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Database: PDB
Entry: 4QVL
LinkDB: 4QVL
Original site: 4QVL 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           15-JUL-14   4QVL              
TITLE     YCP IN COMPLEX WITH BORTEZOMIB                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;                           
COMPND   3 CHAIN: A, O;                                                         
COMPND   4 SYNONYM: MACROPAIN SUBUNIT Y7, MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND   5 SUBUNIT Y7, PROTEASOME COMPONENT Y7, PROTEINASE YSCE SUBUNIT 7;      
COMPND   6 EC: 3.4.25.1;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;                           
COMPND   9 CHAIN: B, P;                                                         
COMPND  10 SYNONYM: MACROPAIN SUBUNIT Y13, MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  11 SUBUNIT Y13, PROTEASOME COMPONENT Y13, PROTEINASE YSCE SUBUNIT 13;   
COMPND  12 EC: 3.4.25.1;                                                        
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;                           
COMPND  15 CHAIN: C, Q;                                                         
COMPND  16 SYNONYM: MACROPAIN SUBUNIT PRE6, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  17 SUBUNIT PRE6, PROTEASOME COMPONENT PRE6, PROTEINASE YSCE SUBUNIT     
COMPND  18 PRE6;                                                                
COMPND  19 EC: 3.4.25.1;                                                        
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;                           
COMPND  22 CHAIN: D, R;                                                         
COMPND  23 SYNONYM: MACROPAIN SUBUNIT PUP2, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  24 SUBUNIT PUP2, PROTEASOME COMPONENT PUP2, PROTEINASE YSCE SUBUNIT     
COMPND  25 PUP2;                                                                
COMPND  26 EC: 3.4.25.1;                                                        
COMPND  27 MOL_ID: 5;                                                           
COMPND  28 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;                           
COMPND  29 CHAIN: E, S;                                                         
COMPND  30 SYNONYM: MACROPAIN SUBUNIT PRE5, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  31 SUBUNIT PRE5, PROTEASOME COMPONENT PRE5, PROTEINASE YSCE SUBUNIT     
COMPND  32 PRE5;                                                                
COMPND  33 EC: 3.4.25.1;                                                        
COMPND  34 MOL_ID: 6;                                                           
COMPND  35 MOLECULE: PROBABLE PROTEASOME SUBUNIT ALPHA TYPE-7;                  
COMPND  36 CHAIN: F, T;                                                         
COMPND  37 SYNONYM: MACROPAIN SUBUNIT C1, MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  38 SUBUNIT C1, PROTEASOME COMPONENT C1, PROTEINASE YSCE SUBUNIT 1;      
COMPND  39 EC: 3.4.25.1;                                                        
COMPND  40 MOL_ID: 7;                                                           
COMPND  41 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;                           
COMPND  42 CHAIN: G, U;                                                         
COMPND  43 SYNONYM: MACROPAIN SUBUNIT C7-ALPHA, MULTICATALYTIC ENDOPEPTIDASE    
COMPND  44 COMPLEX C7, PROTEASOME COMPONENT C7-ALPHA, PROTEASOME COMPONENT Y8,  
COMPND  45 PROTEINASE YSCE SUBUNIT 7, SCL1 SUPPRESSOR PROTEIN;                  
COMPND  46 EC: 3.4.25.1;                                                        
COMPND  47 MOL_ID: 8;                                                           
COMPND  48 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;                            
COMPND  49 CHAIN: H, V;                                                         
COMPND  50 SYNONYM: MACROPAIN SUBUNIT PUP1, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  51 SUBUNIT PUP1, PROTEASOME COMPONENT PUP1, PROTEINASE YSCE SUBUNIT     
COMPND  52 PUP1;                                                                
COMPND  53 EC: 3.4.25.1;                                                        
COMPND  54 MOL_ID: 9;                                                           
COMPND  55 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;                            
COMPND  56 CHAIN: I, W;                                                         
COMPND  57 SYNONYM: MACROPAIN SUBUNIT PUP3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  58 SUBUNIT PUP3, PROTEASOME COMPONENT PUP3;                             
COMPND  59 EC: 3.4.25.1;                                                        
COMPND  60 MOL_ID: 10;                                                          
COMPND  61 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;                            
COMPND  62 CHAIN: J, X;                                                         
COMPND  63 SYNONYM: MACROPAIN SUBUNIT C11, MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  64 SUBUNIT C11, PROTEASOME COMPONENT C11, PROTEINASE YSCE SUBUNIT 11;   
COMPND  65 EC: 3.4.25.1;                                                        
COMPND  66 MOL_ID: 11;                                                          
COMPND  67 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;                            
COMPND  68 CHAIN: K, Y;                                                         
COMPND  69 SYNONYM: MACROPAIN SUBUNIT PRE2, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  70 SUBUNIT PRE2, PROTEASOME COMPONENT PRE2, PROTEINASE YSCE SUBUNIT     
COMPND  71 PRE2;                                                                
COMPND  72 EC: 3.4.25.1;                                                        
COMPND  73 ENGINEERED: YES;                                                     
COMPND  74 MOL_ID: 12;                                                          
COMPND  75 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;                            
COMPND  76 CHAIN: L, Z;                                                         
COMPND  77 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5, PROTEASOME 
COMPND  78 COMPONENT C5;                                                        
COMPND  79 EC: 3.4.25.1;                                                        
COMPND  80 MOL_ID: 13;                                                          
COMPND  81 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;                            
COMPND  82 CHAIN: M, a;                                                         
COMPND  83 SYNONYM: MACROPAIN SUBUNIT PRE4, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  84 SUBUNIT PRE4, PROTEASOME COMPONENT PRE4, PROTEINASE YSCE SUBUNIT     
COMPND  85 PRE4;                                                                
COMPND  86 EC: 3.4.25.1;                                                        
COMPND  87 MOL_ID: 14;                                                          
COMPND  88 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;                            
COMPND  89 CHAIN: N, b;                                                         
COMPND  90 SYNONYM: MACROPAIN SUBUNIT PRE3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  91 SUBUNIT PRE3, PROTEASOME COMPONENT PRE3, PROTEINASE YSCE SUBUNIT     
COMPND  92 PRE3;                                                                
COMPND  93 EC: 3.4.25.1                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 559292;                                              
SOURCE   5 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   8 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   9 ORGANISM_TAXID: 559292;                                              
SOURCE  10 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  13 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  14 ORGANISM_TAXID: 559292;                                              
SOURCE  15 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  18 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  19 ORGANISM_TAXID: 559292;                                              
SOURCE  20 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  21 MOL_ID: 5;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  23 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  24 ORGANISM_TAXID: 559292;                                              
SOURCE  25 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  26 MOL_ID: 6;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  28 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  29 ORGANISM_TAXID: 559292;                                              
SOURCE  30 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  31 MOL_ID: 7;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  33 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  34 ORGANISM_TAXID: 559292;                                              
SOURCE  35 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  36 MOL_ID: 8;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  38 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  39 ORGANISM_TAXID: 559292;                                              
SOURCE  40 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  41 MOL_ID: 9;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  43 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  44 ORGANISM_TAXID: 559292;                                              
SOURCE  45 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  46 MOL_ID: 10;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  48 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  49 ORGANISM_TAXID: 559292;                                              
SOURCE  50 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  51 MOL_ID: 11;                                                          
SOURCE  52 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  53 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  54 ORGANISM_TAXID: 559292;                                              
SOURCE  55 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  56 GENE: PRE2, DOA3, PRG1, YPR103W, P8283.10;                           
SOURCE  57 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  58 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  59 MOL_ID: 12;                                                          
SOURCE  60 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  61 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  62 ORGANISM_TAXID: 559292;                                              
SOURCE  63 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  64 MOL_ID: 13;                                                          
SOURCE  65 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  66 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  67 ORGANISM_TAXID: 559292;                                              
SOURCE  68 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  69 MOL_ID: 14;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  71 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  72 ORGANISM_TAXID: 559292;                                              
SOURCE  73 STRAIN: ATCC 204508 / S288C                                          
KEYWDS    CANCER, PROTEASOME, BORTEZOMIB, DRUG RESISTANCE, BINDING ANALYSIS,    
KEYWDS   2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.M.HUBER,W.HEINEMEYER,M.GROLL                                        
REVDAT   3   20-SEP-23 4QVL    1       REMARK LINK                              
REVDAT   2   18-FEB-15 4QVL    1       JRNL                                     
REVDAT   1   04-FEB-15 4QVL    0                                                
JRNL        AUTH   E.M.HUBER,W.HEINEMEYER,M.GROLL                               
JRNL        TITL   BORTEZOMIB-RESISTANT MUTANT PROTEASOMES: STRUCTURAL AND      
JRNL        TITL 2 BIOCHEMICAL EVALUATION WITH CARFILZOMIB AND ONX 0914.        
JRNL        REF    STRUCTURE                     V.  23   407 2015              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   25599643                                                     
JRNL        DOI    10.1016/J.STR.2014.11.019                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 229137                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 12060                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 16880                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 888                          
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 49366                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 180                                     
REMARK   3   SOLVENT ATOMS            : 357                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.30000                                              
REMARK   3    B22 (A**2) : -6.88000                                             
REMARK   3    B33 (A**2) : 2.21000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.97000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.292         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.228         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.125        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 50454 ; 0.004 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 48196 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 68262 ; 0.874 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):110966 ; 0.710 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  6314 ; 5.122 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2252 ;34.268 ;24.423       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  8752 ;14.124 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   284 ;13.941 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  7686 ; 0.049 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 57252 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A): 11322 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 25346 ; 2.778 ; 5.668       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 25345 ; 2.778 ; 5.668       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31630 ; 3.757 ; 8.487       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 31631 ; 3.757 ; 8.487       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 25108 ; 2.637 ; 6.064       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 25108 ; 2.637 ; 6.064       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 36632 ; 3.321 ; 8.941       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 54223 ; 4.261 ;44.269       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 54188 ; 4.247 ;44.269       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2): 98650 ; 0.909 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   226 ;28.503 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 97883 ;17.574 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 28                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   250                          
REMARK   3    RESIDUE RANGE :   A   301        A   313                          
REMARK   3    ORIGIN FOR THE GROUP (A):   66.907  -91.890   46.078              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1143 T22:   0.0836                                     
REMARK   3      T33:   0.1386 T12:  -0.0081                                     
REMARK   3      T13:   0.0002 T23:  -0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0154 L22:   0.0300                                     
REMARK   3      L33:   0.0019 L12:  -0.0153                                     
REMARK   3      L13:  -0.0037 L23:   0.0065                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0070 S12:   0.0170 S13:  -0.0132                       
REMARK   3      S21:  -0.0041 S22:   0.0046 S23:  -0.0119                       
REMARK   3      S31:  -0.0074 S32:  -0.0008 S33:   0.0024                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   244                          
REMARK   3    RESIDUE RANGE :   B   301        B   314                          
REMARK   3    ORIGIN FOR THE GROUP (A):   59.520  -87.684   16.497              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1067 T22:   0.0882                                     
REMARK   3      T33:   0.1339 T12:  -0.0063                                     
REMARK   3      T13:   0.0173 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0029 L22:   0.0060                                     
REMARK   3      L33:   0.0023 L12:   0.0007                                     
REMARK   3      L13:  -0.0018 L23:  -0.0008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0077 S12:  -0.0088 S13:  -0.0107                       
REMARK   3      S21:  -0.0190 S22:  -0.0047 S23:   0.0137                       
REMARK   3      S31:   0.0105 S32:   0.0049 S33:   0.0124                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   240                          
REMARK   3    RESIDUE RANGE :   C   301        C   315                          
REMARK   3    ORIGIN FOR THE GROUP (A):   32.327  -87.210    1.187              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1323 T22:   0.0738                                     
REMARK   3      T33:   0.1333 T12:   0.0053                                     
REMARK   3      T13:   0.0015 T23:   0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0422 L22:   0.0203                                     
REMARK   3      L33:   0.0012 L12:   0.0276                                     
REMARK   3      L13:   0.0010 L23:   0.0004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0095 S12:  -0.0137 S13:   0.0030                       
REMARK   3      S21:  -0.0113 S22:   0.0073 S23:   0.0146                       
REMARK   3      S31:   0.0102 S32:   0.0019 S33:   0.0022                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   242                          
REMARK   3    RESIDUE RANGE :   D   301        D   312                          
REMARK   3    ORIGIN FOR THE GROUP (A):    3.111  -89.895   13.717              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0917 T22:   0.0551                                     
REMARK   3      T33:   0.1454 T12:   0.0154                                     
REMARK   3      T13:  -0.0040 T23:   0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0100 L22:   0.0145                                     
REMARK   3      L33:   0.0918 L12:  -0.0071                                     
REMARK   3      L13:   0.0139 L23:  -0.0238                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0013 S12:  -0.0195 S13:  -0.0032                       
REMARK   3      S21:  -0.0133 S22:   0.0057 S23:   0.0280                       
REMARK   3      S31:  -0.0126 S32:   0.0022 S33:  -0.0069                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     3        E   233                          
REMARK   3    RESIDUE RANGE :   E   301        E   305                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.180  -94.265   45.732              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0662 T22:   0.0825                                     
REMARK   3      T33:   0.1308 T12:   0.0197                                     
REMARK   3      T13:   0.0254 T23:  -0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0049 L22:   0.0041                                     
REMARK   3      L33:   0.0281 L12:  -0.0033                                     
REMARK   3      L13:   0.0089 L23:  -0.0031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0110 S12:  -0.0060 S13:  -0.0088                       
REMARK   3      S21:   0.0102 S22:   0.0080 S23:   0.0183                       
REMARK   3      S31:   0.0019 S32:  -0.0141 S33:   0.0030                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     2        F   244                          
REMARK   3    RESIDUE RANGE :   F   301        F   313                          
REMARK   3    ORIGIN FOR THE GROUP (A):   15.222  -94.923   69.895              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1090 T22:   0.0790                                     
REMARK   3      T33:   0.1141 T12:   0.0058                                     
REMARK   3      T13:   0.0424 T23:  -0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0359 L22:   0.0026                                     
REMARK   3      L33:   0.0014 L12:   0.0072                                     
REMARK   3      L13:   0.0009 L23:  -0.0006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0100 S12:  -0.0063 S13:   0.0006                       
REMARK   3      S21:   0.0089 S22:  -0.0085 S23:   0.0085                       
REMARK   3      S31:  -0.0078 S32:   0.0055 S33:  -0.0015                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     2        G   242                          
REMARK   3    RESIDUE RANGE :   G   301        G   302                          
REMARK   3    RESIDUE RANGE :   G   401        G   413                          
REMARK   3    ORIGIN FOR THE GROUP (A):   47.645  -93.264   71.197              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1365 T22:   0.0689                                     
REMARK   3      T33:   0.1248 T12:  -0.0036                                     
REMARK   3      T13:   0.0050 T23:  -0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0238 L22:   0.0266                                     
REMARK   3      L33:   0.0335 L12:   0.0205                                     
REMARK   3      L13:   0.0198 L23:   0.0272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0075 S12:   0.0224 S13:  -0.0023                       
REMARK   3      S21:   0.0212 S22:  -0.0074 S23:  -0.0085                       
REMARK   3      S31:   0.0037 S32:  -0.0074 S33:  -0.0001                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H   226                          
