLY M  13   O  LEU M 137           
SHEET    3 AA3 5 GLY M  19  ASP M  25 -1  O  GLY M  19   N  PHE M  16           
SHEET    4 AA3 5 PHE M 187  VAL M 192 -1  O  GLN M 188   N  ALA M  24           
SHEET    5 AA3 5 VAL M 197  LEU M 203 -1  O  GLU M 200   N  ILE M 189           
SHEET    1 AA4 5 ALA A 159  MET A 162  0                                        
SHEET    2 AA4 5 SER A  34  LYS A  38 -1  N  SER A  34   O  MET A 162           
SHEET    3 AA4 5 VAL A  43  GLU A  48 -1  O  ALA A  46   N  VAL A  35           
SHEET    4 AA4 5 ILE A 207  CYS A 212 -1  O  GLY A 210   N  LEU A  45           
SHEET    5 AA4 5 PHE A 217  ARG A 219 -1  O  ARG A 218   N  ILE A 211           
SHEET    1 AA5 5 GLU A  65  PRO A  66  0                                        
SHEET    2 AA5 5 ILE A  71  GLY A  77 -1  O  LEU A  73   N  GLU A  65           
SHEET    3 AA5 5 VAL A 131  ASN A 139 -1  O  CYS A 136   N  GLY A  72           
SHEET    4 AA5 5 ARG A 142  SER A 148 -1  O  TYR A 144   N  GLY A 137           
SHEET    5 AA5 5 TYR A 154  ALA A 156 -1  O  PHE A 155   N  GLN A 147           
SHEET    1 AA6 5 ALA B 161  ILE B 164  0                                        
SHEET    2 AA6 5 CYS B  34  ILE B  37 -1  N  CYS B  34   O  ILE B 164           
SHEET    3 AA6 5 VAL B  43  ALA B  47 -1  O  ALA B  46   N  LEU B  35           
SHEET    4 AA6 5 GLU B 212  GLU B 219 -1  O  LEU B 216   N  VAL B  43           
SHEET    5 AA6 5 LYS B 222  VAL B 227 -1  O  LYS B 222   N  GLU B 219           
SHEET    1 AA7 6 TYR B  66  LYS B  67  0                                        
SHEET    2 AA7 6 MET B  72  GLY B  78 -1  O  CYS B  74   N  TYR B  66           
SHEET    3 AA7 6 VAL B 132  GLY B 138 -1  O  SER B 133   N  ALA B  77           
SHEET    4 AA7 6 GLN B 146  SER B 150 -1  O  SER B 150   N  LEU B 134           
SHEET    5 AA7 6 TYR B 156  TRP B 159 -1  O  TRP B 159   N  LEU B 147           
SHEET    6 AA7 6 GLN C  54  ASP C  55 -1  O  ASP C  55   N  GLY B 158           
SHEET    1 AA8 4 ALA C 158  ILE C 161  0                                        
SHEET    2 AA8 4 ALA C  32  ARG C  36 -1  N  ALA C  32   O  ILE C 161           
SHEET    3 AA8 4 ILE C  40  GLU C  46 -1  O  GLY C  44   N  VAL C  33           
SHEET    4 AA8 4 ILE C 206  GLU C 207 -1  O  GLU C 207   N  VAL C  45           
SHEET    1 AA9 5 ALA C 158  ILE C 161  0                                        
SHEET    2 AA9 5 ALA C  32  ARG C  36 -1  N  ALA C  32   O  ILE C 161           
SHEET    3 AA9 5 ILE C  40  GLU C  46 -1  O  GLY C  44   N  VAL C  33           
SHEET    4 AA9 5 ALA C 209  ARG C 212 -1  O  MET C 211   N  VAL C  41           
SHEET    5 AA9 5 LYS C 218  ILE C 219 -1  O  LYS C 218   N  VAL C 210           
SHEET    1 AB1 4 VAL C  69  GLY C  75  0                                        
SHEET    2 AB1 4 ILE C 129  PHE C 136 -1  O  LEU C 132   N  ALA C  72           
SHEET    3 AB1 4 PRO C 142  THR C 147 -1  O  THR C 147   N  ALA C 131           
SHEET    4 AB1 4 HIS C 154  ALA C 155 -1  O  HIS C 154   N  GLN C 146           
SHEET    1 AB2 5 ALA D 167  ILE D 170  0                                        
SHEET    2 AB2 5 ALA D  37  THR D  42 -1  N  ALA D  37   O  ILE D 170           
SHEET    3 AB2 5 GLY D  45  GLU D  51 -1  O  ALA D  49   N  ILE D  38           
SHEET    4 AB2 5 ILE D 215  VAL D 220 -1  O  ALA D 218   N  LEU D  48           
