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Database: PDB
Entry: 3RL0
LinkDB: 3RL0
Original site: 3RL0 
HEADER    MEMBRANE PROTEIN/EXOCYTOSIS             19-APR-11   3RL0              
TITLE     TRUNCATED SNARE COMPLEX WITH COMPLEXIN (P1)                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VESICLE-ASSOCIATED MEMBRANE PROTEIN 2;                     
COMPND   3 CHAIN: A, E, I, M, Q, U, Y, c;                                       
COMPND   4 FRAGMENT: UNP RESIDUES 28-60;                                        
COMPND   5 SYNONYM: VAMP-2, SYNAPTOBREVIN-2;                                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SYNTAXIN-1A;                                               
COMPND   9 CHAIN: B, F, J, N, R, V, Z, d;                                       
COMPND  10 FRAGMENT: UNP RESIDUES 191-253;                                      
COMPND  11 SYNONYM: NEURON-SPECIFIC ANTIGEN HPC-1, SYNAPTOTAGMIN-ASSOCIATED 35  
COMPND  12 KDA PROTEIN, P35A;                                                   
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: SYNAPTOSOMAL-ASSOCIATED PROTEIN 25;                        
COMPND  16 CHAIN: C, G, K, O, S, W, a, e;                                       
COMPND  17 FRAGMENT: UNP RESIDUES 7-82;                                         
COMPND  18 SYNONYM: SNAP-25, SUPER PROTEIN, SUP, SYNAPTOSOMAL-ASSOCIATED 25 KDA 
COMPND  19 PROTEIN;                                                             
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 4;                                                           
COMPND  22 MOLECULE: SYNAPTOSOMAL-ASSOCIATED PROTEIN 25;                        
COMPND  23 CHAIN: D, H, L, P, T, X, b, f;                                       
COMPND  24 FRAGMENT: UNP RESIDUES 141-203;                                      
COMPND  25 SYNONYM: SNAP-25, SUPER PROTEIN, SUP, SYNAPTOSOMAL-ASSOCIATED 25 KDA 
COMPND  26 PROTEIN;                                                             
COMPND  27 ENGINEERED: YES;                                                     
COMPND  28 MOL_ID: 5;                                                           
COMPND  29 MOLECULE: COMPLEXIN-1;                                               
COMPND  30 CHAIN: g, h, i, j, k, l, m, n;                                       
COMPND  31 SYNONYM: COMPLEXIN I, CPX I, SYNAPHIN-2;                             
COMPND  32 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: VAMP2, SYB2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  10 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE  11 ORGANISM_TAXID: 10116;                                               
SOURCE  12 GENE: STX1A, SAP;                                                    
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: SNAP25, SNAP;                                                  
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: SNAP25, SNAP;                                                  
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  29 MOL_ID: 5;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  31 ORGANISM_COMMON: HUMAN;                                              
SOURCE  32 ORGANISM_TAXID: 9606;                                                
SOURCE  33 GENE: CPLX1;                                                         
SOURCE  34 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  35 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SNARE PROTEINS, MEMBRANE FUSION, MEMBRANE PROTEIN-EXOCYTOSIS COMPLEX  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.KUEMMEL,K.M.REINISCH                                                
REVDAT   2   24-AUG-11 3RL0    1       JRNL                                     
REVDAT   1   27-JUL-11 3RL0    0                                                
JRNL        AUTH   D.KUMMEL,S.S.KRISHNAKUMAR,D.T.RADOFF,F.LI,C.G.GIRAUDO,       
JRNL        AUTH 2 F.PINCET,J.E.ROTHMAN,K.M.REINISCH                            
JRNL        TITL   COMPLEXIN CROSS-LINKS PREFUSION SNARES INTO A ZIGZAG ARRAY.  
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  18   927 2011              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   21785414                                                     
JRNL        DOI    10.1038/NSMB.2101                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 3.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 32506                          
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) : 0.308                           
REMARK   3   R VALUE            (WORKING SET) : 0.306                           
REMARK   3   FREE R VALUE                     : 0.345                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1872                            
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) : 3.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2271                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17672                                   
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) : 116.78                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.35000                                             
REMARK   3    B22 (A**2) : -15.82000                                            
REMARK   3    B33 (A**2) : 18.54000                                             
REMARK   3    B12 (A**2) : -0.10000                                             
REMARK   3    B13 (A**2) : -0.18000                                             
REMARK   3    B23 (A**2) : -4.36000                                             
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): 0.987         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 1.032         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 174.715       
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.909                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.866                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 19545 ; 0.035 ; 0.030       
REMARK   3   BOND LENGTHS OTHERS               (A): 12115 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 23222 ; 1.011 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 29415 ; 1.102 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2147 ; 4.117 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1012 ;27.809 ;25.632       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3548 ;16.014 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   181 ;12.456 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2579 ; 0.044 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 19530 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  3111 ; 0.014 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 12987 ; 2.646 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4410 ; 0.372 ; 2.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17219 ; 3.718 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6558 ; 3.835 ; 4.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6003 ; 6.530 ; 6.000       
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 : 6                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A E I M Q U Y c                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     28       A      60      1                      
REMARK   3           1     E     28       E      60      1                      
REMARK   3           1     I     28       I      60      1                      
REMARK   3           1     M     28       M      60      1                      
REMARK   3           1     Q     28       Q      60      1                      
REMARK   3           1     U     28       U      60      1                      
REMARK   3           1     Y     28       Y      60      1                      
REMARK   3           1     c     28       c      60      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    444 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    E    (A):    444 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    I    (A):    444 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    M    (A):    444 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    Q    (A):    444 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    U    (A):    444 ; 0.120 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    Y    (A):    444 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    c    (A):    444 ; 0.020 ; 0.050           
REMARK   3   TIGHT THERMAL      1    A (A**2):    444 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      1    E (A**2):    444 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      1    I (A**2):    444 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      1    M (A**2):    444 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      1    Q (A**2):    444 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      1    U (A**2):    444 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      1    Y (A**2):    444 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      1    c (A**2):    444 ; 0.020 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B F J N R V Z d                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    190       B     248      1                      
REMARK   3           1     F    190       F     248      1                      
REMARK   3           1     J    190       J     248      1                      
REMARK   3           1     N    190       N     248      1                      
REMARK   3           1     R    190       R     248      1                      
REMARK   3           1     V    190       V     248      1                      
REMARK   3           1     Z    190       Z     248      1                      
REMARK   3           1     d    190       d     248      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):    718 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    F    (A):    718 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    J    (A):    718 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    N    (A):    718 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    R    (A):    718 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    V    (A):    718 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    Z    (A):    718 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    d    (A):    718 ; 0.030 ; 0.050           
REMARK   3   TIGHT THERMAL      2    B (A**2):    718 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      2    F (A**2):    718 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      2    J (A**2):    718 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      2    N (A**2):    718 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      2    R (A**2):    718 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      2    V (A**2):    718 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      2    Z (A**2):    718 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      2    d (A**2):    718 ; 0.020 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : C G K O S W a e                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C     15       C      78      1                      
REMARK   3           1     G     15       G      78      1                      
REMARK   3           1     K     15       K      78      1                      
REMARK   3           1     O     15       O      78      1                      
REMARK   3           1     S     15       S      78      1                      
REMARK   3           1     W     15       W      78      1                      
REMARK   3           1     a     15       a      78      1                      
REMARK   3           1     e     15       e      78      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    C    (A):    811 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    G    (A):    811 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    K    (A):    811 ; 0.090 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    O    (A):    811 ; 0.070 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    S    (A):    811 ; 0.050 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    W    (A):    811 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    a    (A):    811 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    e    (A):    811 ; 0.030 ; 0.050           
REMARK   3   TIGHT THERMAL      3    C (A**2):    811 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      3    G (A**2):    811 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      3    K (A**2):    811 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      3    O (A**2):    811 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      3    S (A**2):    811 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      3    W (A**2):    811 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      3    a (A**2):    811 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      3    e (A**2):    811 ; 0.020 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : D H L P T X b f                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D    141       D     199      1                      
REMARK   3           1     H    141       H     199      1                      
REMARK   3           1     L    141       L     199      1                      
REMARK   3           1     P    141       P     199      1                      
REMARK   3           1     T    141       T     199      1                      
REMARK   3           1     X    141       X     199      1                      
REMARK   3           1     b    141       b     199      1                      
REMARK   3           1     f    141       f     199      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    D    (A):    729 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    H    (A):    729 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    L    (A):    729 ; 0.050 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    P    (A):    729 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    T    (A):    729 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    X    (A):    729 ; 0.050 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    b    (A):    729 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    f    (A):    729 ; 0.020 ; 0.050           
