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Database: PDB
Entry: 3VON
LinkDB: 3VON
Original site: 3VON 
HEADER    HYDROLASE/LIGASE                        30-JAN-12   3VON              
TITLE     CRYSTALSTRUCTURE OF THE UBIQUITIN PROTEASE                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN THIOESTERASE OTUB1;                              
COMPND   3 CHAIN: A, H, O, V, c, j;                                             
COMPND   4 FRAGMENT: UNP RESIDUES 45-271;                                       
COMPND   5 SYNONYM: DEUBIQUITINATING ENZYME OTUB1, OTU DOMAIN-CONTAINING        
COMPND   6 UBIQUITIN ALDEHYDE-BINDING PROTEIN 1, OTUBAIN-1, HOTU1, UBIQUITIN-   
COMPND   7 SPECIFIC-PROCESSING PROTEASE OTUB1;                                  
COMPND   8 EC: 3.4.19.12;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 2;                 
COMPND  12 CHAIN: B, D, F, I, K, M, P, R, T, W, Y, a, d, f, h, k, m, o;         
COMPND  13 FRAGMENT: UNP RESIDUES 6-143;                                        
COMPND  14 SYNONYM: DDVIT 1, ENTEROCYTE DIFFERENTIATION-ASSOCIATED FACTOR 1,    
COMPND  15 EDAF-1, ENTEROCYTE DIFFERENTIATION-PROMOTING FACTOR 1, EDPF-1, MMS2  
COMPND  16 HOMOLOG, VITAMIN D3-INDUCIBLE PROTEIN;                               
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 3;                                                           
COMPND  19 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 N;                         
COMPND  20 CHAIN: C, E, G, J, L, N, Q, S, U, X, Z, b, e, g, i, l, n, p;         
COMPND  21 FRAGMENT: UNP RESIDUES 3-150;                                        
COMPND  22 SYNONYM: BENDLESS-LIKE UBIQUITIN-CONJUGATING ENZYME, UBC13, UBIQUITIN
COMPND  23 CARRIER PROTEIN N, UBIQUITIN-PROTEIN LIGASE N;                       
COMPND  24 EC: 6.3.2.19;                                                        
COMPND  25 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HSPC263, OTB1, OTU1, OTUB1;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET26B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: MMS2, UBE2V2, UEV2;                                            
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET26B;                                   
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: BLU, UBC13, UBE2N;                                             
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PET26B                                    
KEYWDS    UBIQUITIN PROTEASE, HYDROLASE-LIGASE COMPLEX                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.SATO,S.FUKAI                                                        
REVDAT   1   30-MAY-12 3VON    0                                                
JRNL        AUTH   Y.SATO,A.YAMAGATA,S.GOTO-ITO,K.KUBOTA,K.MIYAMOTO,S.NAKADA,   
JRNL        AUTH 2 S.FUKAI                                                      
JRNL        TITL   MOLECULAR BASIS OF K63-LINKED POLYUBIQUITINATION INHIBITION  
JRNL        TITL 2 BY THE INTERACTION BETWEEN HUMAN DEUBIQUITINATING ENZYME     
JRNL        TITL 3 OTUB1 AND UBIQUITIN-CONJUGATING ENZYME UBC13                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 112834                         
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) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5967                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7840                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.30                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 417                          
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 51450                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.50000                                             
REMARK   3    B22 (A**2) : 2.78000                                              
REMARK   3    B33 (A**2) : 1.72000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.27000                                              
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): 0.614         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.518         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 70.677        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 52637 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 71362 ; 1.009 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  6357 ; 5.007 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2436 ;37.828 ;24.265       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  9369 ;19.788 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   378 ;16.010 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  7763 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 40060 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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): 32177 ; 0.120 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 52298 ; 0.238 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 20460 ; 0.355 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 19064 ; 0.631 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 5                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : D F K M R T Y a f h m o         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     F      6       F     143      4                      
REMARK   3           1     M      6       M     143      4                      
REMARK   3           1     T      6       T     143      4                      
REMARK   3           1     a      6       a     143      4                      
REMARK   3           1     h      6       h     143      4                      
REMARK   3           1     o      6       o     143      4                      
REMARK   3           2     D      6       D     143      4                      
REMARK   3           2     K      6       K     143      4                      
REMARK   3           2     R      6       R     143      4                      
REMARK   3           2     Y      6       Y     143      4                      
REMARK   3           2     f      6       f     143      4                      
REMARK   3           2     m      6       m     143      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   2188 ; 0.460 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):   2188 ; 0.380 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    K    (A):   2188 ; 0.400 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    M    (A):   2188 ; 0.390 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    R    (A):   2188 ; 0.500 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    T    (A):   2188 ; 0.420 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   2188 ; 0.130 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    F (A**2):   2188 ; 0.120 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    K (A**2):   2188 ; 0.130 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    M (A**2):   2188 ; 0.120 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    R (A**2):   2188 ; 0.130 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    T (A**2):   2188 ; 0.120 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C E G J L N Q S U X Z b e g i   
REMARK   3                                      l n p                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 6                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      3       C     115      4                      
REMARK   3           1     J      3       J     115      4                      
REMARK   3           1     Q      3       Q     115      4                      
REMARK   3           1     X      3       X     115      4                      
REMARK   3           1     e      3       e     115      4                      
REMARK   3           1     l      3       l     115      4                      
REMARK   3           2     C    125       C     150      4                      
REMARK   3           2     J    125       J     150      4                      
REMARK   3           2     Q    125       Q     150      4                      
REMARK   3           2     X    125       X     150      4                      
REMARK   3           2     e    125       e     150      4                      
REMARK   3           2     l    125       l     150      4                      
REMARK   3           3     E      3       E     115      4                      
REMARK   3           3     L      3       L     115      4                      
REMARK   3           3     S      3       S     115      4                      
REMARK   3           3     Z      3       Z     115      4                      
REMARK   3           3     g      3       g     115      4                      
REMARK   3           3     n      3       n     115      4                      
REMARK   3           4     E    125       E     150      4                      
REMARK   3           4     L    125       L     150      4                      
REMARK   3           4     S    125       S     150      4                      
REMARK   3           4     Z    125       Z     150      4                      
REMARK   3           4     g    125       g     150      4                      
REMARK   3           4     n    125       n     150      4                      
REMARK   3           5     G      3       G     115      4                      
REMARK   3           5     N      3       N     115      4                      
REMARK   3           5     U      3       U     115      4                      
REMARK   3           5     b      3       b     115      4                      
REMARK   3           5     i      3       i     115      4                      
REMARK   3           5     p      3       p     115      4                      
REMARK   3           6     G    125       G     150      4                      
REMARK   3           6     N    125       N     150      4                      
REMARK   3           6     U    125       U     150      4                      
REMARK   3           6     b    125       b     150      4                      
REMARK   3           6     i    125       i     150      4                      
REMARK   3           6     p    125       p     150      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    C    (A):   3324 ; 0.480 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    E    (A):   3324 ; 0.480 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    G    (A):   3324 ; 0.460 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    J    (A):   3324 ; 0.480 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    L    (A):   3324 ; 0.480 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    N    (A):   3324 ; 0.490 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    C (A**2):   3324 ; 0.140 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    E (A**2):   3324 ; 0.120 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    G (A**2):   3324 ; 0.120 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    J (A**2):   3324 ; 0.130 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    L (A**2):   3324 ; 0.140 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    N (A**2):   3324 ; 0.110 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A H O V c j                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     46       A     237      4                      
REMARK   3           1     H     46       H     237      4                      
REMARK   3           1     O     46       O     237      4                      
REMARK   3           1     V     46       V     237      4                      
REMARK   3           1     c     46       c     237      4                      
REMARK   3           1     j     46       j     237      4                      
REMARK   3           2     A    247       A     269      4                      
REMARK   3           2     H    247       H     269      4                      
REMARK   3           2     O    247       O     269      4                      
REMARK   3           2     V    247       V     269      4                      
REMARK   3           2     c    247       c     269      4                      
REMARK   3           2     j    247       j     269      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):   1676 ; 0.430 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    H    (A):   1676 ; 0.420 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    O    (A):   1676 ; 0.380 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    V    (A):   1676 ; 0.390 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    c    (A):   1676 ; 0.400 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    j    (A):   1676 ; 0.480 ; 0.500           
REMARK   3   MEDIUM THERMAL     3    A (A**2):   1676 ; 0.100 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    H (A**2):   1676 ; 0.090 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    O (A**2):   1676 ; 0.110 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    V (A**2):   1676 ; 0.110 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    c (A**2):   1676 ; 0.110 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    j (A**2):   1676 ; 0.090 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : B P W d                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      6       B     143      4                      
REMARK   3           1     P      6       P     143      4                      
REMARK   3           1     W      6       W     143      4                      
REMARK   3           1     d      6       d     143      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  4    B    (A):   1092 ; 0.330 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  4    P    (A):   1092 ; 0.500 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  4    W    (A):   1092 ; 0.390 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  4    d    (A):   1092 ; 0.350 ; 0.500           
REMARK   3   MEDIUM THERMAL     4    B (A**2):   1092 ; 0.120 ; 2.000           
REMARK   3   MEDIUM THERMAL     4    P (A**2):   1092 ; 0.120 ; 2.000           
REMARK   3   MEDIUM THERMAL     4    W (A**2):   1092 ; 0.100 ; 2.000           
REMARK   3   MEDIUM THERMAL     4    d (A**2):   1092 ; 0.130 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : I k                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     I      6       I     143      4                      
REMARK   3           1     k      6       k     143      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  5    I    (A):   1096 ; 0.320 ; 0.500           
REMARK   3   MEDIUM THERMAL     5    I (A**2):   1096 ; 0.080 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 42                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    45        A   270                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.9040  30.8700 104.2480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2797 T22:   0.6119                                     
REMARK   3      T33:   0.4133 T12:  -0.0763                                     
REMARK   3      T13:   0.0427 T23:  -0.0864                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5385 L22:   4.2952                                     
REMARK   3      L33:   4.1395 L12:  -0.1271                                     
REMARK   3      L13:   1.6969 L23:   0.4758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1696 S12:  -0.1758 S13:   0.1206                       
REMARK   3      S21:   0.0854 S22:  -0.1068 S23:  -0.6086                       
REMARK   3      S31:   0.0740 S32:   0.7210 S33:  -0.0627                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     6        B   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8070  58.8350 132.5320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2270 T22:   0.2181                                     
REMARK   3      T33:   0.2313 T12:   0.0601                                     
REMARK   3      T13:  -0.0592 T23:  -0.1119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8131 L22:   4.4283                                     
REMARK   3      L33:   9.6507 L12:  -0.2108                                     
REMARK   3      L13:  -0.8149 L23:   4.2386                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1278 S12:   0.0846 S13:   0.1616                       
REMARK   3      S21:  -0.2825 S22:   0.1344 S23:  -0.0486                       
REMARK   3      S31:  -0.4209 S32:   0.1933 S33:  -0.0066                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     4        C   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3630  40.5570 105.4010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1261 T22:   0.1473                                     
REMARK   3      T33:   0.0471 T12:  -0.0202                                     
REMARK   3      T13:  -0.0435 T23:  -0.0576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.6571 L22:   4.2251                                     
REMARK   3      L33:   7.0088 L12:   1.8205                                     
REMARK   3      L13:  -2.6330 L23:   0.5349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0529 S12:   0.2269 S13:   0.0577                       
REMARK   3      S21:  -0.0184 S22:   0.0145 S23:  -0.0545                       
REMARK   3      S31:  -0.1402 S32:  -0.0318 S33:   0.0384                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     7        D   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  89.4820  57.1360 104.0540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4721 T22:   0.2514                                     
REMARK   3      T33:   0.5469 T12:  -0.0182                                     