SHEET    5 AB2 5 HIS D 227  MET D 228 -1  O  HIS D 227   N  THR D 219           
SHEET    1 AB3 5 ILE D  67  GLU D  69  0                                        
SHEET    2 AB3 5 ILE D  74  GLY D  80 -1  O  CYS D  76   N  VAL D  68           
SHEET    3 AB3 5 VAL D 139  ASP D 147 -1  O  GLY D 144   N  GLY D  75           
SHEET    4 AB3 5 GLY D 150  MET D 156 -1  O  GLN D 152   N  GLY D 145           
SHEET    5 AB3 5 VAL D 163  CYS D 165 -1  O  CYS D 165   N  LEU D 153           
SHEET    1 AB4 5 ALA E 158  ILE E 161  0                                        
SHEET    2 AB4 5 THR E  35  LYS E  39 -1  N  GLY E  37   O  MET E 159           
SHEET    3 AB4 5 HIS E  43  LEU E  49 -1  O  VAL E  47   N  VAL E  36           
SHEET    4 AB4 5 VAL E 210  GLY E 216 -1  O  SER E 211   N  ALA E  48           
SHEET    5 AB4 5 THR E 222  TYR E 224 -1  O  TYR E 224   N  ILE E 212           
SHEET    1 AB5 5 ILE E  63  HIS E  65  0                                        
SHEET    2 AB5 5 ILE E  70  GLY E  76 -1  O  ILE E  72   N  LEU E  64           
SHEET    3 AB5 5 VAL E 130  ASP E 138 -1  O  ALA E 135   N  GLY E  71           
SHEET    4 AB5 5 GLY E 141  GLN E 146 -1  O  HIS E 143   N  GLY E 136           
SHEET    5 AB5 5 PHE E 154  CYS E 156 -1  O  PHE E 154   N  GLN E 146           
SHEET    1 AB6 5 GLY F 162  ILE F 165  0                                        
SHEET    2 AB6 5 ALA F  36  ARG F  40 -1  N  GLY F  38   O  CYS F 163           
SHEET    3 AB6 5 GLY F  44  LEU F  52 -1  O  GLY F  48   N  ILE F  37           
SHEET    4 AB6 5 PHE F 209  GLY F 217 -1  O  GLU F 210   N  LYS F  51           
SHEET    5 AB6 5 GLU F 225  ILE F 226 -1  O  GLU F 225   N  TRP F 215           
SHEET    1 AB7 5 LEU F  66  ASN F  68  0                                        
SHEET    2 AB7 5 VAL F  73  GLY F  79 -1  O  MET F  75   N  PHE F  67           
SHEET    3 AB7 5 CYS F 133  SER F 141 -1  O  MET F 136   N  ALA F  76           
SHEET    4 AB7 5 GLY F 145  ILE F 151 -1  O  ILE F 151   N  PHE F 135           
SHEET    5 AB7 5 SER F 157  GLY F 159 -1  O  TYR F 158   N  MET F 150           
SHEET    1 AB8 5 ALA G 165  GLY G 169  0                                        
SHEET    2 AB8 5 THR G  38  VAL G  42 -1  N  ALA G  41   O  THR G 166           
SHEET    3 AB8 5 VAL G  49  GLN G  53 -1  O  VAL G  51   N  VAL G  40           
SHEET    4 AB8 5 ILE G 215  VAL G 219 -1  O  GLY G 218   N  ILE G  50           
SHEET    5 AB8 5 ARG G 228  ILE G 229 -1  O  ARG G 228   N  VAL G 219           
SHEET    1 AB9 4 LEU G  69  LYS G  71  0                                        
SHEET    2 AB9 4 ILE G  76  VAL G  79 -1  O  CYS G  78   N  PHE G  70           
SHEET    3 AB9 4 ILE G 139  ASP G 144 -1  O  ILE G 139   N  VAL G  79           
SHEET    4 AB9 4 GLY G 148  LYS G 153 -1  O  TYR G 152   N  LEU G 140           
SHEET    1 AC1 5 TYR H 124  GLY H 128  0                                        
SHEET    2 AC1 5 THR H   2  TYR H   8 -1  N  ILE H   3   O  MET H 127           
SHEET    3 AC1 5 GLY H  11  ALA H  16 -1  O  GLY H  11   N  TYR H   8           
SHEET    4 AC1 5 ASP H 174  SER H 179 -1  O  ILE H 178   N  ILE H  12           
SHEET    5 AC1 5 LEU H 183  ASP H 184 -1  O  ASP H 184   N  VAL H 177           
SHEET    1 AC2 2 ALA H  20  GLU H  22  0                                        