REMARK   3   TIGHT THERMAL      4    D (A**2):    729 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      4    H (A**2):    729 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      4    L (A**2):    729 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      4    P (A**2):    729 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      4    T (A**2):    729 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      4    X (A**2):    729 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      4    b (A**2):    729 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      4    f (A**2):    729 ; 0.020 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : g h k I                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     g     27       g      70      4                      
REMARK   3           1     h     27       h      70      4                      
REMARK   3           1     k     27       k      70      4                      
REMARK   3           1     I     27       I      70      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  5    g    (A):     22 ; 0.240 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  5    h    (A):     22 ; 0.450 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  5    k    (A):     22 ; 0.190 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  5    I    (A):     22 ; 0.290 ; 0.500           
REMARK   3   MEDIUM THERMAL     5    g (A**2):     22 ; 0.360 ; 2.000           
REMARK   3   MEDIUM THERMAL     5    h (A**2):     22 ; 0.480 ; 2.000           
REMARK   3   MEDIUM THERMAL     5    k (A**2):     22 ; 0.590 ; 2.000           
REMARK   3   MEDIUM THERMAL     5    I (A**2):     22 ; 0.920 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : i j m n                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     i     28       i      70      4                      
REMARK   3           1     j     28       j      70      4                      
REMARK   3           1     m     28       m      70      4                      
REMARK   3           1     n     28       n      70      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  6    i    (A):    581 ; 0.730 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  6    j    (A):    581 ; 0.670 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  6    m    (A):    581 ; 0.710 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  6    n    (A):    581 ; 0.740 ; 0.500           
REMARK   3   MEDIUM THERMAL     6    i (A**2):    581 ; 0.500 ; 2.000           
REMARK   3   MEDIUM THERMAL     6    j (A**2):    581 ; 0.260 ; 2.000           
REMARK   3   MEDIUM THERMAL     6    m (A**2):    581 ; 0.270 ; 2.000           
REMARK   3   MEDIUM THERMAL     6    n (A**2):    581 ; 0.200 ; 2.000           
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 1                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H,-H-K,-L                                       
REMARK   3      TWIN FRACTION : 0.470                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    26        A    60                          
REMARK   3    RESIDUE RANGE :   B   191        B   249                          
REMARK   3    RESIDUE RANGE :   C     8        C    79                          
REMARK   3    RESIDUE RANGE :   D   139        D   200                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6708  25.6650   8.2294              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1584 T22:   0.1438                                     
REMARK   3      T33:   0.2838 T12:  -0.0979                                     
REMARK   3      T13:   0.0434 T23:  -0.1324                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8617 L22:   7.8448                                     
REMARK   3      L33:   1.4232 L12:  -3.9102                                     
REMARK   3      L13:  -0.5567 L23:   0.8157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0888 S12:  -0.1040 S13:   0.1569                       
REMARK   3      S21:  -0.4278 S22:  -0.0207 S23:   0.3382                       
REMARK   3      S31:   0.0673 S32:   0.0488 S33:  -0.0680                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    26        E    60                          
REMARK   3    RESIDUE RANGE :   F   191        F   251                          
REMARK   3    RESIDUE RANGE :   G     8        G    81                          
REMARK   3    RESIDUE RANGE :   H   139        H   199                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.1420 -13.8847  18.5063              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1291 T22:   0.0879                                     
REMARK   3      T33:   0.2151 T12:   0.0312                                     
REMARK   3      T13:   0.0368 T23:  -0.0863                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3450 L22:   8.6394                                     
REMARK   3      L33:   1.1182 L12:   3.4854                                     
REMARK   3      L13:   0.6713 L23:   1.5531                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0134 S12:  -0.0114 S13:   0.0021                       
REMARK   3      S21:   0.6682 S22:   0.0116 S23:   0.3711                       
REMARK   3      S31:   0.1465 S32:   0.1132 S33:  -0.0250                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I    27        I    60                          
REMARK   3    RESIDUE RANGE :   J   190        J   248                          
REMARK   3    RESIDUE RANGE :   K     9        K    79                          
REMARK   3    RESIDUE RANGE :   L   139        L   202                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4619  17.8046   2.3887              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1174 T22:   0.1374                                     
REMARK   3      T33:   0.0194 T12:  -0.1011                                     
REMARK   3      T13:  -0.0239 T23:   0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3338 L22:   7.5439                                     
REMARK   3      L33:   3.7247 L12:  -3.4200                                     
REMARK   3      L13:  -1.9372 L23:   3.3424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0443 S12:  -0.0973 S13:   0.1355                       
REMARK   3      S21:  -0.1796 S22:  -0.0355 S23:   0.0270                       
REMARK   3      S31:  -0.0153 S32:   0.1491 S33:   0.0798                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M    25        M    60                          
REMARK   3    RESIDUE RANGE :   N   191        N   247                          
REMARK   3    RESIDUE RANGE :   O     8        O    79                          
REMARK   3    RESIDUE RANGE :   P   139        P   202                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.4711  -6.4101  26.2915              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0871 T22:   0.0352                                     
REMARK   3      T33:   0.0394 T12:   0.0119                                     
REMARK   3      T13:   0.0475 T23:   0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7011 L22:   4.9728                                     
REMARK   3      L33:   4.9294 L12:   3.4991                                     
REMARK   3      L13:   3.3147 L23:   3.5491                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0217 S12:  -0.2120 S13:  -0.0179                       
REMARK   3      S21:   0.1328 S22:  -0.0887 S23:  -0.0657                       
REMARK   3      S31:   0.0427 S32:  -0.0816 S33:   0.0670                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Q    26        Q    60                          
REMARK   3    RESIDUE RANGE :   R   191        R   251                          
REMARK   3    RESIDUE RANGE :   S    10        S    79                          
REMARK   3    RESIDUE RANGE :   T   139        T   200                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5154 -20.9014 -51.9853              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1027 T22:   0.0636                                     
REMARK   3      T33:   0.2396 T12:  -0.0257                                     
REMARK   3      T13:  -0.0267 T23:  -0.0914                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1998 L22:   8.3427                                     
REMARK   3      L33:   1.1591 L12:  -3.3340                                     
REMARK   3      L13:  -0.6991 L23:   1.4752                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0166 S12:  -0.0679 S13:   0.0350                       
REMARK   3      S21:  -0.4967 S22:   0.0494 S23:   0.3934                       
REMARK   3      S31:  -0.0610 S32:   0.0648 S33:  -0.0328                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   U    26        U    60                          
REMARK   3    RESIDUE RANGE :   V   191        V   248                          
REMARK   3    RESIDUE RANGE :   W     8        W    77                          
REMARK   3    RESIDUE RANGE :   X   139        X   201                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.7666 -60.0400 -41.6340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1419 T22:   0.1262                                     
REMARK   3      T33:   0.1940 T12:   0.0928                                     
REMARK   3      T13:  -0.0289 T23:  -0.0659                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1526 L22:   9.9339                                     
REMARK   3      L33:   0.7946 L12:   4.3560                                     
REMARK   3      L13:   0.1741 L23:   0.4401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0604 S12:   0.0389 S13:  -0.1470                       
REMARK   3      S21:   0.4519 S22:  -0.0352 S23:   0.3857                       
REMARK   3      S31:  -0.0012 S32:   0.0178 S33:  -0.0252                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Y    26        Y    60                          
REMARK   3    RESIDUE RANGE :   Z   190        Z   247                          
REMARK   3    RESIDUE RANGE :   a    10        a    79                          
REMARK   3    RESIDUE RANGE :   b   139        b   199                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4510 -28.5202 -59.4202              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0726 T22:   0.0373                                     
REMARK   3      T33:   0.0113 T12:  -0.0256                                     
REMARK   3      T13:  -0.0145 T23:   0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2488 L22:   5.2286                                     
REMARK   3      L33:   5.0614 L12:  -3.9576                                     
REMARK   3      L13:  -3.4723 L23:   3.3417                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1100 S12:   0.1747 S13:   0.0778                       
REMARK   3      S21:  -0.1571 S22:  -0.0885 S23:  -0.1364                       
REMARK   3      S31:  -0.0372 S32:  -0.1212 S33:  -0.0215                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   c    27        c    60                          
REMARK   3    RESIDUE RANGE :   d   190        d   248                          
REMARK   3    RESIDUE RANGE :   e     8        e    79                          
REMARK   3    RESIDUE RANGE :   f   139        f   200                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2257 -53.7506 -36.6041              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1004 T22:   0.1770                                     
REMARK   3      T33:   0.0622 T12:   0.1169                                     
REMARK   3      T13:   0.0767 T23:   0.1004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4237 L22:   7.8040                                     
REMARK   3      L33:   4.1846 L12:   3.6038                                     
REMARK   3      L13:   1.8902 L23:   2.9165                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0009 S12:   0.0941 S13:   0.0237                       
REMARK   3      S21:   0.2252 S22:  -0.0650 S23:   0.0723                       
REMARK   3      S31:   0.0841 S32:  -0.0366 S33:   0.0659                       
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 :   g    24        g    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.6530  55.3061   4.1753              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9842 T22:   0.7925                                     
REMARK   3      T33:   1.1044 T12:  -0.2610                                     
REMARK   3      T13:   0.2352 T23:   0.0754                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4683 L22:   2.4477                                     
REMARK   3      L33:   0.8420 L12:   2.0885                                     
REMARK   3      L13:   1.1155 L23:   0.7105                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8377 S12:   1.2428 S13:   0.5421                       
REMARK   3      S21:  -0.1539 S22:   1.0455 S23:   1.1989                       
REMARK   3      S31:  -0.3468 S32:   0.7763 S33:  -0.2079                       
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 :   h    25        h    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1893 -43.1112  20.1950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5819 T22:   0.7981                                     
REMARK   3      T33:   2.0196 T12:   0.0930                                     
REMARK   3      T13:   0.3543 T23:   0.5561                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3504 L22:   0.0806                                     
REMARK   3      L33:   0.4236 L12:  -0.1654                                     
REMARK   3      L13:   0.3283 L23:  -0.1533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1132 S12:  -0.0067 S13:  -0.6365                       
