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Database: PDB
Entry: 2QC8
LinkDB: 2QC8
Original site: 2QC8 
HEADER    LIGASE                                  19-JUN-07   2QC8              
TITLE     CRYSTAL STRUCTURE OF HUMAN GLUTAMINE SYNTHETASE IN COMPLEX WITH ADP   
TITLE    2 AND METHIONINE SULFOXIMINE PHOSPHATE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMINE SYNTHETASE;                                      
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 SYNONYM: GLUTAMATE-AMMONIA LIGASE, GS;                               
COMPND   5 EC: 6.3.1.2;                                                         
COMPND   6 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: GLUL, GLNS;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)GOLD PRARE2;                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4                                 
KEYWDS    AMINO-ACID BIOSYNTHESIS, LIGASE, SYNTHETASE, STRUCTURAL GENOMICS,     
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.KARLBERG,L.LEHTIO,C.H.ARROWSMITH,H.BERGLUND,R.D.BUSAM,R.COLLINS,    
AUTHOR   2 L.G.DAHLGREN,A.EDWARDS,S.FLODIN,A.FLORES,S.GRASLUND,M.HAMMARSTROM,   
AUTHOR   3 M.HOGBOM,I.JOHANSSON,A.KALLAS,T.KOTENYOVA,M.MOCHE,P.NORDLUND,        
AUTHOR   4 T.NYMAN,C.PERSSON,J.SAGEMARK,M.SUNDSTROM,A.G.THORSELL,S.VAN DEN      
AUTHOR   5 BERG,J.WEIGELT,L.HOLMBERG-SCHIAVONE,STRUCTURAL GENOMICS CONSORTIUM   
AUTHOR   6 (SGC)                                                                
REVDAT   5   13-JUL-11 2QC8    1       VERSN                                    
REVDAT   4   24-FEB-09 2QC8    1       VERSN                                    
REVDAT   3   18-DEC-07 2QC8    1       JRNL                                     
REVDAT   2   27-NOV-07 2QC8    1       JRNL                                     
REVDAT   1   03-JUL-07 2QC8    0                                                
JRNL        AUTH   W.W.KRAJEWSKI,R.COLLINS,L.HOLMBERG-SCHIAVONE,T.A.JONES,      
JRNL        AUTH 2 T.KARLBERG,S.L.MOWBRAY                                       
JRNL        TITL   CRYSTAL STRUCTURES OF MAMMALIAN GLUTAMINE SYNTHETASES        
JRNL        TITL 2 ILLUSTRATE SUBSTRATE-INDUCED CONFORMATIONAL CHANGES AND      
JRNL        TITL 3 PROVIDE OPPORTUNITIES FOR DRUG AND HERBICIDE DESIGN.         
JRNL        REF    J.MOL.BIOL.                   V. 375   217 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18005987                                                     
JRNL        DOI    10.1016/J.JMB.2007.10.029                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0032                                      
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 123433                         
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) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6497                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9094                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 479                          
REMARK   3   BIN FREE R VALUE                    : 0.3000                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 28146                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 460                                     
REMARK   3   SOLVENT ATOMS            : 231                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.827         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.277         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.187         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.298        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 29330 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 20417 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 39745 ; 1.592 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 49193 ; 0.943 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3549 ;11.089 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1440 ;37.616 ;23.403       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4740 ;14.998 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   240 ;16.467 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4020 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 32893 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  6259 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  6220 ; 0.213 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 21699 ; 0.202 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 14173 ; 0.186 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A): 15102 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   874 ; 0.141 ; 0.200       
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):    32 ; 0.438 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    42 ; 0.293 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.087 ; 0.200       
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): 22600 ; 0.720 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  7237 ; 0.133 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 28445 ; 0.893 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13824 ; 1.491 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11300 ; 2.178 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G H I J             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 6                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     10       A      54      3                      
REMARK   3           1     B     10       B      54      3                      
REMARK   3           1     C     10       C      54      3                      
REMARK   3           1     D     10       D      54      3                      
REMARK   3           1     E     10       E      54      3                      
REMARK   3           1     F     10       F      54      3                      
REMARK   3           1     G     10       G      54      3                      
REMARK   3           1     H     10       H      54      3                      
REMARK   3           1     I     10       I      54      3                      
REMARK   3           1     J     10       J      54      3                      
REMARK   3           2     A     56       A     106      3                      
REMARK   3           2     B     56       B     106      3                      
REMARK   3           2     C     56       C     106      3                      
REMARK   3           2     D     56       D     106      3                      
REMARK   3           2     E     56       E     106      3                      
REMARK   3           2     F     56       F     106      3                      
REMARK   3           2     G     56       G     106      3                      
REMARK   3           2     H     56       H     106      3                      
REMARK   3           2     I     56       I     106      3                      
REMARK   3           2     J     56       J     106      3                      
REMARK   3           3     A    108       A     122      3                      
REMARK   3           3     B    108       B     122      3                      
REMARK   3           3     C    108       C     122      3                      
REMARK   3           3     D    108       D     122      3                      
REMARK   3           3     E    108       E     122      3                      
REMARK   3           3     F    108       F     122      3                      
REMARK   3           3     G    108       G     122      3                      
REMARK   3           3     H    108       H     122      3                      
REMARK   3           3     I    108       I     122      3                      
REMARK   3           3     J    108       J     122      3                      