REMARK   3    RESIDUE RANGE :   H   301        H   301                          
REMARK   3    RESIDUE RANGE :   H   401        H   413                          
REMARK   3    ORIGIN FOR THE GROUP (A):   67.603 -129.352   47.519              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0913 T22:   0.0798                                     
REMARK   3      T33:   0.1335 T12:  -0.0023                                     
REMARK   3      T13:   0.0019 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0015 L22:   0.0213                                     
REMARK   3      L33:   0.0040 L12:   0.0011                                     
REMARK   3      L13:  -0.0024 L23:  -0.0019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0076 S12:   0.0072 S13:   0.0052                       
REMARK   3      S21:   0.0354 S22:  -0.0009 S23:  -0.0309                       
REMARK   3      S31:  -0.0107 S32:  -0.0130 S33:  -0.0067                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     1        I   204                          
REMARK   3    RESIDUE RANGE :   I   301        I   301                          
REMARK   3    RESIDUE RANGE :   I   401        I   410                          
REMARK   3    ORIGIN FOR THE GROUP (A):   68.237 -127.240   20.984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1006 T22:   0.0838                                     
REMARK   3      T33:   0.1350 T12:  -0.0060                                     
REMARK   3      T13:   0.0194 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0077 L22:   0.0593                                     
REMARK   3      L33:   0.0093 L12:  -0.0184                                     
REMARK   3      L13:   0.0023 L23:  -0.0162                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0064 S12:   0.0042 S13:  -0.0006                       
REMARK   3      S21:   0.0091 S22:  -0.0099 S23:  -0.0162                       
REMARK   3      S31:  -0.0191 S32:  -0.0097 S33:   0.0035                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     1        J   195                          
REMARK   3    RESIDUE RANGE :   J   201        J   201                          
REMARK   3    RESIDUE RANGE :   J   301        J   313                          
REMARK   3    ORIGIN FOR THE GROUP (A):   44.730 -126.335   -0.539              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1101 T22:   0.0773                                     
REMARK   3      T33:   0.1083 T12:   0.0012                                     
REMARK   3      T13:   0.0255 T23:   0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0230 L22:   0.0447                                     
REMARK   3      L33:   0.0029 L12:   0.0257                                     
REMARK   3      L13:  -0.0058 L23:  -0.0046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0118 S12:  -0.0170 S13:   0.0258                       
REMARK   3      S21:  -0.0213 S22:  -0.0063 S23:   0.0110                       
REMARK   3      S31:   0.0010 S32:   0.0119 S33:  -0.0055                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K     1        K   212                          
REMARK   3    RESIDUE RANGE :   K   301        K   302                          
REMARK   3    RESIDUE RANGE :   K   401        K   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):   10.929 -130.631    2.510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1079 T22:   0.0687                                     
REMARK   3      T33:   0.1285 T12:   0.0055                                     
REMARK   3      T13:  -0.0159 T23:   0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0035 L22:   0.0424                                     
REMARK   3      L33:   0.0062 L12:   0.0080                                     
REMARK   3      L13:  -0.0001 L23:   0.0033                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0007 S12:   0.0014 S13:   0.0184                       
REMARK   3      S21:  -0.0095 S22:   0.0023 S23:   0.0193                       
REMARK   3      S31:  -0.0104 S32:   0.0178 S33:  -0.0016                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L   222                          
REMARK   3    RESIDUE RANGE :   L   301        L   325                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -4.508 -134.130   28.632              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0881 T22:   0.0797                                     
REMARK   3      T33:   0.1508 T12:   0.0101                                     
REMARK   3      T13:   0.0045 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0035 L22:   0.0023                                     
REMARK   3      L33:   0.0057 L12:   0.0007                                     
REMARK   3      L13:  -0.0032 L23:  -0.0024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0029 S12:  -0.0110 S13:   0.0157                       
REMARK   3      S21:   0.0134 S22:   0.0038 S23:   0.0063                       
REMARK   3      S31:  -0.0163 S32:   0.0117 S33:  -0.0067                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M     1        M   233                          
REMARK   3    RESIDUE RANGE :   M   301        M   317                          
REMARK   3    ORIGIN FOR THE GROUP (A):    7.866 -137.716   60.453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1116 T22:   0.0888                                     
REMARK   3      T33:   0.1347 T12:   0.0020                                     
REMARK   3      T13:   0.0175 T23:   0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0039 L22:   0.0965                                     
REMARK   3      L33:   0.0010 L12:  -0.0147                                     
REMARK   3      L13:   0.0009 L23:  -0.0074                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0093 S12:  -0.0017 S13:   0.0060                       
REMARK   3      S21:   0.0169 S22:  -0.0082 S23:   0.0144                       
REMARK   3      S31:  -0.0011 S32:   0.0066 S33:  -0.0011                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N     1        N   196                          
REMARK   3    RESIDUE RANGE :   N   201        N   203                          
REMARK   3    RESIDUE RANGE :   N   301        N   316                          
REMARK   3    ORIGIN FOR THE GROUP (A):   39.859 -133.942   70.729              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1316 T22:   0.0863                                     
REMARK   3      T33:   0.1181 T12:  -0.0026                                     
REMARK   3      T13:   0.0015 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0543 L22:   0.0926                                     
REMARK   3      L33:   0.0162 L12:  -0.0360                                     
REMARK   3      L13:  -0.0252 L23:   0.0340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0083 S12:  -0.0050 S13:  -0.0004                       
REMARK   3      S21:   0.0225 S22:  -0.0126 S23:   0.0064                       
REMARK   3      S31:   0.0020 S32:  -0.0043 S33:   0.0042                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   O     1        O   250                          
REMARK   3    RESIDUE RANGE :   O   301        O   304                          
REMARK   3    ORIGIN FOR THE GROUP (A):    1.785 -206.284   36.738              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0965 T22:   0.0823                                     
REMARK   3      T33:   0.1416 T12:  -0.0161                                     
REMARK   3      T13:  -0.0126 T23:   0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0285 L22:   0.0603                                     
REMARK   3      L33:   0.0179 L12:   0.0211                                     
REMARK   3      L13:  -0.0036 L23:   0.0171                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0004 S12:   0.0202 S13:   0.0073                       
REMARK   3      S21:  -0.0041 S22:   0.0007 S23:  -0.0063                       
REMARK   3      S31:   0.0238 S32:  -0.0025 S33:  -0.0003                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   P     1        P   244                          
REMARK   3    RESIDUE RANGE :   P   301        P   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):    8.384 -205.145    6.680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1149 T22:   0.0737                                     
REMARK   3      T33:   0.1473 T12:  -0.0019                                     
REMARK   3      T13:  -0.0176 T23:  -0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0037 L22:   0.0025                                     
REMARK   3      L33:   0.0233 L12:  -0.0002                                     
REMARK   3      L13:   0.0067 L23:  -0.0019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0156 S12:  -0.0081 S13:   0.0095                       
REMARK   3      S21:  -0.0083 S22:   0.0018 S23:  -0.0148                       
REMARK   3      S31:  -0.0098 S32:  -0.0105 S33:   0.0138                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Q     1        Q   240                          
REMARK   3    RESIDUE RANGE :   Q   301        Q   309                          
REMARK   3    ORIGIN FOR THE GROUP (A):   35.486 -203.092   -9.118              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1303 T22:   0.0635                                     
REMARK   3      T33:   0.1135 T12:   0.0232                                     
REMARK   3      T13:  -0.0025 T23:  -0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0100 L22:   0.0056                                     
REMARK   3      L33:   0.0196 L12:  -0.0049                                     
REMARK   3      L13:   0.0076 L23:  -0.0091                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0261 S12:  -0.0164 S13:  -0.0095                       
REMARK   3      S21:  -0.0212 S22:   0.0073 S23:   0.0155                       
REMARK   3      S31:   0.0193 S32:   0.0041 S33:  -0.0334                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   R     1        R   242                          
REMARK   3    RESIDUE RANGE :   R   301        R   307                          
REMARK   3    ORIGIN FOR THE GROUP (A):   64.925 -202.584    3.270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0849 T22:   0.0377                                     
REMARK   3      T33:   0.1135 T12:   0.0361                                     
REMARK   3      T13:   0.0352 T23:  -0.0291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0156 L22:   0.0198                                     
REMARK   3      L33:   0.0612 L12:  -0.0107                                     
REMARK   3      L13:  -0.0247 L23:   0.0024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0031 S12:  -0.0104 S13:   0.0116                       
REMARK   3      S21:  -0.0336 S22:  -0.0112 S23:  -0.0224                       
REMARK   3      S31:   0.0346 S32:   0.0239 S33:   0.0143                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   S     3        S   233                          
REMARK   3    RESIDUE RANGE :   S   301        S   306                          
REMARK   3    ORIGIN FOR THE GROUP (A):   71.858 -203.773   35.228              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0691 T22:   0.0661                                     
REMARK   3      T33:   0.1578 T12:   0.0290                                     
REMARK   3      T13:  -0.0095 T23:  -0.0218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0082 L22:   0.0228                                     
REMARK   3      L33:   0.0327 L12:   0.0108                                     
REMARK   3      L13:   0.0137 L23:   0.0263                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0251 S12:  -0.0038 S13:  -0.0009                       
REMARK   3      S21:   0.0287 S22:   0.0081 S23:  -0.0381                       
REMARK   3      S31:   0.0290 S32:  -0.0096 S33:  -0.0332                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   T     2        T   244                          
REMARK   3    RESIDUE RANGE :   T   301        T   313                          
REMARK   3    ORIGIN FOR THE GROUP (A):   53.948 -207.397   59.474              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1235 T22:   0.0438                                     
REMARK   3      T33:   0.1337 T12:   0.0102                                     
REMARK   3      T13:  -0.0401 T23:   0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0162 L22:   0.0065                                     
REMARK   3      L33:   0.0058 L12:   0.0095                                     
REMARK   3      L13:   0.0054 L23:   0.0050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0344 S12:  -0.0068 S13:  -0.0277                       
REMARK   3      S21:   0.0183 S22:  -0.0147 S23:  -0.0206                       
REMARK   3      S31:   0.0034 S32:  -0.0146 S33:  -0.0197                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   U     2        U   242                          
REMARK   3    RESIDUE RANGE :   U   301        U   301                          
REMARK   3    RESIDUE RANGE :   U   401        U   408                          
REMARK   3    ORIGIN FOR THE GROUP (A):   21.627 -209.447   61.118              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1425 T22:   0.0699                                     
REMARK   3      T33:   0.1332 T12:  -0.0080                                     
REMARK   3      T13:  -0.0132 T23:   0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0033 L22:   0.0022                                     
REMARK   3      L33:   0.0013 L12:   0.0015                                     
REMARK   3      L13:  -0.0016 L23:  -0.0016                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0009 S12:   0.0136 S13:   0.0103                       
REMARK   3      S21:   0.0136 S22:   0.0068 S23:   0.0049                       
REMARK   3      S31:  -0.0072 S32:  -0.0057 S33:  -0.0059                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   V     1        V   226                          
REMARK   3    RESIDUE RANGE :   V   301        V   302                          
REMARK   3    RESIDUE RANGE :   V   401        V   418                          
REMARK   3    ORIGIN FOR THE GROUP (A):    1.226 -169.666   44.728              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0950 T22:   0.0842                                     
REMARK   3      T33:   0.1430 T12:  -0.0110                                     
REMARK   3      T13:   0.0055 T23:   0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0014 L22:   0.0086                                     
REMARK   3      L33:   0.0098 L12:   0.0005                                     
REMARK   3      L13:   0.0016 L23:  -0.0030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0120 S12:  -0.0007 S13:  -0.0076                       
REMARK   3      S21:   0.0086 S22:  -0.0094 S23:   0.0203                       
REMARK   3      S31:   0.0241 S32:   0.0084 S33:  -0.0025                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   W     1        W   204                          
REMARK   3    RESIDUE RANGE :   W   301        W   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):    0.046 -167.097   18.196              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1113 T22:   0.0775                                     
REMARK   3      T33:   0.1485 T12:  -0.0001                                     
REMARK   3      T13:  -0.0145 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0335 L22:   0.1162                                     
REMARK   3      L33:   0.0042 L12:   0.0613                                     
REMARK   3      L13:   0.0075 L23:   0.0150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0014 S12:  -0.0045 S13:  -0.0027                       
REMARK   3      S21:  -0.0062 S22:   0.0012 S23:   0.0151                       
REMARK   3      S31:   0.0098 S32:   0.0101 S33:   0.0002                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X     1        X   195                          
REMARK   3    RESIDUE RANGE :   X   201        X   221                          
REMARK   3    ORIGIN FOR THE GROUP (A):   23.111 -164.175   -3.698              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1344 T22:   0.0812                                     
REMARK   3      T33:   0.1353 T12:   0.0056                                     
REMARK   3      T13:  -0.0154 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0034 L22:   0.0083                                     
REMARK   3      L33:   0.0006 L12:  -0.0033                                     
REMARK   3      L13:   0.0009 L23:  -0.0003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0132 S12:  -0.0068 S13:  -0.0156                       
REMARK   3      S21:  -0.0325 S22:  -0.0049 S23:   0.0091                       
REMARK   3      S31:  -0.0004 S32:  -0.0002 S33:  -0.0083                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Y     1        Y   212                          
REMARK   3    RESIDUE RANGE :   Y   301        Y   302                          
REMARK   3    RESIDUE RANGE :   Y   401        Y   415                          
REMARK   3    ORIGIN FOR THE GROUP (A):   56.981 -160.469   -0.625              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1014 T22:   0.0790                                     
REMARK   3      T33:   0.1149 T12:   0.0047                                     
REMARK   3      T13:   0.0290 T23:  -0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0042 L22:   0.0027                                     
REMARK   3      L33:   0.0082 L12:   0.0023                                     
REMARK   3      L13:   0.0058 L23:   0.0038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0120 S12:  -0.0052 S13:  -0.0087                       
REMARK   3      S21:   0.0125 S22:   0.0045 S23:  -0.0051                       
REMARK   3      S31:   0.0206 S32:  -0.0023 S33:  -0.0165                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Z     1        Z   222                          
REMARK   3    RESIDUE RANGE :   Z   301        Z   301                          
REMARK   3    RESIDUE RANGE :   Z   401        Z   413                          
REMARK   3    ORIGIN FOR THE GROUP (A):   72.923 -161.552   25.390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0853 T22:   0.0883                                     
REMARK   3      T33:   0.1450 T12:   0.0102                                     
REMARK   3      T13:   0.0127 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0150 L22:   0.0844                                     
REMARK   3      L33:   0.0227 L12:   0.0329                                     
REMARK   3      L13:  -0.0114 L23:  -0.0334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0078 S12:  -0.0171 S13:  -0.0151                       
REMARK   3      S21:   0.0211 S22:  -0.0098 S23:  -0.0238                       
REMARK   3      S31:   0.0142 S32:  -0.0014 S33:   0.0021                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   a     1        a   233                          
REMARK   3    RESIDUE RANGE :   a   301        a   323                          
REMARK   3    ORIGIN FOR THE GROUP (A):   61.241 -163.591   57.567              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1252 T22:   0.0751                                     
REMARK   3      T33:   0.1432 T12:   0.0005                                     
REMARK   3      T13:  -0.0110 T23:   0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0110 L22:   0.0633                                     
REMARK   3      L33:   0.0113 L12:  -0.0131                                     
REMARK   3      L13:  -0.0024 L23:   0.0219                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0062 S12:   0.0145 S13:  -0.0069                       
REMARK   3      S21:   0.0214 S22:  -0.0071 S23:  -0.0068                       
REMARK   3      S31:   0.0026 S32:  -0.0115 S33:   0.0010                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   b     1        b   196                          
REMARK   3    RESIDUE RANGE :   b   201        b   202                          
REMARK   3    RESIDUE RANGE :   b   301        b   310                          
REMARK   3    ORIGIN FOR THE GROUP (A):   29.472 -169.184   67.753              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1349 T22:   0.0859                                     
REMARK   3      T33:   0.1254 T12:  -0.0037                                     
REMARK   3      T13:  -0.0001 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0119 L22:   0.0542                                     
REMARK   3      L33:   0.0012 L12:   0.0224                                     
REMARK   3      L13:  -0.0006 L23:   0.0025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0110 S12:   0.0138 S13:   0.0027                       
REMARK   3      S21:   0.0289 S22:  -0.0026 S23:  -0.0123                       
REMARK   3      S31:   0.0024 S32:  -0.0088 S33:  -0.0084                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4QVL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000086568.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT. SI(111)     
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS, XSCALE                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 241198                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1RYP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM MGAC2, 13% MPD, PH 6.8, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      150.10500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: AU CONTAINS ONE BIOLOGICAL ASSEMBLY.                         