SHEET    2 AC2 2 VAL H  25  ASP H  28 -1  O  ALA H  27   N  ALA H  20           
SHEET    1 AC3 5 ILE H  34  PHE H  36  0                                        
SHEET    2 AC3 5 ILE H  41  GLY H  47 -1  O  CYS H  43   N  HIS H  35           
SHEET    3 AC3 5 ALA H  96  ASP H 104 -1  O  GLY H 101   N  TYR H  42           
SHEET    4 AC3 5 GLY H 107  ILE H 113 -1  O  ILE H 113   N  LEU H  98           
SHEET    5 AC3 5 THR H 119  LYS H 121 -1  O  ASP H 120   N  SER H 112           
SHEET    1 AC4 6 VAL H 211  PRO H 218  0                                        
SHEET    2 AC4 6 LYS I 193  LEU I 199 -1  O  THR I 198   N  LEU H 212           
SHEET    3 AC4 6 VAL I 184  ILE I 189 -1  N  VAL I 186   O  ARG I 197           
SHEET    4 AC4 6 VAL I  19  ASP I  24 -1  N  VAL I  19   O  ILE I 189           
SHEET    5 AC4 6 ALA I   9  LYS I  14 -1  N  MET I  11   O  ALA I  22           
SHEET    6 AC4 6 PHE I 135  GLY I 139 -1  O  SER I 138   N  VAL I  10           
SHEET    1 AC5 2 PHE I  27  ILE I  29  0                                        
SHEET    2 AC5 2 GLN I  32  THR I  35 -1  O  GLN I  32   N  ILE I  29           
SHEET    1 AC6 5 ILE I  41  PRO I  43  0                                        
SHEET    2 AC6 5 LEU I  48  GLY I  54 -1  O  ILE I  50   N  PHE I  42           
SHEET    3 AC6 5 THR I 104  LEU I 111 -1  O  VAL I 107   N  GLY I  51           
SHEET    4 AC6 5 PRO I 118  LEU I 123 -1  O  CYS I 121   N  ILE I 108           
SHEET    5 AC6 5 PRO I 129  VAL I 131 -1  O  MET I 130   N  SER I 122           
SHEET    1 AC7 5 PHE J 129  HIS J 132  0                                        
SHEET    2 AC7 5 LEU J   4  GLN J   8 -1  N  GLY J   6   O  ALA J 130           
SHEET    3 AC7 5 VAL J  13  ASP J  18 -1  O  LEU J  14   N  ILE J   7           
SHEET    4 AC7 5 THR J 177  ASP J 184 -1  O  ARG J 181   N  VAL J  15           
SHEET    5 AC7 5 GLY J 187  ASP J 190 -1  O  GLY J 187   N  ASP J 184           
SHEET    1 AC8 5 PHE J 129  HIS J 132  0                                        
SHEET    2 AC8 5 LEU J   4  GLN J   8 -1  N  GLY J   6   O  ALA J 130           
SHEET    3 AC8 5 VAL J  13  ASP J  18 -1  O  LEU J  14   N  ILE J   7           
SHEET    4 AC8 5 THR J 177  ASP J 184 -1  O  ARG J 181   N  VAL J  15           
SHEET    5 AC8 5 ILE J 194  SER J 195 -1  O  ILE J 194   N  PHE J 178           
SHEET    1 AC9 2 ALA J  21  SER J  23  0                                        
SHEET    2 AC9 2 VAL J  26  LYS J  29 -1  O  VAL J  26   N  SER J  23           
SHEET    1 AD1 5 MET J  35  SER J  39  0                                        
SHEET    2 AD1 5 ILE J  42  GLY J  48 -1  O  LEU J  44   N  PHE J  36           
SHEET    3 AD1 5 VAL J 100  ASP J 108 -1  O  ASN J 101   N  VAL J  47           
SHEET    4 AD1 5 GLY J 112  MET J 118 -1  O  ALA J 114   N  GLY J 106           
SHEET    5 AD1 5 LEU J 124  LYS J 126 -1  O  ALA J 125   N  TYR J 117           
SHEET    1 AD2 5 THR K 125  GLY K 129  0                                        
SHEET    2 AD2 5 THR K   2  PHE K   8 -1  N  THR K   3   O  VAL K 128           
SHEET    3 AD2 5 GLY K  11  ALA K  16 -1  O  GLY K  11   N  PHE K   8           
SHEET    4 AD2 5 ALA K 173  ARG K 180 -1  O  TYR K 177   N  VAL K  14           
SHEET    5 AD2 5 GLY K 183  ASN K 191 -1  O  ASP K 190   N  VAL K 174           