REMARK   3           4     A    124       A     281      3                      
REMARK   3           4     B    124       B     281      3                      
REMARK   3           4     C    124       C     281      3                      
REMARK   3           4     D    124       D     281      3                      
REMARK   3           4     E    124       E     281      3                      
REMARK   3           4     F    124       F     281      3                      
REMARK   3           4     G    124       G     281      3                      
REMARK   3           4     H    124       H     281      3                      
REMARK   3           4     I    124       I     281      3                      
REMARK   3           4     J    124       J     281      3                      
REMARK   3           5     A    283       A     310      3                      
REMARK   3           5     B    283       B     310      3                      
REMARK   3           5     C    283       C     310      3                      
REMARK   3           5     D    283       D     310      3                      
REMARK   3           5     E    283       E     310      3                      
REMARK   3           5     F    283       F     310      3                      
REMARK   3           5     G    283       G     310      3                      
REMARK   3           5     H    283       H     310      3                      
REMARK   3           5     I    283       I     310      3                      
REMARK   3           5     J    283       J     310      3                      
REMARK   3           6     A    312       A     365      4                      
REMARK   3           6     B    312       B     365      4                      
REMARK   3           6     C    312       C     365      4                      
REMARK   3           6     D    312       D     365      4                      
REMARK   3           6     E    312       E     364      4                      
REMARK   3           6     F    312       F     365      4                      
REMARK   3           6     G    312       G     365      4                      
REMARK   3           6     H    312       H     365      4                      
REMARK   3           6     I    312       I     365      4                      
REMARK   3           6     J    312       J     365      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1732 ;  0.13 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1732 ;  0.13 ;  0.00           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   1732 ;  0.11 ;  0.00           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   1732 ;  0.12 ;  0.00           
REMARK   3   TIGHT POSITIONAL   1    E    (A):   1732 ;  0.12 ;  0.00           
REMARK   3   TIGHT POSITIONAL   1    F    (A):   1732 ;  0.12 ;  0.00           
REMARK   3   TIGHT POSITIONAL   1    G    (A):   1732 ;  0.12 ;  0.00           
REMARK   3   TIGHT POSITIONAL   1    H    (A):   1732 ;  0.12 ;  0.00           
REMARK   3   TIGHT POSITIONAL   1    I    (A):   1732 ;  0.12 ;  0.00           
REMARK   3   TIGHT POSITIONAL   1    J    (A):   1732 ;  0.12 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    713 ;  0.16 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    713 ;  0.18 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    713 ;  0.15 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):    713 ;  0.14 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):    713 ;  0.14 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):    713 ;  0.15 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    G    (A):    713 ;  0.17 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    H    (A):    713 ;  0.17 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    I    (A):    713 ;  0.14 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    J    (A):    713 ;  0.15 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   2309 ;  0.19 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   2309 ;  0.24 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):   2309 ;  0.18 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   2309 ;  0.18 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    E    (A):   2309 ;  0.19 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    F    (A):   2309 ;  0.20 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    G    (A):   2309 ;  0.19 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    H    (A):   2309 ;  0.18 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    I    (A):   2309 ;  0.24 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    J    (A):   2309 ;  0.21 ;  0.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1732 ;  0.42 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1732 ;  0.47 ;  0.00           
REMARK   3   TIGHT THERMAL      1    C (A**2):   1732 ;  0.48 ;  0.00           
REMARK   3   TIGHT THERMAL      1    D (A**2):   1732 ;  0.42 ;  0.00           
REMARK   3   TIGHT THERMAL      1    E (A**2):   1732 ;  0.42 ;  0.00           
REMARK   3   TIGHT THERMAL      1    F (A**2):   1732 ;  0.33 ;  0.00           
REMARK   3   TIGHT THERMAL      1    G (A**2):   1732 ;  0.31 ;  0.00           
REMARK   3   TIGHT THERMAL      1    H (A**2):   1732 ;  0.35 ;  0.00           
REMARK   3   TIGHT THERMAL      1    I (A**2):   1732 ;  0.35 ;  0.00           
REMARK   3   TIGHT THERMAL      1    J (A**2):   1732 ;  0.30 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    713 ;  0.46 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    713 ;  0.53 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    713 ;  0.55 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):    713 ;  0.48 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    E (A**2):    713 ;  0.48 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    F (A**2):    713 ;  0.31 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    G (A**2):    713 ;  0.34 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    H (A**2):    713 ;  0.35 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    I (A**2):    713 ;  0.35 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    J (A**2):    713 ;  0.40 ;  0.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   2309 ;  0.59 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   2309 ;  0.65 ;  0.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):   2309 ;  0.68 ;  0.00           
REMARK   3   LOOSE THERMAL      1    D (A**2):   2309 ;  0.61 ;  0.00           
REMARK   3   LOOSE THERMAL      1    E (A**2):   2309 ;  0.62 ;  0.00           
REMARK   3   LOOSE THERMAL      1    F (A**2):   2309 ;  0.47 ;  0.00           
REMARK   3   LOOSE THERMAL      1    G (A**2):   2309 ;  0.46 ;  0.00           
REMARK   3   LOOSE THERMAL      1    H (A**2):   2309 ;  0.48 ;  0.00           
REMARK   3   LOOSE THERMAL      1    I (A**2):   2309 ;  0.48 ;  0.00           
REMARK   3   LOOSE THERMAL      1    J (A**2):   2309 ;  0.47 ;  0.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A   365                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.7550  33.9080 -23.5870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1653 T22:  -0.0739                                     
REMARK   3      T33:   0.0341 T12:  -0.0168                                     
REMARK   3      T13:   0.0164 T23:   0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9585 L22:   0.3036                                     
REMARK   3      L33:   0.2482 L12:  -0.0431                                     
REMARK   3      L13:   0.2733 L23:  -0.0974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0257 S12:   0.0644 S13:   0.2027                       