REMARK   3      S21:   0.1397 S22:   0.2350 S23:   0.3340                       
REMARK   3      S31:  -0.3168 S32:   0.2947 S33:  -0.1218                       
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 :   j    26        j    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7044  14.4418  45.5089              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1244 T22:   0.8227                                     
REMARK   3      T33:   0.3577 T12:  -0.0257                                     
REMARK   3      T13:   0.2047 T23:  -0.0873                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2946 L22:  49.7643                                     
REMARK   3      L33:   8.7008 L12: -17.2041                                     
REMARK   3      L13:  -7.1277 L23:  20.6915                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0154 S12:  -0.3863 S13:  -0.2640                       
REMARK   3      S21:   0.9931 S22:   0.9605 S23:   0.7205                       
REMARK   3      S31:   0.2832 S32:   0.5861 S33:   0.0550                       
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 :   k    25        k    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7408   7.6995 -53.4913              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2775 T22:   1.1089                                     
REMARK   3      T33:   1.5388 T12:   0.2251                                     
REMARK   3      T13:  -0.0828 T23:   0.2007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9668 L22:   0.0037                                     
REMARK   3      L33:   0.1117 L12:   0.0736                                     
REMARK   3      L13:  -0.3807 L23:  -0.0164                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3301 S12:   1.5355 S13:   1.6816                       
REMARK   3      S21:  -0.0302 S22:   0.2725 S23:   0.0690                       
REMARK   3      S31:   0.3313 S32:   0.0227 S33:   0.0576                       
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 :   l    24        l    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.0912 -90.5350 -37.4695              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8051 T22:   0.2632                                     
REMARK   3      T33:   0.7795 T12:   0.1676                                     
REMARK   3      T13:  -0.0591 T23:  -0.0700                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7526 L22:  20.8305                                     
REMARK   3      L33:   2.0734 L12:  -5.2732                                     
REMARK   3      L13:  -1.5638 L23:   6.3545                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4536 S12:  -0.3320 S13:  -0.1475                       
REMARK   3      S21:  -0.6172 S22:   0.6224 S23:   0.5021                       
REMARK   3      S31:  -0.2418 S32:   0.2905 S33:  -0.1687                       
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 :   m    26        m    70                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.4177 -50.4061 -78.9744              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9872 T22:   0.7123                                     
REMARK   3      T33:   0.2536 T12:  -0.0909                                     
REMARK   3      T13:  -0.1194 T23:  -0.0490                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4943 L22:  27.9779                                     
REMARK   3      L33:   3.4562 L12:   7.7009                                     
REMARK   3      L13:   2.6982 L23:   9.7593                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6123 S12:   0.3457 S13:  -0.0868                       
REMARK   3      S21:  -0.0271 S22:   0.8312 S23:  -0.2049                       
REMARK   3      S31:   0.0468 S32:   0.3102 S33:  -0.2189                       
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 :   n    26        n    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.9386 -28.5611 -20.3604              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7860 T22:   0.8131                                     
REMARK   3      T33:   0.3403 T12:   0.0666                                     
REMARK   3      T13:   0.0932 T23:  -0.0676                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6422 L22:  44.2569                                     
REMARK   3      L33:   2.0149 L12: -10.3225                                     
REMARK   3      L13:  -2.2223 L23:   9.4247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5932 S12:  -0.2563 S13:  -0.0549                       
REMARK   3      S21:   0.7161 S22:   0.6195 S23:  -0.0843                       
REMARK   3      S31:   0.2087 S32:   0.0858 S33:  -0.0263                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3RL0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065062.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9797                             
REMARK 200  MONOCHROMATOR                  : CRYOGENICALLY COOLED DOUBLE        
REMARK 200                                   CRYSTAL MONOCHROMETER              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 83.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.94                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13-15% POLYETHYLENEGLYCOL (PEG)          
REMARK 280  5000MME, 0.2 M AMMONIUM SULFATE, 0.01 M EDTA, AND 0.1 M TRIS PH     
REMARK 280  7.5, VAPOR DIFFUSION, TEMPERATURE 294K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8                                  
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H, h                         
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L, 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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P, 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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, R, S, T, k                         
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, V, W, X, 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: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Y, Z, a, b, m                         
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: c, d, e, f, 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 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     GLY A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     GLY B   189                                                      
REMARK 465     SER B   190                                                      
REMARK 465     ASP B   250                                                      
REMARK 465     THR B   251                                                      
REMARK 465     LYS B   252                                                      
REMARK 465     LYS B   253                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     MET C     6                                                      
REMARK 465     MET C     7                                                      
REMARK 465     ASP C    80                                                      
REMARK 465     LEU C    81                                                      
REMARK 465     GLY C    82                                                      
REMARK 465     TRP C    83                                                      
REMARK 465     LYS D   201                                                      
REMARK 465     MET D   202                                                      
REMARK 465     LEU D   203                                                      
REMARK 465     GLY E    24                                                      
REMARK 465     PRO E    25                                                      
REMARK 465     GLY F   189                                                      
REMARK 465     SER F   190                                                      
REMARK 465     LYS F   252                                                      
REMARK 465     LYS F   253                                                      
REMARK 465     GLY G     3                                                      
REMARK 465     SER G     4                                                      
REMARK 465     HIS G     5                                                      
REMARK 465     MET G     6                                                      
REMARK 465     MET G     7                                                      
REMARK 465     GLY G    82                                                      
REMARK 465     TRP G    83                                                      
REMARK 465     THR H   200                                                      
REMARK 465     LYS H   201                                                      
REMARK 465     MET H   202                                                      
REMARK 465     LEU H   203                                                      
REMARK 465     GLY I    24                                                      
REMARK 465     PRO I    25                                                      
REMARK 465     LEU I    26                                                      
REMARK 465     GLY J   189                                                      
REMARK 465     SER J   249                                                      
REMARK 465     ASP J   250                                                      
REMARK 465     THR J   251                                                      
REMARK 465     LYS J   252                                                      
REMARK 465     LYS J   253                                                      
REMARK 465     GLY K     3                                                      
REMARK 465     SER K     4                                                      
REMARK 465     HIS K     5                                                      
REMARK 465     MET K     6                                                      
REMARK 465     MET K     7                                                      
REMARK 465     ARG K     8                                                      
REMARK 465     ASP K    80                                                      
REMARK 465     LEU K    81                                                      
REMARK 465     GLY K    82                                                      
REMARK 465     TRP K    83                                                      
REMARK 465     LEU L   203                                                      
REMARK 465     GLY M    24                                                      
REMARK 465     GLY N   189                                                      
REMARK 465     SER N   190                                                      
REMARK 465     VAL N   248                                                      
REMARK 465     SER N   249                                                      
REMARK 465     ASP N   250                                                      
REMARK 465     THR N   251                                                      
REMARK 465     LYS N   252                                                      
REMARK 465     LYS N   253                                                      
REMARK 465     GLY O     3                                                      
REMARK 465     SER O     4                                                      
REMARK 465     HIS O     5                                                      
REMARK 465     MET O     6                                                      
REMARK 465     MET O     7                                                      
REMARK 465     ASP O    80                                                      
REMARK 465     LEU O    81                                                      
REMARK 465     GLY O    82                                                      
REMARK 465     TRP O    83                                                      
REMARK 465     LEU P   203                                                      
REMARK 465     GLY Q    24                                                      
REMARK 465     PRO Q    25                                                      
REMARK 465     GLY R   189                                                      
REMARK 465     SER R   190                                                      
REMARK 465     LYS R   252                                                      
REMARK 465     LYS R   253                                                      
REMARK 465     GLY S     3                                                      
REMARK 465     SER S     4                                                      
REMARK 465     HIS S     5                                                      
REMARK 465     MET S     6                                                      
REMARK 465     MET S     7                                                      
REMARK 465     ARG S     8                                                      
REMARK 465     ASN S     9                                                      
REMARK 465     ASP S    80                                                      
REMARK 465     LEU S    81                                                      
REMARK 465     GLY S    82                                                      
REMARK 465     TRP S    83                                                      
REMARK 465     LYS T   201                                                      
REMARK 465     MET T   202                                                      
REMARK 465     LEU T   203                                                      
REMARK 465     GLY U    24                                                      
REMARK 465     PRO U    25                                                      
REMARK 465     GLY V   189                                                      
REMARK 465     SER V   190                                                      
REMARK 465     SER V   249                                                      