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: 124890 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 212880 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -478.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, 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     MET B     0                                                      
REMARK 465     LYS B   245                                                      
REMARK 465     LYS B   246                                                      
REMARK 465     ASP B   247                                                      
REMARK 465     GLU B   248                                                      
REMARK 465     ASP B   249                                                      
REMARK 465     GLU B   250                                                      
REMARK 465     GLU B   251                                                      
REMARK 465     ALA B   252                                                      
REMARK 465     ASP B   253                                                      
REMARK 465     GLU B   254                                                      
REMARK 465     ASP B   255                                                      
REMARK 465     MET B   256                                                      
REMARK 465     LYS B   257                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     GLN C   241                                                      
REMARK 465     GLN C   242                                                      
REMARK 465     GLU C   243                                                      
REMARK 465     GLN C   244                                                      
REMARK 465     ASP C   245                                                      
REMARK 465     LYS C   246                                                      
REMARK 465     LYS C   247                                                      
REMARK 465     LYS C   248                                                      
REMARK 465     LYS C   249                                                      
REMARK 465     SER C   250                                                      
REMARK 465     ASN C   251                                                      
REMARK 465     HIS C   252                                                      
REMARK 465     MET D    -7                                                      
REMARK 465     PHE D    -6                                                      
REMARK 465     LEU D    -5                                                      
REMARK 465     THR D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     GLU D    -1                                                      
REMARK 465     TYR D     0                                                      
REMARK 465     GLY D   118                                                      
REMARK 465     ALA D   119                                                      
REMARK 465     SER D   120                                                      
REMARK 465     GLY D   121                                                      
REMARK 465     GLU D   122                                                      
REMARK 465     GLU D   123                                                      
REMARK 465     ARG D   124                                                      
REMARK 465     SER D   243                                                      
REMARK 465     PRO D   244                                                      
REMARK 465     GLU D   245                                                      
REMARK 465     GLU D   246                                                      
REMARK 465     ALA D   247                                                      
REMARK 465     ASP D   248                                                      
REMARK 465     VAL D   249                                                      
REMARK 465     GLU D   250                                                      
REMARK 465     MET D   251                                                      
REMARK 465     SER D   252                                                      
REMARK 465     MET E     0                                                      
REMARK 465     PHE E     1                                                      
REMARK 465     ARG E     2                                                      
REMARK 465     MET F    -3                                                      
REMARK 465     THR F    -2                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     ILE F     0                                                      
REMARK 465     GLY F     1                                                      
REMARK 465     GLY F   245                                                      
REMARK 465     ASP F   246                                                      
REMARK 465     ASP F   247                                                      
REMARK 465     ASP F   248                                                      
REMARK 465     GLU F   249                                                      
REMARK 465     ASP F   250                                                      
REMARK 465     GLU F   251                                                      
REMARK 465     ASP F   252                                                      
REMARK 465     ASP F   253                                                      
REMARK 465     SER F   254                                                      
REMARK 465     ASP F   255                                                      
REMARK 465     ASN F   256                                                      
REMARK 465     VAL F   257                                                      
REMARK 465     MET F   258                                                      
REMARK 465     SER F   259                                                      
REMARK 465     SER F   260                                                      
REMARK 465     ASP F   261                                                      
REMARK 465     ASP F   262                                                      
REMARK 465     GLU F   263                                                      
REMARK 465     ASN F   264                                                      
REMARK 465     ALA F   265                                                      
REMARK 465     PRO F   266                                                      
REMARK 465     VAL F   267                                                      
REMARK 465     ALA F   268                                                      
REMARK 465     THR F   269                                                      
REMARK 465     ASN F   270                                                      
REMARK 465     ALA F   271                                                      
REMARK 465     ASN F   272                                                      
REMARK 465     ALA F   273                                                      
REMARK 465     THR F   274                                                      
REMARK 465     THR F   275                                                      
REMARK 465     ASP F   276                                                      
REMARK 465     GLN F   277                                                      
REMARK 465     GLU F   278                                                      
REMARK 465     GLY F   279                                                      
REMARK 465     ASP F   280                                                      
REMARK 465     ILE F   281                                                      
REMARK 465     HIS F   282                                                      
REMARK 465     LEU F   283                                                      
REMARK 465     GLU F   284                                                      
REMARK 465     MET G    -8                                                      
REMARK 465     SER G    -7                                                      
REMARK 465     GLY G    -6                                                      
REMARK 465     ALA G    -5                                                      
REMARK 465     ALA G    -4                                                      
REMARK 465     ALA G    -3                                                      
REMARK 465     ALA G    -2                                                      
REMARK 465     SER G    -1                                                      
REMARK 465     ALA G     0                                                      
REMARK 465     ALA G     1                                                      
REMARK 465     ASP G   243                                                      
REMARK 465     GLN H   227                                                      
REMARK 465     VAL H   228                                                      
REMARK 465     ASP H   229                                                      
REMARK 465     ILE H   230                                                      
REMARK 465     THR H   231                                                      
REMARK 465     ALA H   232                                                      
REMARK 465     MET I     0                                                      
REMARK 465     GLN J   196                                                      
REMARK 465     ALA J   197                                                      
REMARK 465     GLN J   198                                                      
REMARK 465     THR M   -12                                                      
REMARK 465     GLN M   -11                                                      
REMARK 465     ILE M   -10                                                      
REMARK 465     ALA M    -9                                                      
REMARK 465     ASN M    -8                                                      
REMARK 465     ALA M    -7                                                      
REMARK 465     GLY M    -6                                                      
REMARK 465     ALA M    -5                                                      
REMARK 465     SER M    -4                                                      
REMARK 465     PRO M    -3                                                      
REMARK 465     MET M    -2                                                      
REMARK 465     VAL M    -1                                                      
REMARK 465     ASN M     0                                                      
REMARK 465     MET P     0                                                      
REMARK 465     LYS P   245                                                      
REMARK 465     LYS P   246                                                      
REMARK 465     ASP P   247                                                      
REMARK 465     GLU P   248                                                      
REMARK 465     ASP P   249                                                      
REMARK 465     GLU P   250                                                      
REMARK 465     GLU P   251                                                      
REMARK 465     ALA P   252                                                      
REMARK 465     ASP P   253                                                      
REMARK 465     GLU P   254                                                      
REMARK 465     ASP P   255                                                      
REMARK 465     MET P   256                                                      
REMARK 465     LYS P   257                                                      
REMARK 465     MET Q    -1                                                      
REMARK 465     SER Q     0                                                      
REMARK 465     GLN Q   241                                                      
REMARK 465     GLN Q   242                                                      
REMARK 465     GLU Q   243                                                      
REMARK 465     GLN Q   244                                                      
REMARK 465     ASP Q   245                                                      
REMARK 465     LYS Q   246                                                      
REMARK 465     LYS Q   247                                                      
REMARK 465     LYS Q   248                                                      
REMARK 465     LYS Q   249                                                      
REMARK 465     SER Q   250                                                      
REMARK 465     ASN Q   251                                                      
REMARK 465     HIS Q   252                                                      
REMARK 465     MET R    -7                                                      
REMARK 465     PHE R    -6                                                      
REMARK 465     LEU R    -5                                                      
REMARK 465     THR R    -4                                                      
REMARK 465     ARG R    -3                                                      
REMARK 465     SER R    -2                                                      
REMARK 465     GLU R    -1                                                      
REMARK 465     TYR R     0                                                      
REMARK 465     GLY R   118                                                      
REMARK 465     ALA R   119                                                      
REMARK 465     SER R   120                                                      
REMARK 465     GLY R   121                                                      
REMARK 465     GLU R   122                                                      
REMARK 465     GLU R   123                                                      
REMARK 465     ARG R   124                                                      
REMARK 465     SER R   243                                                      
REMARK 465     PRO R   244                                                      
REMARK 465     GLU R   245                                                      
REMARK 465     GLU R   246                                                      
REMARK 465     ALA R   247                                                      
REMARK 465     ASP R   248                                                      
REMARK 465     VAL R   249                                                      
REMARK 465     GLU R   250                                                      
REMARK 465     MET R   251                                                      
REMARK 465     SER R   252                                                      
REMARK 465     MET S     0                                                      
REMARK 465     PHE S     1                                                      
REMARK 465     ARG S     2                                                      
REMARK 465     MET T    -3                                                      
REMARK 465     THR T    -2                                                      
REMARK 465     SER T    -1                                                      
REMARK 465     ILE T     0                                                      
REMARK 465     GLY T     1                                                      
REMARK 465     GLY T   245                                                      
REMARK 465     ASP T   246                                                      
REMARK 465     ASP T   247                                                      
REMARK 465     ASP T   248                                                      
REMARK 465     GLU T   249                                                      
REMARK 465     ASP T   250                                                      
REMARK 465     GLU T   251                                                      
REMARK 465     ASP T   252                                                      
REMARK 465     ASP T   253                                                      
REMARK 465     SER T   254                                                      
REMARK 465     ASP T   255                                                      
REMARK 465     ASN T   256                                                      
REMARK 465     VAL T   257                                                      
REMARK 465     MET T   258                                                      
REMARK 465     SER T   259                                                      
REMARK 465     SER T   260                                                      
REMARK 465     ASP T   261                                                      
REMARK 465     ASP T   262                                                      
REMARK 465     GLU T   263                                                      
REMARK 465     ASN T   264                                                      
REMARK 465     ALA T   265                                                      
REMARK 465     PRO T   266                                                      
REMARK 465     VAL T   267                                                      
REMARK 465     ALA T   268                                                      
REMARK 465     THR T   269                                                      
REMARK 465     ASN T   270                                                      
REMARK 465     ALA T   271                                                      
REMARK 465     ASN T   272                                                      
REMARK 465     ALA T   273                                                      
REMARK 465     THR T   274                                                      
REMARK 465     THR T   275                                                      
REMARK 465     ASP T   276                                                      
REMARK 465     GLN T   277                                                      
REMARK 465     GLU T   278                                                      
REMARK 465     GLY T   279                                                      
REMARK 465     ASP T   280                                                      
REMARK 465     ILE T   281                                                      
REMARK 465     HIS T   282                                                      
REMARK 465     LEU T   283                                                      
REMARK 465     GLU T   284                                                      
REMARK 465     MET U    -8                                                      
REMARK 465     SER U    -7                                                      
REMARK 465     GLY U    -6                                                      
REMARK 465     ALA U    -5                                                      
REMARK 465     ALA U    -4                                                      
REMARK 465     ALA U    -3                                                      
REMARK 465     ALA U    -2                                                      
REMARK 465     SER U    -1                                                      
REMARK 465     ALA U     0                                                      
REMARK 465     ALA U     1                                                      
REMARK 465     ASP U   243                                                      
REMARK 465     GLN V   227                                                      
REMARK 465     VAL V   228                                                      
REMARK 465     ASP V   229                                                      
REMARK 465     ILE V   230                                                      
REMARK 465     THR V   231                                                      
REMARK 465     ALA V   232                                                      
REMARK 465     MET W     0                                                      
REMARK 465     GLN X   196                                                      
REMARK 465     ALA X   197                                                      
REMARK 465     GLN X   198                                                      