SHEET    1 AD3 2 ALA K  20  ALA K  22  0                                        
SHEET    2 AD3 2 TYR K  25  SER K  28 -1  O  TYR K  25   N  ALA K  22           
SHEET    1 AD4 5 VAL K  34  ASN K  38  0                                        
SHEET    2 AD4 5 LEU K  41  THR K  44 -1  O  GLY K  43   N  ILE K  35           
SHEET    3 AD4 5 GLY K  98  ASP K 105 -1  O  CYS K 102   N  LEU K  42           
SHEET    4 AD4 5 GLY K 108  ASP K 115 -1  O  VAL K 114   N  THR K  99           
SHEET    5 AD4 5 ARG K 120  SER K 122 -1  O  ILE K 121   N  TYR K 113           
SHEET    1 AD5 5 PHE L 135  GLY L 139  0                                        
SHEET    2 AD5 5 THR L  11  ALA L  16 -1  N  ALA L  14   O  LYS L 136           
SHEET    3 AD5 5 ALA L  21  SER L  25 -1  O  ALA L  24   N  LEU L  13           
SHEET    4 AD5 5 ARG L 194  VAL L 198 -1  O  CYS L 196   N  VAL L  23           
SHEET    5 AD5 5 ILE L 203  THR L 207 -1  O  ARG L 204   N  ILE L 197           
SHEET    1 AD6 2 LEU L  29  GLU L  31  0                                        
SHEET    2 AD6 2 SER L  34  THR L  37 -1  O  HIS L  36   N  LEU L  29           
SHEET    1 AD7 5 CYS L  43  THR L  47  0                                        
SHEET    2 AD7 5 THR L  50  GLY L  56 -1  O  ILE L  52   N  TYR L  44           
SHEET    3 AD7 5 VAL L 106  LEU L 113 -1  O  GLY L 111   N  VAL L  51           
SHEET    4 AD7 5 GLY L 119  PHE L 124 -1  O  TYR L 122   N  ILE L 110           
SHEET    5 AD7 5 TYR L 130  ASP L 133 -1  O  ASP L 133   N  VAL L 121           
SHEET    1 AD8 5 PHE N 125  GLY N 129  0                                        
SHEET    2 AD8 5 THR N   2  PHE N   8 -1  N  ALA N   5   O  ALA N 126           
SHEET    3 AD8 5 GLY N  11  ALA N  16 -1  O  VAL N  13   N  VAL N   6           
SHEET    4 AD8 5 ILE N 174  ALA N 180 -1  O  ALA N 177   N  LEU N  14           
SHEET    5 AD8 5 GLY N 183  LEU N 189 -1  O  LEU N 189   N  ILE N 174           
SHEET    1 AD9 2 THR N  20  THR N  22  0                                        
SHEET    2 AD9 2 TYR N  25  ASN N  28 -1  O  ASN N  28   N  THR N  20           
SHEET    1 AE1 5 LEU N  34  PRO N  36  0                                        
SHEET    2 AE1 5 ILE N  41  GLY N  47 -1  O  CYS N  43   N  THR N  35           
SHEET    3 AE1 5 ALA N  96  ASP N 104 -1  O  ALA N 101   N  PHE N  42           
SHEET    4 AE1 5 GLY N 108  VAL N 114 -1  O  TYR N 112   N  ILE N 100           
SHEET    5 AE1 5 VAL N 121  ARG N 122 -1  O  VAL N 121   N  SER N 113           
SHEET    1 AE2 5 ALA O 159  MET O 162  0                                        
SHEET    2 AE2 5 SER O  34  LYS O  38 -1  N  SER O  34   O  MET O 162           
SHEET    3 AE2 5 VAL O  43  GLU O  48 -1  O  ALA O  46   N  VAL O  35           
SHEET    4 AE2 5 ILE O 207  CYS O 212 -1  O  GLY O 210   N  LEU O  45           
SHEET    5 AE2 5 PHE O 217  ARG O 219 -1  O  ARG O 218   N  ILE O 211           
SHEET    1 AE3 5 GLU O  65  PRO O  66  0                                        
SHEET    2 AE3 5 ILE O  71  GLY O  77 -1  O  LEU O  73   N  GLU O  65           
SHEET    3 AE3 5 VAL O 131  ASN O 139 -1  O  LEU O 134   N  VAL O  74           
SHEET    4 AE3 5 ARG O 142  SER O 148 -1  O  TYR O 144   N  GLY O 137           
SHEET    5 AE3 5 TYR O 154  ALA O 156 -1  O  PHE O 155   N  GLN O 147           