REMARK   3      T13:   0.1442 T23:   0.0804                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2032 L22:   4.9413                                     
REMARK   3      L33:  11.6749 L12:  -1.1388                                     
REMARK   3      L13:  -2.8588 L23:   2.5643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2867 S12:  -0.2935 S13:   0.2678                       
REMARK   3      S21:  -0.4735 S22:  -0.0448 S23:   0.1491                       
REMARK   3      S31:  -1.6597 S32:   0.3071 S33:  -0.2419                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     4        E   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  86.9990  34.9240  80.2620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3386 T22:   0.5007                                     
REMARK   3      T33:   0.2621 T12:   0.0388                                     
REMARK   3      T13:  -0.1302 T23:  -0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.6443 L22:   6.4545                                     
REMARK   3      L33:   4.3785 L12:  -0.3379                                     
REMARK   3      L13:  -3.8211 L23:   2.0271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1482 S12:   0.4903 S13:  -0.5225                       
REMARK   3      S21:  -0.2395 S22:  -0.5347 S23:   0.8964                       
REMARK   3      S31:  -0.0500 S32:  -1.0300 S33:   0.3865                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     6        F   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.0020  14.9920  74.8580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2353 T22:   0.1685                                     
REMARK   3      T33:   0.1171 T12:  -0.0585                                     
REMARK   3      T13:  -0.0520 T23:  -0.1009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5969 L22:   3.6212                                     
REMARK   3      L33:   3.6137 L12:  -3.5043                                     
REMARK   3      L13:  -3.8424 L23:   0.8000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0951 S12:  -0.3725 S13:   0.5055                       
REMARK   3      S21:   0.1660 S22:   0.0350 S23:  -0.3547                       
REMARK   3      S31:  -0.1887 S32:   0.1109 S33:  -0.1301                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     4        G   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4330  26.5880  78.1910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1069 T22:   0.0881                                     
REMARK   3      T33:   0.1246 T12:  -0.0613                                     
REMARK   3      T13:   0.0212 T23:  -0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0241 L22:   2.1431                                     
REMARK   3      L33:  12.5571 L12:  -1.0577                                     
REMARK   3      L13:   1.1429 L23:  -0.0947                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0801 S12:   0.1675 S13:   0.3825                       
REMARK   3      S21:  -0.1470 S22:  -0.0427 S23:  -0.1354                       
REMARK   3      S31:  -0.3109 S32:  -0.2435 S33:  -0.0374                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    45        H   270                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.6160  76.1480 107.1130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5291 T22:   1.7682                                     
REMARK   3      T33:   0.8488 T12:  -0.1825                                     
REMARK   3      T13:  -0.0316 T23:   0.0306                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0507 L22:   2.8611                                     
REMARK   3      L33:   5.8551 L12:  -0.4305                                     
REMARK   3      L13:   2.2152 L23:   0.7205                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0347 S12:  -0.3129 S13:  -0.2707                       
REMARK   3      S21:   0.1449 S22:   0.1223 S23:  -0.5125                       
REMARK   3      S31:   0.1253 S32:   1.7762 S33:  -0.1570                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     6        I   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4840 103.4920 134.3220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2783 T22:   0.3226                                     
REMARK   3      T33:   0.6425 T12:  -0.0463                                     
REMARK   3      T13:  -0.1309 T23:   0.0513                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6323 L22:   5.7880                                     
REMARK   3      L33:  14.6593 L12:   1.8013                                     
REMARK   3      L13:   1.1022 L23:   5.6512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5109 S12:   0.0184 S13:   0.8669                       
REMARK   3      S21:  -0.3147 S22:  -0.1031 S23:   0.9506                       
REMARK   3      S31:  -0.4729 S32:   0.3639 S33:   0.6140                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     4        J   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1560  87.3260 106.1580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3233 T22:   0.4245                                     
REMARK   3      T33:   0.2620 T12:  -0.1313                                     
REMARK   3      T13:  -0.1073 T23:   0.1801                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.6188 L22:   5.6489                                     
REMARK   3      L33:   4.9796 L12:   2.4475                                     
REMARK   3      L13:  -0.2197 L23:  -0.1660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1130 S12:   0.2660 S13:  -0.0862                       
REMARK   3      S21:   0.1832 S22:  -0.2011 S23:  -0.2686                       
REMARK   3      S31:  -0.0326 S32:   0.6430 S33:   0.3141                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K     6        K   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  88.8000 103.7430 103.9630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2009 T22:   0.3339                                     
REMARK   3      T33:   0.3374 T12:  -0.1145                                     
REMARK   3      T13:   0.0408 T23:   0.2276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5886 L22:   4.4352                                     
REMARK   3      L33:   6.0778 L12:  -1.6744                                     
REMARK   3      L13:  -0.5765 L23:   3.1076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1459 S12:   0.2160 S13:  -0.1121                       
REMARK   3      S21:  -0.0249 S22:   0.1856 S23:   0.1360                       
REMARK   3      S31:  -0.1523 S32:  -0.0461 S33:  -0.0397                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     4        L   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  86.8220  81.0770  80.3420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3350 T22:   0.4645                                     
REMARK   3      T33:   0.4149 T12:  -0.0783                                     
REMARK   3      T13:  -0.1144 T23:   0.0347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.1933 L22:   4.3679                                     
REMARK   3      L33:   5.3572 L12:   0.7072                                     
REMARK   3      L13:  -2.8528 L23:   0.2713                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3008 S12:   0.0662 S13:  -0.7434                       
REMARK   3      S21:  -0.2071 S22:  -0.5984 S23:   0.6246                       
REMARK   3      S31:   0.3068 S32:  -1.0313 S33:   0.2977                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M     6        M   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.9770  61.2860  75.8680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2930 T22:   0.1988                                     
REMARK   3      T33:   0.2656 T12:  -0.0602                                     
REMARK   3      T13:  -0.0196 T23:   0.0273                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.7725 L22:   2.7369                                     
REMARK   3      L33:   3.3848 L12:  -2.9807                                     
REMARK   3      L13:  -3.1298 L23:  -0.0960                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1566 S12:  -0.3325 S13:   0.1318                       
REMARK   3      S21:   0.1358 S22:   0.0654 S23:  -0.0277                       
REMARK   3      S31:  -0.1884 S32:   0.0017 S33:  -0.2220                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N     4        N   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.5020  73.1800  78.8100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1988 T22:   0.2755                                     
REMARK   3      T33:   0.3859 T12:  -0.0121                                     
REMARK   3      T13:   0.0019 T23:   0.1130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6149 L22:   2.3532                                     
REMARK   3      L33:  10.9653 L12:  -0.9071                                     
REMARK   3      L13:   0.6610 L23:   0.7000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1404 S12:   0.0127 S13:   0.2756                       
REMARK   3      S21:  -0.1365 S22:  -0.2126 S23:   0.0183                       
REMARK   3      S31:  -0.2235 S32:  -0.2576 S33:   0.3530                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   O    45        O   271                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.3650 119.6400 105.6810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3172 T22:   0.4745                                     
REMARK   3      T33:   0.4127 T12:  -0.0459                                     
REMARK   3      T13:   0.0292 T23:   0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1256 L22:   3.0857                                     
REMARK   3      L33:   4.0410 L12:  -0.3861                                     
REMARK   3      L13:   2.6039 L23:  -0.3785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1226 S12:  -0.0201 S13:  -0.6863                       
REMARK   3      S21:  -0.0049 S22:  -0.0025 S23:   0.0415                       
REMARK   3      S31:   0.3179 S32:   0.2876 S33:  -0.1201                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   P     6        P   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0190 150.6490 131.1390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4462 T22:   1.0125                                     
REMARK   3      T33:   0.4793 T12:   0.3598                                     
REMARK   3      T13:  -0.0990 T23:  -0.2976                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5703 L22:   6.8847                                     
REMARK   3      L33:  10.0707 L12:  -0.9032                                     
REMARK   3      L13:  -1.2725 L23:   5.8623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5603 S12:  -1.1519 S13:   0.3524                       
REMARK   3      S21:   0.3387 S22:   0.7334 S23:  -0.0410                       
REMARK   3      S31:   0.0678 S32:   0.6674 S33:  -0.1731                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Q     4        Q   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.9160 131.6650 104.2920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2727 T22:   0.2387                                     
REMARK   3      T33:   0.1500 T12:   0.0729                                     
REMARK   3      T13:  -0.0805 T23:   0.0254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.8056 L22:   4.0760                                     
REMARK   3      L33:   2.7654 L12:   2.1046                                     
REMARK   3      L13:  -0.3473 L23:   1.1404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0430 S12:  -0.2022 S13:  -0.3649                       
REMARK   3      S21:  -0.0451 S22:  -0.0930 S23:   0.0358                       
REMARK   3      S31:  -0.1122 S32:  -0.1333 S33:   0.1360                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   R     7        R   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  89.0650 148.0130 102.3060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2255 T22:   0.2353                                     
REMARK   3      T33:   0.4150 T12:  -0.0304                                     
REMARK   3      T13:   0.0693 T23:   0.1751                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3668 L22:   6.2068                                     
REMARK   3      L33:   8.2798 L12:  -0.4116                                     
REMARK   3      L13:  -1.4020 L23:   3.5439                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1541 S12:   0.0949 S13:   0.2764                       
REMARK   3      S21:  -0.1484 S22:   0.3047 S23:  -0.2842                       
REMARK   3      S31:  -0.4061 S32:  -0.0559 S33:  -0.4588                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   S     3        S   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  87.2980 125.4320  78.9920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2709 T22:   0.4401                                     
REMARK   3      T33:   0.0650 T12:  -0.0818                                     
REMARK   3      T13:  -0.0674 T23:   0.1355                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.0764 L22:   5.3862                                     
REMARK   3      L33:   4.4716 L12:   2.7144                                     
REMARK   3      L13:  -3.9665 L23:  -0.7628                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0195 S12:   0.5082 S13:  -0.0188                       
REMARK   3      S21:  -0.4693 S22:  -0.0088 S23:   0.1154                       
REMARK   3      S31:   0.2215 S32:  -0.7065 S33:  -0.0108                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   T     6        T   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.2850 105.7770  73.8380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3225 T22:   0.2800                                     
REMARK   3      T33:   0.5120 T12:  -0.1704                                     
REMARK   3      T13:  -0.0228 T23:  -0.0812                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4045 L22:   2.8229                                     
REMARK   3      L33:   5.2556 L12:  -3.8674                                     
REMARK   3      L13:  -4.5293 L23:   0.1083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1891 S12:  -0.7341 S13:   0.8035                       
REMARK   3      S21:   0.0621 S22:   0.1035 S23:  -0.4724                       
REMARK   3      S31:  -0.1846 S32:   0.3187 S33:  -0.2925                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   U     4        U   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.8130 117.4770  76.9540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1949 T22:   0.2332                                     
REMARK   3      T33:   0.2970 T12:  -0.1112                                     
REMARK   3      T13:   0.0621 T23:  -0.0440                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8692 L22:   1.9703                                     
REMARK   3      L33:  12.3417 L12:  -0.5344                                     
REMARK   3      L13:   1.2278 L23:   0.4175                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0222 S12:   0.3063 S13:   0.2189                       
REMARK   3      S21:  -0.1106 S22:  -0.0650 S23:  -0.2726                       
REMARK   3      S31:  -0.1633 S32:  -0.5446 S33:   0.0428                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   V    45        V   271                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3530 177.7980  23.1680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3386 T22:   0.4358                                     
REMARK   3      T33:   0.3623 T12:   0.0741                                     
REMARK   3      T13:  -0.0489 T23:   0.0290                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0269 L22:   3.2813                                     
REMARK   3      L33:   4.7189 L12:   0.1249                                     
REMARK   3      L13:  -2.8906 L23:  -0.3172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1763 S12:  -0.0042 S13:   0.7283                       
REMARK   3      S21:  -0.0095 S22:  -0.0135 S23:  -0.0037                       
REMARK   3      S31:  -0.3307 S32:   0.3650 S33:  -0.1627                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   W     7        W   143                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.8670 146.7220  -2.5530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4588 T22:   0.9718                                     
REMARK   3      T33:   0.4840 T12:  -0.2713                                     
REMARK   3      T13:   0.1076 T23:  -0.3243                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1706 L22:   4.5466                                     
REMARK   3      L33:   9.3808 L12:   1.2730                                     
REMARK   3      L13:   0.6817 L23:   4.6694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4397 S12:   0.9069 S13:  -0.4623                       
REMARK   3      S21:  -0.3357 S22:   0.6866 S23:   0.0211                       
REMARK   3      S31:  -0.0622 S32:   0.5782 S33:  -0.2470                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X     4        X   150                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.0900 165.8040  24.1910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2896 T22:   0.2361                                     