REMARK   3      S21:  -0.0290 S22:   0.0195 S23:   0.0432                       
REMARK   3      S31:  -0.0410 S32:   0.0020 S33:   0.0061                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    10        B   365                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.3790   9.7490 -15.8070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2440 T22:  -0.0331                                     
REMARK   3      T33:  -0.0815 T12:  -0.0180                                     
REMARK   3      T13:   0.0048 T23:   0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5004 L22:   0.7758                                     
REMARK   3      L33:   0.0369 L12:   0.1297                                     
REMARK   3      L13:   0.1294 L23:  -0.0167                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0170 S12:   0.0457 S13:  -0.0020                       
REMARK   3      S21:  -0.0239 S22:  -0.0260 S23:   0.0394                       
REMARK   3      S31:   0.0199 S32:  -0.0287 S33:   0.0090                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    10        C   365                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.0660 -27.3920 -19.1160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2313 T22:  -0.0844                                     
REMARK   3      T33:  -0.0434 T12:   0.0065                                     
REMARK   3      T13:   0.0175 T23:   0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8924 L22:   0.3287                                     
REMARK   3      L33:   0.1064 L12:   0.1045                                     
REMARK   3      L13:   0.0974 L23:  -0.0228                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0173 S12:   0.0641 S13:  -0.0864                       
REMARK   3      S21:  -0.0244 S22:   0.0305 S23:  -0.0077                       
REMARK   3      S31:  -0.0351 S32:  -0.0084 S33:  -0.0132                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    10        D   365                          
REMARK   3    ORIGIN FOR THE GROUP (A): -69.1440 -26.4380 -29.1350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2306 T22:  -0.0413                                     
REMARK   3      T33:  -0.0338 T12:  -0.0215                                     
REMARK   3      T13:   0.0105 T23:  -0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6912 L22:   0.7057                                     
REMARK   3      L33:   0.0376 L12:  -0.2140                                     
REMARK   3      L13:   0.0776 L23:  -0.1192                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0075 S12:   0.0872 S13:  -0.0726                       
REMARK   3      S21:  -0.0776 S22:   0.0203 S23:   0.0347                       
REMARK   3      S31:  -0.0265 S32:   0.0052 S33:  -0.0278                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    10        E   364                          
REMARK   3    ORIGIN FOR THE GROUP (A): -80.1740  11.2260 -31.7250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2145 T22:  -0.0313                                     
REMARK   3      T33:  -0.0161 T12:   0.0291                                     
REMARK   3      T13:  -0.0063 T23:   0.0307                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8690 L22:   0.7916                                     
REMARK   3      L33:   0.0479 L12:   0.2816                                     
REMARK   3      L13:   0.0847 L23:   0.1296                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0180 S12:   0.0447 S13:   0.0973                       
REMARK   3      S21:  -0.0893 S22:   0.0127 S23:   0.0827                       
REMARK   3      S31:  -0.0156 S32:   0.0466 S33:   0.0053                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    10        F   365                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.0870  33.8920 -69.3090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1010 T22:   0.1993                                     
REMARK   3      T33:   0.0965 T12:  -0.0653                                     
REMARK   3      T13:   0.0042 T23:   0.1728                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1111 L22:   0.5265                                     
REMARK   3      L33:   0.6060 L12:   0.0073                                     
REMARK   3      L13:   0.2731 L23:  -0.2223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0675 S12:   0.2535 S13:   0.2940                       
REMARK   3      S21:  -0.0712 S22:  -0.0002 S23:  -0.1398                       
REMARK   3      S31:  -0.2707 S32:   0.0446 S33:   0.0676                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G    10        G   365                          
REMARK   3    ORIGIN FOR THE GROUP (A): -67.1260  14.1350 -78.0100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0136 T22:   0.4316                                     
REMARK   3      T33:   0.0212 T12:  -0.0172                                     
REMARK   3      T13:  -0.0566 T23:   0.1059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4974 L22:   1.0235                                     
REMARK   3      L33:   0.3643 L12:   0.0339                                     
REMARK   3      L13:  -0.0762 L23:  -0.1036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0143 S12:   0.2870 S13:   0.1104                       
REMARK   3      S21:  -0.1604 S22:   0.0163 S23:   0.1790                       
REMARK   3      S31:  -0.0106 S32:  -0.2341 S33:  -0.0306                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    10        H   365                          
REMARK   3    ORIGIN FOR THE GROUP (A): -59.0750 -24.5600 -76.1320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0980 T22:   0.3118                                     
REMARK   3      T33:   0.0359 T12:  -0.1232                                     
REMARK   3      T13:   0.0328 T23:  -0.1230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9860 L22:   0.7083                                     
REMARK   3      L33:   0.4044 L12:  -0.2243                                     
REMARK   3      L13:   0.0219 L23:  -0.1679                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0971 S12:   0.3292 S13:  -0.1996                       
REMARK   3      S21:  -0.1889 S22:   0.0811 S23:   0.1504                       
REMARK   3      S31:   0.1821 S32:  -0.1158 S33:   0.0160                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I    10        I   365                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1900 -28.6670 -66.0770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0232 T22:   0.2653                                     
REMARK   3      T33:   0.1457 T12:   0.0717                                     
REMARK   3      T13:   0.1654 T23:  -0.0415                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8991 L22:   0.8823                                     
REMARK   3      L33:   0.4542 L12:   0.4373                                     
REMARK   3      L13:  -0.0439 L23:   0.0347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0867 S12:   0.1315 S13:  -0.2759                       
REMARK   3      S21:  -0.2134 S22:  -0.0200 S23:  -0.2612                       
REMARK   3      S31:   0.1689 S32:   0.1802 S33:   0.1068                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J    10        J   365                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5720   7.4120 -62.0030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0989 T22:   0.3741                                     