SHEET    1 AE4 5 ALA P 161  ILE P 164  0                                        
SHEET    2 AE4 5 CYS P  34  LEU P  38 -1  N  CYS P  34   O  ILE P 164           
SHEET    3 AE4 5 VAL P  43  ALA P  47 -1  O  ALA P  46   N  LEU P  35           
SHEET    4 AE4 5 ILE P 213  GLU P 219 -1  O  LEU P 216   N  VAL P  43           
SHEET    5 AE4 5 LYS P 222  VAL P 227 -1  O  VAL P 224   N  THR P 217           
SHEET    1 AE5 6 TYR P  66  LYS P  67  0                                        
SHEET    2 AE5 6 MET P  72  GLY P  78 -1  O  CYS P  74   N  TYR P  66           
SHEET    3 AE5 6 VAL P 132  GLY P 138 -1  O  SER P 133   N  ALA P  77           
SHEET    4 AE5 6 GLN P 146  SER P 150 -1  O  GLN P 146   N  GLY P 138           
SHEET    5 AE5 6 TYR P 156  TRP P 159 -1  O  TRP P 159   N  LEU P 147           
SHEET    6 AE5 6 GLN Q  54  ASP Q  55 -1  O  ASP Q  55   N  GLY P 158           
SHEET    1 AE6 5 ALA Q 158  ILE Q 161  0                                        
SHEET    2 AE6 5 ALA Q  32  ARG Q  36 -1  N  ALA Q  32   O  ILE Q 161           
SHEET    3 AE6 5 ILE Q  40  GLU Q  46 -1  O  GLY Q  44   N  VAL Q  33           
SHEET    4 AE6 5 ILE Q 206  ARG Q 212 -1  O  GLU Q 207   N  VAL Q  45           
SHEET    5 AE6 5 LYS Q 218  ILE Q 219 -1  O  LYS Q 218   N  VAL Q 210           
SHEET    1 AE7 5 VAL Q  69  GLY Q  75  0                                        
SHEET    2 AE7 5 ILE Q 129  PHE Q 136 -1  O  LEU Q 132   N  ALA Q  72           
SHEET    3 AE7 5 PRO Q 142  THR Q 147 -1  O  THR Q 147   N  ALA Q 131           
SHEET    4 AE7 5 TYR Q 153  TRP Q 156 -1  O  HIS Q 154   N  GLN Q 146           
SHEET    5 AE7 5 MET R  59  GLU R  60 -1  O  GLU R  60   N  ALA Q 155           
SHEET    1 AE8 5 ALA R 167  ILE R 170  0                                        
SHEET    2 AE8 5 ALA R  37  THR R  42 -1  N  GLY R  39   O  ARG R 168           
SHEET    3 AE8 5 GLY R  45  GLU R  51 -1  O  ALA R  49   N  ILE R  38           
SHEET    4 AE8 5 ILE R 215  VAL R 220 -1  O  GLU R 216   N  VAL R  50           
SHEET    5 AE8 5 HIS R 227  MET R 228 -1  O  HIS R 227   N  THR R 219           
SHEET    1 AE9 5 ILE R  67  ASP R  71  0                                        
SHEET    2 AE9 5 ILE R  74  GLY R  80 -1  O  ILE R  74   N  ILE R  70           
SHEET    3 AE9 5 VAL R 139  ASP R 147 -1  O  GLY R 144   N  GLY R  75           
SHEET    4 AE9 5 GLY R 150  MET R 156 -1  O  PHE R 154   N  PHE R 143           
SHEET    5 AE9 5 VAL R 163  CYS R 165 -1  O  CYS R 165   N  LEU R 153           
SHEET    1 AF1 5 ALA S 158  ILE S 161  0                                        
SHEET    2 AF1 5 THR S  35  LYS S  39 -1  N  GLY S  37   O  MET S 159           
SHEET    3 AF1 5 ALA S  44  LEU S  49 -1  O  VAL S  47   N  VAL S  36           
SHEET    4 AF1 5 VAL S 210  VAL S 215 -1  O  SER S 211   N  ALA S  48           
SHEET    5 AF1 5 THR S 222  TYR S 224 -1  O  TYR S 224   N  ILE S 212           
SHEET    1 AF2 5 ILE S  63  HIS S  65  0                                        
SHEET    2 AF2 5 ILE S  70  GLY S  76 -1  O  ILE S  72   N  LEU S  64           
SHEET    3 AF2 5 VAL S 130  ASP S 138 -1  O  ALA S 135   N  GLY S  71           
SHEET    4 AF2 5 GLY S 141  THR S 147 -1  O  HIS S 143   N  GLY S 136           
SHEET    5 AF2 5 PHE S 154  CYS S 156 -1  O  PHE S 154   N  GLN S 146           