REMARK   3      T33:   0.1825 T12:  -0.0633                                     
REMARK   3      T13:   0.0482 T23:  -0.0387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.9880 L22:   4.1177                                     
REMARK   3      L33:   2.5293 L12:  -1.8066                                     
REMARK   3      L13:   0.6214 L23:   1.1272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1928 S12:   0.1240 S13:   0.3963                       
REMARK   3      S21:   0.1980 S22:   0.1285 S23:   0.0333                       
REMARK   3      S31:   0.0469 S32:  -0.1423 S33:   0.0642                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Y     7        Y   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.0990 149.4750  26.2380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2403 T22:   0.2348                                     
REMARK   3      T33:   0.4336 T12:   0.0414                                     
REMARK   3      T13:  -0.1060 T23:   0.1695                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1261 L22:   6.0240                                     
REMARK   3      L33:   9.8596 L12:   0.4553                                     
REMARK   3      L13:   0.9184 L23:   3.5994                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1840 S12:  -0.1558 S13:  -0.2817                       
REMARK   3      S21:   0.0956 S22:   0.2208 S23:  -0.1410                       
REMARK   3      S31:   0.5501 S32:   0.0683 S33:  -0.4048                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Z     3        Z   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.2700 172.0130  49.5630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3247 T22:   0.4493                                     
REMARK   3      T33:   0.0658 T12:   0.0722                                     
REMARK   3      T13:   0.0145 T23:   0.1184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.5058 L22:   4.1172                                     
REMARK   3      L33:   4.3215 L12:  -0.8972                                     
REMARK   3      L13:   2.7001 L23:  -0.7794                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0267 S12:  -0.6471 S13:   0.1279                       
REMARK   3      S21:   0.5247 S22:   0.0249 S23:   0.2098                       
REMARK   3      S31:  -0.2448 S32:  -0.7227 S33:  -0.0516                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   a     6        a   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.7380 191.6530  54.6800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3191 T22:   0.1966                                     
REMARK   3      T33:   0.4948 T12:   0.1458                                     
REMARK   3      T13:   0.0156 T23:  -0.0601                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.9610 L22:   3.0653                                     
REMARK   3      L33:   4.2876 L12:   3.9331                                     
REMARK   3      L13:   4.1620 L23:   1.2809                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1186 S12:   0.8316 S13:  -0.7363                       
REMARK   3      S21:  -0.0591 S22:   0.0607 S23:  -0.4474                       
REMARK   3      S31:   0.2375 S32:   0.2622 S33:  -0.1793                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   b     4        b   150                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.2170 179.9930  51.5920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2023 T22:   0.1551                                     
REMARK   3      T33:   0.3325 T12:   0.0935                                     
REMARK   3      T13:  -0.0731 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0198 L22:   1.8023                                     
REMARK   3      L33:  12.0674 L12:   0.7607                                     
REMARK   3      L13:  -1.3075 L23:   0.6612                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0089 S12:  -0.2012 S13:  -0.3035                       
REMARK   3      S21:   0.0775 S22:  -0.0222 S23:  -0.1546                       
REMARK   3      S31:   0.2133 S32:  -0.4421 S33:   0.0133                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   c    45        c   270                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0500 129.8180  23.7880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3255 T22:   0.5646                                     
REMARK   3      T33:   0.4073 T12:   0.0555                                     
REMARK   3      T13:  -0.0580 T23:  -0.0664                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3405 L22:   3.7557                                     
REMARK   3      L33:   4.1766 L12:   0.0720                                     
REMARK   3      L13:  -2.4481 L23:   0.6192                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1629 S12:   0.1380 S13:  -0.0971                       
REMARK   3      S21:  -0.0699 S22:  -0.1505 S23:  -0.6797                       
REMARK   3      S31:  -0.0969 S32:   0.6447 S33:  -0.0124                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   d     6        d   143                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.1120 101.3220  -4.0110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2062 T22:   0.2350                                     
REMARK   3      T33:   0.2533 T12:  -0.0432                                     
REMARK   3      T13:   0.0115 T23:  -0.0922                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7660 L22:   4.3693                                     
REMARK   3      L33:   9.9391 L12:   0.6292                                     
REMARK   3      L13:   0.6687 L23:   4.0485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1431 S12:  -0.1224 S13:  -0.1568                       
REMARK   3      S21:   0.2250 S22:   0.1696 S23:  -0.0327                       
REMARK   3      S31:   0.4734 S32:   0.1155 S33:  -0.0265                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   e     4        e   150                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.6610 119.4850  22.9960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1397 T22:   0.1569                                     
REMARK   3      T33:   0.0275 T12:  -0.0053                                     
REMARK   3      T13:   0.0082 T23:  -0.0619                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.9507 L22:   5.1710                                     
REMARK   3      L33:   5.8045 L12:  -1.9839                                     
REMARK   3      L13:   1.1956 L23:   1.1869                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1125 S12:  -0.0577 S13:   0.0609                       
REMARK   3      S21:   0.0380 S22:   0.0345 S23:  -0.0873                       
REMARK   3      S31:   0.1198 S32:   0.0148 S33:   0.0780                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   f     7        f   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.4840 103.0590  24.4520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5356 T22:   0.2154                                     
REMARK   3      T33:   0.5635 T12:   0.0201                                     
REMARK   3      T13:  -0.1725 T23:   0.0803                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7841 L22:   4.6021                                     
REMARK   3      L33:   9.2710 L12:   1.6505                                     
REMARK   3      L13:   2.7431 L23:   2.4328                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4349 S12:   0.2927 S13:  -0.1378                       
REMARK   3      S21:   0.4270 S22:  -0.1320 S23:   0.2141                       
REMARK   3      S31:   1.4759 S32:   0.2390 S33:  -0.3029                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   g     3        g   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.0560 125.2170  48.2660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3651 T22:   0.4737                                     
REMARK   3      T33:   0.2321 T12:  -0.0603                                     
REMARK   3      T13:   0.0987 T23:  -0.0013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.4106 L22:   5.3070                                     
REMARK   3      L33:   4.1723 L12:   0.6259                                     
REMARK   3      L13:   3.4743 L23:   2.2532                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2159 S12:  -0.4241 S13:   0.6344                       
REMARK   3      S21:   0.3775 S22:  -0.5387 S23:   0.9744                       
REMARK   3      S31:   0.1708 S32:  -1.0191 S33:   0.3228                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   h     6        h   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.0290 145.1760  53.7040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2914 T22:   0.1501                                     
REMARK   3      T33:   0.1039 T12:   0.0340                                     
REMARK   3      T13:  -0.0181 T23:  -0.1029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8319 L22:   3.1357                                     
REMARK   3      L33:   3.1132 L12:   3.1772                                     
REMARK   3      L13:   3.6504 L23:   1.1226                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0005 S12:   0.4445 S13:  -0.5591                       
REMARK   3      S21:  -0.1353 S22:   0.0768 S23:  -0.3149                       
REMARK   3      S31:   0.2270 S32:   0.1457 S33:  -0.0763                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   i     3        i   150                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.5450 133.6000  50.2800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1463 T22:   0.1036                                     
REMARK   3      T33:   0.0561 T12:   0.0662                                     
REMARK   3      T13:  -0.0223 T23:  -0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6514 L22:   1.3432                                     
REMARK   3      L33:  13.5529 L12:   1.4337                                     
REMARK   3      L13:  -1.3832 L23:   0.9401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0269 S12:  -0.3118 S13:  -0.2193                       
REMARK   3      S21:   0.0601 S22:   0.0047 S23:  -0.0564                       
REMARK   3      S31:   0.3359 S32:  -0.2199 S33:   0.0222                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   j    46        j   270                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.6970  84.0050  21.7750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6174 T22:   1.8340                                     
REMARK   3      T33:   0.8685 T12:   0.1610                                     
REMARK   3      T13:   0.0246 T23:   0.1625                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4040 L22:   2.6029                                     
REMARK   3      L33:   4.2347 L12:   0.6101                                     
REMARK   3      L13:  -2.2154 L23:   0.7983                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0036 S12:   0.1900 S13:   0.1969                       
REMARK   3      S21:  -0.1225 S22:  -0.0260 S23:  -0.5938                       
REMARK   3      S31:  -0.1981 S32:   1.5575 S33:   0.0224                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 37                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   k     6        k   143                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.4950  56.6890  -5.8290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3273 T22:   0.3459                                     
REMARK   3      T33:   0.6653 T12:   0.0389                                     
REMARK   3      T13:   0.1056 T23:   0.0651                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1309 L22:   5.3040                                     
REMARK   3      L33:  13.4063 L12:  -1.3092                                     
REMARK   3      L13:  -1.6468 L23:   6.2987                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4752 S12:   0.0093 S13:  -0.8002                       
REMARK   3      S21:   0.1744 S22:  -0.1564 S23:   1.0396                       
REMARK   3      S31:   0.2684 S32:   0.6417 S33:   0.6316                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 38                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   l     4        l   150                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.8790  72.8150  22.4100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2979 T22:   0.4728                                     
REMARK   3      T33:   0.2853 T12:   0.1549                                     
REMARK   3      T13:   0.0799 T23:   0.2260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.2957 L22:   6.6403                                     
REMARK   3      L33:   5.4594 L12:  -2.8492                                     
REMARK   3      L13:   0.1878 L23:   0.0741                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1445 S12:  -0.4433 S13:   0.0474                       
REMARK   3      S21:  -0.0114 S22:  -0.1815 S23:  -0.3563                       
REMARK   3      S31:   0.0020 S32:   0.6458 S33:   0.3261                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 39                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   m     7        m   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.8260  56.4610  24.5940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1975 T22:   0.3442                                     
REMARK   3      T33:   0.3535 T12:   0.0969                                     
REMARK   3      T13:  -0.0902 T23:   0.2485                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1537 L22:   4.8025                                     
REMARK   3      L33:   8.0598 L12:   1.9214                                     
REMARK   3      L13:   0.0614 L23:   4.0117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0876 S12:  -0.1343 S13:   0.1768                       
REMARK   3      S21:   0.0734 S22:   0.0555 S23:   0.1474                       
REMARK   3      S31:   0.2199 S32:   0.0559 S33:   0.0322                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 40                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   n     4        n   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.8060  79.1400  48.1360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3517 T22:   0.5413                                     
REMARK   3      T33:   0.4967 T12:   0.0510                                     
REMARK   3      T13:   0.1274 T23:   0.0767                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.1180 L22:   4.5318                                     
REMARK   3      L33:   4.5433 L12:  -0.3036                                     
REMARK   3      L13:   2.8067 L23:   1.3588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2273 S12:  -0.2208 S13:   0.9329                       
REMARK   3      S21:   0.0836 S22:  -0.5966 S23:   0.4875                       
REMARK   3      S31:  -0.2112 S32:  -1.1146 S33:   0.3693                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 41                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   o     6        o   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.0380  98.9010  52.6310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3142 T22:   0.1723                                     
REMARK   3      T33:   0.2698 T12:   0.0383                                     
REMARK   3      T13:   0.0235 T23:   0.0714                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.3846 L22:   2.5425                                     
REMARK   3      L33:   3.8299 L12:   2.5726                                     
REMARK   3      L13:   3.8673 L23:   0.6795                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1189 S12:   0.3307 S13:  -0.3070                       
REMARK   3      S21:  -0.0698 S22:   0.0748 S23:  -0.1082                       
REMARK   3      S31:   0.2661 S32:   0.0536 S33:  -0.1937                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 42                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   p     3        p   150                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.4950  87.0710  49.6360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2230 T22:   0.2042                                     
REMARK   3      T33:   0.4733 T12:  -0.0013                                     
REMARK   3      T13:  -0.0009 T23:   0.1132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7169 L22:   1.9699                                     
REMARK   3      L33:  13.1085 L12:   1.0052                                     
REMARK   3      L13:  -0.3900 L23:   0.7639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1458 S12:  -0.0485 S13:  -0.2340                       
REMARK   3      S21:   0.0769 S22:  -0.1057 S23:   0.0815                       
REMARK   3      S31:   0.3165 S32:  -0.1998 S33:   0.2515                       
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 3VON COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB095307.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 121981                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.080                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 2ZFY AND 1J7D                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 90MM TRIS-HCL BUFFER (PH 8.5), 19% PEG   