REMARK   3      T33:   0.1743 T12:  -0.0835                                     
REMARK   3      T13:   0.0791 T23:   0.1256                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6677 L22:   1.2717                                     
REMARK   3      L33:   0.4455 L12:  -0.1474                                     
REMARK   3      L13:   0.0336 L23:  -0.2846                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0058 S12:   0.1969 S13:   0.0752                       
REMARK   3      S21:  -0.0911 S22:  -0.1245 S23:  -0.3904                       
REMARK   3      S31:  -0.0739 S32:   0.2708 S33:   0.1304                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2QC8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043416.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00595                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 129787                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : 0.09200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.32400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2OJW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1M SODIUM MALONATE, 0.5% JEFFAMINE     
REMARK 280  ED-2001, 0.1M HEPES, PH 7.0, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 298K, PH 7.00                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       90.60500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.04000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       90.60500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       63.04000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     VAL A    -8                                                      
REMARK 465     ASP A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     THR A    -4                                                      
REMARK 465     GLU A    -3                                                      
REMARK 465     ASN A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     TYR A     0                                                      
REMARK 465     PHE A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     MET B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     VAL B    -8                                                      
REMARK 465     ASP B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     THR B    -4                                                      
REMARK 465     GLU B    -3                                                      
REMARK 465     ASN B    -2                                                      
REMARK 465     LEU B    -1                                                      
REMARK 465     TYR B     0                                                      
REMARK 465     PHE B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     MET C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     SER C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     GLY C    -9                                                      
REMARK 465     VAL C    -8                                                      
REMARK 465     ASP C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     GLY C    -5                                                      
REMARK 465     THR C    -4                                                      
REMARK 465     GLU C    -3                                                      
REMARK 465     ASN C    -2                                                      
REMARK 465     LEU C    -1                                                      
REMARK 465     TYR C     0                                                      
REMARK 465     PHE C     1                                                      
REMARK 465     GLN C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     MET C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     SER C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     LEU C     9                                                      
REMARK 465     MET D   -18                                                      
REMARK 465     HIS D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     SER D   -11                                                      
REMARK 465     SER D   -10                                                      
REMARK 465     GLY D    -9                                                      
REMARK 465     VAL D    -8                                                      
REMARK 465     ASP D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     GLY D    -5                                                      
REMARK 465     THR D    -4                                                      
REMARK 465     GLU D    -3                                                      
REMARK 465     ASN D    -2                                                      
REMARK 465     LEU D    -1                                                      
REMARK 465     TYR D     0                                                      
REMARK 465     PHE D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     MET D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     SER D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 465     LEU D     9                                                      
REMARK 465     MET E   -18                                                      
REMARK 465     HIS E   -17                                                      
REMARK 465     HIS E   -16                                                      
REMARK 465     HIS E   -15                                                      
REMARK 465     HIS E   -14                                                      
REMARK 465     HIS E   -13                                                      
REMARK 465     HIS E   -12                                                      
REMARK 465     SER E   -11                                                      
REMARK 465     SER E   -10                                                      
REMARK 465     GLY E    -9                                                      
REMARK 465     VAL E    -8                                                      
REMARK 465     ASP E    -7                                                      
REMARK 465     LEU E    -6                                                      
REMARK 465     GLY E    -5                                                      
REMARK 465     THR E    -4                                                      
REMARK 465     GLU E    -3                                                      
REMARK 465     ASN E    -2                                                      
REMARK 465     LEU E    -1                                                      
REMARK 465     TYR E     0                                                      
REMARK 465     PHE E     1                                                      
REMARK 465     GLN E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     MET E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     SER E     6                                                      
REMARK 465     SER E     7                                                      
REMARK 465     HIS E     8                                                      
REMARK 465     LEU E     9                                                      
REMARK 465     GLY E   365                                                      
REMARK 465     MET F   -18                                                      
REMARK 465     HIS F   -17                                                      
REMARK 465     HIS F   -16                                                      
REMARK 465     HIS F   -15                                                      
REMARK 465     HIS F   -14                                                      