SHEET    1 AF3 5 GLY T 162  ILE T 165  0                                        
SHEET    2 AF3 5 ALA T  36  ARG T  40 -1  N  GLY T  38   O  CYS T 163           
SHEET    3 AF3 5 GLY T  44  LEU T  52 -1  O  GLY T  48   N  ILE T  37           
SHEET    4 AF3 5 PHE T 209  GLY T 217 -1  O  GLU T 210   N  LYS T  51           
SHEET    5 AF3 5 GLU T 225  ILE T 226 -1  O  GLU T 225   N  TRP T 215           
SHEET    1 AF4 5 LEU T  66  ASP T  70  0                                        
SHEET    2 AF4 5 VAL T  73  GLY T  79 -1  O  MET T  75   N  PHE T  67           
SHEET    3 AF4 5 CYS T 133  SER T 141 -1  O  MET T 136   N  ALA T  76           
SHEET    4 AF4 5 GLY T 145  ILE T 151 -1  O  ILE T 151   N  PHE T 135           
SHEET    5 AF4 5 SER T 157  GLY T 159 -1  O  TYR T 158   N  MET T 150           
SHEET    1 AF5 5 ALA U 165  GLY U 169  0                                        
SHEET    2 AF5 5 THR U  38  VAL U  42 -1  N  ALA U  41   O  THR U 166           
SHEET    3 AF5 5 VAL U  49  GLN U  53 -1  O  VAL U  49   N  VAL U  42           
SHEET    4 AF5 5 ILE U 215  VAL U 219 -1  O  GLY U 218   N  ILE U  50           
SHEET    5 AF5 5 ARG U 228  ILE U 229 -1  O  ARG U 228   N  VAL U 219           
SHEET    1 AF6 4 LEU U  69  LYS U  71  0                                        
SHEET    2 AF6 4 ILE U  76  VAL U  79 -1  O  CYS U  78   N  PHE U  70           
SHEET    3 AF6 4 ILE U 139  ASP U 144 -1  O  ILE U 139   N  VAL U  79           
SHEET    4 AF6 4 GLY U 148  LYS U 153 -1  O  GLY U 148   N  ASP U 144           
SHEET    1 AF7 5 TYR V 124  GLY V 128  0                                        
SHEET    2 AF7 5 THR V   2  TYR V   8 -1  N  ILE V   3   O  MET V 127           
SHEET    3 AF7 5 GLY V  11  ALA V  16 -1  O  GLY V  11   N  TYR V   8           
SHEET    4 AF7 5 ASP V 174  SER V 179 -1  O  ILE V 178   N  ILE V  12           
SHEET    5 AF7 5 LYS V 182  ASP V 184 -1  O  ASP V 184   N  VAL V 177           
SHEET    1 AF8 2 ALA V  20  GLU V  22  0                                        
SHEET    2 AF8 2 VAL V  25  ASP V  28 -1  O  ALA V  27   N  ALA V  20           
SHEET    1 AF9 5 ILE V  34  PHE V  36  0                                        
SHEET    2 AF9 5 TYR V  42  GLY V  47 -1  O  CYS V  43   N  HIS V  35           
SHEET    3 AF9 5 ALA V  96  ASP V 104 -1  O  GLY V 101   N  TYR V  42           
SHEET    4 AF9 5 GLY V 107  ILE V 113 -1  O  ILE V 113   N  LEU V  98           
SHEET    5 AF9 5 THR V 119  LYS V 121 -1  O  ASP V 120   N  SER V 112           
SHEET    1 AG1 6 VAL V 211  PRO V 218  0                                        
SHEET    2 AG1 6 LYS W 193  LEU W 199 -1  O  THR W 198   N  LEU V 212           
SHEET    3 AG1 6 VAL W 184  ILE W 189 -1  N  VAL W 186   O  ARG W 197           
SHEET    4 AG1 6 VAL W  19  ASP W  24 -1  N  ILE W  21   O  HIS W 187           
SHEET    5 AG1 6 ALA W   9  LYS W  14 -1  N  ALA W   9   O  ASP W  24           
SHEET    6 AG1 6 PHE W 135  GLY W 139 -1  O  SER W 138   N  VAL W  10           
SHEET    1 AG2 2 PHE W  27  ILE W  29  0                                        
SHEET    2 AG2 2 GLN W  32  THR W  35 -1  O  GLN W  32   N  ILE W  29           
SHEET    1 AG3 5 ILE W  41  PRO W  43  0                                        
SHEET    2 AG3 5 LEU W  48  GLY W  54 -1  O  ILE W  50   N  PHE W  42           