REMARK 280  3350, 10MM EDTA SODIUM SALT, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  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       68.64250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,      
REMARK 300              16, 17, 18                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I, J                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, P, Q                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, S                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 9                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, U                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 10                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: V, W, X                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 11                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Y, Z                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 12                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 13                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: c, d, e                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 14                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: f, g                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 15                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: h, i                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 16                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: j, k, l                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 17                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: m, n                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 18                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: o, p                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    44                                                      
REMARK 465     TYR A    61                                                      
REMARK 465     ALA A    62                                                      
REMARK 465     GLU A    63                                                      
REMARK 465     ASP A    64                                                      
REMARK 465     ASP A    65                                                      
REMARK 465     ASN A    66                                                      
REMARK 465     ILE A    67                                                      
REMARK 465     TYR A    68                                                      
REMARK 465     ARG A   238                                                      
REMARK 465     GLY A   239                                                      
REMARK 465     GLU A   240                                                      
REMARK 465     GLY A   241                                                      
REMARK 465     GLY A   242                                                      
REMARK 465     THR A   243                                                      
REMARK 465     THR A   244                                                      
REMARK 465     ASN A   245                                                      
REMARK 465     LYS A   271                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     GLY E     3                                                      
REMARK 465     GLY G     3                                                      
REMARK 465     SER H    44                                                      
REMARK 465     TYR H    61                                                      
REMARK 465     ALA H    62                                                      
REMARK 465     GLU H    63                                                      
REMARK 465     MET H   236                                                      
REMARK 465     ASP H   237                                                      
REMARK 465     ARG H   238                                                      
REMARK 465     GLY H   239                                                      
REMARK 465     GLU H   240                                                      
REMARK 465     GLY H   241                                                      
REMARK 465     GLY H   242                                                      
REMARK 465     THR H   243                                                      
REMARK 465     THR H   244                                                      
REMARK 465     LYS H   271                                                      
REMARK 465     GLY J     3                                                      
REMARK 465     GLY L     3                                                      
REMARK 465     GLY N     3                                                      
REMARK 465     SER O    44                                                      
REMARK 465     GLU O    63                                                      
REMARK 465     ASP O    64                                                      
REMARK 465     ASP O    65                                                      
REMARK 465     ARG O   238                                                      
REMARK 465     GLY O   239                                                      
REMARK 465     GLU O   240                                                      
REMARK 465     GLY O   241                                                      
REMARK 465     GLY O   242                                                      
REMARK 465     THR O   243                                                      
REMARK 465     THR O   244                                                      
REMARK 465     ASN O   245                                                      
REMARK 465     GLY Q     3                                                      
REMARK 465     GLY R     6                                                      
REMARK 465     GLY U     3                                                      
REMARK 465     SER V    44                                                      
REMARK 465     TYR V    61                                                      
REMARK 465     ALA V    62                                                      
REMARK 465     GLU V    63                                                      
REMARK 465     ASP V    64                                                      
REMARK 465     ASP V    65                                                      
REMARK 465     ARG V   238                                                      
REMARK 465     GLY V   239                                                      
REMARK 465     GLU V   240                                                      
REMARK 465     GLY V   241                                                      
REMARK 465     GLY V   242                                                      
REMARK 465     THR V   243                                                      
REMARK 465     THR V   244                                                      
REMARK 465     GLY W     6                                                      
REMARK 465     GLY X     3                                                      
REMARK 465     GLY Y     6                                                      
REMARK 465     GLY b     3                                                      
REMARK 465     SER c    44                                                      
REMARK 465     TYR c    61                                                      
REMARK 465     ALA c    62                                                      
REMARK 465     GLU c    63                                                      
REMARK 465     ASP c    64                                                      
REMARK 465     ASP c    65                                                      
REMARK 465     ARG c   238                                                      
REMARK 465     GLY c   239                                                      
REMARK 465     GLU c   240                                                      
REMARK 465     GLY c   241                                                      
REMARK 465     LYS c   271                                                      
REMARK 465     GLY e     3                                                      
REMARK 465     GLY f     6                                                      
REMARK 465     SER j    44                                                      
REMARK 465     ASN j    45                                                      
REMARK 465     TYR j    61                                                      
REMARK 465     ALA j    62                                                      
REMARK 465     GLU j    63                                                      
REMARK 465     ASP j    64                                                      
REMARK 465     ASP j    65                                                      
REMARK 465     ASN j    66                                                      
REMARK 465     TYR j   235                                                      
REMARK 465     MET j   236                                                      
REMARK 465     ASP j   237                                                      
REMARK 465     ARG j   238                                                      
REMARK 465     GLY j   239                                                      
REMARK 465     GLU j   240                                                      
REMARK 465     GLY j   241                                                      
REMARK 465     GLY j   242                                                      
REMARK 465     THR j   243                                                      
REMARK 465     LYS j   271                                                      
REMARK 465     GLY l     3                                                      
REMARK 465     GLY m     6                                                      
REMARK 465     GLY n     3                                                      
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    GLU N    18     NH2  ARG N   102              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU C 106   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    LEU G 121   CA  -  CB  -  CG  ANGL. DEV. =  16.7 DEGREES          
REMARK 500    LEU e 106   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    LEU l 106   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 186       37.58    -93.07                                   
REMARK 500    VAL A 208      -61.90   -104.33                                   
REMARK 500    ASP A 216     -169.11   -128.34                                   
REMARK 500    PRO A 263      100.46    -49.38                                   
REMARK 500    PRO B  71       -7.63    -55.06                                   
REMARK 500    LYS B 108       49.21    -99.64                                   
REMARK 500    ALA C  32       -4.22    -59.18                                   
REMARK 500    LYS C  92     -101.89   -144.63                                   
REMARK 500    LYS C  94       40.77    -93.95                                   
REMARK 500    ASN C 116     -178.80    -52.39                                   
REMARK 500    ASP C 119      103.19     80.73                                   
REMARK 500    THR C 131      -72.30   -115.26                                   
REMARK 500    ASP D  40       96.71    -67.95                                   
REMARK 500    ASN D  57       -0.97    -56.32                                   
REMARK 500    GLU D  59      135.75    -38.02                                   
REMARK 500    PRO D  71        7.46    -69.87                                   
REMARK 500    ASP E  44        6.21     59.02                                   
REMARK 500    ILE E  90        3.82    -68.96                                   
REMARK 500    LYS E  92      -58.83   -150.02                                   
REMARK 500    ASP F  40       95.88    -67.31                                   
REMARK 500    ASN F  92       90.48    -63.47                                   
REMARK 500    ASN F  93      -43.79      1.80                                   
REMARK 500    LYS F 108       40.31   -100.17                                   
REMARK 500    GLU G  18       78.28   -116.38                                   
REMARK 500    ASP G  44       -5.53     69.65                                   
REMARK 500    LYS G  92      -51.95   -152.01                                   
REMARK 500    LYS G  94       40.44   -109.23                                   
REMARK 500    PRO G 117       31.10    -90.04                                   
REMARK 500    ASP G 119     -161.31    -73.04                                   
REMARK 500    ALA G 122       19.44    -69.33                                   
REMARK 500    LYS H  78      -31.23   -130.29                                   
REMARK 500    GLN H 152       89.10    -37.12                                   
REMARK 500    GLU H 186       41.15    -96.22                                   
REMARK 500    PRO H 263       95.56    -47.05                                   
REMARK 500    VAL I  26       99.85     44.34                                   
REMARK 500    ARG I  55       11.11     84.65                                   
REMARK 500    ASN I  60       -6.27     61.55                                   
REMARK 500    ASN I  93       -8.61   -143.29                                   
REMARK 500    MET I  97       95.71    -64.05                                   
REMARK 500    VAL I 105      -80.86    -76.23                                   
REMARK 500    LEU I 106      -36.08    -39.30                                   
REMARK 500    ALA I 107      -88.18    -57.72                                   
REMARK 500    LYS I 116      -70.42    -46.31                                   
REMARK 500    ARG J   6      -36.04    -38.99                                   
REMARK 500    ASP J  44       -0.02     69.21                                   
REMARK 500    PRO J  46        3.86    -62.80                                   
REMARK 500    LYS J  92     -109.65   -121.11                                   
REMARK 500    ASN J 123     -178.44    -59.17                                   
REMARK 500    THR J 131      -70.26    -98.90                                   
REMARK 500    ASP K  38        7.36    -67.24                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     177 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3VON A   45   271  UNP    Q96FW1   OTUB1_HUMAN     45    271             
DBREF  3VON B    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON C    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON D    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON E    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON F    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON G    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON H   45   271  UNP    Q96FW1   OTUB1_HUMAN     45    271             
DBREF  3VON I    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON J    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON K    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON L    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON M    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON N    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON O   45   271  UNP    Q96FW1   OTUB1_HUMAN     45    271             
DBREF  3VON P    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON Q    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON R    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON S    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON T    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON U    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON V   45   271  UNP    Q96FW1   OTUB1_HUMAN     45    271             
DBREF  3VON W    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON X    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON Y    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON Z    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON a    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON b    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON c   45   271  UNP    Q96FW1   OTUB1_HUMAN     45    271             
DBREF  3VON d    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON e    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON f    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON g    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON h    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON i    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON j   45   271  UNP    Q96FW1   OTUB1_HUMAN     45    271             
DBREF  3VON k    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON l    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON m    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON n    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
DBREF  3VON o    6   143  UNP    Q15819   UB2V2_HUMAN      6    143             
DBREF  3VON p    3   150  UNP    P61088   UBE2N_HUMAN      3    150             
SEQADV 3VON SER A   44  UNP  Q96FW1              EXPRESSION TAG                 
SEQADV 3VON SER H   44  UNP  Q96FW1              EXPRESSION TAG                 
SEQADV 3VON SER O   44  UNP  Q96FW1              EXPRESSION TAG                 
SEQADV 3VON SER V   44  UNP  Q96FW1              EXPRESSION TAG                 