REMARK 465     THR a   -12                                                      
REMARK 465     GLN a   -11                                                      
REMARK 465     ILE a   -10                                                      
REMARK 465     ALA a    -9                                                      
REMARK 465     ASN a    -8                                                      
REMARK 465     ALA a    -7                                                      
REMARK 465     GLY a    -6                                                      
REMARK 465     ALA a    -5                                                      
REMARK 465     SER a    -4                                                      
REMARK 465     PRO a    -3                                                      
REMARK 465     MET a    -2                                                      
REMARK 465     VAL a    -1                                                      
REMARK 465     ASN a     0                                                      
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    ARG X     8     OH   TYR X   148              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A   2      140.27     58.79                                   
REMARK 500    TYR A  97      -65.49   -149.11                                   
REMARK 500    ALA A 249       44.20    -94.96                                   
REMARK 500    ARG B   8       76.21     60.71                                   
REMARK 500    THR B  10       56.16   -114.87                                   
REMARK 500    VAL B  51       90.90    -10.27                                   
REMARK 500    ASN B 220      100.29    -52.73                                   
REMARK 500    ASP B 221     -178.90     72.53                                   
REMARK 500    PRO C 183      105.88    -43.88                                   
REMARK 500    GLN C 202      -98.65    112.43                                   
REMARK 500    ALA C 205     -106.38    -82.54                                   
REMARK 500    ARG D  45       71.59     56.38                                   
REMARK 500    SER E  39     -155.73   -111.28                                   
REMARK 500    ASP E 137     -160.62   -122.83                                   
REMARK 500    ASP E 202      -55.35     67.20                                   
REMARK 500    CYS F  38     -169.17   -110.99                                   
REMARK 500    ASP F  67     -133.61     56.56                                   
REMARK 500    LYS F 100      -54.31     76.89                                   
REMARK 500    ASP F 138     -167.97   -126.61                                   
REMARK 500    SER H 171     -112.67     66.02                                   
REMARK 500    ASN H 194       44.66   -140.85                                   
REMARK 500    GLN I  31     -109.26     57.99                                   
REMARK 500    ASP I 192       33.14   -147.27                                   
REMARK 500    GLN I 203       46.86   -104.05                                   
REMARK 500    ASP J   2      -95.94   -106.70                                   
REMARK 500    VAL J   9     -167.03   -104.89                                   
REMARK 500    SER J  31       32.83   -148.49                                   
REMARK 500    ASP L  32     -115.84     50.52                                   
REMARK 500    LYS L 100       42.71   -108.63                                   
REMARK 500    PHE L 103       68.97   -158.91                                   
REMARK 500    ASN L 165       74.39     51.45                                   
REMARK 500    ASP L 200      -66.01     68.28                                   
REMARK 500    ILE M   5      -77.78   -107.92                                   
REMARK 500    THR M   9     -152.33    -90.66                                   
REMARK 500    ALA M  83     -114.00   -144.99                                   
REMARK 500    LYS N 107     -147.15     63.62                                   
REMARK 500    THR O   2      140.42     58.92                                   
REMARK 500    TYR O  97      -65.85   -149.03                                   
REMARK 500    ALA O 249       44.40    -94.95                                   
REMARK 500    ARG P   8       76.01     60.92                                   
REMARK 500    THR P  10       55.97   -114.68                                   
REMARK 500    VAL P  51       90.88    -10.38                                   
REMARK 500    ASN P 220      100.43    -52.65                                   
REMARK 500    ASP P 221     -178.77     72.50                                   
REMARK 500    PRO Q 183      105.96    -43.93                                   
REMARK 500    GLN Q 202      -98.46    112.59                                   
REMARK 500    ALA Q 205     -106.49    -82.67                                   
REMARK 500    ARG R  45       71.73     56.20                                   
REMARK 500    SER S  39     -155.50   -111.18                                   
REMARK 500    ASP S 137     -160.46   -122.89                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      71 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G   8   OG1                                                    
REMARK 620 2 TYR G 119   O    77.1                                              
REMARK 620 3 ARG G 122   O    77.5  71.3                                        
REMARK 620 4 MET G 125   O   154.6  79.4  85.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA I 174   O                                                      
REMARK 620 2 ASP I 177   O    69.2                                              
REMARK 620 3 SER I 180   O    81.1  80.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG Y 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I 204   O                                                      
REMARK 620 2 ALA Y 165   O   106.6                                              
REMARK 620 3 ASP Y 168   O   154.4  92.8                                        
REMARK 620 4 SER Y 171   O    90.5  83.6  74.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG K 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA K 165   O                                                      
REMARK 620 2 ASP K 168   O    97.2                                              
REMARK 620 3 SER K 171   O    86.8  79.5                                        
REMARK 620 4 ASP W 204   O   103.5 156.4  90.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG V 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L 222   OXT                                                    
REMARK 620 2 ILE V 163   O    97.2                                              
REMARK 620 3 ASP V 166   O   139.3 109.5                                        
REMARK 620 4 SER V 169   O    82.2  86.5  69.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG N 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE N 163   O                                                      
REMARK 620 2 ASP N 166   O    71.3                                              
REMARK 620 3 SER N 169   O    99.4  68.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG Z 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR Z 192   O                                                      
REMARK 620 2 VAL Z 198   O    91.5                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 H 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 K 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 N 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL N 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL U 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 V 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG V 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 Y 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 b 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL b 202                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QTR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QUX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QUY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QV0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QV1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QV3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QV4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QV5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QV6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QV7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QV8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QV9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QVM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QVN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QVP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QVQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1RYP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QWR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QWS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QWU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QWX   RELATED DB: PDB                                   
DBREF  4QVL A    1   250  UNP    P23639   PSA2_YEAST       1    250             
DBREF  4QVL B    0   257  UNP    P23638   PSA3_YEAST       1    258             
DBREF  4QVL C   -1   252  UNP    P40303   PSA4_YEAST       1    254             
DBREF  4QVL D   -7   252  UNP    P32379   PSA5_YEAST       1    260             
DBREF  4QVL E    0   233  UNP    P40302   PSA6_YEAST       1    234             
DBREF  4QVL F   -3   284  UNP    P21242   PSA7_YEAST       1    288             
DBREF  4QVL G   -8   243  UNP    P21243   PSA1_YEAST       1    252             
DBREF  4QVL H    1   232  UNP    P25043   PSB2_YEAST      30    261             
DBREF  4QVL I    0   204  UNP    P25451   PSB3_YEAST       1    205             
DBREF  4QVL J    1   198  UNP    P22141   PSB4_YEAST       1    198             
DBREF  4QVL K    1   212  UNP    P30656   PSB5_YEAST      76    287             
DBREF  4QVL L    1   222  UNP    P23724   PSB6_YEAST      20    241             
DBREF  4QVL M  -12   233  UNP    P30657   PSB7_YEAST      21    266             
DBREF  4QVL N    1   196  UNP    P38624   PSB1_YEAST      20    215             
DBREF  4QVL O    1   250  UNP    P23639   PSA2_YEAST       1    250             
DBREF  4QVL P    0   257  UNP    P23638   PSA3_YEAST       1    258             
DBREF  4QVL Q   -1   252  UNP    P40303   PSA4_YEAST       1    254             
DBREF  4QVL R   -7   252  UNP    P32379   PSA5_YEAST       1    260             
DBREF  4QVL S    0   233  UNP    P40302   PSA6_YEAST       1    234             
DBREF  4QVL T   -3   284  UNP    P21242   PSA7_YEAST       1    288             
DBREF  4QVL U   -8   243  UNP    P21243   PSA1_YEAST       1    252             
DBREF  4QVL V    1   232  UNP    P25043   PSB2_YEAST      30    261             
DBREF  4QVL W    0   204  UNP    P25451   PSB3_YEAST       1    205             
DBREF  4QVL X    1   198  UNP    P22141   PSB4_YEAST       1    198             
DBREF  4QVL Y    1   212  UNP    P30656   PSB5_YEAST      76    287             
DBREF  4QVL Z    1   222  UNP    P23724   PSB6_YEAST      20    241             
DBREF  4QVL a  -12   233  UNP    P30657   PSB7_YEAST      21    266             
DBREF  4QVL b    1   196  UNP    P38624   PSB1_YEAST      20    215             
SEQRES   1 A  250  MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER          
SEQRES   2 A  250  PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR          
SEQRES   3 A  250  ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA          
SEQRES   4 A  250  THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER          
SEQRES   5 A  250  SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER          
SEQRES   6 A  250  LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET          
SEQRES   7 A  250  GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS          
SEQRES   8 A  250  VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR          
SEQRES   9 A  250  PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE          
SEQRES  10 A  250  MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE          
SEQRES  11 A  250  GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN          
SEQRES  12 A  250  GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR          
SEQRES  13 A  250  PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL          
SEQRES  14 A  250  ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU          
SEQRES  15 A  250  LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR          
SEQRES  16 A  250  LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR          
SEQRES  17 A  250  ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU          
SEQRES  18 A  250  LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG          
SEQRES  19 A  250  PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU          
SEQRES  20 A  250  GLU ALA LEU                                                  
SEQRES   1 B  258  MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE          
SEQRES   2 B  258  SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU          
SEQRES   3 B  258  GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET          
SEQRES   4 B  258  ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL          
SEQRES   5 B  258  THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS          
SEQRES   6 B  258  LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA          
SEQRES   7 B  258  GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA          
SEQRES   8 B  258  ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU          
SEQRES   9 B  258  ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP          
SEQRES  10 B  258  ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO          
SEQRES  11 B  258  PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG          
SEQRES  12 B  258  TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN          
SEQRES  13 B  258  TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR          
SEQRES  14 B  258  SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP          
SEQRES  15 B  258  ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS          
SEQRES  16 B  258  THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR          
SEQRES  17 B  258  ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN          
SEQRES  18 B  258  ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU          
SEQRES  19 B  258  ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS          
SEQRES  20 B  258  ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS                  
SEQRES   1 C  254  MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO          
SEQRES   2 C  254  ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA          
SEQRES   3 C  254  VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS          
SEQRES   4 C  254  ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU          
SEQRES   5 C  254  LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER          
SEQRES   6 C  254  LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU          
SEQRES   7 C  254  ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL          
SEQRES   8 C  254  GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL          
SEQRES   9 C  254  THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN          
SEQRES  10 C  254  GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY          
SEQRES  11 C  254  VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP          
SEQRES  12 C  254  GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR          
SEQRES  13 C  254  SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS          
SEQRES  14 C  254  THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS          
SEQRES  15 C  254  GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR          
SEQRES  16 C  254  VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS          
SEQRES  17 C  254  ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE          
SEQRES  18 C  254  VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR          
SEQRES  19 C  254  GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP          
SEQRES  20 C  254  LYS LYS LYS LYS SER ASN HIS                                  
SEQRES   1 D  260  MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER          
SEQRES   2 D  260  THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR          
SEQRES   3 D  260  SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY          
SEQRES   4 D  260  ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS          
SEQRES   5 D  260  ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU          
SEQRES   6 D  260  LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET          
SEQRES   7 D  260  SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS          
SEQRES   8 D  260  ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP          
SEQRES   9 D  260  GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS          
SEQRES  10 D  260  ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU          
SEQRES  11 D  260  GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU          
SEQRES  12 D  260  ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE          
SEQRES  13 D  260  HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA          
SEQRES  14 D  260  LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU          
SEQRES  15 D  260  LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU          
SEQRES  16 D  260  ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET          
SEQRES  17 D  260  GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS          
SEQRES  18 D  260  ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU          
SEQRES  19 D  260  LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU          
SEQRES  20 D  260  ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER          
SEQRES   1 E  234  MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE          
SEQRES   2 E  234  SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU          
SEQRES   3 E  234  GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG          
SEQRES   4 E  234  SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN          
SEQRES   5 E  234  ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS          
SEQRES   6 E  234  CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA          
SEQRES   7 E  234  PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN          
SEQRES   8 E  234  CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA          
SEQRES   9 E  234  VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN          
SEQRES  10 E  234  LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL          
SEQRES  11 E  234  GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS          
SEQRES  12 E  234  LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU          
SEQRES  13 E  234  TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS          
SEQRES  14 E  234  THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE          
SEQRES  15 E  234  ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU          
SEQRES  16 E  234  ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL          
SEQRES  17 E  234  ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO          
SEQRES  18 E  234  PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE          
SEQRES   1 F  288  MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER          
SEQRES   2 F  288  VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR          
SEQRES   3 F  288  ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY          
SEQRES   4 F  288  ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS          
SEQRES   5 F  288  LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL          
SEQRES   6 F  288  LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR          
SEQRES   7 F  288  SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG          
SEQRES   8 F  288  GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS          