REMARK 465     HIS F   -13                                                      
REMARK 465     HIS F   -12                                                      
REMARK 465     SER F   -11                                                      
REMARK 465     SER F   -10                                                      
REMARK 465     GLY F    -9                                                      
REMARK 465     VAL F    -8                                                      
REMARK 465     ASP F    -7                                                      
REMARK 465     LEU F    -6                                                      
REMARK 465     GLY F    -5                                                      
REMARK 465     THR F    -4                                                      
REMARK 465     GLU F    -3                                                      
REMARK 465     ASN F    -2                                                      
REMARK 465     LEU F    -1                                                      
REMARK 465     TYR F     0                                                      
REMARK 465     PHE F     1                                                      
REMARK 465     GLN F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     MET F     4                                                      
REMARK 465     ALA F     5                                                      
REMARK 465     SER F     6                                                      
REMARK 465     SER F     7                                                      
REMARK 465     HIS F     8                                                      
REMARK 465     LEU F     9                                                      
REMARK 465     MET G   -18                                                      
REMARK 465     HIS G   -17                                                      
REMARK 465     HIS G   -16                                                      
REMARK 465     HIS G   -15                                                      
REMARK 465     HIS G   -14                                                      
REMARK 465     HIS G   -13                                                      
REMARK 465     HIS G   -12                                                      
REMARK 465     SER G   -11                                                      
REMARK 465     SER G   -10                                                      
REMARK 465     GLY G    -9                                                      
REMARK 465     VAL G    -8                                                      
REMARK 465     ASP G    -7                                                      
REMARK 465     LEU G    -6                                                      
REMARK 465     GLY G    -5                                                      
REMARK 465     THR G    -4                                                      
REMARK 465     GLU G    -3                                                      
REMARK 465     ASN G    -2                                                      
REMARK 465     LEU G    -1                                                      
REMARK 465     TYR G     0                                                      
REMARK 465     PHE G     1                                                      
REMARK 465     GLN G     2                                                      
REMARK 465     SER G     3                                                      
REMARK 465     MET G     4                                                      
REMARK 465     ALA G     5                                                      
REMARK 465     SER G     6                                                      
REMARK 465     SER G     7                                                      
REMARK 465     HIS G     8                                                      
REMARK 465     LEU G     9                                                      
REMARK 465     MET H   -18                                                      
REMARK 465     HIS H   -17                                                      
REMARK 465     HIS H   -16                                                      
REMARK 465     HIS H   -15                                                      
REMARK 465     HIS H   -14                                                      
REMARK 465     HIS H   -13                                                      
REMARK 465     HIS H   -12                                                      
REMARK 465     SER H   -11                                                      
REMARK 465     SER H   -10                                                      
REMARK 465     GLY H    -9                                                      
REMARK 465     VAL H    -8                                                      
REMARK 465     ASP H    -7                                                      
REMARK 465     LEU H    -6                                                      
REMARK 465     GLY H    -5                                                      
REMARK 465     THR H    -4                                                      
REMARK 465     GLU H    -3                                                      
REMARK 465     ASN H    -2                                                      
REMARK 465     LEU H    -1                                                      
REMARK 465     TYR H     0                                                      
REMARK 465     PHE H     1                                                      
REMARK 465     GLN H     2                                                      
REMARK 465     SER H     3                                                      
REMARK 465     MET H     4                                                      
REMARK 465     ALA H     5                                                      
REMARK 465     SER H     6                                                      
REMARK 465     SER H     7                                                      
REMARK 465     HIS H     8                                                      
REMARK 465     LEU H     9                                                      
REMARK 465     MET I   -18                                                      
REMARK 465     HIS I   -17                                                      
REMARK 465     HIS I   -16                                                      
REMARK 465     HIS I   -15                                                      
REMARK 465     HIS I   -14                                                      
REMARK 465     HIS I   -13                                                      
REMARK 465     HIS I   -12                                                      
REMARK 465     SER I   -11                                                      
REMARK 465     SER I   -10                                                      
REMARK 465     GLY I    -9                                                      
REMARK 465     VAL I    -8                                                      
REMARK 465     ASP I    -7                                                      
REMARK 465     LEU I    -6                                                      
REMARK 465     GLY I    -5                                                      
REMARK 465     THR I    -4                                                      
REMARK 465     GLU I    -3                                                      
REMARK 465     ASN I    -2                                                      
REMARK 465     LEU I    -1                                                      