SHEET    3 AG3 5 THR W 104  LEU W 111 -1  O  VAL W 107   N  GLY W  51           
SHEET    4 AG3 5 PRO W 118  SER W 122 -1  O  CYS W 121   N  ILE W 108           
SHEET    5 AG3 5 MET W 130  VAL W 131 -1  O  MET W 130   N  SER W 122           
SHEET    1 AG4 5 PHE X 129  HIS X 132  0                                        
SHEET    2 AG4 5 LEU X   4  GLN X   8 -1  N  GLY X   6   O  ALA X 130           
SHEET    3 AG4 5 VAL X  13  ASP X  18 -1  O  LEU X  14   N  ILE X   7           
SHEET    4 AG4 5 THR X 177  ASP X 184 -1  O  ARG X 181   N  VAL X  15           
SHEET    5 AG4 5 GLY X 187  ASP X 190 -1  O  HIS X 189   N  ILE X 182           
SHEET    1 AG5 5 PHE X 129  HIS X 132  0                                        
SHEET    2 AG5 5 LEU X   4  GLN X   8 -1  N  GLY X   6   O  ALA X 130           
SHEET    3 AG5 5 VAL X  13  ASP X  18 -1  O  LEU X  14   N  ILE X   7           
SHEET    4 AG5 5 THR X 177  ASP X 184 -1  O  ARG X 181   N  VAL X  15           
SHEET    5 AG5 5 ILE X 194  SER X 195 -1  O  ILE X 194   N  PHE X 178           
SHEET    1 AG6 2 ALA X  21  SER X  23  0                                        
SHEET    2 AG6 2 VAL X  26  LYS X  29 -1  O  VAL X  26   N  SER X  23           
SHEET    1 AG7 5 MET X  35  SER X  39  0                                        
SHEET    2 AG7 5 ILE X  42  GLY X  48 -1  O  ILE X  42   N  MET X  38           
SHEET    3 AG7 5 VAL X 100  ASP X 108 -1  O  ASN X 101   N  VAL X  47           
SHEET    4 AG7 5 GLY X 112  MET X 118 -1  O  ALA X 114   N  GLY X 106           
SHEET    5 AG7 5 LEU X 124  LYS X 126 -1  O  ALA X 125   N  TYR X 117           
SHEET    1 AG8 5 THR Y 125  GLY Y 129  0                                        
SHEET    2 AG8 5 THR Y   2  PHE Y   8 -1  N  THR Y   3   O  VAL Y 128           
SHEET    3 AG8 5 GLY Y  11  ALA Y  16 -1  O  ALA Y  15   N  LEU Y   4           
SHEET    4 AG8 5 ALA Y 173  ARG Y 180 -1  O  TYR Y 177   N  VAL Y  14           
SHEET    5 AG8 5 GLY Y 183  ASN Y 191 -1  O  ASP Y 190   N  VAL Y 174           
SHEET    1 AG9 2 ALA Y  20  ALA Y  22  0                                        
SHEET    2 AG9 2 TYR Y  25  SER Y  28 -1  O  TYR Y  25   N  ALA Y  22           
SHEET    1 AH1 5 VAL Y  34  ASN Y  38  0                                        
SHEET    2 AH1 5 LEU Y  41  THR Y  44 -1  O  GLY Y  43   N  ILE Y  35           
SHEET    3 AH1 5 GLY Y  98  ASP Y 105 -1  O  CYS Y 102   N  LEU Y  42           
SHEET    4 AH1 5 GLY Y 108  ASP Y 115 -1  O  TYR Y 112   N  ILE Y 101           
SHEET    5 AH1 5 ARG Y 120  SER Y 122 -1  O  ILE Y 121   N  TYR Y 113           
SHEET    1 AH2 5 PHE Z 135  GLY Z 139  0                                        
SHEET    2 AH2 5 THR Z  11  ALA Z  16 -1  N  ALA Z  14   O  LYS Z 136           
SHEET    3 AH2 5 ALA Z  21  SER Z  25 -1  O  ALA Z  24   N  LEU Z  13           
SHEET    4 AH2 5 ARG Z 194  VAL Z 198 -1  O  CYS Z 196   N  VAL Z  23           
SHEET    5 AH2 5 ILE Z 203  THR Z 207 -1  O  GLU Z 206   N  ILE Z 195           
SHEET    1 AH3 2 LEU Z  29  GLU Z  31  0                                        
SHEET    2 AH3 2 SER Z  34  THR Z  37 -1  O  HIS Z  36   N  LEU Z  29           
SHEET    1 AH4 5 CYS Z  43  THR Z  47  0                                        
SHEET    2 AH4 5 THR Z  50  GLY Z  53 -1  O  ILE Z  52   N  TYR Z  44           