SEQRES   9 F  288  THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY          
SEQRES  10 F  288  GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG          
SEQRES  11 F  288  PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS          
SEQRES  12 F  288  ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER          
SEQRES  13 F  288  TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG          
SEQRES  14 F  288  GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS          
SEQRES  15 F  288  HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN          
SEQRES  16 F  288  ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS          
SEQRES  17 F  288  GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU          
SEQRES  18 F  288  SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP          
SEQRES  19 F  288  LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE          
SEQRES  20 F  288  ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN          
SEQRES  21 F  288  VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR          
SEQRES  22 F  288  ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS          
SEQRES  23 F  288  LEU GLU                                                      
SEQRES   1 G  252  MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP          
SEQRES   2 G  252  ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR          
SEQRES   3 G  252  GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN          
SEQRES   4 G  252  ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL          
SEQRES   5 G  252  VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP          
SEQRES   6 G  252  PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR          
SEQRES   7 G  252  ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG          
SEQRES   8 G  252  ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE          
SEQRES   9 G  252  ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU          
SEQRES  10 G  252  ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN          
SEQRES  11 G  252  ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE          
SEQRES  12 G  252  VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS          
SEQRES  13 G  252  THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR          
SEQRES  14 G  252  ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU          
SEQRES  15 G  252  GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN          
SEQRES  16 G  252  GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR          
SEQRES  17 G  252  HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN          
SEQRES  18 G  252  ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE          
SEQRES  19 G  252  THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA          
SEQRES  20 G  252  ILE ALA GLU GLN ASP                                          
SEQRES   1 H  232  THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL          
SEQRES   2 H  232  ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL          
SEQRES   3 H  232  ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO          
SEQRES   4 H  232  LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR          
SEQRES   5 H  232  GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU          
SEQRES   6 H  232  HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER          
SEQRES   7 H  232  ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN          
SEQRES   8 H  232  GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP          
SEQRES   9 H  232  PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY          
SEQRES  10 H  232  SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY          
SEQRES  11 H  232  SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS          
SEQRES  12 H  232  GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER          
SEQRES  13 H  232  ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER          
SEQRES  14 H  232  GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS          
SEQRES  15 H  232  ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL          
SEQRES  16 H  232  ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY          
SEQRES  17 H  232  THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS          
SEQRES  18 H  232  ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA                  
SEQRES   1 I  205  MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL          
SEQRES   2 I  205  ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP          
SEQRES   3 I  205  LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS          
SEQRES   4 I  205  PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY          
SEQRES   5 I  205  ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU          
SEQRES   6 I  205  MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU          
SEQRES   7 I  205  GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL          
SEQRES   8 I  205  SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE          
SEQRES   9 I  205  VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY          
SEQRES  10 I  205  LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE          
SEQRES  11 I  205  ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER          
SEQRES  12 I  205  ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO          
SEQRES  13 I  205  ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN          
SEQRES  14 I  205  ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY          
SEQRES  15 I  205  TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL          
SEQRES  16 I  205  VAL LYS ARG TYR LEU LYS MET ARG GLN ASP                      
SEQRES   1 J  198  MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL          
SEQRES   2 J  198  ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER          
SEQRES   3 J  198  VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER          
SEQRES   4 J  198  PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP          
SEQRES   5 J  198  THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN          
SEQRES   6 J  198  LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN          
SEQRES   7 J  198  ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER          
SEQRES   8 J  198  ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE          
SEQRES   9 J  198  GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR          
SEQRES  10 J  198  GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR          
SEQRES  11 J  198  GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU          
SEQRES  12 J  198  LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU          
SEQRES  13 J  198  GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU          
SEQRES  14 J  198  LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS          
SEQRES  15 J  198  ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE          
SEQRES  16 J  198  GLN ALA GLN                                                  
SEQRES   1 K  212  THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE          
SEQRES   2 K  212  VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL          
SEQRES   3 K  212  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 K  212  PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 K  212  GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU          
SEQRES   6 K  212  HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 K  212  ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS          
SEQRES   8 K  212  GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR          
SEQRES   9 K  212  THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER          
SEQRES  10 K  212  ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY          
SEQRES  11 K  212  SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN          
SEQRES  12 K  212  TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU          
SEQRES  13 K  212  GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA          
SEQRES  14 K  212  TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU          
SEQRES  15 K  212  ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU          
SEQRES  16 K  212  LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN          
SEQRES  17 K  212  ASN VAL ILE GLY                                              
SEQRES   1 L  222  GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU          
SEQRES   2 L  222  GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP          
SEQRES   3 L  222  THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR          
SEQRES   4 L  222  GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET          
SEQRES   5 L  222  SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL          
SEQRES   6 L  222  LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP          
SEQRES   7 L  222  HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG          
SEQRES   8 L  222  ASN ILE GLN HIS LEU LEU TYR GLY LYS ARG PHE PHE PRO          
SEQRES   9 L  222  TYR TYR VAL HIS THR ILE ILE ALA GLY LEU ASP GLU ASP          
SEQRES  10 L  222  GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER          
SEQRES  11 L  222  TYR GLU ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA          
SEQRES  12 L  222  SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE          
SEQRES  13 L  222  LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS          
SEQRES  14 L  222  LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS          
SEQRES  15 L  222  LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS          
SEQRES  16 L  222  ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR          
SEQRES  17 L  222  LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG          
SEQRES  18 L  222  ASP                                                          
SEQRES   1 M  246  THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN          
SEQRES   2 M  246  THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER          
SEQRES   3 M  246  MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN          
SEQRES   4 M  246  LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL          
SEQRES   5 M  246  GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY          
SEQRES   6 M  246  ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG          
SEQRES   7 M  246  LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN          
SEQRES   8 M  246  PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR          
SEQRES   9 M  246  ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG          
SEQRES  10 M  246  SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA          
SEQRES  11 M  246  GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL          
SEQRES  12 M  246  ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA          
SEQRES  13 M  246  THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG          
SEQRES  14 M  246  LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR          
SEQRES  15 M  246  VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG          
SEQRES  16 M  246  VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE          
SEQRES  17 M  246  SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE          
SEQRES  18 M  246  LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE          
SEQRES  19 M  246  ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE              
SEQRES   1 N  196  THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE          
SEQRES   2 N  196  LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE          
SEQRES   3 N  196  ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP          
SEQRES   4 N  196  LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 N  196  GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU          
SEQRES   6 N  196  TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA          
SEQRES   7 N  196  ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP          
SEQRES   8 N  196  ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP          
SEQRES   9 N  196  LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY          
SEQRES  10 N  196  SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY          
SEQRES  11 N  196  SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG          
SEQRES  12 N  196  GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS          
SEQRES  13 N  196  HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER          
SEQRES  14 N  196  GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY          
SEQRES  15 N  196  VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN          
SEQRES  16 N  196  LEU                                                          
SEQRES   1 O  250  MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER          
SEQRES   2 O  250  PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR          
SEQRES   3 O  250  ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA          
SEQRES   4 O  250  THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER          
SEQRES   5 O  250  SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER          
SEQRES   6 O  250  LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET          
SEQRES   7 O  250  GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS          
SEQRES   8 O  250  VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR          
SEQRES   9 O  250  PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE          
SEQRES  10 O  250  MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE          
SEQRES  11 O  250  GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN          
SEQRES  12 O  250  GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR          
SEQRES  13 O  250  PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL          
SEQRES  14 O  250  ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU          
SEQRES  15 O  250  LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR          
SEQRES  16 O  250  LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR          
SEQRES  17 O  250  ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU          
SEQRES  18 O  250  LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG          
SEQRES  19 O  250  PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU          
SEQRES  20 O  250  GLU ALA LEU                                                  
SEQRES   1 P  258  MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE          
SEQRES   2 P  258  SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU          
SEQRES   3 P  258  GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET          
SEQRES   4 P  258  ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL          
SEQRES   5 P  258  THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS          
SEQRES   6 P  258  LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA          
SEQRES   7 P  258  GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA          
SEQRES   8 P  258  ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU          
SEQRES   9 P  258  ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP          
SEQRES  10 P  258  ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO          
SEQRES  11 P  258  PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG          
SEQRES  12 P  258  TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN          
SEQRES  13 P  258  TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR          
SEQRES  14 P  258  SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP          
SEQRES  15 P  258  ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS          
SEQRES  16 P  258  THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR          
SEQRES  17 P  258  ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN          
SEQRES  18 P  258  ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU          
SEQRES  19 P  258  ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS          
SEQRES  20 P  258  ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS                  
SEQRES   1 Q  254  MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO          
SEQRES   2 Q  254  ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA          
SEQRES   3 Q  254  VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS          
SEQRES   4 Q  254  ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU          
SEQRES   5 Q  254  LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER          
SEQRES   6 Q  254  LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU          
SEQRES   7 Q  254  ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL          
SEQRES   8 Q  254  GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL          
SEQRES   9 Q  254  THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN          
SEQRES  10 Q  254  GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY          
SEQRES  11 Q  254  VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP          
SEQRES  12 Q  254  GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR          
SEQRES  13 Q  254  SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS          
SEQRES  14 Q  254  THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS          
SEQRES  15 Q  254  GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR          
SEQRES  16 Q  254  VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS          
SEQRES  17 Q  254  ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE          
SEQRES  18 Q  254  VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR          
SEQRES  19 Q  254  GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP          
SEQRES  20 Q  254  LYS LYS LYS LYS SER ASN HIS                                  
SEQRES   1 R  260  MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER          
SEQRES   2 R  260  THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR          
SEQRES   3 R  260  SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY          
SEQRES   4 R  260  ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS          
SEQRES   5 R  260  ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU          
SEQRES   6 R  260  LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET          
SEQRES   7 R  260  SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS          
SEQRES   8 R  260  ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP          
SEQRES   9 R  260  GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS          
SEQRES  10 R  260  ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU          
SEQRES  11 R  260  GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU          
SEQRES  12 R  260  ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE          
SEQRES  13 R  260  HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA          
SEQRES  14 R  260  LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU          
SEQRES  15 R  260  LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU          
SEQRES  16 R  260  ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET          
SEQRES  17 R  260  GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS          
SEQRES  18 R  260  ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU          
SEQRES  19 R  260  LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU          
SEQRES  20 R  260  ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER          
SEQRES   1 S  234  MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE          
SEQRES   2 S  234  SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU          
SEQRES   3 S  234  GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG          
SEQRES   4 S  234  SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN          
SEQRES   5 S  234  ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS          
SEQRES   6 S  234  CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA          
SEQRES   7 S  234  PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN          
SEQRES   8 S  234  CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA          
SEQRES   9 S  234  VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN          
SEQRES  10 S  234  LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL          