REMARK 465     TYR I     0                                                      
REMARK 465     PHE I     1                                                      
REMARK 465     GLN I     2                                                      
REMARK 465     SER I     3                                                      
REMARK 465     MET I     4                                                      
REMARK 465     ALA I     5                                                      
REMARK 465     SER I     6                                                      
REMARK 465     SER I     7                                                      
REMARK 465     HIS I     8                                                      
REMARK 465     LEU I     9                                                      
REMARK 465     MET J   -18                                                      
REMARK 465     HIS J   -17                                                      
REMARK 465     HIS J   -16                                                      
REMARK 465     HIS J   -15                                                      
REMARK 465     HIS J   -14                                                      
REMARK 465     HIS J   -13                                                      
REMARK 465     HIS J   -12                                                      
REMARK 465     SER J   -11                                                      
REMARK 465     SER J   -10                                                      
REMARK 465     GLY J    -9                                                      
REMARK 465     VAL J    -8                                                      
REMARK 465     ASP J    -7                                                      
REMARK 465     LEU J    -6                                                      
REMARK 465     GLY J    -5                                                      
REMARK 465     THR J    -4                                                      
REMARK 465     GLU J    -3                                                      
REMARK 465     ASN J    -2                                                      
REMARK 465     LEU J    -1                                                      
REMARK 465     TYR J     0                                                      
REMARK 465     PHE J     1                                                      
REMARK 465     GLN J     2                                                      
REMARK 465     SER J     3                                                      
REMARK 465     MET J     4                                                      
REMARK 465     ALA J     5                                                      
REMARK 465     SER J     6                                                      
REMARK 465     SER J     7                                                      
REMARK 465     HIS J     8                                                      
REMARK 465     LEU J     9                                                      
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     GLU A  24    CD   OE1  OE2                                       
REMARK 470     GLU B  24    CD   OE1  OE2                                       
REMARK 470     GLU C  24    CD   OE1  OE2                                       
REMARK 470     GLU D  24    CD   OE1  OE2                                       
REMARK 470     GLU E  24    CD   OE1  OE2                                       
REMARK 470     GLU F  24    CD   OE1  OE2                                       
REMARK 470     GLU G  24    CD   OE1  OE2                                       
REMARK 470     GLU H  24    CD   OE1  OE2                                       
REMARK 470     GLU I  24    CD   OE1  OE2                                       
REMARK 470     GLU J  24    CD   OE1  OE2                                       
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   NZ   LYS B    91     O    HOH B   739              1.69            
REMARK 500   OD1  ASP H    92     O    HOH H   604              1.81            
REMARK 500   SG   CYS C    53     OE2  GLU C    56              1.92            
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   SG   CYS A    53     OE2  GLU C    56     4455     2.05            
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    CYS C 209   CB    CYS C 209   SG     -0.096                       
REMARK 500    CYS D 209   CB    CYS D 209   SG     -0.096                       
REMARK 500    CYS E 209   CB    CYS E 209   SG     -0.111                       
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 B 299   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG C 299   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG C 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG D  41   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP D 122   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG E  41   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP E 295   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG E 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG J 299   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 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    LYS A  91      170.43     70.03                                   
REMARK 500    ARG A 169      -21.30   -146.39                                   
REMARK 500    ALA B  82      -51.20   -121.18                                   
REMARK 500    LYS B  91      165.63     74.43                                   
REMARK 500    ARG B 106        6.85     59.72                                   
REMARK 500    ARG B 169      -29.76   -150.40                                   
REMARK 500    ALA B 200       -2.21     79.76                                   
REMARK 500    TRP C  60     -158.43   -141.37                                   
REMARK 500    LYS C  91      166.10     71.20                                   
REMARK 500    ARG C 169      -19.10   -148.35                                   
REMARK 500    TRP D  60     -159.70   -150.01                                   
REMARK 500    LYS D  91      172.74     74.77                                   
REMARK 500    HIS D 128       61.57     39.83                                   
REMARK 500    ARG D 169      -24.95   -150.12                                   
REMARK 500    ALA D 200       -1.81     80.09                                   
REMARK 500    ASN E  74       65.19   -150.36                                   
REMARK 500    ALA E  82      -54.06   -122.39                                   
REMARK 500    LYS E  91      174.92     66.85                                   
REMARK 500    ARG E 169      -19.62   -145.83                                   
REMARK 500    LYS F  91      167.40     82.88                                   
REMARK 500    ARG F 169      -37.77   -150.16                                   
REMARK 500    ASN F 246       46.08    -79.42                                   
REMARK 500    TRP G  60     -158.52   -146.56                                   
REMARK 500    ASN G  74       71.25   -158.93                                   
REMARK 500    LYS G  91      161.66     72.43                                   
REMARK 500    THR G 142      -38.94    -30.75                                   
REMARK 500    ARG G 169      -23.75   -150.08                                   
REMARK 500    GLU G 263      170.57    -57.48                                   
REMARK 500    ARG G 280       35.82   -147.51                                   
REMARK 500    TRP H  60     -156.52   -147.36                                   