REMARK 465     ASP V   250                                                      
REMARK 465     THR V   251                                                      
REMARK 465     LYS V   252                                                      
REMARK 465     LYS V   253                                                      
REMARK 465     GLY W     3                                                      
REMARK 465     SER W     4                                                      
REMARK 465     HIS W     5                                                      
REMARK 465     MET W     6                                                      
REMARK 465     MET W     7                                                      
REMARK 465     LEU W    78                                                      
REMARK 465     LYS W    79                                                      
REMARK 465     ASP W    80                                                      
REMARK 465     LEU W    81                                                      
REMARK 465     GLY W    82                                                      
REMARK 465     TRP W    83                                                      
REMARK 465     MET X   202                                                      
REMARK 465     LEU X   203                                                      
REMARK 465     GLY Y    24                                                      
REMARK 465     PRO Y    25                                                      
REMARK 465     GLY Z   189                                                      
REMARK 465     VAL Z   248                                                      
REMARK 465     SER Z   249                                                      
REMARK 465     ASP Z   250                                                      
REMARK 465     THR Z   251                                                      
REMARK 465     LYS Z   252                                                      
REMARK 465     LYS Z   253                                                      
REMARK 465     GLY a     3                                                      
REMARK 465     SER a     4                                                      
REMARK 465     HIS a     5                                                      
REMARK 465     MET a     6                                                      
REMARK 465     MET a     7                                                      
REMARK 465     ARG a     8                                                      
REMARK 465     ASN a     9                                                      
REMARK 465     ASP a    80                                                      
REMARK 465     LEU a    81                                                      
REMARK 465     GLY a    82                                                      
REMARK 465     TRP a    83                                                      
REMARK 465     THR b   200                                                      
REMARK 465     LYS b   201                                                      
REMARK 465     MET b   202                                                      
REMARK 465     LEU b   203                                                      
REMARK 465     GLY c    24                                                      
REMARK 465     PRO c    25                                                      
REMARK 465     LEU c    26                                                      
REMARK 465     GLY d   189                                                      
REMARK 465     SER d   249                                                      
REMARK 465     ASP d   250                                                      
REMARK 465     THR d   251                                                      
REMARK 465     LYS d   252                                                      
REMARK 465     LYS d   253                                                      
REMARK 465     GLY e     3                                                      
REMARK 465     SER e     4                                                      
REMARK 465     HIS e     5                                                      
REMARK 465     MET e     6                                                      
REMARK 465     MET e     7                                                      
REMARK 465     ASP e    80                                                      
REMARK 465     LEU e    81                                                      
REMARK 465     GLY e    82                                                      
REMARK 465     TRP e    83                                                      
REMARK 465     LYS f   201                                                      
REMARK 465     MET f   202                                                      
REMARK 465     LEU f   203                                                      
REMARK 465     GLY g    21                                                      
REMARK 465     PRO g    22                                                      
REMARK 465     LEU g    23                                                      
REMARK 465     GLY g    71                                                      
REMARK 465     ILE g    72                                                      
REMARK 465     LYS g    73                                                      
REMARK 465     LYS g    74                                                      
REMARK 465     LYS g    75                                                      
REMARK 465     GLU g    76                                                      
REMARK 465     GLU g    77                                                      
REMARK 465     ARG g    78                                                      
REMARK 465     GLU g    79                                                      
REMARK 465     ALA g    80                                                      
REMARK 465     GLU g    81                                                      
REMARK 465     ALA g    82                                                      
REMARK 465     GLN g    83                                                      
REMARK 465     GLY h    21                                                      
REMARK 465     PRO h    22                                                      
REMARK 465     LEU h    23                                                      
REMARK 465     GLY h    24                                                      
REMARK 465     GLY h    71                                                      
REMARK 465     ILE h    72                                                      
REMARK 465     LYS h    73                                                      
REMARK 465     LYS h    74                                                      
REMARK 465     LYS h    75                                                      
REMARK 465     GLU h    76                                                      
REMARK 465     GLU h    77                                                      
REMARK 465     ARG h    78                                                      
REMARK 465     GLU h    79                                                      
REMARK 465     ALA h    80                                                      
REMARK 465     GLU h    81                                                      
REMARK 465     ALA h    82                                                      
REMARK 465     GLN h    83                                                      
REMARK 465     GLY i    21                                                      
REMARK 465     PRO i    22                                                      
REMARK 465     LEU i    23                                                      
REMARK 465     GLY i    24                                                      
REMARK 465     SER i    25                                                      
REMARK 465     GLY i    71                                                      
REMARK 465     ILE i    72                                                      
REMARK 465     LYS i    73                                                      
REMARK 465     LYS i    74                                                      
REMARK 465     LYS i    75                                                      
REMARK 465     GLU i    76                                                      
REMARK 465     GLU i    77                                                      
REMARK 465     ARG i    78                                                      
REMARK 465     GLU i    79                                                      
REMARK 465     ALA i    80                                                      
REMARK 465     GLU i    81                                                      
REMARK 465     ALA i    82                                                      
REMARK 465     GLN i    83                                                      
REMARK 465     GLY j    21                                                      
REMARK 465     PRO j    22                                                      
REMARK 465     LEU j    23                                                      
REMARK 465     GLY j    24                                                      
REMARK 465     SER j    25                                                      
REMARK 465     GLY j    71                                                      
REMARK 465     ILE j    72                                                      
REMARK 465     LYS j    73                                                      
REMARK 465     LYS j    74                                                      
REMARK 465     LYS j    75                                                      
REMARK 465     GLU j    76                                                      
REMARK 465     GLU j    77                                                      
REMARK 465     ARG j    78                                                      
REMARK 465     GLU j    79                                                      
REMARK 465     ALA j    80                                                      
REMARK 465     GLU j    81                                                      
REMARK 465     ALA j    82                                                      
REMARK 465     GLN j    83                                                      
REMARK 465     GLY k    21                                                      
REMARK 465     PRO k    22                                                      
REMARK 465     LEU k    23                                                      
REMARK 465     GLY k    24                                                      
REMARK 465     GLY k    71                                                      
REMARK 465     ILE k    72                                                      
REMARK 465     LYS k    73                                                      
REMARK 465     LYS k    74                                                      
REMARK 465     LYS k    75                                                      
REMARK 465     GLU k    76                                                      
REMARK 465     GLU k    77                                                      
REMARK 465     ARG k    78                                                      
REMARK 465     GLU k    79                                                      
REMARK 465     ALA k    80                                                      
REMARK 465     GLU k    81                                                      
REMARK 465     ALA k    82                                                      
REMARK 465     GLN k    83                                                      
REMARK 465     GLY l    21                                                      
REMARK 465     PRO l    22                                                      
REMARK 465     LEU l    23                                                      
REMARK 465     GLY l    71                                                      
REMARK 465     ILE l    72                                                      
REMARK 465     LYS l    73                                                      
REMARK 465     LYS l    74                                                      
REMARK 465     LYS l    75                                                      
REMARK 465     GLU l    76                                                      
REMARK 465     GLU l    77                                                      
REMARK 465     ARG l    78                                                      
REMARK 465     GLU l    79                                                      
REMARK 465     ALA l    80                                                      
REMARK 465     GLU l    81                                                      
REMARK 465     ALA l    82                                                      
REMARK 465     GLN l    83                                                      
REMARK 465     GLY m    21                                                      
REMARK 465     PRO m    22                                                      
REMARK 465     LEU m    23                                                      
REMARK 465     GLY m    24                                                      
REMARK 465     SER m    25                                                      
REMARK 465     GLY m    71                                                      
REMARK 465     ILE m    72                                                      
REMARK 465     LYS m    73                                                      
REMARK 465     LYS m    74                                                      
REMARK 465     LYS m    75                                                      
REMARK 465     GLU m    76                                                      