SEQRES  11 S  234  GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS          
SEQRES  12 S  234  LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU          
SEQRES  13 S  234  TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS          
SEQRES  14 S  234  THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE          
SEQRES  15 S  234  ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU          
SEQRES  16 S  234  ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL          
SEQRES  17 S  234  ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO          
SEQRES  18 S  234  PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE          
SEQRES   1 T  288  MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER          
SEQRES   2 T  288  VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR          
SEQRES   3 T  288  ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY          
SEQRES   4 T  288  ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS          
SEQRES   5 T  288  LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL          
SEQRES   6 T  288  LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR          
SEQRES   7 T  288  SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG          
SEQRES   8 T  288  GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS          
SEQRES   9 T  288  THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY          
SEQRES  10 T  288  GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG          
SEQRES  11 T  288  PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS          
SEQRES  12 T  288  ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER          
SEQRES  13 T  288  TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG          
SEQRES  14 T  288  GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS          
SEQRES  15 T  288  HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN          
SEQRES  16 T  288  ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS          
SEQRES  17 T  288  GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU          
SEQRES  18 T  288  SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP          
SEQRES  19 T  288  LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE          
SEQRES  20 T  288  ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN          
SEQRES  21 T  288  VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR          
SEQRES  22 T  288  ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS          
SEQRES  23 T  288  LEU GLU                                                      
SEQRES   1 U  252  MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP          
SEQRES   2 U  252  ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR          
SEQRES   3 U  252  GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN          
SEQRES   4 U  252  ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL          
SEQRES   5 U  252  VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP          
SEQRES   6 U  252  PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR          
SEQRES   7 U  252  ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG          
SEQRES   8 U  252  ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE          
SEQRES   9 U  252  ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU          
SEQRES  10 U  252  ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN          
SEQRES  11 U  252  ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE          
SEQRES  12 U  252  VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS          
SEQRES  13 U  252  THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR          
SEQRES  14 U  252  ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU          
SEQRES  15 U  252  GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN          
SEQRES  16 U  252  GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR          
SEQRES  17 U  252  HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN          
SEQRES  18 U  252  ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE          
SEQRES  19 U  252  THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA          
SEQRES  20 U  252  ILE ALA GLU GLN ASP                                          
SEQRES   1 V  232  THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL          
SEQRES   2 V  232  ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL          
SEQRES   3 V  232  ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO          
SEQRES   4 V  232  LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR          
SEQRES   5 V  232  GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU          
SEQRES   6 V  232  HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER          
SEQRES   7 V  232  ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN          
SEQRES   8 V  232  GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP          
SEQRES   9 V  232  PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY          
SEQRES  10 V  232  SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY          
SEQRES  11 V  232  SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS          
SEQRES  12 V  232  GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER          
SEQRES  13 V  232  ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER          
SEQRES  14 V  232  GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS          
SEQRES  15 V  232  ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL          
SEQRES  16 V  232  ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY          
SEQRES  17 V  232  THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS          
SEQRES  18 V  232  ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA                  
SEQRES   1 W  205  MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL          
SEQRES   2 W  205  ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP          
SEQRES   3 W  205  LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS          
SEQRES   4 W  205  PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY          
SEQRES   5 W  205  ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU          
SEQRES   6 W  205  MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU          
SEQRES   7 W  205  GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL          
SEQRES   8 W  205  SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE          
SEQRES   9 W  205  VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY          
SEQRES  10 W  205  LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE          
SEQRES  11 W  205  ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER          
SEQRES  12 W  205  ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO          
SEQRES  13 W  205  ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN          
SEQRES  14 W  205  ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY          
SEQRES  15 W  205  TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL          
SEQRES  16 W  205  VAL LYS ARG TYR LEU LYS MET ARG GLN ASP                      
SEQRES   1 X  198  MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL          
SEQRES   2 X  198  ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER          
SEQRES   3 X  198  VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER          
SEQRES   4 X  198  PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP          
SEQRES   5 X  198  THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN          
SEQRES   6 X  198  LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN          
SEQRES   7 X  198  ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER          
SEQRES   8 X  198  ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE          
SEQRES   9 X  198  GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR          
SEQRES  10 X  198  GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR          
SEQRES  11 X  198  GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU          
SEQRES  12 X  198  LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU          
SEQRES  13 X  198  GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU          
SEQRES  14 X  198  LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS          
SEQRES  15 X  198  ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE          
SEQRES  16 X  198  GLN ALA GLN                                                  
SEQRES   1 Y  212  THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE          
SEQRES   2 Y  212  VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL          
SEQRES   3 Y  212  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 Y  212  PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 Y  212  GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU          
SEQRES   6 Y  212  HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 Y  212  ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS          
SEQRES   8 Y  212  GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR          
SEQRES   9 Y  212  THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER          
SEQRES  10 Y  212  ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY          
SEQRES  11 Y  212  SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN          
SEQRES  12 Y  212  TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU          
SEQRES  13 Y  212  GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA          
SEQRES  14 Y  212  TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU          
SEQRES  15 Y  212  ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU          
SEQRES  16 Y  212  LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN          
SEQRES  17 Y  212  ASN VAL ILE GLY                                              
SEQRES   1 Z  222  GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU          
SEQRES   2 Z  222  GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP          
SEQRES   3 Z  222  THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR          
SEQRES   4 Z  222  GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET          
SEQRES   5 Z  222  SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL          
SEQRES   6 Z  222  LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP          
SEQRES   7 Z  222  HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG          
SEQRES   8 Z  222  ASN ILE GLN HIS LEU LEU TYR GLY LYS ARG PHE PHE PRO          
SEQRES   9 Z  222  TYR TYR VAL HIS THR ILE ILE ALA GLY LEU ASP GLU ASP          
SEQRES  10 Z  222  GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER          
SEQRES  11 Z  222  TYR GLU ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA          
SEQRES  12 Z  222  SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE          
SEQRES  13 Z  222  LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS          
SEQRES  14 Z  222  LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS          
SEQRES  15 Z  222  LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS          
SEQRES  16 Z  222  ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR          
SEQRES  17 Z  222  LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG          
SEQRES  18 Z  222  ASP                                                          
SEQRES   1 a  246  THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN          
SEQRES   2 a  246  THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER          
SEQRES   3 a  246  MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN          
SEQRES   4 a  246  LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL          
SEQRES   5 a  246  GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY          
SEQRES   6 a  246  ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG          
SEQRES   7 a  246  LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN          
SEQRES   8 a  246  PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR          
SEQRES   9 a  246  ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG          
SEQRES  10 a  246  SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA          
SEQRES  11 a  246  GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL          
SEQRES  12 a  246  ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA          
SEQRES  13 a  246  THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG          
SEQRES  14 a  246  LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR          
SEQRES  15 a  246  VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG          
SEQRES  16 a  246  VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE          
SEQRES  17 a  246  SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE          
SEQRES  18 a  246  LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE          
SEQRES  19 a  246  ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE              
SEQRES   1 b  196  THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE          
SEQRES   2 b  196  LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE          
SEQRES   3 b  196  ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP          
SEQRES   4 b  196  LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 b  196  GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU          
SEQRES   6 b  196  TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA          
SEQRES   7 b  196  ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP          
SEQRES   8 b  196  ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP          
SEQRES   9 b  196  LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY          
SEQRES  10 b  196  SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY          
SEQRES  11 b  196  SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG          
SEQRES  12 b  196  GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS          
SEQRES  13 b  196  HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER          
SEQRES  14 b  196  GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY          
SEQRES  15 b  196  VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN          
SEQRES  16 b  196  LEU                                                          
HET     MG  G 301       1                                                       
HET     CL  G 302       1                                                       
HET    BO2  H 301      28                                                       
HET     MG  I 301       1                                                       
HET     MG  J 201       1                                                       
HET    BO2  K 301      28                                                       
HET     MG  K 302       1                                                       
HET    BO2  N 201      28                                                       
HET     MG  N 202       1                                                       
HET     CL  N 203       1                                                       
HET     CL  U 301       1                                                       
HET    BO2  V 301      28                                                       
HET     MG  V 302       1                                                       
HET    BO2  Y 301      28                                                       
HET     MG  Y 302       1                                                       
HET     MG  Z 301       1                                                       
HET    BO2  b 201      28                                                       
HET     CL  b 202       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-          
HETNAM   2 BO2  YLCARBONYL)-L-PHENYLALANINAMIDE                                 
HETSYN     BO2 BORTEZOMIB                                                       
FORMUL  29   MG    8(MG 2+)                                                     
FORMUL  30   CL    4(CL 1-)                                                     
FORMUL  31  BO2    6(C19 H25 B N4 O4)                                           
FORMUL  47  HOH   *357(H2 O)                                                    
HELIX    1   1 LEU A   18  GLY A   31  1                                  14    
HELIX    2   2 MET A   78  SER A   96  1                                  19    
HELIX    3   3 TYR A   97  GLY A  102  1                                   6    
HELIX    4   4 PRO A  106  ALA A  121  1                                  16    
HELIX    5   5 GLY A  167  TRP A  179  1                                  13    
HELIX    6   6 GLU A  184  VAL A  200  1                                  17    
HELIX    7   7 ASN A  218  LEU A  222  5                                   5    
HELIX    8   8 THR A  239  ALA A  249  1                                  11    
HELIX    9   9 GLY B    1  ASP B    6  5                                   6    
HELIX   10  10 LEU B   18  SER B   29  1                                  12    
HELIX   11  11 LEU B   79  ASN B  102  1                                  24    
HELIX   12  12 PRO B  106  HIS B  124  1                                  19    
HELIX   13  13 ASN B  167  TYR B  179  1                                  13    
HELIX   14  14 LYS B  184  THR B  200  1                                  17    
HELIX   15  15 THR B  206  ASP B  208  5                                   3    
HELIX   16  16 LYS B  230  THR B  241  1                                  12    
HELIX   17  17 ILE C   15  GLY C   28  1                                  14    
HELIX   18  18 LEU C   76  GLU C   99  1                                  24    
HELIX   19  19 THR C  103  TYR C  118  1                                  16    
HELIX   20  20 ASN C  165  TYR C  177  1                                  13    
HELIX   21  21 THR C  185  GLU C  199  1                                  15    
HELIX   22  22 SER C  223  GLN C  239  1                                  17    
HELIX   23  23 LEU D   13  LEU D   25  1                                  13    
HELIX   24  24 GLU D   52  ILE D   56  5                                   5    
HELIX   25  25 ASP D   76  ASP D   96  1                                  21    
HELIX   26  26 ASN D  100  LEU D  113  1                                  14    
HELIX   27  27 GLY D  167  TRP D  179  1                                  13    
HELIX   28  28 THR D  184  MET D  200  1                                  17    
HELIX   29  29 ASP D  224  ALA D  241  1                                  18    
HELIX   30  30 LEU E   18  GLY E   31  1                                  14    
HELIX   31  31 LEU E   76  ASN E   99  1                                  24    
HELIX   32  32 ALA E  103  SER E  121  1                                  19    
HELIX   33  33 ARG E  163  ILE E  179  1                                  17    
HELIX   34  34 ASN E  184  SER E  197  1                                  14    
HELIX   35  35 GLN E  198  LEU E  200  5                                   3    
HELIX   36  36 ASP E  225  ILE E  233  5                                   9    
HELIX   37  37 ASN F   17  GLY F   30  1                                  14    
HELIX   38  38 LEU F   77  LYS F  100  1                                  24    
HELIX   39  39 PRO F  104  HIS F  119  1                                  16    
HELIX   40  40 GLY F  164  HIS F  179  1                                  16    
HELIX   41  41 SER F  184  HIS F  200  1                                  17    
HELIX   42  42 GLU F  201  LYS F  204  5                                   4    
HELIX   43  43 LYS F  228  ASN F  244  1                                  17    
HELIX   44  44 GLY G    2  HIS G    6  5                                   5    
HELIX   45  45 LEU G   16  THR G   26  1                                  11    
HELIX   46  46 ASP G   56  VAL G   60  5                                   5    
HELIX   47  47 PRO G   77  GLY G  100  1                                  24    
HELIX   48  48 PRO G  104  ARG G  122  1                                  19    
HELIX   49  49 LYS G  165  LYS G  181  1                                  17    
HELIX   50  50 SER G  189  GLY G  206  1                                  18    
HELIX   51  51 SER G  228  GLU G  241  1                                  14    
HELIX   52  52 THR H   48  SER H   71  1                                  24    
HELIX   53  53 ARG H   75  TYR H   90  1                                  16    