SEQADV 3VON SER c   44  UNP  Q96FW1              EXPRESSION TAG                 
SEQADV 3VON SER j   44  UNP  Q96FW1              EXPRESSION TAG                 
SEQRES   1 A  228  SER ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SER VAL          
SEQRES   2 A  228  LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE TYR GLN          
SEQRES   3 A  228  GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER TYR ILE          
SEQRES   4 A  228  ARG LYS THR ARG PRO ASP GLY ASN CYS PHE TYR ARG ALA          
SEQRES   5 A  228  PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP ASP SER          
SEQRES   6 A  228  LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA LYS SER          
SEQRES   7 A  228  LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU PHE THR          
SEQRES   8 A  228  ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU ILE GLU          
SEQRES   9 A  228  GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU LEU ALA          
SEQRES  10 A  228  SER PHE ASN ASP GLN SER THR SER ASP TYR LEU VAL VAL          
SEQRES  11 A  228  TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN ARG GLU          
SEQRES  12 A  228  SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY ARG THR          
SEQRES  13 A  228  VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO MET CYS          
SEQRES  14 A  228  LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU ALA GLN          
SEQRES  15 A  228  ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET ASP ARG          
SEQRES  16 A  228  GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE PRO GLU          
SEQRES  17 A  228  GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG PRO GLY          
SEQRES  18 A  228  HIS TYR ASP ILE LEU TYR LYS                                  
SEQRES   1 B  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 B  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 B  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 B  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 B  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 B  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 B  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 B  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 B  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 B  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 B  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 C  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 C  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 C  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 C  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 C  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 C  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 C  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 C  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 C  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 C  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 C  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 C  148  LEU TYR ALA MET ASN                                          
SEQRES   1 D  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 D  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 D  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 D  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 D  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 D  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 D  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 D  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 D  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 D  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 D  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 E  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 E  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 E  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 E  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 E  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 E  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 E  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 E  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 E  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 E  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 E  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 E  148  LEU TYR ALA MET ASN                                          
SEQRES   1 F  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 F  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 F  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 F  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 F  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 F  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 F  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 F  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 F  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 F  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 F  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 G  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 G  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 G  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 G  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 G  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 G  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 G  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 G  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 G  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 G  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 G  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 G  148  LEU TYR ALA MET ASN                                          
SEQRES   1 H  228  SER ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SER VAL          
SEQRES   2 H  228  LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE TYR GLN          
SEQRES   3 H  228  GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER TYR ILE          
SEQRES   4 H  228  ARG LYS THR ARG PRO ASP GLY ASN CYS PHE TYR ARG ALA          
SEQRES   5 H  228  PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP ASP SER          
SEQRES   6 H  228  LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA LYS SER          
SEQRES   7 H  228  LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU PHE THR          
SEQRES   8 H  228  ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU ILE GLU          
SEQRES   9 H  228  GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU LEU ALA          
SEQRES  10 H  228  SER PHE ASN ASP GLN SER THR SER ASP TYR LEU VAL VAL          
SEQRES  11 H  228  TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN ARG GLU          
SEQRES  12 H  228  SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY ARG THR          
SEQRES  13 H  228  VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO MET CYS          
SEQRES  14 H  228  LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU ALA GLN          
SEQRES  15 H  228  ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET ASP ARG          
SEQRES  16 H  228  GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE PRO GLU          
SEQRES  17 H  228  GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG PRO GLY          
SEQRES  18 H  228  HIS TYR ASP ILE LEU TYR LYS                                  
SEQRES   1 I  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 I  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 I  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 I  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 I  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 I  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 I  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 I  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 I  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 I  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 I  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 J  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 J  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 J  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 J  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 J  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 J  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 J  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 J  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 J  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 J  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 J  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 J  148  LEU TYR ALA MET ASN                                          
SEQRES   1 K  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 K  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 K  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 K  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 K  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 K  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 K  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 K  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 K  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 K  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 K  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 L  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 L  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 L  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 L  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 L  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 L  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 L  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 L  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 L  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 L  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 L  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 L  148  LEU TYR ALA MET ASN                                          
SEQRES   1 M  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 M  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 M  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 M  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 M  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 M  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 M  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 M  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 M  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 M  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 M  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 N  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 N  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 N  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 N  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 N  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 N  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 N  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 N  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 N  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 N  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 N  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 N  148  LEU TYR ALA MET ASN                                          
SEQRES   1 O  228  SER ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SER VAL          
SEQRES   2 O  228  LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE TYR GLN          
SEQRES   3 O  228  GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER TYR ILE          
SEQRES   4 O  228  ARG LYS THR ARG PRO ASP GLY ASN CYS PHE TYR ARG ALA          
SEQRES   5 O  228  PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP ASP SER          
SEQRES   6 O  228  LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA LYS SER          
SEQRES   7 O  228  LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU PHE THR          
SEQRES   8 O  228  ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU ILE GLU          
SEQRES   9 O  228  GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU LEU ALA          
SEQRES  10 O  228  SER PHE ASN ASP GLN SER THR SER ASP TYR LEU VAL VAL          
SEQRES  11 O  228  TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN ARG GLU          
SEQRES  12 O  228  SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY ARG THR          
SEQRES  13 O  228  VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO MET CYS          
SEQRES  14 O  228  LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU ALA GLN          
SEQRES  15 O  228  ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET ASP ARG          
SEQRES  16 O  228  GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE PRO GLU          
SEQRES  17 O  228  GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG PRO GLY          
SEQRES  18 O  228  HIS TYR ASP ILE LEU TYR LYS                                  
SEQRES   1 P  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 P  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 P  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 P  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 P  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 P  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 P  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 P  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 P  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 P  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 P  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 Q  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 Q  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 Q  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 Q  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 Q  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 Q  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 Q  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 Q  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 Q  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 Q  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 Q  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 Q  148  LEU TYR ALA MET ASN                                          
SEQRES   1 R  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 R  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 R  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 R  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 R  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 R  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 R  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 R  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 R  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 R  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 R  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 S  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 S  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 S  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 S  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 S  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 S  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 S  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 S  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 S  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 S  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 S  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 S  148  LEU TYR ALA MET ASN                                          
SEQRES   1 T  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 T  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 T  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 T  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 T  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 T  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 T  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 T  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 T  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 T  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 T  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 U  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 U  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 U  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 U  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 U  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 U  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 U  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 U  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 U  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 U  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 U  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 U  148  LEU TYR ALA MET ASN                                          
SEQRES   1 V  228  SER ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SER VAL          
SEQRES   2 V  228  LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE TYR GLN          
SEQRES   3 V  228  GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER TYR ILE          
SEQRES   4 V  228  ARG LYS THR ARG PRO ASP GLY ASN CYS PHE TYR ARG ALA          
SEQRES   5 V  228  PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP ASP SER          
SEQRES   6 V  228  LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA LYS SER          
SEQRES   7 V  228  LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU PHE THR          
SEQRES   8 V  228  ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU ILE GLU          
SEQRES   9 V  228  GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU LEU ALA          