REMARK 465     GLU m    77                                                      
REMARK 465     ARG m    78                                                      
REMARK 465     GLU m    79                                                      
REMARK 465     ALA m    80                                                      
REMARK 465     GLU m    81                                                      
REMARK 465     ALA m    82                                                      
REMARK 465     GLN m    83                                                      
REMARK 465     GLY n    21                                                      
REMARK 465     PRO n    22                                                      
REMARK 465     LEU n    23                                                      
REMARK 465     GLY n    24                                                      
REMARK 465     SER n    25                                                      
REMARK 465     GLY n    71                                                      
REMARK 465     ILE n    72                                                      
REMARK 465     LYS n    73                                                      
REMARK 465     LYS n    74                                                      
REMARK 465     LYS n    75                                                      
REMARK 465     GLU n    76                                                      
REMARK 465     GLU n    77                                                      
REMARK 465     ARG n    78                                                      
REMARK 465     GLU n    79                                                      
REMARK 465     ALA n    80                                                      
REMARK 465     GLU n    81                                                      
REMARK 465     ALA n    82                                                      
REMARK 465     GLN n    83                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A  26    CG   CD1  CD2                                       
REMARK 470     GLU O  10    CG   CD   OE1  OE2                                  
REMARK 470     LYS T 189    CG   CD   CE   NZ                                   
REMARK 470     GLN c  58    CG   CD   OE1  NE2                                  
REMARK 470     MET f 182    CG   SD   CE                                        
REMARK 470     LYS f 189    CG   CD   CE   NZ                                   
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU B  234   CG   CD   OE1  OE2                                  
REMARK 480     GLU B  238   CG   CD   OE1  OE2                                  
REMARK 480     ARG C    8   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG C   16   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS C   76   CG   CD   CE   NZ                                   
REMARK 480     LYS C   79   CG   CD   CE   NZ                                   
REMARK 480     THR D  200   OG1  CG2                                            
REMARK 480     LEU E   26   CG   CD1  CD2                                       
REMARK 480     ARG F  198   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU F  238   CG   CD   OE1  OE2                                  
REMARK 480     ARG G    8   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN G   34   CG   CD   OE1  NE2                                  
REMARK 480     LYS G   72   CG   CD   CE   NZ                                   
REMARK 480     LYS G   76   CG   CD   CE   NZ                                   
REMARK 480     LYS G   79   CG   CD   CE   NZ                                   
REMARK 480     ASP G   80   CG   OD1  OD2                                       
REMARK 480     LEU G   81   CG   CD1  CD2                                       
REMARK 480     ASP H  193   CG   OD1  OD2                                       
REMARK 480     GLU H  194   CG   CD   OE1  OE2                                  
REMARK 480     LYS K   72   CG   CD   CE   NZ                                   
REMARK 480     GLU K   73   CG   CD   OE1  OE2                                  
REMARK 480     GLU K   75   CG   CD   OE1  OE2                                  
REMARK 480     LYS K   76   CG   CD   CE   NZ                                   
REMARK 480     LEU K   78   CG   CD1  CD2                                       
REMARK 480     LYS K   79   CG   CD   CE   NZ                                   
REMARK 480     ASP L  193   CG   OD1  OD2                                       
REMARK 480     GLU L  194   CG   CD   OE1  OE2                                  
REMARK 480     LEU M   26   CG   CD1  CD2                                       
REMARK 480     GLU N  194   CD   OE1  OE2                                       
REMARK 480     ARG N  198   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG N  210   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG O    8   NE   CZ   NH1  NH2                                  
REMARK 480     ARG O   16   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN O   34   CB   CG   CD   OE1  NE2                             
REMARK 480     LEU O   78   CG   CD1  CD2                                       
REMARK 480     LYS O   79   CG   CD   CE   NZ                                   
REMARK 480     LYS P  201   CG   CD   CE   NZ                                   
REMARK 480     LEU Q   26   CG   CD1  CD2                                       
REMARK 480     ARG R  198   NE   CZ   NH1  NH2                                  
REMARK 480     GLU R  238   CG   CD   OE1  OE2                                  
REMARK 480     GLU S   10   CG   CD   OE1  OE2                                  
REMARK 480     LYS S   79   CG   CD   CE   NZ                                   
REMARK 480     ARG V  210   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU V  245   CG   CD   OE1  OE2                                  
REMARK 480     ARG V  246   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG W    8   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN W   34   CG   CD   OE1  NE2                                  
REMARK 480     LYS W   72   CG   CD   CE   NZ                                   
REMARK 480     LYS W   76   CG   CD   CE   NZ                                   
REMARK 480     ASP X  193   CG   OD1  OD2                                       
REMARK 480     LYS X  201   CG   CD   CE   NZ                                   
REMARK 480     ARG Z  198   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG a   16   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN a   34   CG   CD   OE1  NE2                                  
REMARK 480     GLU b  194   CG   CD   OE1  OE2                                  
REMARK 480     ARG b  198   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU c   55   CG   CD   OE1  OE2                                  
REMARK 480     ARG d  210   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG d  246   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG e    8   NE   CZ   NH1  NH2                                  
REMARK 480     ARG e   16   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS e   72   CG   CD   CE   NZ                                   
REMARK 480     GLU e   73   CG   CD   OE1  OE2                                  
REMARK 480     GLU e   75   CG   CD   OE1  OE2                                  
REMARK 480     LYS e   76   CG   CD   CE   NZ                                   
REMARK 480     LEU e   78   CG   CD1  CD2                                       
REMARK 480     LYS e   79   CG   CD   CE   NZ                                   
REMARK 480     ARG f  191   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS i   26   CG   CD   CE   NZ                                   
REMARK 480     GLU i   47   CD   OE1  OE2                                       
REMARK 480     LYS j   26   CG   CD   CE   NZ                                   
REMARK 480     ARG j   48   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG k   42   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS m   26   CG   CD   CE   NZ                                   
REMARK 480     ARG m   67   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS n   26   CG   CD   CE   NZ                                   
REMARK 480     ARG n   42   CD   NE   CZ   NH1  NH2                             
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   OE2  GLU G    75     CD   LYS G    79              1.65            
REMARK 500   OE2  GLU N   206     NH2  ARG N   210              1.65            
REMARK 500   NZ   LYS S    79     CB   ALA T   199              1.69            
REMARK 500   CG   MET F   221     NH1  ARG N   210              1.76            
REMARK 500   OE1  GLU C    13     NH2  ARG C    16              1.86            
REMARK 500   OE2  GLU G    13     NH2  ARG G    17              1.86            
REMARK 500   NZ   LYS S    79     CA   ALA T   199              1.90            
REMARK 500   CD   GLU N   206     NH2  ARG N   210              2.03            
REMARK 500   ND2  ASN T   159     OD1  ASP W    23              2.04            
REMARK 500   OE2  GLU O    13     NH2  ARG O    17              2.05            
REMARK 500   CG1  ILE Z   195     NH2  ARG Z   198              2.10            
REMARK 500   CZ   ARG W    45     NH1  ARG e    31              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    ALA V   247     NH2  ARG k    42     1445     1.04            
REMARK 500   C    ALA b   199     NH2  ARG j    48     1544     1.06            
REMARK 500   O    ALA b   199     NH2  ARG j    48     1544     1.27            
REMARK 500   O    ALA b   199     CZ   ARG j    48     1544     1.58            
REMARK 500   OE1  GLU B   238     OE2  GLU K    10     1655     1.58            
REMARK 500   OE1  GLU B   234     NH1  ARG K    17     1655     1.74            
REMARK 500   O    ALA V   247     CZ   ARG k    42     1445     1.79            
REMARK 500   C    ALA b   199     CZ   ARG j    48     1544     2.05            
REMARK 500   O    ALA b   199     NH1  ARG j    48     1544     2.08            
REMARK 500   OD1  ASP C    23     ND2  ASN H   159     1655     2.08            
REMARK 500   O    ALA V   247     NH1  ARG k    42     1445     2.13            
REMARK 500   NE2  GLN S    20     OE1  GLU Z   228     1655     2.14            
REMARK 500   C    ALA V   247     NH2  ARG k    42     1445     2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG C  16   CB    ARG C  16   CG      0.191                       
REMARK 500    ARG C  17   CG    ARG C  17   CD     -0.152                       
REMARK 500    LYS C  79   CB    LYS C  79   CG     -0.324                       
REMARK 500    ARG G  17   CG    ARG G  17   CD     -0.166                       
REMARK 500    GLN G  34   CB    GLN G  34   CG      0.213                       
REMARK 500    ASP G  80   CB    ASP G  80   CG      0.202                       
REMARK 500    ASP H 193   CB    ASP H 193   CG     -0.200                       
REMARK 500    ARG K  17   CG    ARG K  17   CD     -0.226                       
REMARK 500    ARG K  17   CZ    ARG K  17   NH2    -0.102                       
REMARK 500    GLU K  75   CB    GLU K  75   CG     -0.185                       
REMARK 500    GLU L 194   CB    GLU L 194   CG      0.167                       
REMARK 500    GLU N 194   CG    GLU N 194   CD      0.128                       
REMARK 500    ARG N 210   CB    ARG N 210   CG      0.213                       
REMARK 500    ARG O   8   CD    ARG O   8   NE      0.242                       
REMARK 500    ARG O  16   CB    ARG O  16   CG      0.287                       
REMARK 500    ARG O  17   CG    ARG O  17   CD     -0.157                       
REMARK 500    LYS O  79   CB    LYS O  79   CG      0.179                       
REMARK 500    ARG S  17   CG    ARG S  17   CD     -0.178                       
REMARK 500    ARG S  17   CZ    ARG S  17   NH1    -0.087                       
REMARK 500    ARG U  47   CG    ARG U  47   CD     -0.200                       
REMARK 500    GLU V 245   CB    GLU V 245   CG     -0.173                       
REMARK 500    ARG V 246   CB    ARG V 246   CG      0.203                       
REMARK 500    ARG W  17   CG    ARG W  17   CD     -0.159                       
REMARK 500    GLN W  34   CB    GLN W  34   CG      0.242                       
REMARK 500    ARG a  17   CG    ARG a  17   CD     -0.162                       
REMARK 500    ARG d 246   CB    ARG d 246   CG      0.167                       
REMARK 500    ARG e  17   CG    ARG e  17   CD     -0.165                       
REMARK 500    LYS e  72   CB    LYS e  72   CG     -0.184                       
REMARK 500    GLU e  73   CB    GLU e  73   CG      0.259                       
REMARK 500    ARG f 191   CB    ARG f 191   CG      0.221                       
REMARK 500    LYS i  26   CB    LYS i  26   CG     -0.343                       
REMARK 500    GLU i  47   CG    GLU i  47   CD     -0.128                       
REMARK 500    ARG m  67   CB    ARG m  67   CG     -0.279                       
REMARK 500    LYS n  26   CB    LYS n  26   CG     -0.173                       
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    ARG C  16   CA  -  CB  -  CG  ANGL. DEV. = -18.8 DEGREES          
REMARK 500    ARG C  31   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    LYS C  79   CA  -  CB  -  CG  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    THR D 200   CA  -  CB  -  CG2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG G  31   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ASP G  80   CA  -  CB  -  CG  ANGL. DEV. = -16.6 DEGREES          
REMARK 500    ASP G  80   CB  -  CG  -  OD1 ANGL. DEV. =  12.2 DEGREES          
REMARK 500    ASP G  80   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ASP H 193   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG K  17   CD  -  NE  -  CZ  ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    ARG K  17   NH1 -  CZ  -  NH2 ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    ARG K  17   NE  -  CZ  -  NH2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG K  31   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    GLU K  75   CA  -  CB  -  CG  ANGL. DEV. = -15.9 DEGREES          