HELIX   54  54 GLY H  130  TRP H  142  1                                  13    
HELIX   55  55 THR H  147  ASP H  166  1                                  20    
HELIX   56  56 ASP I    2  ILE I    6  5                                   5    
HELIX   57  57 LEU I   55  GLU I   78  1                                  24    
HELIX   58  58 GLU I   82  GLU I   96  1                                  15    
HELIX   59  59 ALA I  141  TYR I  153  1                                  13    
HELIX   60  60 GLU I  158  ASP I  175  1                                  18    
HELIX   61  61 GLY J   51  ASP J   72  1                                  22    
HELIX   62  62 SER J   76  ILE J   92  1                                  17    
HELIX   63  63 TYR J  135  TYR J  148  1                                  14    
HELIX   64  64 THR J  153  MET J  172  1                                  20    
HELIX   65  65 GLY K   48  LYS K   71  1                                  24    
HELIX   66  66 SER K   75  TYR K   90  1                                  16    
HELIX   67  67 GLY K  132  TYR K  144  1                                  13    
HELIX   68  68 SER K  149  ASP K  168  1                                  20    
HELIX   69  69 VAL K  193  GLY K  205  1                                  13    
HELIX   70  70 PHE L   57  HIS L   79  1                                  23    
HELIX   71  71 SER L   85  GLY L   99  1                                  15    
HELIX   72  72 ALA L  142  VAL L  154  1                                  13    
HELIX   73  73 SER L  176  HIS L  195  1                                  20    
HELIX   74  74 ILE M   57  TYR M   76  1                                  20    
HELIX   75  75 GLU M   88  LYS M  106  1                                  19    
HELIX   76  76 GLY M  145  LYS M  157  1                                  13    
HELIX   77  77 ARG M  161  ILE M  165  5                                   5    
HELIX   78  78 THR M  169  ASP M  188  1                                  20    
HELIX   79  79 TRP M  219  ILE M  225  5                                   7    
HELIX   80  80 SER N   48  GLY N   71  1                                  24    
HELIX   81  81 SER N   74  ASN N   89  1                                  16    
HELIX   82  82 GLY N  128  PHE N  133  5                                   6    
HELIX   83  83 ILE N  134  PHE N  142  1                                   9    
HELIX   84  84 SER N  147  ASP N  166  1                                  20    
HELIX   85  85 TYR N  189  GLU N  194  1                                   6    
HELIX   86  86 LEU O   18  GLY O   31  1                                  14    
HELIX   87  87 MET O   78  SER O   96  1                                  19    
HELIX   88  88 TYR O   97  GLY O  102  1                                   6    
HELIX   89  89 PRO O  106  ALA O  121  1                                  16    
HELIX   90  90 GLY O  167  TRP O  179  1                                  13    
HELIX   91  91 GLU O  184  VAL O  200  1                                  17    
HELIX   92  92 ASN O  218  LEU O  222  5                                   5    
HELIX   93  93 THR O  239  ALA O  249  1                                  11    
HELIX   94  94 GLY P    1  ASP P    6  5                                   6    
HELIX   95  95 LEU P   18  SER P   29  1                                  12    
HELIX   96  96 GLU P   57  SER P   61  5                                   5    
HELIX   97  97 LEU P   79  ASN P  102  1                                  24    
HELIX   98  98 PRO P  106  HIS P  124  1                                  19    
HELIX   99  99 ASN P  167  TYR P  179  1                                  13    
HELIX  100 100 LYS P  184  THR P  200  1                                  17    
HELIX  101 101 THR P  206  ASP P  208  5                                   3    
HELIX  102 102 LYS P  230  THR P  241  1                                  12    
HELIX  103 103 ILE Q   15  GLY Q   28  1                                  14    
HELIX  104 104 LEU Q   76  GLU Q   99  1                                  24    
HELIX  105 105 THR Q  103  TYR Q  118  1                                  16    
HELIX  106 106 ASN Q  165  TYR Q  177  1                                  13    
HELIX  107 107 THR Q  185  GLU Q  199  1                                  15    
HELIX  108 108 SER Q  223  GLN Q  239  1                                  17    
HELIX  109 109 LEU R   13  LEU R   25  1                                  13    
HELIX  110 110 GLU R   52  ILE R   56  5                                   5    
HELIX  111 111 ASP R   76  ASP R   96  1                                  21    
HELIX  112 112 ASN R  100  LEU R  113  1                                  14    
HELIX  113 113 GLY R  167  TRP R  179  1                                  13    
HELIX  114 114 THR R  184  MET R  200  1                                  17    
HELIX  115 115 ASP R  224  ALA R  241  1                                  18    
HELIX  116 116 LEU S   18  GLY S   31  1                                  14    
HELIX  117 117 LEU S   76  ASN S   99  1                                  24    
HELIX  118 118 ALA S  103  SER S  121  1                                  19    
HELIX  119 119 ARG S  163  ILE S  179  1                                  17    
HELIX  120 120 ASN S  184  SER S  197  1                                  14    
HELIX  121 121 GLN S  198  LEU S  200  5                                   3    
HELIX  122 122 ASP S  225  ILE S  233  5                                   9    
HELIX  123 123 ASN T   17  GLY T   30  1                                  14    
HELIX  124 124 LEU T   77  LYS T  100  1                                  24    
HELIX  125 125 PRO T  104  HIS T  119  1                                  16    
HELIX  126 126 GLY T  164  HIS T  179  1                                  16    
HELIX  127 127 SER T  184  HIS T  200  1                                  17    
HELIX  128 128 GLU T  201  LYS T  204  5                                   4    
HELIX  129 129 LYS T  228  ASN T  244  1                                  17    
HELIX  130 130 GLY U    2  HIS U    6  5                                   5    
HELIX  131 131 LEU U   16  THR U   26  1                                  11    
HELIX  132 132 ASP U   56  VAL U   60  5                                   5    
HELIX  133 133 PRO U   77  GLY U  100  1                                  24    
HELIX  134 134 PRO U  104  ARG U  122  1                                  19    
HELIX  135 135 LYS U  165  LYS U  181  1                                  17    
HELIX  136 136 SER U  189  GLY U  206  1                                  18    
HELIX  137 137 SER U  228  GLU U  241  1                                  14    
HELIX  138 138 THR V   48  SER V   71  1                                  24    
HELIX  139 139 ARG V   75  TYR V   90  1                                  16    
HELIX  140 140 GLY V  130  TRP V  142  1                                  13    
HELIX  141 141 THR V  147  ASP V  166  1                                  20    
HELIX  142 142 ASP W    2  ILE W    6  5                                   5    
HELIX  143 143 LEU W   55  GLU W   78  1                                  24    
HELIX  144 144 GLU W   82  GLU W   96  1                                  15    
HELIX  145 145 ALA W  141  TYR W  153  1                                  13    
HELIX  146 146 GLU W  158  ASP W  175  1                                  18    
HELIX  147 147 GLY X   51  ASP X   72  1                                  22    
HELIX  148 148 SER X   76  ILE X   92  1                                  17    
HELIX  149 149 TYR X  135  TYR X  148  1                                  14    
HELIX  150 150 THR X  153  MET X  172  1                                  20    
HELIX  151 151 GLY Y   48  LYS Y   71  1                                  24    
HELIX  152 152 SER Y   75  TYR Y   90  1                                  16    
HELIX  153 153 GLY Y  132  TYR Y  144  1                                  13    
HELIX  154 154 SER Y  149  ASP Y  168  1                                  20    
HELIX  155 155 VAL Y  193  GLY Y  205  1                                  13    
HELIX  156 156 PHE Z   57  HIS Z   79  1                                  23    
HELIX  157 157 SER Z   85  GLY Z   99  1                                  15    
HELIX  158 158 ALA Z  142  VAL Z  154  1                                  13    
HELIX  159 159 SER Z  176  HIS Z  195  1                                  20    
HELIX  160 160 ILE a   57  TYR a   76  1                                  20    
HELIX  161 161 GLU a   88  LYS a  106  1                                  19    
HELIX  162 162 GLY a  145  LYS a  157  1                                  13    
HELIX  163 163 ARG a  161  ILE a  165  5                                   5    
HELIX  164 164 THR a  169  ASP a  188  1                                  20    
HELIX  165 165 TRP a  219  ILE a  225  5                                   7    
HELIX  166 166 SER b   48  GLY b   71  1                                  24    
HELIX  167 167 SER b   74  ASN b   89  1                                  16    
HELIX  168 168 GLY b  128  PHE b  133  5                                   6    
HELIX  169 169 ILE b  134  PHE b  142  1                                   9    
HELIX  170 170 SER b  147  ASP b  166  1                                  20    
HELIX  171 171 TYR b  189  GLU b  194  1                                   6    
SHEET    1   A 5 ALA A 161  ILE A 164  0                                        
SHEET    2   A 5 SER A  34  LYS A  38 -1  N  SER A  34   O  ILE A 164           
SHEET    3   A 5 VAL A  43  GLU A  48 -1  O  VAL A  44   N  ILE A  37           
SHEET    4   A 5 ILE A 209  ILE A 214 -1  O  ILE A 214   N  VAL A  43           
SHEET    5   A 5 PHE A 235  LYS A 237 -1  O  ARG A 236   N  ILE A 213           
SHEET    1   B 5 SER A  65  THR A  68  0                                        
SHEET    2   B 5 ILE A  71  GLY A  77 -1  O  ALA A  73   N  SER A  65           
SHEET    3   B 5 VAL A 132  ASP A 140 -1  O  ALA A 137   N  GLY A  72           
SHEET    4   B 5 GLY A 144  VAL A 150 -1  O  TYR A 148   N  ILE A 136           
SHEET    5   B 5 TYR A 156  PRO A 158 -1  O  PHE A 157   N  GLN A 149           
SHEET    1   C 6 TYR A 224  THR A 225  0                                        
SHEET    2   C 6 ALA H 184  LEU H 191  1  O  TYR H 186   N  THR A 225           
SHEET    3   C 6 VAL H 173  GLU H 179 -1  N  VAL H 177   O  GLU H 185           
SHEET    4   C 6 GLY H  11  ASP H  17 -1  N  ALA H  16   O  ASP H 174           
SHEET    5   C 6 ILE H   3  PHE H   8 -1  N  VAL H   6   O  VAL H  13           
SHEET    6   C 6 TYR H 124  LEU H 127 -1  O  LEU H 125   N  GLY H   5           
SHEET    1   D 5 ALA B 161  VAL B 164  0                                        
SHEET    2   D 5 ALA B  34  ALA B  39 -1  N  GLY B  36   O  ILE B 162           
SHEET    3   D 5 GLY B  42  GLU B  48 -1  O  ALA B  46   N  ILE B  35           
SHEET    4   D 5 LEU B 210  ARG B 216 -1  O  ALA B 213   N  LEU B  45           
SHEET    5   D 5 TYR B 225  ILE B 228 -1  O  TYR B 225   N  ARG B 216           
SHEET    1   E 5 LEU B  65  LYS B  67  0                                        
SHEET    2   E 5 ILE B  72  GLY B  78 -1  O  VAL B  74   N  TYR B  66           
SHEET    3   E 5 VAL B 132  ASP B 140 -1  O  ALA B 137   N  ALA B  73           
SHEET    4   E 5 GLY B 144  SER B 150 -1  O  TYR B 148   N  TYR B 136           
SHEET    5   E 5 TYR B 156  TRP B 159 -1  O  TRP B 159   N  LEU B 147           
SHEET    1   F 5 ALA C 159  ILE C 162  0                                        
SHEET    2   F 5 ALA C  31  LYS C  35 -1  N  GLY C  33   O  GLN C 160           
SHEET    3   F 5 VAL C  40  GLU C  45 -1  O  VAL C  41   N  VAL C  34           
SHEET    4   F 5 ILE C 208  LYS C 214 -1  O  VAL C 213   N  VAL C  40           
SHEET    5   F 5 ASP C 218  ALA C 221 -1  O  ASP C 218   N  LYS C 214           
SHEET    1   G 5 SER C  63  LYS C  64  0                                        
SHEET    2   G 5 VAL C  69  GLY C  75 -1  O  LEU C  71   N  SER C  63           
SHEET    3   G 5 VAL C 129  GLY C 135 -1  O  ALA C 134   N  VAL C  70           
SHEET    4   G 5 LYS C 144  THR C 148 -1  O  TYR C 146   N  ILE C 133           
SHEET    5   G 5 TYR C 154  SER C 156 -1  O  SER C 155   N  GLN C 147           
SHEET    1   H 5 ALA D 161  ILE D 164  0                                        
SHEET    2   H 5 ALA D  29  ALA D  33 -1  N  GLY D  31   O  LYS D 162           
SHEET    3   H 5 VAL D  38  GLU D  43 -1  O  GLY D  41   N  ILE D  30           
SHEET    4   H 5 ALA D 209  THR D 215 -1  O  SER D 212   N  LEU D  40           
SHEET    5   H 5 GLY D 219  ILE D 222 -1  O  LYS D 221   N  CYS D 213           
SHEET    1   I 5 ILE D  59  ASP D  63  0                                        
SHEET    2   I 5 ILE D  66  GLY D  72 -1  O  CYS D  68   N  VAL D  60           
SHEET    3   I 5 VAL D 132  ASP D 140 -1  O  ALA D 137   N  GLY D  67           
SHEET    4   I 5 GLY D 144  ALA D 150 -1  O  PHE D 148   N  ILE D 136           
SHEET    5   I 5 PHE D 156  ARG D 158 -1  O  TYR D 157   N  HIS D 149           
SHEET    1   J 5 GLY E 157  ILE E 160  0                                        
SHEET    2   J 5 THR E  34  ARG E  38 -1  N  GLY E  36   O  THR E 158           
SHEET    3   J 5 HIS E  42  LEU E  48 -1  O  VAL E  46   N  VAL E  35           
SHEET    4   J 5 LEU E 210  GLY E 216 -1  O  SER E 211   N  ALA E  47           
SHEET    5   J 5 THR E 219  TYR E 224 -1  O  TYR E 224   N  ILE E 212           
SHEET    1   K 5 ILE E  62  ASP E  66  0                                        
SHEET    2   K 5 MET E  69  GLY E  75 -1  O  MET E  69   N  ASP E  66           
SHEET    3   K 5 VAL E 129  ASP E 137 -1  O  GLY E 130   N  ALA E  74           
SHEET    4   K 5 GLY E 140  PHE E 146 -1  O  PHE E 146   N  LEU E 131           
SHEET    5   K 5 VAL E 152  GLU E 154 -1  O  THR E 153   N  GLU E 145           
SHEET    1   L 5 GLY F 158  THR F 161  0                                        
SHEET    2   L 5 SER F  33  LYS F  37 -1  N  GLY F  35   O  ALA F 159           
SHEET    3   L 5 GLY F  41  LEU F  49 -1  O  ALA F  45   N  ILE F  34           
SHEET    4   L 5 PHE F 208  SER F 216 -1  O  SER F 213   N  PHE F  44           
SHEET    5   L 5 HIS F 224  PHE F 226 -1  O  LYS F 225   N  TRP F 214           
SHEET    1   M 5 GLN F  64  VAL F  66  0                                        
SHEET    2   M 5 ILE F  70  GLY F  76 -1  O  CYS F  72   N  GLN F  64           
SHEET    3   M 5 VAL F 130  ASP F 138 -1  O  ILE F 133   N  VAL F  73           
SHEET    4   M 5 GLY F 141  LEU F 147 -1  O  TYR F 145   N  PHE F 134           
SHEET    5   M 5 TYR F 153  GLY F 155 -1  O  TRP F 154   N  MET F 146           
SHEET    1   N 5 ALA G 159  THR G 162  0                                        
SHEET    2   N 5 SER G  33  ARG G  37 -1  N  SER G  33   O  THR G 162           
SHEET    3   N 5 THR G  42  GLN G  47 -1  O  ILE G  45   N  LEU G  34           
SHEET    4   N 5 LEU G 214  THR G 220 -1  O  GLY G 217   N  VAL G  44           
SHEET    5   N 5 LYS G 223  THR G 226 -1  O  PHE G 225   N  VAL G 218           
SHEET    1   O 5 ILE G  63  CYS G  65  0                                        
SHEET    2   O 5 GLY G  71  ASN G  75 -1  O  MET G  72   N  PHE G  64           
SHEET    3   O 5 ILE G 131  ASP G 138 -1  O  VAL G 135   N  GLY G  71           
SHEET    4   O 5 GLY G 142  THR G 148 -1  O  TYR G 146   N  PHE G 134           
SHEET    5   O 5 TYR G 154  TYR G 157 -1  O  TYR G 157   N  ILE G 145           
SHEET    1   P 2 SER H  20  GLN H  22  0                                        
SHEET    2   P 2 ILE H  25  ASP H  28 -1  O  ASP H  28   N  SER H  20           
SHEET    1   Q 5 LEU H  34  SER H  38  0                                        
SHEET    2   Q 5 ILE H  41  GLY H  47 -1  O  CYS H  43   N  HIS H  35           
SHEET    3   Q 5 ALA H  96  ASP H 104 -1  O  TYR H  97   N  ALA H  46           
SHEET    4   Q 5 GLY H 107  ILE H 113 -1  O  ILE H 113   N  LEU H  98           
SHEET    5   Q 5 THR H 119  VAL H 121 -1  O  ASP H 120   N  SER H 112           
SHEET    1   R 6 VAL H 212  ILE H 217  0                                        
SHEET    2   R 6 GLU I 193  LEU I 199 -1  O  TYR I 198   N  LEU H 213           
SHEET    3   R 6 ALA I 184  LYS I 190 -1  N  ILE I 188   O  VAL I 195           
SHEET    4   R 6 CYS I  19  ASP I  25 -1  N  VAL I  20   O  ILE I 189           
SHEET    5   R 6 ILE I  10  GLY I  16 -1  N  VAL I  12   O  ALA I  23           
SHEET    6   R 6 PHE I 135  GLY I 139 -1  O  ILE I 136   N  ALA I  13           
SHEET    1   S 2 LEU I  28  SER I  30  0                                        
SHEET    2   S 2 LEU I  33  SER I  36 -1  O  LEU I  33   N  SER I  30           
SHEET    1   T 5 ILE I  42  TYR I  45  0                                        
SHEET    2   T 5 VAL I  48  GLY I  54 -1  O  LEU I  50   N  PHE I  43           
SHEET    3   T 5 VAL I 104  ILE I 111 -1  O  VAL I 107   N  GLY I  51           
SHEET    4   T 5 PRO I 118  PHE I 123 -1  O  ALA I 121   N  VAL I 108           
SHEET    5   T 5 ILE I 129  ASP I 130 -1  O  ASP I 130   N  GLY I 122           
SHEET    1   U 5 TYR J 130  HIS J 133  0                                        
SHEET    2   U 5 ILE J   4  ARG J   8 -1  N  GLY J   6   O  GLY J 131           
SHEET    3   U 5 SER J  12  SER J  18 -1  O  ALA J  16   N  LEU J   5           
SHEET    4   U 5 VAL J 179  ASP J 185 -1  O  ILE J 180   N  SER J  17           
SHEET    5   U 5 GLY J 188  VAL J 192 -1  O  ARG J 190   N  ILE J 183           
SHEET    1   V 2 VAL J  21  ARG J  23  0                                        
SHEET    2   V 2 SER J  26  LYS J  29 -1  O  SER J  26   N  ARG J  23           
SHEET    1   W 5 THR J  35  SER J  39  0                                        
SHEET    2   W 5 THR J  42  GLY J  48 -1  O  THR J  42   N  SER J  39           
SHEET    3   W 5 VAL J 100  ASP J 108 -1  O  GLY J 105   N  LEU J  43           
SHEET    4   W 5 LYS J 113  ILE J 119 -1  O  ILE J 119   N  VAL J 102           
SHEET    5   W 5 LYS J 125  LEU J 128 -1  O  VAL J 126   N  GLN J 118           
SHEET    1   X 5 ILE K 126  VAL K 129  0                                        
SHEET    2   X 5 THR K   3  PHE K   8 -1  N  THR K   3   O  VAL K 129           
SHEET    3   X 5 GLY K  11  VAL K  16 -1  O  ALA K  15   N  LEU K   4           
SHEET    4   X 5 SER K 174  THR K 181 -1  O  VAL K 180   N  ILE K  12           
SHEET    5   X 5 GLY K 184  ASP K 192 -1  O  HIS K 188   N  LEU K 177           
SHEET    1   Y 2 ALA K  20  ALA K  22  0                                        
SHEET    2   Y 2 TRP K  25  SER K  28 -1  O  TRP K  25   N  ALA K  22           
SHEET    1   Z 5 VAL K  34  GLU K  36  0                                        
SHEET    2   Z 5 LEU K  41  THR K  44 -1  O  GLY K  43   N  ILE K  35           
SHEET    3   Z 5 GLY K  98  THR K 105 -1  O  CYS K 102   N  LEU K  42           
SHEET    4   Z 5 GLY K 109  ASP K 116 -1  O  VAL K 115   N  THR K  99           
SHEET    5   Z 5 ARG K 121  LYS K 123 -1  O  LEU K 122   N  TYR K 114           
SHEET    1  AA 5 CYS L 136  GLY L 140  0                                        
SHEET    2  AA 5 THR L  11  ALA L  16 -1  N  GLY L  14   O  ARG L 137           
SHEET    3  AA 5 ALA L  21  ASP L  26 -1  O  ALA L  24   N  LEU L  13           
SHEET    4  AA 5 GLY L 201  THR L 208 -1  O  VAL L 207   N  ALA L  21           
SHEET    5  AA 5 GLY L 211  GLU L 218 -1  O  TYR L 217   N  LEU L 202           
SHEET    1  AB 2 ASN L  29  THR L  31  0                                        
SHEET    2  AB 2 SER L  34  SER L  37 -1  O  ASN L  36   N  ASN L  29           
SHEET    1  AC 5 VAL L  43  ASP L  45  0                                        
SHEET    2  AC 5 VAL L  51  GLY L  56 -1  O  MET L  52   N  PHE L  44           
SHEET    3  AC 5 VAL L 107  LEU L 114 -1  O  HIS L 108   N  ASN L  55           
SHEET    4  AC 5 GLY L 120  PHE L 125 -1  O  ALA L 121   N  GLY L 113           
SHEET    5  AC 5 TYR L 131  GLU L 134 -1  O  GLU L 134   N  VAL L 122           
SHEET    1  AD 5 LEU M  33  PHE M  36  0                                        
SHEET    2  AD 5 GLY M  28  TYR M  30 -1  N  TYR M  30   O  LEU M  33           
SHEET    3  AD 5 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4  AD 5 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5  AD 5 LEU M  42  VAL M  45 -1  N  ILE M  43   O  VAL M  51           