SHEET    3 AH4 5 ILE Z 109  LEU Z 113 -1  O  GLY Z 111   N  VAL Z  51           
SHEET    4 AH4 5 GLY Z 119  PHE Z 124 -1  O  TYR Z 122   N  ILE Z 110           
SHEET    5 AH4 5 TYR Z 130  ASP Z 133 -1  O  ASP Z 133   N  VAL Z 121           
SHEET    1 AH5 5 LEU a  33  PHE a  36  0                                        
SHEET    2 AH5 5 GLY a  28  TYR a  30 -1  N  GLY a  28   O  PHE a  36           
SHEET    3 AH5 5 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4 AH5 5 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5 AH5 5 ILE a  42  ASN a  46 -1  N  MET a  43   O  LEU a  51           
SHEET    1 AH6 7 LEU a  33  PHE a  36  0                                        
SHEET    2 AH6 7 GLY a  28  TYR a  30 -1  N  GLY a  28   O  PHE a  36           
SHEET    3 AH6 7 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4 AH6 7 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5 AH6 7 ASN a 108  ALA a 116 -1  O  GLY a 113   N  MET a  50           
SHEET    6 AH6 7 GLU a 119  ASP a 126 -1  O  VAL a 125   N  MET a 110           
SHEET    7 AH6 7 ALA a 131  GLU a 133 -1  O  TYR a 132   N  TYR a 124           
SHEET    1 AH7 5 SER a 136  ALA a 138  0                                        
SHEET    2 AH7 5 VAL a  11  PHE a  16 -1  N  GLY a  13   O  LEU a 137           
SHEET    3 AH7 5 GLY a  19  ASP a  25 -1  O  GLY a  19   N  PHE a  16           
SHEET    4 AH7 5 PHE a 187  THR a 193 -1  O  GLN a 188   N  ALA a  24           
SHEET    5 AH7 5 GLY a 196  LEU a 203 -1  O  GLU a 200   N  ILE a 189           
SHEET    1 AH8 5 PHE b 125  GLY b 129  0                                        
SHEET    2 AH8 5 THR b   2  PHE b   8 -1  N  ALA b   5   O  ALA b 126           
SHEET    3 AH8 5 GLY b  11  ALA b  16 -1  O  VAL b  13   N  VAL b   6           
SHEET    4 AH8 5 ILE b 174  ALA b 180 -1  O  ALA b 177   N  LEU b  14           
SHEET    5 AH8 5 GLY b 183  LEU b 189 -1  O  LEU b 189   N  ILE b 174           
SHEET    1 AH9 2 THR b  20  THR b  22  0                                        
SHEET    2 AH9 2 TYR b  25  ASN b  28 -1  O  ASN b  28   N  THR b  20           
SHEET    1 AI1 5 LEU b  34  PRO b  36  0                                        
SHEET    2 AI1 5 ILE b  41  GLY b  47 -1  O  CYS b  43   N  THR b  35           
SHEET    3 AI1 5 ALA b  96  ASP b 104 -1  O  ALA b 101   N  PHE b  42           
SHEET    4 AI1 5 GLY b 108  VAL b 114 -1  O  TYR b 112   N  ILE b 100           
SHEET    5 AI1 5 VAL b 121  ARG b 122 -1  O  VAL b 121   N  SER b 113           
CISPEP   1 GLY M  201    PRO M  202          0         2.07                     
CISPEP   2 ARG H  187    PRO H  188          0        -6.92                     
CISPEP   3 ARG H  187    PRO H  188          0        -7.07                     
CISPEP   4 GLU S  234    GLY S  235          0         0.61                     
CISPEP   5 GLY S  235    LEU S  236          0        -8.49                     
CISPEP   6 ARG V  187    PRO V  188          0        -9.58                     
CISPEP   7 GLY a  201    PRO a  202          0         2.43                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.002566  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.002566  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002566        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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