REMARK 500    LYS K  76   CA  -  CB  -  CG  ANGL. DEV. = -19.2 DEGREES          
REMARK 500    ARG L 198   CB  -  CG  -  CD  ANGL. DEV. =  21.0 DEGREES          
REMARK 500    ARG O   8   CG  -  CD  -  NE  ANGL. DEV. = -17.1 DEGREES          
REMARK 500    ARG O   8   CD  -  NE  -  CZ  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    ARG O  31   CD  -  NE  -  CZ  ANGL. DEV. =  -8.4 DEGREES          
REMARK 500    ARG O  31   NE  -  CZ  -  NH1 ANGL. DEV. = -11.0 DEGREES          
REMARK 500    ARG O  31   NE  -  CZ  -  NH2 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    LYS O  79   CA  -  CB  -  CG  ANGL. DEV. =  23.4 DEGREES          
REMARK 500    ARG S  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ARG S  31   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG U  47   CD  -  NE  -  CZ  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    ARG U  47   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG U  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP U  51   OD1 -  CG  -  OD2 ANGL. DEV. = -17.8 DEGREES          
REMARK 500    ASP U  51   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP U  51   CB  -  CG  -  OD2 ANGL. DEV. =  12.0 DEGREES          
REMARK 500    ARG V 246   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    ARG V 246   CB  -  CG  -  CD  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    ARG W  31   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG a  31   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    GLU b 194   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    ARG e  31   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    GLU e  73   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    ARG m  67   CA  -  CB  -  CG  ANGL. DEV. =  16.5 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    LEU C  78       33.54    -91.62                                   
REMARK 500    ASP G  80      -82.87   -125.40                                   
REMARK 500    LEU S  78      -72.81    -98.96                                   
REMARK 500    GLU W  13      -70.33    -62.27                                   
REMARK 500    ALA Z 191      -43.09    -26.90                                   
REMARK 500    LEU e  11      -72.38    -65.77                                   
REMARK 500    ARG g  63      -72.35    -54.83                                   
REMARK 500    LYS h  32      -70.34    -62.17                                   
REMARK 500    GLU h  56      -75.07    -41.75                                   
REMARK 500    LYS n  32      -71.53    -51.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU g   27     PRO g   28                  149.80                    
REMARK 500 LEU h   27     PRO h   28                  140.34                    
REMARK 500 LEU l   27     PRO l   28                  148.68                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG O   8         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RK2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3RK3   RELATED DB: PDB                                   
DBREF  3RL0 A   28    60  UNP    P63027   VAMP2_HUMAN     28     60             
DBREF  3RL0 B  191   253  UNP    P32851   STX1A_RAT      191    253             
DBREF  3RL0 C    7    82  UNP    P60880   SNP25_HUMAN      7     82             
DBREF  3RL0 D  141   203  UNP    P60880   SNP25_HUMAN    141    203             
DBREF  3RL0 E   28    60  UNP    P63027   VAMP2_HUMAN     28     60             
DBREF  3RL0 F  191   253  UNP    P32851   STX1A_RAT      191    253             
DBREF  3RL0 G    7    82  UNP    P60880   SNP25_HUMAN      7     82             
DBREF  3RL0 H  141   203  UNP    P60880   SNP25_HUMAN    141    203             
DBREF  3RL0 I   28    60  UNP    P63027   VAMP2_HUMAN     28     60             
DBREF  3RL0 J  191   253  UNP    P32851   STX1A_RAT      191    253             
DBREF  3RL0 K    7    82  UNP    P60880   SNP25_HUMAN      7     82             
DBREF  3RL0 L  141   203  UNP    P60880   SNP25_HUMAN    141    203             
DBREF  3RL0 M   28    60  UNP    P63027   VAMP2_HUMAN     28     60             
DBREF  3RL0 N  191   253  UNP    P32851   STX1A_RAT      191    253             
DBREF  3RL0 O    7    82  UNP    P60880   SNP25_HUMAN      7     82             
DBREF  3RL0 P  141   203  UNP    P60880   SNP25_HUMAN    141    203             
DBREF  3RL0 Q   28    60  UNP    P63027   VAMP2_HUMAN     28     60             
DBREF  3RL0 R  191   253  UNP    P32851   STX1A_RAT      191    253             
DBREF  3RL0 S    7    82  UNP    P60880   SNP25_HUMAN      7     82             
DBREF  3RL0 T  141   203  UNP    P60880   SNP25_HUMAN    141    203             
DBREF  3RL0 U   28    60  UNP    P63027   VAMP2_HUMAN     28     60             
DBREF  3RL0 V  191   253  UNP    P32851   STX1A_RAT      191    253             
DBREF  3RL0 W    7    82  UNP    P60880   SNP25_HUMAN      7     82             
DBREF  3RL0 X  141   203  UNP    P60880   SNP25_HUMAN    141    203             
DBREF  3RL0 Y   28    60  UNP    P63027   VAMP2_HUMAN     28     60             
DBREF  3RL0 Z  191   253  UNP    P32851   STX1A_RAT      191    253             
DBREF  3RL0 a    7    82  UNP    P60880   SNP25_HUMAN      7     82             
DBREF  3RL0 b  141   203  UNP    P60880   SNP25_HUMAN    141    203             
DBREF  3RL0 c   28    60  UNP    P63027   VAMP2_HUMAN     28     60             
DBREF  3RL0 d  191   253  UNP    P32851   STX1A_RAT      191    253             
DBREF  3RL0 e    7    82  UNP    P60880   SNP25_HUMAN      7     82             
DBREF  3RL0 f  141   203  UNP    P60880   SNP25_HUMAN    141    203             
DBREF  3RL0 g   26    83  UNP    O14810   CPLX1_HUMAN     26     83             
DBREF  3RL0 h   26    83  UNP    O14810   CPLX1_HUMAN     26     83             
DBREF  3RL0 i   26    83  UNP    O14810   CPLX1_HUMAN     26     83             
DBREF  3RL0 j   26    83  UNP    O14810   CPLX1_HUMAN     26     83             
DBREF  3RL0 k   26    83  UNP    O14810   CPLX1_HUMAN     26     83             
DBREF  3RL0 l   26    83  UNP    O14810   CPLX1_HUMAN     26     83             
DBREF  3RL0 m   26    83  UNP    O14810   CPLX1_HUMAN     26     83             
DBREF  3RL0 n   26    83  UNP    O14810   CPLX1_HUMAN     26     83             
SEQADV 3RL0 GLY A   24  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 PRO A   25  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 LEU A   26  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY A   27  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY B  189  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 SER B  190  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 GLY C    3  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER C    4  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 HIS C    5  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 MET C    6  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 TRP C   83  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY D  139  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER D  140  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY E   24  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 PRO E   25  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 LEU E   26  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY E   27  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY F  189  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 SER F  190  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 GLY G    3  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER G    4  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 HIS G    5  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 MET G    6  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 TRP G   83  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY H  139  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER H  140  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY I   24  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 PRO I   25  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 LEU I   26  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY I   27  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY J  189  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 SER J  190  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 GLY K    3  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER K    4  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 HIS K    5  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 MET K    6  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 TRP K   83  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY L  139  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER L  140  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY M   24  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 PRO M   25  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 LEU M   26  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY M   27  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY N  189  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 SER N  190  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 GLY O    3  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER O    4  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 HIS O    5  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 MET O    6  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 TRP O   83  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY P  139  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER P  140  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY Q   24  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 PRO Q   25  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 LEU Q   26  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY Q   27  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY R  189  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 SER R  190  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 GLY S    3  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER S    4  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 HIS S    5  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 MET S    6  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 TRP S   83  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY T  139  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER T  140  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY U   24  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 PRO U   25  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 LEU U   26  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY U   27  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY V  189  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 SER V  190  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 GLY W    3  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER W    4  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 HIS W    5  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 MET W    6  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 TRP W   83  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY X  139  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER X  140  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY Y   24  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 PRO Y   25  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 LEU Y   26  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY Y   27  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY Z  189  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 SER Z  190  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 GLY a    3  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER a    4  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 HIS a    5  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 MET a    6  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 TRP a   83  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY b  139  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER b  140  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY c   24  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 PRO c   25  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 LEU c   26  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY c   27  UNP  P63027              EXPRESSION TAG                 
SEQADV 3RL0 GLY d  189  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 SER d  190  UNP  P32851              EXPRESSION TAG                 
SEQADV 3RL0 GLY e    3  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER e    4  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 HIS e    5  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 MET e    6  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 TRP e   83  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY f  139  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 SER f  140  UNP  P60880              EXPRESSION TAG                 
SEQADV 3RL0 GLY g   21  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 PRO g   22  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU g   23  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 GLY g   24  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 SER g   25  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU g   27  UNP  O14810    ASP    27 ENGINEERED MUTATION            
SEQADV 3RL0 MSE g   34  UNP  O14810    GLU    34 ENGINEERED MUTATION            
SEQADV 3RL0 ALA g   37  UNP  O14810    ARG    37 ENGINEERED MUTATION            
SEQADV 3RL0 GLY h   21  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 PRO h   22  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU h   23  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 GLY h   24  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 SER h   25  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU h   27  UNP  O14810    ASP    27 ENGINEERED MUTATION            