SHEET    1  AE 7 LEU M  33  PHE M  36  0                                        
SHEET    2  AE 7 GLY M  28  TYR M  30 -1  N  TYR M  30   O  LEU M  33           
SHEET    3  AE 7 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4  AE 7 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5  AE 7 ASN M 112  VAL M 119 -1  O  ALA M 117   N  VAL M  50           
SHEET    6  AE 7 GLN M 125  ASN M 131 -1  O  VAL M 130   N  ILE M 114           
SHEET    7  AE 7 THR M 136  SER M 138 -1  O  TYR M 137   N  TYR M 129           
SHEET    1  AF 5 THR M 141  ALA M 143  0                                        
SHEET    2  AF 5 VAL M  11  TYR M  16 -1  N  SER M  13   O  LEU M 142           
SHEET    3  AF 5 GLY M  19  ASP M  25 -1  O  GLY M  19   N  TYR M  16           
SHEET    4  AF 5 ASN M 194  ASP M 201 -1  O  ALA M 198   N  ILE M  22           
SHEET    5  AF 5 GLY M 205  GLN M 213 -1  O  LYS M 209   N  LEU M 197           
SHEET    1  AG 5 TYR N 124  ALA N 127  0                                        
SHEET    2  AG 5 ILE N   3  PHE N   8 -1  N  ALA N   5   O  ALA N 125           
SHEET    3  AG 5 GLY N  11  ALA N  16 -1  O  GLY N  15   N  MET N   4           
SHEET    4  AG 5 ILE N 173  THR N 179 -1  O  LEU N 178   N  VAL N  12           
SHEET    5  AG 5 GLY N 182  PHE N 188 -1  O  GLU N 184   N  VAL N 177           
SHEET    1  AH 2 THR N  20  THR N  22  0                                        
SHEET    2  AH 2 TYR N  25  ASN N  28 -1  O  TYR N  25   N  THR N  22           
SHEET    1  AI 5 LEU N  34  HIS N  38  0                                        
SHEET    2  AI 5 ILE N  41  GLY N  47 -1  O  CYS N  43   N  THR N  35           
SHEET    3  AI 5 ALA N  95  TYR N 102 -1  O  GLY N  96   N  SER N  46           
SHEET    4  AI 5 GLY N 108  ILE N 113 -1  O  TYR N 111   N  VAL N  99           
SHEET    5  AI 5 HIS N 120  LEU N 122 -1  O  HIS N 120   N  THR N 112           
SHEET    1  AJ 5 ALA O 161  ILE O 164  0                                        
SHEET    2  AJ 5 SER O  34  LYS O  38 -1  N  SER O  34   O  ILE O 164           
SHEET    3  AJ 5 VAL O  43  GLU O  48 -1  O  VAL O  44   N  ILE O  37           
SHEET    4  AJ 5 ILE O 209  ILE O 214 -1  O  ILE O 214   N  VAL O  43           
SHEET    5  AJ 5 PHE O 235  LYS O 237 -1  O  ARG O 236   N  ILE O 213           
SHEET    1  AK 6 ALA O  56  MET O  57  0                                        
SHEET    2  AK 6 TYR U 154  TYR U 157 -1  O  GLY U 156   N  MET O  57           
SHEET    3  AK 6 GLY U 142  THR U 148 -1  N  ILE U 145   O  TYR U 157           
SHEET    4  AK 6 ILE U 131  ASP U 138 -1  N  PHE U 134   O  TYR U 146           
SHEET    5  AK 6 GLY U  71  ASN U  75 -1  N  GLY U  71   O  VAL U 135           
SHEET    6  AK 6 ILE U  63  CYS U  65 -1  N  PHE U  64   O  MET U  72           
SHEET    1  AL 5 SER O  65  THR O  68  0                                        
SHEET    2  AL 5 ILE O  71  GLY O  77 -1  O  ALA O  73   N  SER O  65           
SHEET    3  AL 5 VAL O 132  ASP O 140 -1  O  ALA O 137   N  GLY O  72           
SHEET    4  AL 5 GLY O 144  VAL O 150 -1  O  TYR O 148   N  ILE O 136           
SHEET    5  AL 5 TYR O 156  PRO O 158 -1  O  PHE O 157   N  GLN O 149           
SHEET    1  AM 6 TYR O 224  THR O 225  0                                        
SHEET    2  AM 6 ALA V 184  LEU V 191  1  O  TYR V 186   N  THR O 225           
SHEET    3  AM 6 VAL V 173  GLU V 179 -1  N  VAL V 175   O  LEU V 187           
SHEET    4  AM 6 GLY V  11  ASP V  17 -1  N  ALA V  16   O  ASP V 174           
SHEET    5  AM 6 ILE V   3  PHE V   8 -1  N  VAL V   6   O  VAL V  13           
SHEET    6  AM 6 TYR V 124  LEU V 127 -1  O  LEU V 127   N  ILE V   3           
SHEET    1  AN 5 ALA P 161  VAL P 164  0                                        
SHEET    2  AN 5 ALA P  34  ALA P  39 -1  N  GLY P  36   O  ILE P 162           
SHEET    3  AN 5 GLY P  42  GLU P  48 -1  O  ALA P  46   N  ILE P  35           
SHEET    4  AN 5 LEU P 210  ARG P 216 -1  O  ALA P 213   N  LEU P  45           
SHEET    5  AN 5 TYR P 225  ILE P 228 -1  O  TYR P 225   N  ARG P 216           
SHEET    1  AO 5 LEU P  65  LYS P  67  0                                        
SHEET    2  AO 5 ILE P  72  GLY P  78 -1  O  VAL P  74   N  TYR P  66           
SHEET    3  AO 5 VAL P 132  ASP P 140 -1  O  ALA P 137   N  ALA P  73           
SHEET    4  AO 5 GLY P 144  SER P 150 -1  O  TYR P 148   N  TYR P 136           
SHEET    5  AO 5 TYR P 156  TRP P 159 -1  O  TRP P 159   N  LEU P 147           
SHEET    1  AP 5 ALA Q 159  ILE Q 162  0                                        
SHEET    2  AP 5 ALA Q  31  LYS Q  35 -1  N  GLY Q  33   O  GLN Q 160           
SHEET    3  AP 5 VAL Q  40  GLU Q  45 -1  O  GLY Q  43   N  VAL Q  32           
SHEET    4  AP 5 ILE Q 208  LYS Q 214 -1  O  VAL Q 213   N  VAL Q  40           
SHEET    5  AP 5 ASP Q 218  ALA Q 221 -1  O  ASP Q 218   N  LYS Q 214           
SHEET    1  AQ 5 SER Q  63  LYS Q  64  0                                        
SHEET    2  AQ 5 VAL Q  69  GLY Q  75 -1  O  LEU Q  71   N  SER Q  63           
SHEET    3  AQ 5 VAL Q 129  GLY Q 135 -1  O  ALA Q 134   N  VAL Q  70           
SHEET    4  AQ 5 LYS Q 144  THR Q 148 -1  O  TYR Q 146   N  ILE Q 133           
SHEET    5  AQ 5 TYR Q 154  SER Q 156 -1  O  SER Q 155   N  GLN Q 147           
SHEET    1  AR 5 ALA R 161  ILE R 164  0                                        
SHEET    2  AR 5 ALA R  29  ALA R  33 -1  N  GLY R  31   O  LYS R 162           
SHEET    3  AR 5 VAL R  38  GLU R  43 -1  O  GLY R  41   N  ILE R  30           
SHEET    4  AR 5 ALA R 209  THR R 215 -1  O  SER R 212   N  LEU R  40           
SHEET    5  AR 5 GLY R 219  ILE R 222 -1  O  LYS R 221   N  CYS R 213           
SHEET    1  AS 5 ILE R  59  ASP R  63  0                                        
SHEET    2  AS 5 ILE R  66  GLY R  72 -1  O  CYS R  68   N  VAL R  60           
SHEET    3  AS 5 VAL R 132  ASP R 140 -1  O  ALA R 137   N  GLY R  67           
SHEET    4  AS 5 GLY R 144  ALA R 150 -1  O  PHE R 148   N  ILE R 136           
SHEET    5  AS 5 PHE R 156  ARG R 158 -1  O  TYR R 157   N  HIS R 149           
SHEET    1  AT 5 GLY S 157  ILE S 160  0                                        
SHEET    2  AT 5 THR S  34  ARG S  38 -1  N  GLY S  36   O  THR S 158           
SHEET    3  AT 5 HIS S  42  LEU S  48 -1  O  VAL S  46   N  VAL S  35           
SHEET    4  AT 5 LEU S 210  GLY S 216 -1  O  SER S 211   N  ALA S  47           
SHEET    5  AT 5 THR S 219  TYR S 224 -1  O  TYR S 224   N  ILE S 212           
SHEET    1  AU 5 ILE S  62  ASP S  66  0                                        
SHEET    2  AU 5 MET S  69  GLY S  75 -1  O  MET S  69   N  ASP S  66           
SHEET    3  AU 5 VAL S 129  ASP S 137 -1  O  GLY S 130   N  ALA S  74           
SHEET    4  AU 5 GLY S 140  PHE S 146 -1  O  PHE S 146   N  LEU S 131           
SHEET    5  AU 5 VAL S 152  GLU S 154 -1  O  THR S 153   N  GLU S 145           
SHEET    1  AV 5 GLY T 158  THR T 161  0                                        
SHEET    2  AV 5 SER T  33  LYS T  37 -1  N  GLY T  35   O  ALA T 159           
SHEET    3  AV 5 GLY T  41  LEU T  49 -1  O  ALA T  45   N  ILE T  34           
SHEET    4  AV 5 PHE T 208  SER T 216 -1  O  SER T 213   N  PHE T  44           
SHEET    5  AV 5 HIS T 224  PHE T 226 -1  O  LYS T 225   N  TRP T 214           
SHEET    1  AW 5 GLN T  64  VAL T  66  0                                        
SHEET    2  AW 5 ILE T  70  GLY T  76 -1  O  CYS T  72   N  GLN T  64           
SHEET    3  AW 5 VAL T 130  ASP T 138 -1  O  ILE T 133   N  VAL T  73           
SHEET    4  AW 5 GLY T 141  LEU T 147 -1  O  TYR T 145   N  PHE T 134           
SHEET    5  AW 5 TYR T 153  GLY T 155 -1  O  TRP T 154   N  MET T 146           
SHEET    1  AX 5 ALA U 159  THR U 162  0                                        
SHEET    2  AX 5 SER U  33  ARG U  37 -1  N  SER U  33   O  THR U 162           
SHEET    3  AX 5 THR U  42  GLN U  47 -1  O  ILE U  45   N  LEU U  34           
SHEET    4  AX 5 LEU U 214  THR U 220 -1  O  GLY U 217   N  VAL U  44           
SHEET    5  AX 5 LYS U 223  THR U 226 -1  O  PHE U 225   N  VAL U 218           
SHEET    1  AY 2 SER V  20  GLN V  22  0                                        
SHEET    2  AY 2 ILE V  25  ASP V  28 -1  O  ASP V  28   N  SER V  20           
SHEET    1  AZ 5 LEU V  34  SER V  38  0                                        
SHEET    2  AZ 5 ILE V  41  GLY V  47 -1  O  CYS V  43   N  HIS V  35           
SHEET    3  AZ 5 ALA V  96  ASP V 104 -1  O  TYR V  97   N  ALA V  46           
SHEET    4  AZ 5 GLY V 107  ILE V 113 -1  O  ILE V 113   N  LEU V  98           
SHEET    5  AZ 5 THR V 119  VAL V 121 -1  O  ASP V 120   N  SER V 112           
SHEET    1  BA 6 VAL V 212  ILE V 217  0                                        
SHEET    2  BA 6 GLU W 193  LEU W 199 -1  O  TYR W 198   N  LEU V 213           
SHEET    3  BA 6 ALA W 184  LYS W 190 -1  N  ILE W 188   O  VAL W 195           
SHEET    4  BA 6 CYS W  19  ASP W  25 -1  N  VAL W  20   O  ILE W 189           
SHEET    5  BA 6 ILE W  10  GLY W  16 -1  N  VAL W  12   O  ALA W  23           
SHEET    6  BA 6 PHE W 135  GLY W 139 -1  O  ILE W 136   N  ALA W  13           
SHEET    1  BB 2 LEU W  28  SER W  30  0                                        
SHEET    2  BB 2 LEU W  33  SER W  36 -1  O  LEU W  33   N  SER W  30           
SHEET    1  BC 5 ILE W  42  TYR W  45  0                                        
SHEET    2  BC 5 VAL W  48  GLY W  54 -1  O  LEU W  50   N  PHE W  43           
SHEET    3  BC 5 VAL W 104  ILE W 111 -1  O  VAL W 107   N  GLY W  51           
SHEET    4  BC 5 PRO W 118  PHE W 123 -1  O  ALA W 121   N  VAL W 108           
SHEET    5  BC 5 ILE W 129  ASP W 130 -1  O  ASP W 130   N  GLY W 122           
SHEET    1  BD 5 TYR X 130  HIS X 133  0                                        
SHEET    2  BD 5 ILE X   4  ARG X   8 -1  N  GLY X   6   O  GLY X 131           
SHEET    3  BD 5 SER X  12  SER X  18 -1  O  ALA X  16   N  LEU X   5           
SHEET    4  BD 5 VAL X 179  ASP X 185 -1  O  ILE X 180   N  SER X  17           
SHEET    5  BD 5 GLY X 188  VAL X 192 -1  O  ARG X 190   N  ILE X 183           
SHEET    1  BE 2 VAL X  21  ARG X  23  0                                        
SHEET    2  BE 2 SER X  26  LYS X  29 -1  O  LYS X  29   N  VAL X  21           
SHEET    1  BF 5 THR X  35  SER X  39  0                                        
SHEET    2  BF 5 THR X  42  GLY X  48 -1  O  THR X  42   N  SER X  39           
SHEET    3  BF 5 VAL X 100  ASP X 108 -1  O  GLY X 105   N  LEU X  43           
SHEET    4  BF 5 LYS X 113  ILE X 119 -1  O  ILE X 119   N  VAL X 102           
SHEET    5  BF 5 LYS X 125  LEU X 128 -1  O  VAL X 126   N  GLN X 118           
SHEET    1  BG 5 ILE Y 126  VAL Y 129  0                                        
SHEET    2  BG 5 THR Y   3  PHE Y   8 -1  N  THR Y   3   O  VAL Y 129           
SHEET    3  BG 5 GLY Y  11  VAL Y  16 -1  O  ALA Y  15   N  LEU Y   4           
SHEET    4  BG 5 SER Y 174  THR Y 181 -1  O  VAL Y 180   N  ILE Y  12           
SHEET    5  BG 5 GLY Y 184  ASP Y 192 -1  O  HIS Y 188   N  LEU Y 177           
SHEET    1  BH 2 ALA Y  20  ALA Y  22  0                                        
SHEET    2  BH 2 TRP Y  25  SER Y  28 -1  O  TRP Y  25   N  ALA Y  22           
SHEET    1  BI 5 VAL Y  34  GLU Y  36  0                                        
SHEET    2  BI 5 LEU Y  41  THR Y  44 -1  O  GLY Y  43   N  ILE Y  35           
SHEET    3  BI 5 GLY Y  98  THR Y 105 -1  O  CYS Y 102   N  LEU Y  42           
SHEET    4  BI 5 GLY Y 109  ASP Y 116 -1  O  VAL Y 115   N  THR Y  99           
SHEET    5  BI 5 ARG Y 121  LYS Y 123 -1  O  LEU Y 122   N  TYR Y 114           
SHEET    1  BJ 5 CYS Z 136  GLY Z 140  0                                        
SHEET    2  BJ 5 THR Z  11  ALA Z  16 -1  N  GLY Z  14   O  ARG Z 137           
SHEET    3  BJ 5 ALA Z  21  ASP Z  26 -1  O  ALA Z  24   N  LEU Z  13           
SHEET    4  BJ 5 GLY Z 201  THR Z 208 -1  O  VAL Z 207   N  ALA Z  21           
SHEET    5  BJ 5 GLY Z 211  GLU Z 218 -1  O  TYR Z 217   N  LEU Z 202           
SHEET    1  BK 2 ASN Z  29  THR Z  31  0                                        
SHEET    2  BK 2 SER Z  34  SER Z  37 -1  O  ASN Z  36   N  ASN Z  29           
SHEET    1  BL 5 VAL Z  43  ASP Z  45  0                                        
SHEET    2  BL 5 VAL Z  51  GLY Z  56 -1  O  MET Z  52   N  PHE Z  44           
SHEET    3  BL 5 VAL Z 107  LEU Z 114 -1  O  HIS Z 108   N  ASN Z  55           
SHEET    4  BL 5 GLY Z 120  PHE Z 125 -1  O  ALA Z 121   N  GLY Z 113           
SHEET    5  BL 5 TYR Z 131  GLU Z 134 -1  O  GLU Z 134   N  VAL Z 122           
SHEET    1  BM 5 LEU a  33  PHE a  36  0                                        
SHEET    2  BM 5 GLY a  28  TYR a  30 -1  N  TYR a  30   O  LEU a  33           
SHEET    3  BM 5 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4  BM 5 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5  BM 5 LEU a  42  PRO a  44 -1  N  ILE a  43   O  VAL a  51           
SHEET    1  BN 7 LEU a  33  PHE a  36  0                                        
SHEET    2  BN 7 GLY a  28  TYR a  30 -1  N  TYR a  30   O  LEU a  33           
SHEET    3  BN 7 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4  BN 7 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5  BN 7 ASN a 112  VAL a 119 -1  O  ALA a 117   N  VAL a  50           
SHEET    6  BN 7 GLN a 125  ASN a 131 -1  O  VAL a 130   N  ILE a 114           
SHEET    7  BN 7 THR a 136  SER a 138 -1  O  TYR a 137   N  TYR a 129           
SHEET    1  BO 5 THR a 141  ALA a 143  0                                        
SHEET    2  BO 5 VAL a  11  TYR a  16 -1  N  SER a  13   O  LEU a 142           
SHEET    3  BO 5 GLY a  19  ASP a  25 -1  O  GLY a  19   N  TYR a  16           
SHEET    4  BO 5 ASN a 194  ASP a 201 -1  O  ALA a 198   N  ILE a  22           
SHEET    5  BO 5 GLY a 205  GLN a 213 -1  O  LYS a 209   N  LEU a 197           
SHEET    1  BP 5 TYR b 124  ALA b 127  0                                        
SHEET    2  BP 5 ILE b   3  PHE b   8 -1  N  ALA b   5   O  ALA b 125           
SHEET    3  BP 5 GLY b  11  ALA b  16 -1  O  GLY b  15   N  MET b   4           
SHEET    4  BP 5 ILE b 173  THR b 179 -1  O  LEU b 178   N  VAL b  12           
SHEET    5  BP 5 GLY b 182  PHE b 188 -1  O  GLU b 184   N  VAL b 177           
SHEET    1  BQ 2 THR b  20  THR b  22  0                                        
SHEET    2  BQ 2 TYR b  25  ASN b  28 -1  O  TYR b  25   N  THR b  22           
SHEET    1  BR 5 LEU b  34  HIS b  38  0                                        
SHEET    2  BR 5 ILE b  41  GLY b  47 -1  O  CYS b  43   N  THR b  35           
SHEET    3  BR 5 ALA b  95  TYR b 102 -1  O  GLY b  96   N  SER b  46           
SHEET    4  BR 5 GLY b 108  ILE b 113 -1  O  TYR b 111   N  VAL b  99           
SHEET    5  BR 5 HIS b 120  LEU b 122 -1  O  HIS b 120   N  THR b 112           
LINK         OG1 THR H   1                 B26 BO2 H 301     1555   1555  1.44  
LINK         OG1 THR K   1                 B26 BO2 K 301     1555   1555  1.44  
LINK         OG1 THR N   1                 B26 BO2 N 201     1555   1555  1.44  
LINK         OG1 THR V   1                 B26 BO2 V 301     1555   1555  1.43  
LINK         OG1 THR Y   1                 B26 BO2 Y 301     1555   1555  1.44  
LINK         OG1 THR b   1                 B26 BO2 b 201     1555   1555  1.43  
LINK         OG1 THR G   8                MG    MG G 301     1555   1555  2.58  
LINK         O   TYR G 119                MG    MG G 301     1555   1555  2.80  
LINK         O   ARG G 122                MG    MG G 301     1555   1555  2.57  
LINK         O   MET G 125                MG    MG G 301     1555   1555  2.19  
LINK         O   ALA I 174                MG    MG I 301     1555   1555  2.75  
LINK         O   ASP I 177                MG    MG I 301     1555   1555  2.34  
LINK         O   SER I 180                MG    MG I 301     1555   1555  2.76  
LINK         O   ASP I 204                MG    MG Y 302     1555   1555  2.27  
LINK         O   ALA K 165                MG    MG K 302     1555   1555  2.37  
LINK         O   ASP K 168                MG    MG K 302     1555   1555  2.17  
LINK         O   SER K 171                MG    MG K 302     1555   1555  2.75  
LINK        MG    MG K 302                 O   ASP W 204     1555   1555  2.36  
LINK         OXT ASP L 222                MG    MG V 302     1555   1555  2.16  
LINK         O   ILE N 163                MG    MG N 202     1555   1555  2.62  
LINK         O   ASP N 166                MG    MG N 202     1555   1555  2.85  
LINK         O   SER N 169                MG    MG N 202     1555   1555  2.50  
LINK         O   ILE V 163                MG    MG V 302     1555   1555  2.15  
LINK         O   ASP V 166                MG    MG V 302     1555   1555  2.27  
LINK         O   SER V 169                MG    MG V 302     1555   1555  2.77  
LINK         O   ALA Y 165                MG    MG Y 302     1555   1555  2.43  
LINK         O   ASP Y 168                MG    MG Y 302     1555   1555  2.30  
LINK         O   SER Y 171                MG    MG Y 302     1555   1555  2.86  
LINK         O   THR Z 192                MG    MG Z 301     1555   1555  2.98  
LINK         O   VAL Z 198                MG    MG Z 301     1555   1555  2.45  
SITE     1 AC1  5 THR G   8  TYR G 119  ARG G 122  ALA G 123                    
SITE     2 AC1  5 MET G 125                                                     
SITE     1 AC2  3 ARG G 111  ASN G 114  TYR H  69                               
SITE     1 AC3  9 THR H   1  SER H  20  THR H  21  GLN H  22                    
SITE     2 AC3  9 GLY H  45  GLY H  47  ALA H  49  THR H  52                    
SITE     3 AC3  9 ASP I 124                                                     
SITE     1 AC4  3 ALA I 174  ASP I 177  SER I 180                               
SITE     1 AC5  1 GLN J 118                                                     
SITE     1 AC6  7 THR K   1  ALA K  20  THR K  21  MET K  45                    
SITE     2 AC6  7 GLY K  47  ALA K  49  ASP L 126                               
SITE     1 AC7  5 ALA K 165  ASP K 168  ALA K 169  SER K 171                    
SITE     2 AC7  5 ASP W 204                                                     
SITE     1 AC8  9 HIS H 114  SER H 118  THR N   1  THR N  20                    
SITE     2 AC8  9 THR N  21  THR N  22  ARG N  45  GLY N  47                    
SITE     3 AC8  9 ALA N  49                                                     
SITE     1 AC9  5 ARG N  19  ILE N 163  ASP N 166  SER N 169                    
SITE     2 AC9  5 LEU a  34                                                     
SITE     1 BC1  3 THR N  31  ARG N  45  GLN N  53                               
SITE     1 BC2  3 ARG U 111  ASN U 114  TYR V  69                               
SITE     1 BC3  9 THR V   1  SER V  20  THR V  21  GLN V  22                    
SITE     2 BC3  9 GLY V  45  GLY V  47  ALA V  49  THR V  52                    
SITE     3 BC3  9 ASP W 124                                                     
SITE     1 BC4  4 ASP L 222  ILE V 163  ASP V 166  SER V 169                    
SITE     1 BC5  7 THR Y   1  ALA Y  20  THR Y  21  MET Y  45                    
SITE     2 BC5  7 GLY Y  47  ALA Y  49  ASP Z 126                               
SITE     1 BC6  5 ASP I 204  ALA Y 165  ASP Y 168  ALA Y 169                    
SITE     2 BC6  5 SER Y 171                                                     
SITE     1 BC7  5 ARG Z  28  THR Z 192  HIS Z 195  VAL Z 198                    
SITE     2 BC7  5 ASP Z 222                                                     
SITE     1 BC8  9 HIS V 114  SER V 118  THR b   1  THR b  20                    
SITE     2 BC8  9 THR b  21  THR b  22  ARG b  45  GLY b  47                    
SITE     3 BC8  9 ALA b  49                                                     
SITE     1 BC9  2 ARG b  45  GLN b  53                                          
CRYST1  134.910  300.210  144.760  90.00 112.85  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007412  0.000000  0.003123        0.00000                         
SCALE2      0.000000  0.003331  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007496        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2 -0.999581 -0.002243  0.028872       67.17099    1                    
MTRIX2   2 -0.002809 -0.984788 -0.173738     -288.64862    1                    
MTRIX3   2  0.028822 -0.173746  0.984369      -25.97725    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system