SEQRES  10 V  228  SER PHE ASN ASP GLN SER THR SER ASP TYR LEU VAL VAL          
SEQRES  11 V  228  TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN ARG GLU          
SEQRES  12 V  228  SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY ARG THR          
SEQRES  13 V  228  VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO MET CYS          
SEQRES  14 V  228  LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU ALA GLN          
SEQRES  15 V  228  ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET ASP ARG          
SEQRES  16 V  228  GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE PRO GLU          
SEQRES  17 V  228  GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG PRO GLY          
SEQRES  18 V  228  HIS TYR ASP ILE LEU TYR LYS                                  
SEQRES   1 W  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 W  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 W  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 W  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 W  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 W  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 W  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 W  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 W  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 W  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 W  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 X  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 X  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 X  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 X  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 X  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 X  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 X  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 X  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 X  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 X  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 X  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 X  148  LEU TYR ALA MET ASN                                          
SEQRES   1 Y  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 Y  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 Y  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 Y  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 Y  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 Y  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 Y  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 Y  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 Y  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 Y  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 Y  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 Z  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 Z  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 Z  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 Z  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 Z  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 Z  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 Z  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 Z  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 Z  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 Z  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 Z  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 Z  148  LEU TYR ALA MET ASN                                          
SEQRES   1 a  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 a  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 a  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 a  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 a  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 a  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 a  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 a  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 a  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 a  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 a  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 b  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 b  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 b  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 b  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 b  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 b  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 b  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 b  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 b  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 b  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 b  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 b  148  LEU TYR ALA MET ASN                                          
SEQRES   1 c  228  SER ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SER VAL          
SEQRES   2 c  228  LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE TYR GLN          
SEQRES   3 c  228  GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER TYR ILE          
SEQRES   4 c  228  ARG LYS THR ARG PRO ASP GLY ASN CYS PHE TYR ARG ALA          
SEQRES   5 c  228  PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP ASP SER          
SEQRES   6 c  228  LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA LYS SER          
SEQRES   7 c  228  LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU PHE THR          
SEQRES   8 c  228  ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU ILE GLU          
SEQRES   9 c  228  GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU LEU ALA          
SEQRES  10 c  228  SER PHE ASN ASP GLN SER THR SER ASP TYR LEU VAL VAL          
SEQRES  11 c  228  TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN ARG GLU          
SEQRES  12 c  228  SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY ARG THR          
SEQRES  13 c  228  VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO MET CYS          
SEQRES  14 c  228  LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU ALA GLN          
SEQRES  15 c  228  ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET ASP ARG          
SEQRES  16 c  228  GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE PRO GLU          
SEQRES  17 c  228  GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG PRO GLY          
SEQRES  18 c  228  HIS TYR ASP ILE LEU TYR LYS                                  
SEQRES   1 d  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 d  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 d  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 d  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 d  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 d  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 d  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 d  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 d  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 d  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 d  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 e  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 e  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 e  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 e  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 e  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 e  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 e  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 e  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 e  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 e  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 e  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 e  148  LEU TYR ALA MET ASN                                          
SEQRES   1 f  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 f  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 f  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 f  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 f  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 f  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 f  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 f  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 f  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 f  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 f  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 g  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 g  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 g  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 g  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 g  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 g  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 g  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 g  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 g  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 g  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 g  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 g  148  LEU TYR ALA MET ASN                                          
SEQRES   1 h  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 h  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 h  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 h  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 h  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 h  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 h  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 h  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 h  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 h  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 h  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 i  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 i  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 i  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 i  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 i  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 i  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 i  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 i  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 i  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 i  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 i  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 i  148  LEU TYR ALA MET ASN                                          
SEQRES   1 j  228  SER ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SER VAL          
SEQRES   2 j  228  LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE TYR GLN          
SEQRES   3 j  228  GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER TYR ILE          
SEQRES   4 j  228  ARG LYS THR ARG PRO ASP GLY ASN CYS PHE TYR ARG ALA          
SEQRES   5 j  228  PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP ASP SER          
SEQRES   6 j  228  LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA LYS SER          
SEQRES   7 j  228  LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU PHE THR          
SEQRES   8 j  228  ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU ILE GLU          
SEQRES   9 j  228  GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU LEU ALA          
SEQRES  10 j  228  SER PHE ASN ASP GLN SER THR SER ASP TYR LEU VAL VAL          
SEQRES  11 j  228  TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN ARG GLU          
SEQRES  12 j  228  SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY ARG THR          
SEQRES  13 j  228  VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO MET CYS          
SEQRES  14 j  228  LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU ALA GLN          
SEQRES  15 j  228  ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET ASP ARG          
SEQRES  16 j  228  GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE PRO GLU          
SEQRES  17 j  228  GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG PRO GLY          
SEQRES  18 j  228  HIS TYR ASP ILE LEU TYR LYS                                  
SEQRES   1 k  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 k  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 k  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 k  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 k  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 k  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 k  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 k  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 k  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 k  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 k  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 l  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 l  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 l  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 l  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 l  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 l  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 l  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 l  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 l  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 l  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 l  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 l  148  LEU TYR ALA MET ASN                                          
SEQRES   1 m  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 m  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 m  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 m  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 m  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 m  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 m  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 m  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 m  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 m  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 m  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 n  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 n  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 n  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 n  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 n  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 n  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 n  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 n  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 n  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 n  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 n  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 n  148  LEU TYR ALA MET ASN                                          
SEQRES   1 o  138  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   2 o  138  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   3 o  138  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   4 o  138  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   5 o  138  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   6 o  138  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   7 o  138  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   8 o  138  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES   9 o  138  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  10 o  138  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  11 o  138  GLN PRO PRO GLU GLY GLN THR TYR                              
SEQRES   1 p  148  GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN ARG LEU          
SEQRES   2 p  148  LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP          
SEQRES   3 p  148  GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY          
SEQRES   4 p  148  PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE LYS LEU          
SEQRES   5 p  148  GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA ALA PRO          
SEQRES   6 p  148  LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO ASN VAL          
SEQRES   7 p  148  ASP LYS LEU GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP          
SEQRES   8 p  148  LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL LEU LEU          
SEQRES   9 p  148  SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO ASP ASP          
SEQRES  10 p  148  PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS THR ASN          
SEQRES  11 p  148  GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP THR ARG          
SEQRES  12 p  148  LEU TYR ALA MET ASN                                          
HELIX    1   1 SER A   55  GLU A   60  5                                   6    
HELIX    2   2 GLN A   70  LYS A   77  1                                   8    
HELIX    3   3 ASN A   90  LEU A  104  1                                  15    
HELIX    4   4 ASP A  107  SER A  127  1                                  21    
HELIX    5   5 THR A  131  LYS A  151  1                                  21    
HELIX    6   6 SER A  154  ASN A  163  1                                  10    
HELIX    7   7 ASP A  164  GLU A  186  1                                  23    
HELIX    8   8 GLU A  186  GLU A  191  1                                   6    
HELIX    9   9 HIS A  192  ILE A  194  5                                   3    
HELIX   10  10 THR A  199  GLU A  207  1                                   9    
HELIX   11  11 ASP A  216  SER A  228  1                                  13    
HELIX   12  12 PRO B   10  GLY B   25  1                                  16    
HELIX   13  13 ILE B  103  LYS B  108  1                                   6    
HELIX   14  14 SER B  114  MET B  126  1                                  13    
HELIX   15  15 PRO C    5  GLU C   18  1                                  14    
HELIX   16  16 LEU C   88  LYS C   92  5                                   5    