REMARK 500    LYS H  91      170.98     70.70                                   
REMARK 500    ARG H 106       16.76     56.72                                   
REMARK 500    ASP H 143        4.82    -66.55                                   
REMARK 500    ARG H 169      -19.06   -150.30                                   
REMARK 500    ARG H 280       39.12   -140.14                                   
REMARK 500    ALA I  82      -57.79   -124.92                                   
REMARK 500    LYS I  91      179.65     74.80                                   
REMARK 500    ARG I 169      -23.55   -149.00                                   
REMARK 500    TRP J  60     -159.87   -152.44                                   
REMARK 500    LYS J  91      157.22     72.76                                   
REMARK 500    THR J 142      -31.98    -35.77                                   
REMARK 500    ALA J 200       -2.13     82.46                                   
REMARK 500    ASN J 246       46.77    -83.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS C  91        24.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 134   OE1                                                    
REMARK 620 2 GLU A 203   OE2  90.5                                              
REMARK 620 3 HOH A 729   O   170.4  80.2                                        
REMARK 620 4 ADP A 501   O1B  92.1 173.2  96.8                                  
REMARK 620 5 P3S A 601   O3A  86.2 106.6  98.9  79.8                            
REMARK 620 6 ADP A 501   O2A  83.5  87.5  93.4  86.6 162.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 134   OE1                                                    
REMARK 620 2 GLU A 134   OE2  54.9                                              
REMARK 620 3 GLU A 338   OE2 133.4  80.4                                        
REMARK 620 4 ADP A 501   O3B  85.1  67.5  89.7                                  
REMARK 620 5 P3S A 601   O2A 104.2 157.9 121.5 106.7                            
REMARK 620 6 HIS A 253   ND1  92.0  98.3  81.3 164.5  88.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 136   OE2                                                    
REMARK 620 2 GLU A 196   OE1  83.6                                              
REMARK 620 3 GLU A 203   OE1 113.5  84.5                                        
REMARK 620 4 P3S A 601   O3A 156.5 106.2  89.0                                  
REMARK 620 5 HOH A 704   O    90.5 169.8  90.3  82.4                            
REMARK 620 6 P3S A 601   NE   96.3  86.2 147.4  63.9 102.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 134   OE1                                                    
REMARK 620 2 GLU B 203   OE2  89.7                                              
REMARK 620 3 P3S B 601   O3A  90.2 100.9                                        
REMARK 620 4 ADP B 501   O2A  83.2  89.5 167.7                                  
REMARK 620 5 HOH B 741   O   167.3  79.5  98.1  90.2                            
REMARK 620 6 ADP B 501   O3B  97.9 168.6  87.7  82.9  92.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 134   OE1                                                    
REMARK 620 2 GLU B 134   OE2  58.6                                              
REMARK 620 3 GLU B 338   OE2 146.1  90.9                                        
REMARK 620 4 P3S B 601   O2A  98.8 154.0 113.9                                  
REMARK 620 5 ADP B 501   O2B  94.9  78.2  92.5  92.5                            
REMARK 620 6 HIS B 253   ND1  90.3 102.4  81.7  89.4 174.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 136   OE2                                                    
REMARK 620 2 GLU B 196   OE1  81.2                                              
REMARK 620 3 GLU B 203   OE1 103.2  87.8                                        
REMARK 620 4 P3S B 601   O3A 164.2 106.8  90.9                                  
REMARK 620 5 HOH B 744   O    89.7 169.3  88.7  83.4                            
REMARK 620 6 P3S B 601   NE   99.4  92.1 157.1  67.2  95.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 134   OE1                                                    
REMARK 620 2 GLU C 134   OE2  56.2                                              
REMARK 620 3 GLU C 338   OE2 141.6  85.4                                        
REMARK 620 4 ADP C 501   O2B  81.7  73.6  89.3                                  
REMARK 620 5 P3S C 601   O2A  92.8 147.1 125.0  92.9                            
REMARK 620 6 HIS C 253   ND1  97.6  97.8  85.2 170.2  96.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 134   OE1                                                    
REMARK 620 2 GLU C 203   OE2  87.5                                              
REMARK 620 3 ADP C 501   O3B  89.9 169.3                                        
REMARK 620 4 P3S C 601   O3A  91.0 102.4  88.0                                  
REMARK 620 5 HOH C 738   O   164.5  87.7  92.1 104.5                            
REMARK 620 6 ADP C 501   O2A  79.8  85.2  84.1 167.8  85.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 136   OE2                                                    
REMARK 620 2 GLU C 196   OE1  89.4                                              
REMARK 620 3 GLU C 203   OE1 114.7  87.6                                        
REMARK 620 4 HOH C 740   O    88.5 171.3  85.6                                  
REMARK 620 5 P3S C 601   O3A 153.6 105.0  88.3  80.2                            
REMARK 620 6 P3S C 601   NE   98.2  98.6 146.6  90.0  58.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 134   OE1                                                    
REMARK 620 2 GLU D 134   OE2  55.7                                              
REMARK 620 3 GLU D 338   OE2 153.6  98.8                                        
REMARK 620 4 P3S D 601   O2A  97.9 152.3 108.3                                  
REMARK 620 5 ADP D 501   O2B  94.9  79.8  86.0  96.1                            
REMARK 620 6 HIS D 253   ND1  95.7 101.6  82.0  88.0 168.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 134   OE1                                                    
REMARK 620 2 GLU D 203   OE2  87.2                                              
REMARK 620 3 P3S D 601   O3A  86.9 104.5                                        
REMARK 620 4 ADP D 501   O2A  85.5  85.1 167.5                                  
REMARK 620 5 ADP D 501   O3B  86.6 168.0  85.4  84.2                            
REMARK 620 6 HOH D 747   O   162.8  84.6 109.8  78.7  98.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 136   OE2                                                    
REMARK 620 2 GLU D 196   OE1  82.8                                              
REMARK 620 3 GLU D 203   OE1 106.2  85.6                                        
REMARK 620 4 P3S D 601   O3A 163.2 111.0  85.0                                  
REMARK 620 5 P3S D 601   NE  100.3  98.2 153.5  69.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 134   OE1                                                    
REMARK 620 2 GLU E 134   OE2  55.2                                              
REMARK 620 3 GLU E 338   OE2 143.6  91.4                                        
REMARK 620 4 P3S E 601   O2A  97.5 147.9 118.5                                  
REMARK 620 5 ADP E 501   O2B  84.2  71.1  99.4  91.5                            
REMARK 620 6 HIS E 253   ND1  94.2 100.5  76.6  97.6 170.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 134   OE1                                                    
REMARK 620 2 GLU E 203   OE2  82.0                                              
REMARK 620 3 P3S E 601   O3A  86.3  98.4                                        
REMARK 620 4 ADP E 501   O3B 101.9 170.7  90.3                                  