SEQADV 3RL0 MSE h   34  UNP  O14810    GLU    34 ENGINEERED MUTATION            
SEQADV 3RL0 ALA h   37  UNP  O14810    ARG    37 ENGINEERED MUTATION            
SEQADV 3RL0 GLY i   21  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 PRO i   22  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU i   23  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 GLY i   24  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 SER i   25  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU i   27  UNP  O14810    ASP    27 ENGINEERED MUTATION            
SEQADV 3RL0 MSE i   34  UNP  O14810    GLU    34 ENGINEERED MUTATION            
SEQADV 3RL0 ALA i   37  UNP  O14810    ARG    37 ENGINEERED MUTATION            
SEQADV 3RL0 GLY j   21  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 PRO j   22  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU j   23  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 GLY j   24  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 SER j   25  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU j   27  UNP  O14810    ASP    27 ENGINEERED MUTATION            
SEQADV 3RL0 MSE j   34  UNP  O14810    GLU    34 ENGINEERED MUTATION            
SEQADV 3RL0 ALA j   37  UNP  O14810    ARG    37 ENGINEERED MUTATION            
SEQADV 3RL0 GLY k   21  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 PRO k   22  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU k   23  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 GLY k   24  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 SER k   25  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU k   27  UNP  O14810    ASP    27 ENGINEERED MUTATION            
SEQADV 3RL0 MSE k   34  UNP  O14810    GLU    34 ENGINEERED MUTATION            
SEQADV 3RL0 ALA k   37  UNP  O14810    ARG    37 ENGINEERED MUTATION            
SEQADV 3RL0 GLY l   21  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 PRO l   22  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU l   23  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 GLY l   24  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 SER l   25  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU l   27  UNP  O14810    ASP    27 ENGINEERED MUTATION            
SEQADV 3RL0 MSE l   34  UNP  O14810    GLU    34 ENGINEERED MUTATION            
SEQADV 3RL0 ALA l   37  UNP  O14810    ARG    37 ENGINEERED MUTATION            
SEQADV 3RL0 GLY m   21  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 PRO m   22  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU m   23  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 GLY m   24  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 SER m   25  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU m   27  UNP  O14810    ASP    27 ENGINEERED MUTATION            
SEQADV 3RL0 MSE m   34  UNP  O14810    GLU    34 ENGINEERED MUTATION            
SEQADV 3RL0 ALA m   37  UNP  O14810    ARG    37 ENGINEERED MUTATION            
SEQADV 3RL0 GLY n   21  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 PRO n   22  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU n   23  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 GLY n   24  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 SER n   25  UNP  O14810              EXPRESSION TAG                 
SEQADV 3RL0 LEU n   27  UNP  O14810    ASP    27 ENGINEERED MUTATION            
SEQADV 3RL0 MSE n   34  UNP  O14810    GLU    34 ENGINEERED MUTATION            
SEQADV 3RL0 ALA n   37  UNP  O14810    ARG    37 ENGINEERED MUTATION            
SEQRES   1 A   37  GLY PRO LEU GLY SER ASN ARG ARG LEU GLN GLN THR GLN          
SEQRES   2 A   37  ALA GLN VAL ASP GLU VAL VAL ASP ILE MET ARG VAL ASN          
SEQRES   3 A   37  VAL ASP LYS VAL LEU GLU ARG ASP GLN LYS LEU                  
SEQRES   1 B   65  GLY SER ALA LEU SER GLU ILE GLU THR ARG HIS SER GLU          
SEQRES   2 B   65  ILE ILE LYS LEU GLU ASN SER ILE ARG GLU LEU HIS ASP          
SEQRES   3 B   65  MET PHE MET ASP MET ALA MET LEU VAL GLU SER GLN GLY          
SEQRES   4 B   65  GLU MET ILE ASP ARG ILE GLU TYR ASN VAL GLU HIS ALA          
SEQRES   5 B   65  VAL ASP TYR VAL GLU ARG ALA VAL SER ASP THR LYS LYS          
SEQRES   1 C   81  GLY SER HIS MET MET ARG ASN GLU LEU GLU GLU MET GLN          
SEQRES   2 C   81  ARG ARG ALA ASP GLN LEU ALA ASP GLU SER LEU GLU SER          
SEQRES   3 C   81  THR ARG ARG MET LEU GLN LEU VAL GLU GLU SER LYS ASP          
SEQRES   4 C   81  ALA GLY ILE ARG THR LEU VAL MET LEU ASP GLU GLN GLY          
SEQRES   5 C   81  GLU GLN LEU ASP ARG VAL GLU GLU GLY MET ASN HIS ILE          
SEQRES   6 C   81  ASN GLN ASP MET LYS GLU ALA GLU LYS ASN LEU LYS ASP          
SEQRES   7 C   81  LEU GLY TRP                                                  
SEQRES   1 D   65  GLY SER ALA ARG GLU ASN GLU MET ASP GLU ASN LEU GLU          
SEQRES   2 D   65  GLN VAL SER GLY ILE ILE GLY ASN LEU ARG HIS MET ALA          
SEQRES   3 D   65  LEU ASP MET GLY ASN GLU ILE ASP THR GLN ASN ARG GLN          
SEQRES   4 D   65  ILE ASP ARG ILE MET GLU LYS ALA ASP SER ASN LYS THR          
SEQRES   5 D   65  ARG ILE ASP GLU ALA ASN GLN ARG ALA THR LYS MET LEU          
SEQRES   1 E   37  GLY PRO LEU GLY SER ASN ARG ARG LEU GLN GLN THR GLN          
SEQRES   2 E   37  ALA GLN VAL ASP GLU VAL VAL ASP ILE MET ARG VAL ASN          
SEQRES   3 E   37  VAL ASP LYS VAL LEU GLU ARG ASP GLN LYS LEU                  
SEQRES   1 F   65  GLY SER ALA LEU SER GLU ILE GLU THR ARG HIS SER GLU          
SEQRES   2 F   65  ILE ILE LYS LEU GLU ASN SER ILE ARG GLU LEU HIS ASP          
SEQRES   3 F   65  MET PHE MET ASP MET ALA MET LEU VAL GLU SER GLN GLY          
SEQRES   4 F   65  GLU MET ILE ASP ARG ILE GLU TYR ASN VAL GLU HIS ALA          
SEQRES   5 F   65  VAL ASP TYR VAL GLU ARG ALA VAL SER ASP THR LYS LYS          
SEQRES   1 G   81  GLY SER HIS MET MET ARG ASN GLU LEU GLU GLU MET GLN          
SEQRES   2 G   81  ARG ARG ALA ASP GLN LEU ALA ASP GLU SER LEU GLU SER          
SEQRES   3 G   81  THR ARG ARG MET LEU GLN LEU VAL GLU GLU SER LYS ASP          
SEQRES   4 G   81  ALA GLY ILE ARG THR LEU VAL MET LEU ASP GLU GLN GLY          
SEQRES   5 G   81  GLU GLN LEU ASP ARG VAL GLU GLU GLY MET ASN HIS ILE          
SEQRES   6 G   81  ASN GLN ASP MET LYS GLU ALA GLU LYS ASN LEU LYS ASP          
SEQRES   7 G   81  LEU GLY TRP                                                  
SEQRES   1 H   65  GLY SER ALA ARG GLU ASN GLU MET ASP GLU ASN LEU GLU          
SEQRES   2 H   65  GLN VAL SER GLY ILE ILE GLY ASN LEU ARG HIS MET ALA          
SEQRES   3 H   65  LEU ASP MET GLY ASN GLU ILE ASP THR GLN ASN ARG GLN          
SEQRES   4 H   65  ILE ASP ARG ILE MET GLU LYS ALA ASP SER ASN LYS THR          
SEQRES   5 H   65  ARG ILE ASP GLU ALA ASN GLN ARG ALA THR LYS MET LEU          
SEQRES   1 I   37  GLY PRO LEU GLY SER ASN ARG ARG LEU GLN GLN THR GLN          
SEQRES   2 I   37  ALA GLN VAL ASP GLU VAL VAL ASP ILE MET ARG VAL ASN          
SEQRES   3 I   37  VAL ASP LYS VAL LEU GLU ARG ASP GLN LYS LEU                  
SEQRES   1 J   65  GLY SER ALA LEU SER GLU ILE GLU THR ARG HIS SER GLU          
SEQRES   2 J   65  ILE ILE LYS LEU GLU ASN SER ILE ARG GLU LEU HIS ASP          
SEQRES   3 J   65  MET PHE MET ASP MET ALA MET LEU VAL GLU SER GLN GLY          
SEQRES   4 J   65  GLU MET ILE ASP ARG ILE GLU TYR ASN VAL GLU HIS ALA          
SEQRES   5 J   65  VAL ASP TYR VAL GLU ARG ALA VAL SER ASP THR LYS LYS          
SEQRES   1 K   81  GLY SER HIS MET MET ARG ASN GLU LEU GLU GLU MET GLN          
SEQRES   2 K   81  ARG ARG ALA ASP GLN LEU ALA ASP GLU SER LEU GLU SER          
SEQRES   3 K   81  THR ARG ARG MET LEU GLN LEU VAL GLU GLU SER LYS ASP          
SEQRES   4 K   81  ALA GLY ILE ARG THR LEU VAL MET LEU ASP GLU GLN GLY          
SEQRES   5 K   81  GLU GLN LEU ASP ARG VAL GLU GLU GLY MET ASN HIS ILE          
SEQRES   6 K   81  ASN GLN ASP MET LYS GLU ALA GLU LYS ASN LEU LYS ASP          
SEQRES   7 K   81  LEU GLY TRP                                                  
SEQRES   1 L   65  GLY SER ALA ARG GLU ASN GLU MET ASP GLU ASN LEU GLU          
SEQRES   2 L   65  GLN VAL SER GLY ILE ILE GLY ASN LEU ARG HIS MET ALA          
SEQRES   3 L   65  LEU ASP MET GLY ASN GLU ILE ASP THR GLN ASN ARG GLN          
SEQRES   4 L   65  ILE ASP ARG ILE MET GLU LYS ALA ASP SER ASN LYS THR          
SEQRES   5 L   65  ARG ILE ASP GLU ALA ASN GLN ARG ALA THR LYS MET LEU          
SEQRES   1 M   37  GLY PRO LEU GLY SER ASN ARG ARG LEU GLN GLN THR GLN          
SEQRES   2 M   37  ALA GLN VAL ASP GLU VAL VAL ASP ILE MET ARG VAL ASN          
SEQRES   3 M   37  VAL ASP LYS VAL LEU GLU ARG ASP GLN LYS LEU                  
SEQRES   1 N   65  GLY SER ALA LEU SER GLU ILE GLU THR ARG HIS SER GLU          
SEQRES   2 N   65  ILE ILE LYS LEU GLU ASN SER ILE ARG GLU LEU HIS ASP          
SEQRES   3 N   65  MET PHE MET ASP MET ALA MET LEU VAL GLU SER GLN GLY          
SEQRES   4 N   65  GLU MET ILE ASP ARG ILE GLU TYR ASN VAL GLU HIS ALA          
SEQRES   5 N   65  VAL ASP TYR VAL GLU ARG ALA VAL SER ASP THR LYS LYS          
SEQRES   1 O   81  GLY SER HIS MET MET ARG ASN GLU LEU GLU GLU MET GLN          
SEQRES   2 O   81  ARG ARG ALA ASP GLN LEU ALA ASP GLU SER LEU GLU SER          
SEQRES   3 O   81  THR ARG ARG MET LEU GLN LEU VAL GLU GLU SER LYS ASP          
SEQRES   4 O   81  ALA GLY ILE ARG THR LEU VAL MET LEU ASP GLU GLN GLY          
SEQRES   5 O   81  GLU GLN LEU ASP ARG VAL GLU GLU GLY MET ASN HIS ILE          
SEQRES   6 O   81  ASN GLN ASP MET LYS GLU ALA GLU LYS ASN LEU LYS ASP          
SEQRES   7 O   81  LEU GLY TRP                                                  
SEQRES   1 P   65  GLY SER ALA ARG GLU ASN GLU MET ASP GLU ASN LEU GLU          
SEQRES   2 P   65  GLN VAL SER GLY ILE ILE GLY ASN LEU ARG HIS MET ALA          
SEQRES   3 P   65  LEU ASP MET GLY ASN GLU ILE ASP THR GLN ASN ARG GLN          
SEQRES   4 P   65  ILE ASP ARG ILE MET GLU LYS ALA ASP SER ASN LYS THR          
SEQRES   5 P   65  ARG ILE ASP GLU ALA ASN GLN ARG ALA THR LYS MET LEU          
SEQRES   1 Q   37  GLY PRO LEU GLY SER ASN ARG ARG LEU GLN GLN THR GLN          
SEQRES   2 Q   37  ALA GLN VAL ASP GLU VAL VAL ASP ILE MET ARG VAL ASN          
SEQRES   3 Q   37  VAL ASP LYS VAL LEU GLU ARG ASP GLN LYS LEU                  
SEQRES   1 R   65  GLY SER ALA LEU SER GLU ILE GLU THR ARG HIS SER GLU          
SEQRES   2 R   65  ILE ILE LYS LEU GLU ASN SER ILE ARG GLU LEU HIS ASP          
SEQRES   3 R   65  MET PHE MET ASP MET ALA MET LEU VAL GLU SER GLN GLY          
SEQRES   4 R   65  GLU MET ILE ASP ARG ILE GLU TYR ASN VAL GLU HIS ALA          
SEQRES   5 R   65  VAL ASP TYR VAL GLU ARG ALA VAL SER ASP THR LYS LYS          
SEQRES   1 S   81  GLY SER HIS MET MET ARG ASN GLU LEU GLU GLU MET GLN          
SEQRES   2 S   81  ARG ARG ALA ASP GLN LEU ALA ASP GLU SER LEU GLU SER          
SEQRES   3 S   81  THR ARG ARG MET LEU GLN LEU VAL GLU GLU SER LYS ASP          
SEQRES   4 S   81  ALA GLY ILE ARG THR LEU VAL MET LEU ASP GLU GLN GLY          
SEQRES   5 S   81  GLU GLN LEU ASP ARG VAL GLU GLU GLY MET ASN HIS ILE          
SEQRES   6 S   81  ASN GLN ASP MET LYS GLU ALA GLU LYS ASN LEU LYS ASP          
SEQRES   7 S   81  LEU GLY TRP                                                  
SEQRES   1 T   65  GLY SER ALA ARG GLU ASN GLU MET ASP GLU ASN LEU GLU          
SEQRES   2 T   65  GLN VAL SER GLY ILE ILE GLY ASN LEU ARG HIS MET ALA          
SEQRES   3 T   65  LEU ASP MET GLY ASN GLU ILE ASP THR GLN ASN ARG GLN          
SEQRES   4 T   65  ILE ASP ARG ILE MET GLU LYS ALA ASP SER ASN LYS THR          
SEQRES   5 T   65  ARG ILE ASP GLU ALA ASN GLN ARG ALA THR LYS MET LEU          
SEQRES   1 U   37  GLY PRO LEU GLY SER ASN ARG ARG LEU GLN GLN THR GLN          
SEQRES   2 U   37  ALA GLN VAL ASP GLU VAL VAL ASP ILE MET ARG VAL ASN          
SEQRES   3 U   37  VAL ASP LYS VAL LEU GLU ARG ASP GLN LYS LEU                  
SEQRES   1 V   65  GLY SER ALA LEU SER GLU ILE GLU THR ARG HIS SER GLU          
SEQRES   2 V   65  ILE ILE LYS LEU GLU ASN SER ILE ARG GLU LEU HIS ASP          
SEQRES   3 V   65  MET PHE MET ASP MET ALA MET LEU VAL GLU SER GLN GLY          
SEQRES   4 V   65  GLU MET ILE ASP ARG ILE GLU TYR ASN VAL GLU HIS ALA          
SEQRES   5 V   65  VAL ASP TYR VAL GLU ARG ALA VAL SER ASP THR LYS LYS          
SEQRES   1 W   81  GLY SER HIS MET MET ARG ASN GLU LEU GLU GLU MET GLN          
SEQRES   2 W   81  ARG ARG ALA ASP GLN LEU ALA ASP GLU SER LEU GLU SER          
SEQRES   3 W   81  THR ARG ARG MET LEU GLN LEU VAL GLU GLU SER LYS ASP          
SEQRES   4 W   81  ALA GLY ILE ARG THR LEU VAL MET LEU ASP GLU GLN GLY          
SEQRES   5 W   81  GLU GLN LEU ASP ARG VAL GLU GLU GLY MET ASN HIS ILE          
SEQRES   6 W   81  ASN GLN ASP MET LYS GLU ALA GLU LYS ASN LEU LYS ASP          
SEQRES   7 W   81  LEU GLY TRP                                                  
SEQRES   1 X   65  GLY SER ALA ARG GLU ASN GLU MET ASP GLU ASN LEU GLU          
SEQRES   2 X   65  GLN VAL SER GLY ILE ILE GLY ASN LEU ARG HIS MET ALA          
SEQRES   3 X   65  LEU ASP MET GLY ASN GLU ILE ASP THR GLN ASN ARG GLN          
SEQRES   4 X   65  ILE ASP ARG ILE MET GLU LYS ALA ASP SER ASN LYS THR          
SEQRES   5 X   65  ARG ILE ASP GLU ALA ASN GLN ARG ALA THR LYS MET LEU          
SEQRES   1 Y   37  GLY PRO LEU GLY SER ASN ARG ARG LEU GLN GLN THR GLN          
SEQRES   2 Y   37  ALA GLN VAL ASP GLU VAL VAL ASP ILE MET ARG VAL ASN          
SEQRES   3 Y   37  VAL ASP LYS VAL LEU GLU ARG ASP GLN LYS LEU                  
SEQRES   1 Z   65  GLY SER ALA LEU SER GLU ILE GLU THR ARG HIS SER GLU          
SEQRES   2 Z   65  ILE ILE LYS LEU GLU ASN SER ILE ARG GLU LEU HIS ASP          
SEQRES   3 Z   65  MET PHE MET ASP MET ALA MET LEU VAL GLU SER GLN GLY          
SEQRES   4 Z   65  GLU MET ILE ASP ARG ILE GLU TYR ASN VAL GLU HIS ALA          
SEQRES   5 Z   65  VAL ASP TYR VAL GLU ARG ALA VAL SER ASP THR LYS LYS          
SEQRES   1 a   81  GLY SER HIS MET MET ARG ASN GLU LEU GLU GLU MET GLN          
SEQRES   2 a   81  ARG ARG ALA ASP GLN LEU ALA ASP GLU SER LEU GLU SER          
SEQRES   3 a   81  THR ARG ARG MET LEU GLN LEU VAL GLU GLU SER LYS ASP          