HELIX   17  17 GLN C  100  ALA C  114  1                                  15    
HELIX   18  18 ASN C  123  THR C  131  1                                   9    
HELIX   19  19 ASN C  132  MET C  149  1                                  18    
HELIX   20  20 PRO D   10  GLY D   25  1                                  16    
HELIX   21  21 ASP D   99  SER D  102  5                                   4    
HELIX   22  22 ILE D  103  LYS D  108  1                                   6    
HELIX   23  23 SER D  114  MET D  126  1                                  13    
HELIX   24  24 PRO E    5  GLU E   18  1                                  14    
HELIX   25  25 LEU E   88  LYS E   92  5                                   5    
HELIX   26  26 GLN E  100  ALA E  114  1                                  15    
HELIX   27  27 ASP E  124  ASN E  132  1                                   9    
HELIX   28  28 ASN E  132  ALA E  148  1                                  17    
HELIX   29  29 PRO F   10  GLY F   25  1                                  16    
HELIX   30  30 ILE F  103  LYS F  108  1                                   6    
HELIX   31  31 SER F  114  MET F  126  1                                  13    
HELIX   32  32 PRO G    5  GLU G   18  1                                  14    
HELIX   33  33 LEU G   88  LYS G   92  5                                   5    
HELIX   34  34 GLN G  100  ALA G  114  1                                  15    
HELIX   35  35 ASN G  123  ASN G  132  1                                  10    
HELIX   36  36 ASN G  132  ALA G  148  1                                  17    
HELIX   37  37 SER H   55  TYR H   58  5                                   4    
HELIX   38  38 TYR H   68  LYS H   77  1                                  10    
HELIX   39  39 ASN H   90  GLU H  102  1                                  13    
HELIX   40  40 ALA H  103  ASP H  106  5                                   4    
HELIX   41  41 ASP H  107  SER H  127  1                                  21    
HELIX   42  42 THR H  131  LEU H  145  1                                  15    
HELIX   43  43 ILE H  146  LYS H  151  1                                   6    
HELIX   44  44 SER H  154  ASN H  163  1                                  10    
HELIX   45  45 ASP H  164  GLU H  186  1                                  23    
HELIX   46  46 GLU H  186  GLU H  191  1                                   6    
HELIX   47  47 HIS H  192  ILE H  194  5                                   3    
HELIX   48  48 THR H  199  VAL H  208  1                                  10    
HELIX   49  49 ASP H  216  LEU H  227  1                                  12    
HELIX   50  50 PRO I   10  GLY I   25  1                                  16    
HELIX   51  51 ILE I  103  LYS I  108  1                                   6    
HELIX   52  52 SER I  114  LEU I  125  1                                  12    
HELIX   53  53 SER I  128  LYS I  133  1                                   6    
HELIX   54  54 PRO J    5  GLU J   18  1                                  14    
HELIX   55  55 LEU J   88  LYS J   92  5                                   5    
HELIX   56  56 GLN J  100  ALA J  114  1                                  15    
HELIX   57  57 ASN J  123  ASN J  132  1                                  10    
HELIX   58  58 ASN J  132  ALA J  148  1                                  17    
HELIX   59  59 PRO K   10  GLY K   25  1                                  16    
HELIX   60  60 ASP K   99  SER K  102  5                                   4    
HELIX   61  61 ILE K  103  LYS K  108  1                                   6    
HELIX   62  62 SER K  114  MET K  126  1                                  13    
HELIX   63  63 SER K  128  LYS K  133  1                                   6    
HELIX   64  64 PRO L    5  GLU L   18  1                                  14    
HELIX   65  65 LEU L   88  LYS L   92  5                                   5    
HELIX   66  66 GLN L  100  ALA L  114  1                                  15    
HELIX   67  67 ASN L  123  ASN L  132  1                                  10    
HELIX   68  68 ASN L  132  ALA L  148  1                                  17    
HELIX   69  69 PRO M   10  GLY M   25  1                                  16    
HELIX   70  70 ASP M   99  SER M  102  5                                   4    
HELIX   71  71 ILE M  103  LYS M  108  1                                   6    
HELIX   72  72 SER M  114  MET M  126  1                                  13    
HELIX   73  73 PRO N    5  GLU N   18  1                                  14    
HELIX   74  74 GLN N  100  ALA N  114  1                                  15    
HELIX   75  75 ASN N  123  ASN N  132  1                                  10    
HELIX   76  76 ASN N  132  ALA N  148  1                                  17    
HELIX   77  77 VAL O   56  TYR O   61  1                                   6    
HELIX   78  78 GLN O   69  LYS O   77  1                                   9    
HELIX   79  79 ASN O   90  LEU O  104  1                                  15    
HELIX   80  80 ASP O  107  GLY O  129  1                                  23    
HELIX   81  81 THR O  131  LYS O  151  1                                  21    
HELIX   82  82 SER O  154  PHE O  162  1                                   9    
HELIX   83  83 ASP O  164  GLU O  186  1                                  23    
HELIX   84  84 GLU O  186  GLU O  191  1                                   6    
HELIX   85  85 HIS O  192  ILE O  194  5                                   3    
HELIX   86  86 THR O  199  VAL O  208  1                                  10    
HELIX   87  87 ASP O  216  LEU O  227  1                                  12    
HELIX   88  88 PRO P   10  GLY P   25  1                                  16    
HELIX   89  89 ILE P  103  LYS P  108  1                                   6    
HELIX   90  90 SER P  114  MET P  126  1                                  13    
HELIX   91  91 SER P  128  LYS P  133  1                                   6    
HELIX   92  92 PRO Q    5  GLU Q   18  1                                  14    
HELIX   93  93 LEU Q   88  LYS Q   92  5                                   5    
HELIX   94  94 GLN Q  100  ALA Q  114  1                                  15    
HELIX   95  95 ASN Q  123  ASN Q  132  1                                  10    
HELIX   96  96 ASN Q  132  ALA Q  148  1                                  17    
HELIX   97  97 PRO R   10  GLY R   25  1                                  16    
HELIX   98  98 ASP R   99  SER R  102  5                                   4    
HELIX   99  99 ILE R  103  LYS R  108  1                                   6    
HELIX  100 100 SER R  114  LEU R  125  1                                  12    
HELIX  101 101 SER R  128  LYS R  133  1                                   6    
HELIX  102 102 PRO S    5  GLU S   18  1                                  14    
HELIX  103 103 LEU S   88  LYS S   92  5                                   5    
HELIX  104 104 GLN S  100  ALA S  114  1                                  15    
HELIX  105 105 ASP S  124  ASN S  132  1                                   9    
HELIX  106 106 ASN S  132  ALA S  148  1                                  17    
HELIX  107 107 PRO T   10  GLY T   25  1                                  16    
HELIX  108 108 ASP T   99  SER T  102  5                                   4    
HELIX  109 109 ILE T  103  LYS T  108  1                                   6    
HELIX  110 110 SER T  114  LEU T  125  1                                  12    
HELIX  111 111 PRO U    5  GLU U   18  1                                  14    
HELIX  112 112 LEU U   88  LYS U   92  5                                   5    
HELIX  113 113 GLN U  100  ALA U  114  1                                  15    
HELIX  114 114 ASN U  123  ASN U  132  1                                  10    
HELIX  115 115 ASN U  132  ALA U  148  1                                  17    
HELIX  116 116 SER V   55  TYR V   58  5                                   4    
HELIX  117 117 GLN V   69  LYS V   77  1                                   9    
HELIX  118 118 ASN V   90  LEU V  104  1                                  15    
HELIX  119 119 ASP V  107  SER V  127  1                                  21    
HELIX  120 120 THR V  131  LYS V  151  1                                  21    
HELIX  121 121 SER V  154  ASN V  163  1                                  10    
HELIX  122 122 ASP V  164  GLU V  186  1                                  23    
HELIX  123 123 GLU V  186  GLU V  191  1                                   6    
HELIX  124 124 HIS V  192  ILE V  194  5                                   3    
HELIX  125 125 THR V  199  VAL V  208  1                                  10    
HELIX  126 126 ASP V  216  LEU V  227  1                                  12    
HELIX  127 127 PRO W   10  GLY W   25  1                                  16    
HELIX  128 128 ILE W  103  LYS W  108  1                                   6    
HELIX  129 129 SER W  114  MET W  126  1                                  13    
HELIX  130 130 SER W  128  LYS W  133  1                                   6    
HELIX  131 131 PRO X    5  GLU X   18  1                                  14    
HELIX  132 132 LEU X   88  LYS X   92  5                                   5    
HELIX  133 133 GLN X  100  ALA X  114  1                                  15    
HELIX  134 134 ASN X  123  ASN X  132  1                                  10    
HELIX  135 135 ASN X  132  ALA X  148  1                                  17    
HELIX  136 136 PRO Y   10  GLY Y   25  1                                  16    
HELIX  137 137 ASP Y   99  SER Y  102  5                                   4    
HELIX  138 138 ILE Y  103  LYS Y  108  1                                   6    
HELIX  139 139 SER Y  114  MET Y  126  1                                  13    
HELIX  140 140 SER Y  128  LYS Y  133  1                                   6    
HELIX  141 141 PRO Z    5  GLU Z   18  1                                  14    
HELIX  142 142 LEU Z   88  LYS Z   92  5                                   5    
HELIX  143 143 GLN Z  100  ALA Z  114  1                                  15    
HELIX  144 144 ASP Z  124  ASN Z  132  1                                   9    
HELIX  145 145 ASN Z  132  ALA Z  148  1                                  17    
HELIX  146 146 PRO a   10  GLY a   25  1                                  16    
HELIX  147 147 ASP a   99  SER a  102  5                                   4    
HELIX  148 148 ILE a  103  LYS a  108  1                                   6    
HELIX  149 149 SER a  114  MET a  126  1                                  13    
HELIX  150 150 PRO b    5  GLU b   18  1                                  14    
HELIX  151 151 LEU b   88  LYS b   92  5                                   5    
HELIX  152 152 GLN b  100  ALA b  114  1                                  15    
HELIX  153 153 VAL b  125  ASN b  132  1                                   8    
HELIX  154 154 ASN b  132  ALA b  148  1                                  17    
HELIX  155 155 SER c   55  GLU c   60  5                                   6    
HELIX  156 156 TYR c   68  LYS c   77  1                                  10    
HELIX  157 157 ASN c   90  LEU c  104  1                                  15    
HELIX  158 158 ASP c  107  GLN c  128  1                                  22    
HELIX  159 159 THR c  131  LYS c  151  1                                  21    
HELIX  160 160 SER c  154  ALA c  160  1                                   7    
HELIX  161 161 ASP c  164  GLU c  186  1                                  23    
HELIX  162 162 GLU c  186  GLU c  191  1                                   6    
HELIX  163 163 HIS c  192  ILE c  194  5                                   3    
HELIX  164 164 THR c  199  VAL c  208  1                                  10    
HELIX  165 165 ASP c  216  SER c  228  1                                  13    
HELIX  166 166 PRO d   10  GLY d   25  1                                  16    
HELIX  167 167 SER d  114  MET d  126  1                                  13    
HELIX  168 168 SER d  128  LYS d  133  1                                   6    
HELIX  169 169 PRO e    5  GLU e   18  1                                  14    
HELIX  170 170 LEU e   88  LYS e   92  5                                   5    
HELIX  171 171 GLN e  100  ALA e  114  1                                  15    
HELIX  172 172 VAL e  125  ASN e  132  1                                   8    
HELIX  173 173 ASN e  132  ALA e  148  1                                  17    
HELIX  174 174 PRO f   10  GLY f   25  1                                  16    
HELIX  175 175 ASP f   99  SER f  102  5                                   4    
HELIX  176 176 ILE f  103  LYS f  108  1                                   6    
HELIX  177 177 SER f  114  LEU f  125  1                                  12    
HELIX  178 178 MET f  126  SER f  128  5                                   3    
HELIX  179 179 PRO g    5  GLU g   18  1                                  14    
HELIX  180 180 LEU g   88  LYS g   92  5                                   5    
HELIX  181 181 GLN g  100  ALA g  114  1                                  15    
HELIX  182 182 ASN g  123  ASN g  132  1                                  10    
HELIX  183 183 ASN g  132  ALA g  148  1                                  17    
HELIX  184 184 PRO h   10  GLY h   25  1                                  16    
HELIX  185 185 ILE h  103  LYS h  108  1                                   6    
HELIX  186 186 SER h  114  MET h  126  1                                  13    
HELIX  187 187 PRO i    5  GLU i   18  1                                  14    
HELIX  188 188 LEU i   88  LYS i   92  5                                   5    
HELIX  189 189 GLN i  100  ALA i  114  1                                  15    
HELIX  190 190 ASN i  123  ASN i  132  1                                  10    
HELIX  191 191 ASN i  132  ALA i  148  1                                  17    
HELIX  192 192 SER j   55  TYR j   58  5                                   4    
HELIX  193 193 LYS j   71  LYS j   77  1                                   7    
HELIX  194 194 CYS j   91  HIS j  100  1                                  10    
HELIX  195 195 ASP j  107  SER j  127  1                                  21    
HELIX  196 196 THR j  131  THR j  134  5                                   4    
HELIX  197 197 ILE j  135  LYS j  151  1                                  17    
HELIX  198 198 SER j  154  ASN j  163  1                                  10    
HELIX  199 199 ASP j  164  GLU j  186  1                                  23    
HELIX  200 200 GLU j  186  GLU j  191  1                                   6    
HELIX  201 201 HIS j  192  ILE j  194  5                                   3    
HELIX  202 202 THR j  199  VAL j  208  1                                  10    
HELIX  203 203 ASP j  216  LEU j  227  1                                  12    
HELIX  204 204 PRO k   10  GLY k   25  1                                  16    
HELIX  205 205 SER k  114  LEU k  125  1                                  12    
HELIX  206 206 MET k  126  SER k  128  5                                   3    
HELIX  207 207 PRO l    5  GLU l   18  1                                  14    
HELIX  208 208 LEU l   88  LYS l   92  5                                   5    
HELIX  209 209 GLN l  100  ALA l  114  1                                  15    
HELIX  210 210 ASN l  123  ASN l  132  1                                  10    
HELIX  211 211 ASN l  132  ALA l  148  1                                  17    
HELIX  212 212 PRO m   10  GLY m   25  1                                  16    
HELIX  213 213 ASP m   99  SER m  102  5                                   4    
HELIX  214 214 ILE m  103  LYS m  108  1                                   6    
HELIX  215 215 SER m  114  MET m  126  1                                  13    
HELIX  216 216 PRO n    5  GLU n   18  1                                  14    
HELIX  217 217 LEU n   88  LYS n   92  5                                   5    
HELIX  218 218 GLN n  100  ALA n  114  1                                  15    
HELIX  219 219 ASN n  123  ASN n  132  1                                  10    
HELIX  220 220 ASN n  132  ALA n  148  1                                  17    
HELIX  221 221 PRO o   10  GLY o   25  1                                  16    
HELIX  222 222 ASP o   99  SER o  102  5                                   4    
HELIX  223 223 ILE o  103  LYS o  108  1                                   6    
HELIX  224 224 SER o  114  MET o  126  1                                  13    
HELIX  225 225 PRO p    5  GLU p   18  1                                  14    
HELIX  226 226 LEU p   88  LYS p   92  5                                   5    
HELIX  227 227 GLN p  100  ALA p  114  1                                  15    
HELIX  228 228 VAL p  125  ASN p  132  1                                   8    
HELIX  229 229 ASN p  132  ALA p  148  1                                  17    
SHEET    1   A 6 LEU A  52  GLU A  53  0                                        
SHEET    2   A 6 TYR A  81  ARG A  83 -1  O  ILE A  82   N  LEU A  52           
SHEET    3   A 6 HIS A 265  TYR A 270 -1  O  ILE A 268   N  ARG A  83           
SHEET    4   A 6 VAL A 257  ARG A 262 -1  N  ARG A 262   O  HIS A 265           
SHEET    5   A 6 ILE A 231  TYR A 235  1  N  GLU A 234   O  LEU A 259           
SHEET    6   A 6 HIS A 247  PHE A 249 -1  O  PHE A 249   N  ILE A 231           
SHEET    1   B 4 VAL B  31  SER B  32  0                                        
SHEET    2   B 4 ARG B  45  ILE B  51 -1  O  MET B  49   N  SER B  32           
SHEET    3   B 4 ILE B  62  GLU B  68 -1  O  VAL B  67   N  TRP B  46           
SHEET    4   B 4 SER B  79  PHE B  82 -1  O  ARG B  81   N  LYS B  66           
SHEET    1   C 4 ILE C  23  PRO C  27  0                                        
SHEET    2   C 4 TYR C  34  ALA C  40 -1  O  VAL C  38   N  LYS C  24           
SHEET    3   C 4 THR C  51  PHE C  57 -1  O  LEU C  54   N  VAL C  37           
SHEET    4   C 4 LYS C  68  PHE C  71 -1  O  LYS C  68   N  PHE C  57           
SHEET    1   D 4 VAL D  31  LEU D  35  0                                        
SHEET    2   D 4 ARG D  45  ILE D  51 -1  O  THR D  47   N  GLY D  34           
SHEET    3   D 4 ILE D  62  GLU D  68 -1  O  VAL D  67   N  TRP D  46           
SHEET    4   D 4 SER D  79  PHE D  82 -1  O  SER D  79   N  GLU D  68           
SHEET    1   E 4 ILE E  23  ASP E  28  0                                        
SHEET    2   E 4 ASN E  31  ALA E  40 -1  O  VAL E  38   N  LYS E  24           
SHEET    3   E 4 THR E  51  PHE E  57 -1  O  PHE E  52   N  ILE E  39           
SHEET    4   E 4 LYS E  68  PHE E  71 -1  O  LYS E  68   N  PHE E  57           
SHEET    1   F 4 VAL F  31  LEU F  35  0                                        
SHEET    2   F 4 ARG F  45  ILE F  51 -1  O  THR F  47   N  GLY F  34           
SHEET    3   F 4 ILE F  62  GLU F  68 -1  O  VAL F  67   N  TRP F  46           
SHEET    4   F 4 SER F  79  PHE F  82 -1  O  ARG F  81   N  LYS F  66           
SHEET    1   G 4 ILE G  23  ASP G  28  0                                        
SHEET    2   G 4 ASN G  31  ALA G  40 -1  O  HIS G  36   N  GLU G  26           
SHEET    3   G 4 THR G  51  PHE G  57 -1  O  LEU G  56   N  PHE G  35           
SHEET    4   G 4 LYS G  68  PHE G  71 -1  O  LYS G  68   N  PHE G  57           
SHEET    1   H 6 LEU H  52  GLU H  53  0                                        
SHEET    2   H 6 TYR H  81  ARG H  83 -1  O  ILE H  82   N  LEU H  52           
SHEET    3   H 6 HIS H 265  TYR H 270 -1  O  ILE H 268   N  ARG H  83           
SHEET    4   H 6 VAL H 257  ARG H 262 -1  N  ARG H 262   O  HIS H 265           
SHEET    5   H 6 ILE H 231  GLU H 234  1  N  GLU H 234   O  TYR H 261           
SHEET    6   H 6 HIS H 247  PHE H 249 -1  O  PHE H 249   N  ILE H 231           
SHEET    1   I 4 VAL I  31  LEU I  35  0                                        
SHEET    2   I 4 ARG I  45  ILE I  51 -1  O  MET I  49   N  SER I  32           
SHEET    3   I 4 ILE I  62  GLU I  68 -1  O  VAL I  67   N  TRP I  46           
SHEET    4   I 4 SER I  79  PHE I  82 -1  O  SER I  79   N  GLU I  68           
SHEET    1   J 4 ILE J  23  PRO J  27  0                                        
SHEET    2   J 4 TYR J  34  ALA J  40 -1  O  VAL J  38   N  LYS J  24           
SHEET    3   J 4 THR J  51  PHE J  57 -1  O  PHE J  52   N  ILE J  39           
SHEET    4   J 4 LYS J  68  PHE J  71 -1  O  LYS J  68   N  PHE J  57           
SHEET    1   K 4 VAL K  31  LEU K  35  0                                        
SHEET    2   K 4 ARG K  45  ILE K  51 -1  O  THR K  47   N  GLY K  34           
SHEET    3   K 4 ILE K  62  GLU K  68 -1  O  LEU K  65   N  GLY K  48           
SHEET    4   K 4 SER K  79  PHE K  82 -1  O  ARG K  81   N  LYS K  66           
SHEET    1   L 4 ILE L  23  PRO L  27  0                                        
SHEET    2   L 4 TYR L  34  ALA L  40 -1  O  HIS L  36   N  GLU L  26           
SHEET    3   L 4 THR L  51  PHE L  57 -1  O  LEU L  54   N  VAL L  37           
SHEET    4   L 4 LYS L  68  PHE L  71 -1  O  LYS L  68   N  PHE L  57           
SHEET    1   M 4 VAL M  31  LEU M  35  0                                        
SHEET    2   M 4 ARG M  45  ILE M  51 -1  O  THR M  47   N  GLY M  34           
SHEET    3   M 4 ILE M  62  GLU M  68 -1  O  VAL M  67   N  TRP M  46           
SHEET    4   M 4 SER M  79  PHE M  82 -1  O  ARG M  81   N  LYS M  66           
SHEET    1   N 4 ILE N  23  PRO N  27  0                                        
SHEET    2   N 4 TYR N  34  ALA N  40 -1  O  VAL N  38   N  LYS N  24           
SHEET    3   N 4 THR N  51  PHE N  57 -1  O  LEU N  56   N  PHE N  35           
SHEET    4   N 4 LYS N  68  PHE N  71 -1  O  ARG N  70   N  GLU N  55           
SHEET    1   O 6 LEU O  52  GLU O  53  0                                        
SHEET    2   O 6 TYR O  81  ARG O  83 -1  O  ILE O  82   N  LEU O  52           
SHEET    3   O 6 HIS O 265  TYR O 270 -1  O  TYR O 270   N  TYR O  81           
SHEET    4   O 6 VAL O 257  ARG O 262 -1  N  LEU O 260   O  ASP O 267           
SHEET    5   O 6 ILE O 231  TYR O 235  1  N  GLU O 234   O  LEU O 259           
SHEET    6   O 6 HIS O 247  PHE O 249 -1  O  PHE O 249   N  ILE O 231           
SHEET    1   P 4 VAL P  31  LEU P  35  0                                        
SHEET    2   P 4 ARG P  45  ILE P  51 -1  O  THR P  47   N  GLY P  34           
SHEET    3   P 4 ILE P  62  GLU P  68 -1  O  LEU P  65   N  GLY P  48           
SHEET    4   P 4 SER P  79  PHE P  82 -1  O  ARG P  81   N  LYS P  66           
SHEET    1   Q 4 ILE Q  23  PRO Q  27  0                                        
SHEET    2   Q 4 TYR Q  34  ALA Q  40 -1  O  HIS Q  36   N  GLU Q  26           
SHEET    3   Q 4 THR Q  51  PHE Q  57 -1  O  LEU Q  54   N  VAL Q  37           
SHEET    4   Q 4 LYS Q  68  PHE Q  71 -1  O  LYS Q  68   N  PHE Q  57           
SHEET    1   R 4 VAL R  31  LEU R  35  0                                        
SHEET    2   R 4 ARG R  45  ILE R  51 -1  O  THR R  47   N  GLY R  34           
SHEET    3   R 4 ILE R  62  GLU R  68 -1  O  VAL R  67   N  TRP R  46           
SHEET    4   R 4 SER R  79  PHE R  82 -1  O  ARG R  81   N  LYS R  66           
SHEET    1   S 4 ILE S  23  ASP S  28  0                                        
SHEET    2   S 4 ASN S  31  ALA S  40 -1  O  HIS S  36   N  GLU S  26           
SHEET    3   S 4 THR S  51  PHE S  57 -1  O  LEU S  54   N  VAL S  37           
SHEET    4   S 4 LYS S  68  PHE S  71 -1  O  LYS S  68   N  PHE S  57           
SHEET    1   T 4 VAL T  31  LEU T  35  0                                        
SHEET    2   T 4 ARG T  45  ILE T  51 -1  O  THR T  47   N  GLY T  34           
SHEET    3   T 4 ILE T  62  GLU T  68 -1  O  TYR T  63   N  ILE T  50           
SHEET    4   T 4 SER T  79  PHE T  82 -1  O  SER T  79   N  GLU T  68           
SHEET    1   U 4 ILE U  23  ASP U  28  0                                        
SHEET    2   U 4 ASN U  31  ALA U  40 -1  O  HIS U  36   N  GLU U  26           
SHEET    3   U 4 THR U  51  PHE U  57 -1  O  LEU U  54   N  VAL U  37           
SHEET    4   U 4 LYS U  68  PHE U  71 -1  O  LYS U  68   N  PHE U  57           
SHEET    1   V 6 LEU V  52  GLU V  53  0                                        
SHEET    2   V 6 TYR V  81  ARG V  83 -1  O  ILE V  82   N  LEU V  52           
SHEET    3   V 6 HIS V 265  TYR V 270 -1  O  TYR V 270   N  TYR V  81           
SHEET    4   V 6 VAL V 257  ARG V 262 -1  N  LEU V 260   O  ASP V 267           
SHEET    5   V 6 ILE V 231  TYR V 235  1  N  GLU V 234   O  TYR V 261           
SHEET    6   V 6 PRO V 246  PHE V 249 -1  O  PHE V 249   N  ILE V 231           
SHEET    1   W 4 VAL W  31  LEU W  35  0                                        
SHEET    2   W 4 ARG W  45  ILE W  51 -1  O  THR W  47   N  GLY W  34           
SHEET    3   W 4 ILE W  62  GLU W  68 -1  O  TYR W  63   N  ILE W  50           
SHEET    4   W 4 SER W  79  PHE W  82 -1  O  SER W  79   N  GLU W  68           
SHEET    1   X 4 ILE X  23  ASP X  28  0                                        
SHEET    2   X 4 ASN X  31  ALA X  40 -1  O  VAL X  38   N  LYS X  24           
SHEET    3   X 4 THR X  51  PHE X  57 -1  O  LEU X  54   N  VAL X  37           
SHEET    4   X 4 LYS X  68  PHE X  71 -1  O  LYS X  68   N  PHE X  57           
SHEET    1   Y 4 VAL Y  31  LEU Y  35  0                                        
SHEET    2   Y 4 ARG Y  45  ILE Y  51 -1  O  THR Y  47   N  GLY Y  34           
SHEET    3   Y 4 ILE Y  62  GLU Y  68 -1  O  VAL Y  67   N  TRP Y  46           
SHEET    4   Y 4 SER Y  79  PHE Y  82 -1  O  ARG Y  81   N  LYS Y  66           
SHEET    1   Z 4 ILE Z  23  ASP Z  28  0                                        
SHEET    2   Z 4 ASN Z  31  ALA Z  40 -1  O  HIS Z  36   N  GLU Z  26           
SHEET    3   Z 4 THR Z  51  PHE Z  57 -1  O  PHE Z  52   N  ILE Z  39           
SHEET    4   Z 4 LYS Z  68  PHE Z  71 -1  O  LYS Z  68   N  PHE Z  57           
SHEET    1  AA 4 VAL a  31  LEU a  35  0                                        
SHEET    2  AA 4 ARG a  45  ILE a  51 -1  O  THR a  47   N  GLY a  34           
SHEET    3  AA 4 ILE a  62  GLU a  68 -1  O  VAL a  67   N  TRP a  46           
SHEET    4  AA 4 SER a  79  PHE a  82 -1  O  SER a  79   N  GLU a  68           
SHEET    1  AB 4 ILE b  23  ASP b  28  0                                        
SHEET    2  AB 4 ASN b  31  ALA b  40 -1  O  HIS b  36   N  GLU b  26           
SHEET    3  AB 4 THR b  51  PHE b  57 -1  O  LEU b  56   N  PHE b  35           
SHEET    4  AB 4 LYS b  68  PHE b  71 -1  O  LYS b  68   N  PHE b  57           
SHEET    1  AC 6 LEU c  52  GLU c  53  0                                        
SHEET    2  AC 6 TYR c  81  ARG c  83 -1  O  ILE c  82   N  LEU c  52           
SHEET    3  AC 6 HIS c 265  LEU c 269 -1  O  ILE c 268   N  ARG c  83           
SHEET    4  AC 6 VAL c 257  ARG c 262 -1  N  ARG c 262   O  HIS c 265           
SHEET    5  AC 6 ILE c 231  TYR c 235  1  N  GLU c 234   O  TYR c 261           
SHEET    6  AC 6 ASN c 245  PHE c 249 -1  O  PHE c 249   N  ILE c 231           
SHEET    1  AD 4 VAL d  31  SER d  32  0                                        
SHEET    2  AD 4 ARG d  45  ILE d  51 -1  O  MET d  49   N  SER d  32           
SHEET    3  AD 4 ILE d  62  GLU d  68 -1  O  TYR d  63   N  ILE d  50           
SHEET    4  AD 4 SER d  79  PHE d  82 -1  O  SER d  79   N  GLU d  68           
SHEET    1  AE 4 ILE e  23  PRO e  27  0                                        
SHEET    2  AE 4 TYR e  34  ALA e  40 -1  O  VAL e  38   N  LYS e  24           
SHEET    3  AE 4 THR e  51  PHE e  57 -1  O  LEU e  54   N  VAL e  37           
SHEET    4  AE 4 LYS e  68  PHE e  71 -1  O  LYS e  68   N  PHE e  57           
SHEET    1  AF 4 VAL f  31  LEU f  35  0                                        
SHEET    2  AF 4 ARG f  45  ILE f  51 -1  O  THR f  47   N  GLY f  34           
SHEET    3  AF 4 ILE f  62  GLU f  68 -1  O  VAL f  67   N  TRP f  46           
SHEET    4  AF 4 SER f  79  PHE f  82 -1  O  ARG f  81   N  LYS f  66           
SHEET    1  AG 4 ILE g  23  PRO g  27  0                                        
SHEET    2  AG 4 TYR g  34  ALA g  40 -1  O  VAL g  38   N  LYS g  24           
SHEET    3  AG 4 THR g  51  PHE g  57 -1  O  LEU g  54   N  VAL g  37           
SHEET    4  AG 4 LYS g  68  PHE g  71 -1  O  LYS g  68   N  PHE g  57           
SHEET    1  AH 4 VAL h  31  LEU h  35  0                                        
SHEET    2  AH 4 ARG h  45  ILE h  51 -1  O  THR h  47   N  GLY h  34           
SHEET    3  AH 4 ILE h  62  GLU h  68 -1  O  VAL h  67   N  TRP h  46           
SHEET    4  AH 4 SER h  79  PHE h  82 -1  O  ARG h  81   N  LYS h  66           
SHEET    1  AI 4 ILE i  23  ASP i  28  0                                        
SHEET    2  AI 4 ASN i  31  ALA i  40 -1  O  HIS i  36   N  GLU i  26           
SHEET    3  AI 4 THR i  51  PHE i  57 -1  O  LEU i  54   N  VAL i  37           
SHEET    4  AI 4 LYS i  68  PHE i  71 -1  O  LYS i  68   N  PHE i  57           
SHEET    1  AJ 6 LEU j  52  GLU j  53  0                                        
SHEET    2  AJ 6 TYR j  81  ARG j  83 -1  O  ILE j  82   N  LEU j  52           
SHEET    3  AJ 6 HIS j 265  TYR j 270 -1  O  ILE j 268   N  ARG j  83           
SHEET    4  AJ 6 VAL j 257  ARG j 262 -1  N  ARG j 262   O  HIS j 265           
SHEET    5  AJ 6 ILE j 231  GLU j 234  1  N  GLU j 234   O  TYR j 261           
SHEET    6  AJ 6 HIS j 247  PHE j 249 -1  O  PHE j 249   N  ILE j 231           
SHEET    1  AK 4 VAL k  31  LEU k  35  0                                        
SHEET    2  AK 4 ARG k  45  ILE k  51 -1  O  MET k  49   N  SER k  32           
SHEET    3  AK 4 ILE k  62  GLU k  68 -1  O  TYR k  63   N  ILE k  50           
SHEET    4  AK 4 SER k  79  PHE k  82 -1  O  ARG k  81   N  LYS k  66           
SHEET    1  AL 4 ILE l  23  PRO l  27  0                                        
SHEET    2  AL 4 TYR l  34  ALA l  40 -1  O  VAL l  38   N  LYS l  24           
SHEET    3  AL 4 THR l  51  PHE l  57 -1  O  LEU l  54   N  VAL l  37           
SHEET    4  AL 4 LYS l  68  PHE l  71 -1  O  LYS l  68   N  PHE l  57           
SHEET    1  AM 4 VAL m  31  LEU m  35  0                                        
SHEET    2  AM 4 ARG m  45  ILE m  51 -1  O  THR m  47   N  GLY m  34           
SHEET    3  AM 4 ILE m  62  GLU m  68 -1  O  LEU m  65   N  GLY m  48           
SHEET    4  AM 4 SER m  79  PHE m  82 -1  O  ARG m  81   N  LYS m  66           
SHEET    1  AN 4 ILE n  23  PRO n  27  0                                        
SHEET    2  AN 4 TYR n  34  ALA n  40 -1  O  VAL n  38   N  LYS n  24           
SHEET    3  AN 4 THR n  51  PHE n  57 -1  O  LEU n  54   N  VAL n  37           
SHEET    4  AN 4 LYS n  68  PHE n  71 -1  O  LYS n  68   N  PHE n  57           
SHEET    1  AO 4 VAL o  31  LEU o  35  0                                        
SHEET    2  AO 4 ARG o  45  ILE o  51 -1  O  THR o  47   N  GLY o  34           
SHEET    3  AO 4 ILE o  62  GLU o  68 -1  O  VAL o  67   N  TRP o  46           
SHEET    4  AO 4 SER o  79  PHE o  82 -1  O  ARG o  81   N  LYS o  66           
SHEET    1  AP 4 ILE p  23  ASP p  28  0                                        
SHEET    2  AP 4 ASN p  31  ALA p  40 -1  O  TYR p  34   N  ASP p  28           
SHEET    3  AP 4 THR p  51  PHE p  57 -1  O  LEU p  54   N  VAL p  37           
SHEET    4  AP 4 LYS p  68  PHE p  71 -1  O  LYS p  68   N  PHE p  57           
CISPEP   1 PHE A  249    PRO A  250          0         0.10                     
CISPEP   2 TYR B   73    PRO B   74          0         0.93                     
CISPEP   3 TYR C   62    PRO C   63          0         5.87                     
CISPEP   4 ASN C  116    PRO C  117          0        -1.63                     
CISPEP   5 TYR D   73    PRO D   74          0        -0.23                     
CISPEP   6 TYR E   62    PRO E   63          0         9.11                     
CISPEP   7 TYR F   73    PRO F   74          0         2.89                     
CISPEP   8 TYR G   62    PRO G   63          0         8.92                     
CISPEP   9 PHE H  249    PRO H  250          0        -4.75                     
CISPEP  10 TYR I   73    PRO I   74          0        -1.63                     
CISPEP  11 TYR J   62    PRO J   63          0         7.40                     
CISPEP  12 TYR K   73    PRO K   74          0        -2.37                     
CISPEP  13 TYR L   62    PRO L   63          0         4.58                     
CISPEP  14 TYR M   73    PRO M   74          0         6.90                     
CISPEP  15 TYR N   62    PRO N   63          0         6.51                     
CISPEP  16 PHE O  249    PRO O  250          0        -2.35                     
CISPEP  17 TYR P   73    PRO P   74          0         5.93                     
CISPEP  18 TYR Q   62    PRO Q   63          0         5.77                     
CISPEP  19 TYR R   73    PRO R   74          0         4.50                     
CISPEP  20 TYR S   62    PRO S   63          0         6.81                     
CISPEP  21 TYR T   73    PRO T   74          0        -2.56                     
CISPEP  22 TYR U   62    PRO U   63          0         6.69                     
CISPEP  23 PHE V  249    PRO V  250          0        -4.75                     
CISPEP  24 TYR W   73    PRO W   74          0         4.18                     
CISPEP  25 TYR X   62    PRO X   63          0         6.71                     
CISPEP  26 TYR Y   73    PRO Y   74          0         2.83                     
CISPEP  27 TYR Z   62    PRO Z   63          0        10.73                     
CISPEP  28 TYR a   73    PRO a   74          0        -1.99                     
CISPEP  29 TYR b   62    PRO b   63          0         7.03                     
CISPEP  30 PHE c  249    PRO c  250          0        -4.47                     
CISPEP  31 TYR d   73    PRO d   74          0         5.39                     
CISPEP  32 TYR e   62    PRO e   63          0         4.71                     
CISPEP  33 TYR f   73    PRO f   74          0         1.24                     
CISPEP  34 TYR g   62    PRO g   63          0         4.91                     
CISPEP  35 TYR h   73    PRO h   74          0         5.63                     
CISPEP  36 TYR i   62    PRO i   63          0         8.21                     
CISPEP  37 PHE j  249    PRO j  250          0        -6.14                     
CISPEP  38 TYR k   73    PRO k   74          0         3.91                     
CISPEP  39 TYR l   62    PRO l   63          0         3.90                     
CISPEP  40 TYR m   73    PRO m   74          0        -1.16                     
CISPEP  41 TYR n   62    PRO n   63          0         7.33                     
CISPEP  42 TYR o   73    PRO o   74          0         8.01                     
CISPEP  43 TYR p   62    PRO p   63          0         8.20                     
CRYST1  102.064  137.285  257.109  90.00  90.03  90.00 P 1 21 1     36          
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      0.009798  0.000000  0.000005        0.00000                         
SCALE2      0.000000  0.007284  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003889        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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