SEQRES   4 a   81  ALA GLY ILE ARG THR LEU VAL MET LEU ASP GLU GLN GLY          
SEQRES   5 a   81  GLU GLN LEU ASP ARG VAL GLU GLU GLY MET ASN HIS ILE          
SEQRES   6 a   81  ASN GLN ASP MET LYS GLU ALA GLU LYS ASN LEU LYS ASP          
SEQRES   7 a   81  LEU GLY TRP                                                  
SEQRES   1 b   65  GLY SER ALA ARG GLU ASN GLU MET ASP GLU ASN LEU GLU          
SEQRES   2 b   65  GLN VAL SER GLY ILE ILE GLY ASN LEU ARG HIS MET ALA          
SEQRES   3 b   65  LEU ASP MET GLY ASN GLU ILE ASP THR GLN ASN ARG GLN          
SEQRES   4 b   65  ILE ASP ARG ILE MET GLU LYS ALA ASP SER ASN LYS THR          
SEQRES   5 b   65  ARG ILE ASP GLU ALA ASN GLN ARG ALA THR LYS MET LEU          
SEQRES   1 c   37  GLY PRO LEU GLY SER ASN ARG ARG LEU GLN GLN THR GLN          
SEQRES   2 c   37  ALA GLN VAL ASP GLU VAL VAL ASP ILE MET ARG VAL ASN          
SEQRES   3 c   37  VAL ASP LYS VAL LEU GLU ARG ASP GLN LYS LEU                  
SEQRES   1 d   65  GLY SER ALA LEU SER GLU ILE GLU THR ARG HIS SER GLU          
SEQRES   2 d   65  ILE ILE LYS LEU GLU ASN SER ILE ARG GLU LEU HIS ASP          
SEQRES   3 d   65  MET PHE MET ASP MET ALA MET LEU VAL GLU SER GLN GLY          
SEQRES   4 d   65  GLU MET ILE ASP ARG ILE GLU TYR ASN VAL GLU HIS ALA          
SEQRES   5 d   65  VAL ASP TYR VAL GLU ARG ALA VAL SER ASP THR LYS LYS          
SEQRES   1 e   81  GLY SER HIS MET MET ARG ASN GLU LEU GLU GLU MET GLN          
SEQRES   2 e   81  ARG ARG ALA ASP GLN LEU ALA ASP GLU SER LEU GLU SER          
SEQRES   3 e   81  THR ARG ARG MET LEU GLN LEU VAL GLU GLU SER LYS ASP          
SEQRES   4 e   81  ALA GLY ILE ARG THR LEU VAL MET LEU ASP GLU GLN GLY          
SEQRES   5 e   81  GLU GLN LEU ASP ARG VAL GLU GLU GLY MET ASN HIS ILE          
SEQRES   6 e   81  ASN GLN ASP MET LYS GLU ALA GLU LYS ASN LEU LYS ASP          
SEQRES   7 e   81  LEU GLY TRP                                                  
SEQRES   1 f   65  GLY SER ALA ARG GLU ASN GLU MET ASP GLU ASN LEU GLU          
SEQRES   2 f   65  GLN VAL SER GLY ILE ILE GLY ASN LEU ARG HIS MET ALA          
SEQRES   3 f   65  LEU ASP MET GLY ASN GLU ILE ASP THR GLN ASN ARG GLN          
SEQRES   4 f   65  ILE ASP ARG ILE MET GLU LYS ALA ASP SER ASN LYS THR          
SEQRES   5 f   65  ARG ILE ASP GLU ALA ASN GLN ARG ALA THR LYS MET LEU          
SEQRES   1 g   63  GLY PRO LEU GLY SER LYS LEU PRO ASP ALA ALA LYS LYS          
SEQRES   2 g   63  MSE GLU GLU ALA GLN GLU ALA LEU ARG GLN ALA GLU GLU          
SEQRES   3 g   63  GLU ARG LYS ALA LYS TYR ALA LYS MSE GLU ALA GLU ARG          
SEQRES   4 g   63  GLU ALA VAL ARG GLN GLY ILE ARG ASP LYS TYR GLY ILE          
SEQRES   5 g   63  LYS LYS LYS GLU GLU ARG GLU ALA GLU ALA GLN                  
SEQRES   1 h   63  GLY PRO LEU GLY SER LYS LEU PRO ASP ALA ALA LYS LYS          
SEQRES   2 h   63  MSE GLU GLU ALA GLN GLU ALA LEU ARG GLN ALA GLU GLU          
SEQRES   3 h   63  GLU ARG LYS ALA LYS TYR ALA LYS MSE GLU ALA GLU ARG          
SEQRES   4 h   63  GLU ALA VAL ARG GLN GLY ILE ARG ASP LYS TYR GLY ILE          
SEQRES   5 h   63  LYS LYS LYS GLU GLU ARG GLU ALA GLU ALA GLN                  
SEQRES   1 i   63  GLY PRO LEU GLY SER LYS LEU PRO ASP ALA ALA LYS LYS          
SEQRES   2 i   63  MSE GLU GLU ALA GLN GLU ALA LEU ARG GLN ALA GLU GLU          
SEQRES   3 i   63  GLU ARG LYS ALA LYS TYR ALA LYS MSE GLU ALA GLU ARG          
SEQRES   4 i   63  GLU ALA VAL ARG GLN GLY ILE ARG ASP LYS TYR GLY ILE          
SEQRES   5 i   63  LYS LYS LYS GLU GLU ARG GLU ALA GLU ALA GLN                  
SEQRES   1 j   63  GLY PRO LEU GLY SER LYS LEU PRO ASP ALA ALA LYS LYS          
SEQRES   2 j   63  MSE GLU GLU ALA GLN GLU ALA LEU ARG GLN ALA GLU GLU          
SEQRES   3 j   63  GLU ARG LYS ALA LYS TYR ALA LYS MSE GLU ALA GLU ARG          
SEQRES   4 j   63  GLU ALA VAL ARG GLN GLY ILE ARG ASP LYS TYR GLY ILE          
SEQRES   5 j   63  LYS LYS LYS GLU GLU ARG GLU ALA GLU ALA GLN                  
SEQRES   1 k   63  GLY PRO LEU GLY SER LYS LEU PRO ASP ALA ALA LYS LYS          
SEQRES   2 k   63  MSE GLU GLU ALA GLN GLU ALA LEU ARG GLN ALA GLU GLU          
SEQRES   3 k   63  GLU ARG LYS ALA LYS TYR ALA LYS MSE GLU ALA GLU ARG          
SEQRES   4 k   63  GLU ALA VAL ARG GLN GLY ILE ARG ASP LYS TYR GLY ILE          
SEQRES   5 k   63  LYS LYS LYS GLU GLU ARG GLU ALA GLU ALA GLN                  
SEQRES   1 l   63  GLY PRO LEU GLY SER LYS LEU PRO ASP ALA ALA LYS LYS          
SEQRES   2 l   63  MSE GLU GLU ALA GLN GLU ALA LEU ARG GLN ALA GLU GLU          
SEQRES   3 l   63  GLU ARG LYS ALA LYS TYR ALA LYS MSE GLU ALA GLU ARG          
SEQRES   4 l   63  GLU ALA VAL ARG GLN GLY ILE ARG ASP LYS TYR GLY ILE          
SEQRES   5 l   63  LYS LYS LYS GLU GLU ARG GLU ALA GLU ALA GLN                  
SEQRES   1 m   63  GLY PRO LEU GLY SER LYS LEU PRO ASP ALA ALA LYS LYS          
SEQRES   2 m   63  MSE GLU GLU ALA GLN GLU ALA LEU ARG GLN ALA GLU GLU          
SEQRES   3 m   63  GLU ARG LYS ALA LYS TYR ALA LYS MSE GLU ALA GLU ARG          
SEQRES   4 m   63  GLU ALA VAL ARG GLN GLY ILE ARG ASP LYS TYR GLY ILE          
SEQRES   5 m   63  LYS LYS LYS GLU GLU ARG GLU ALA GLU ALA GLN                  
SEQRES   1 n   63  GLY PRO LEU GLY SER LYS LEU PRO ASP ALA ALA LYS LYS          
SEQRES   2 n   63  MSE GLU GLU ALA GLN GLU ALA LEU ARG GLN ALA GLU GLU          
SEQRES   3 n   63  GLU ARG LYS ALA LYS TYR ALA LYS MSE GLU ALA GLU ARG          
SEQRES   4 n   63  GLU ALA VAL ARG GLN GLY ILE ARG ASP LYS TYR GLY ILE          
SEQRES   5 n   63  LYS LYS LYS GLU GLU ARG GLU ALA GLU ALA GLN                  
MODRES 3RL0 MSE g   34  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE g   55  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE h   34  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE h   55  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE i   34  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE i   55  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE j   34  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE j   55  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE k   34  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE k   55  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE l   34  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE l   55  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE m   34  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE m   55  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE n   34  MET  SELENOMETHIONINE                                   
MODRES 3RL0 MSE n   55  MET  SELENOMETHIONINE                                   
HET    MSE  g  34       8                                                       
HET    MSE  g  55       8                                                       
HET    MSE  h  34       8                                                       
HET    MSE  h  55       8                                                       
HET    MSE  i  34       8                                                       
HET    MSE  i  55       8                                                       
HET    MSE  j  34       8                                                       
HET    MSE  j  55       8                                                       
HET    MSE  k  34       8                                                       
HET    MSE  k  55       8                                                       
HET    MSE  l  34       8                                                       
HET    MSE  l  55       8                                                       
HET    MSE  m  34       8                                                       
HET    MSE  m  55       8                                                       
HET    MSE  n  34       8                                                       
HET    MSE  n  55       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL  33  MSE    16(C5 H11 N O2 SE)                                           
HELIX    1   1 LEU A   26  LEU A   60  1                                  35    
HELIX    2   2 ALA B  191  SER B  249  1                                  59    
HELIX    3   3 ARG C    8  LEU C   78  1                                  71    
HELIX    4   4 GLY D  139  THR D  200  1                                  62    
HELIX    5   5 LEU E   26  LEU E   60  1                                  35    
HELIX    6   6 ALA F  191  THR F  251  1                                  61    
HELIX    7   7 ARG G    8  LEU G   78  1                                  71    
HELIX    8   8 GLY H  139  ALA H  199  1                                  61    
HELIX    9   9 GLY I   27  LEU I   60  1                                  34    
HELIX   10  10 SER J  190  VAL J  248  1                                  59    
HELIX   11  11 ASN K    9  LYS K   79  1                                  71    
HELIX   12  12 GLY L  139  MET L  202  1                                  64    
HELIX   13  13 PRO M   25  LEU M   60  1                                  36    
HELIX   14  14 ALA N  191  ALA N  247  1                                  57    
HELIX   15  15 ARG O    8  LYS O   79  1                                  72    
HELIX   16  16 GLY P  139  MET P  202  1                                  64    
HELIX   17  17 LEU Q   26  LEU Q   60  1                                  35    
HELIX   18  18 ALA R  191  THR R  251  1                                  61    
HELIX   19  19 GLU S   10  LEU S   78  1                                  69    
HELIX   20  20 GLY T  139  THR T  200  1                                  62    
HELIX   21  21 LEU U   26  GLN U   58  1                                  33    
HELIX   22  22 ALA V  191  VAL V  248  1                                  58    
HELIX   23  23 ARG W    8  ASN W   77  1                                  70    
HELIX   24  24 GLY X  139  LYS X  201  1                                  63    
HELIX   25  25 LEU Y   26  LEU Y   60  1                                  35    
HELIX   26  26 SER Z  190  ALA Z  247  1                                  58    
HELIX   27  27 GLU a   10  LYS a   79  1                                  70    
HELIX   28  28 GLY b  139  ALA b  199  1                                  61    
HELIX   29  29 GLY c   27  LEU c   60  1                                  34    
HELIX   30  30 SER d  190  VAL d  248  1                                  59    
HELIX   31  31 LEU e   11  LYS e   79  1                                  69    
HELIX   32  32 GLY f  139  THR f  200  1                                  62    
HELIX   33  33 PRO g   28  TYR g   70  1                                  43    
HELIX   34  34 PRO h   28  TYR h   70  1                                  43    
HELIX   35  35 LEU i   27  TYR i   70  1                                  44    
HELIX   36  36 LYS j   26  TYR j   70  1                                  45    
HELIX   37  37 PRO k   28  TYR k   70  1                                  43    
HELIX   38  38 PRO l   28  TYR l   70  1                                  43    
HELIX   39  39 LYS m   26  TYR m   70  1                                  45    
HELIX   40  40 LEU n   27  TYR n   70  1                                  44    
LINK         C   LYS g  33                 N   MSE g  34     1555   1555  1.33  
LINK         C   MSE g  34                 N   GLU g  35     1555   1555  1.33  
LINK         C   LYS g  54                 N   MSE g  55     1555   1555  1.33  
LINK         C   MSE g  55                 N   GLU g  56     1555   1555  1.33  
LINK         C   LYS h  33                 N   MSE h  34     1555   1555  1.32  
LINK         C   MSE h  34                 N   GLU h  35     1555   1555  1.33  
LINK         C   LYS h  54                 N   MSE h  55     1555   1555  1.32  
LINK         C   MSE h  55                 N   GLU h  56     1555   1555  1.33  
LINK         C   LYS i  33                 N   MSE i  34     1555   1555  1.33  
LINK         C   MSE i  34                 N   GLU i  35     1555   1555  1.33  
LINK         C   LYS i  54                 N   MSE i  55     1555   1555  1.33  
LINK         C   MSE i  55                 N   GLU i  56     1555   1555  1.34  
LINK         C   LYS j  33                 N   MSE j  34     1555   1555  1.33  
LINK         C   MSE j  34                 N   GLU j  35     1555   1555  1.33  
LINK         C   LYS j  54                 N   MSE j  55     1555   1555  1.33  
LINK         C   MSE j  55                 N   GLU j  56     1555   1555  1.33  
LINK         C   LYS k  33                 N   MSE k  34     1555   1555  1.33  
LINK         C   MSE k  34                 N   GLU k  35     1555   1555  1.33  
LINK         C   LYS k  54                 N   MSE k  55     1555   1555  1.33  
LINK         C   MSE k  55                 N   GLU k  56     1555   1555  1.33  
LINK         C   LYS l  33                 N   MSE l  34     1555   1555  1.33  
LINK         C   MSE l  34                 N   GLU l  35     1555   1555  1.33  
LINK         C   LYS l  54                 N   MSE l  55     1555   1555  1.33  
LINK         C   MSE l  55                 N   GLU l  56     1555   1555  1.33  
LINK         C   LYS m  33                 N   MSE m  34     1555   1555  1.33  
LINK         C   MSE m  34                 N   GLU m  35     1555   1555  1.33  
LINK         C   LYS m  54                 N   MSE m  55     1555   1555  1.33  
LINK         C   MSE m  55                 N   GLU m  56     1555   1555  1.33  
LINK         C   LYS n  33                 N   MSE n  34     1555   1555  1.33  
LINK         C   MSE n  34                 N   GLU n  35     1555   1555  1.33  
LINK         C   LYS n  54                 N   MSE n  55     1555   1555  1.33  
LINK         C   MSE n  55                 N   GLU n  56     1555   1555  1.33  
CRYST1   53.745  127.357  142.725 107.49  90.01  90.05 P 1           8          
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      0.018606  0.000016  0.000009        0.00000                         
SCALE2      0.000000  0.007852  0.002474        0.00000                         
SCALE3      0.000000  0.000000  0.007346        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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