REMARK 620 5 HOH E 627   O   168.3  89.1 102.6  85.8                            
REMARK 620 6 ADP E 501   O2A  80.1  83.2 166.0  89.1  91.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 136   OE2                                                    
REMARK 620 2 GLU E 196   OE1  94.3                                              
REMARK 620 3 GLU E 203   OE1 110.6  87.8                                        
REMARK 620 4 P3S E 601   O3A 153.1 108.7  84.7                                  
REMARK 620 5 HOH E 629   O    84.5 168.7  82.2  75.6                            
REMARK 620 6 P3S E 601   NE   97.1 102.6 149.7  65.0  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN F 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F 134   OE1                                                    
REMARK 620 2 GLU F 203   OE2  83.1                                              
REMARK 620 3 HOH F 717   O   167.4  85.0                                        
REMARK 620 4 ADP F 501   O2A  83.9  92.5  92.3                                  
REMARK 620 5 ADP F 501   O3B 106.2 159.7  83.8  71.1                            
REMARK 620 6 P3S F 601   O3A  78.6 108.2 109.4 150.8  91.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN F 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F 134   OE1                                                    
REMARK 620 2 GLU F 134   OE2  52.7                                              
REMARK 620 3 GLU F 338   OE2 132.5  83.7                                        
REMARK 620 4 ADP F 501   O2B  87.4  73.0  98.0                                  
REMARK 620 5 P3S F 601   O2A 105.9 155.1 120.3  95.5                            
REMARK 620 6 HIS F 253   ND1  87.0 100.7  83.2 173.4  89.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN F 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F 136   OE2                                                    
REMARK 620 2 GLU F 196   OE1  79.8                                              
REMARK 620 3 GLU F 203   OE1 114.8  79.9                                        
REMARK 620 4 P3S F 601   NE   91.4  89.0 148.8                                  
REMARK 620 5 P3S F 601   O3A 150.2 117.4  93.1  66.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 134   OE1                                                    
REMARK 620 2 GLU G 134   OE2  56.1                                              
REMARK 620 3 GLU G 338   OE2 144.6  97.4                                        
REMARK 620 4 ADP G 501   O2B  89.6  72.6 105.2                                  
REMARK 620 5 P3S G 601   O2A  95.8 151.3 110.5 105.0                            
REMARK 620 6 HIS G 253   ND1  79.6  93.4  79.2 165.7  85.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 134   OE1                                                    
REMARK 620 2 GLU G 203   OE2  83.3                                              
REMARK 620 3 ADP G 501   O2A  81.0  88.2                                        
REMARK 620 4 ADP G 501   O3B  97.5 166.3  78.4                                  
REMARK 620 5 P3S G 601   O3A  86.0 116.3 150.8  77.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 136   OE2                                                    
REMARK 620 2 GLU G 196   OE1  84.0                                              
REMARK 620 3 GLU G 203   OE1 106.4  82.4                                        
REMARK 620 4 P3S G 601   NE   97.4  87.4 152.8                                  
REMARK 620 5 P3S G 601   O3A 161.6 101.3  91.8  65.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN H 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H 134   OE1                                                    
REMARK 620 2 GLU H 134   OE2  58.3                                              
REMARK 620 3 GLU H 338   OE2 145.8  92.6                                        
REMARK 620 4 ADP H 501   O2B  98.5  81.3  94.0                                  
REMARK 620 5 P3S H 601   O2A  92.6 141.4 121.1  78.5                            
REMARK 620 6 HIS H 253   ND1  91.1 104.9  78.5 170.3 100.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN H 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H 134   OE1                                                    
REMARK 620 2 GLU H 203   OE2  85.7                                              
REMARK 620 3 ADP H 501   O3B 111.8 157.9                                        
REMARK 620 4 ADP H 501   O2A  87.6  84.1  83.4                                  
REMARK 620 5 HOH H 608   O   166.4  81.5  79.7  86.7                            
REMARK 620 6 P3S H 601   O3A 101.6 103.9  86.3 168.2  85.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN H 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H 136   OE2                                                    
REMARK 620 2 GLU H 196   OE1  88.6                                              
REMARK 620 3 GLU H 203   OE1 115.5  84.2                                        
REMARK 620 4 HOH H 609   O    83.1 168.8  92.6                                  
REMARK 620 5 P3S H 601   O3A 156.6  94.3  87.9  96.3                            
REMARK 620 6 P3S H 601   NE   90.5  98.6 154.0  89.0  66.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN I 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU I 134   OE1                                                    
REMARK 620 2 GLU I 134   OE2  55.2                                              
REMARK 620 3 GLU I 338   OE2 152.4 101.6                                        
REMARK 620 4 ADP I 501   O2B  95.3  75.3  92.0                                  
REMARK 620 5 P3S I 601   O2A 101.1 150.1 105.3  91.0                            
REMARK 620 6 HIS I 253   ND1  89.2 100.5  80.2 170.3  96.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN I 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU I 134   OE1                                                    
REMARK 620 2 GLU I 203   OE2  82.2                                              
REMARK 620 3 HOH I 718   O   165.1  91.0                                        
REMARK 620 4 ADP I 501   O2A  90.0  88.6  76.5                                  
REMARK 620 5 ADP I 501   O3B  91.7 170.7  93.2  84.3                            
REMARK 620 6 P3S I 601   O3A  79.3 102.5 115.2 163.3  83.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN I 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU I 136   OE2                                                    
REMARK 620 2 GLU I 196   OE1  86.5                                              
REMARK 620 3 GLU I 203   OE1 104.2  86.3                                        
REMARK 620 4 P3S I 601   O3A 148.4 118.5  96.9                                  
REMARK 620 5 P3S I 601   NE   96.7  98.6 158.8  62.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN J 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU J 134   OE1                                                    
REMARK 620 2 GLU J 203   OE2  72.5                                              
REMARK 620 3 HOH J 717   O   160.9  90.5                                        
REMARK 620 4 ADP J 501   O2A  86.5  86.4  83.7                                  
REMARK 620 5 ADP J 501   O1B 112.0 166.7  82.8  81.4                            
REMARK 620 6 P3S J 601   O3A  88.3 100.2 103.7 169.9  92.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN J 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU J 134   OE2                                                    
REMARK 620 2 GLU J 338   OE2 105.0                                              
REMARK 620 3 P3S J 601   O2A 146.9 106.7                                        
REMARK 620 4 ADP J 501   O3B  77.4 103.5  86.0                                  
REMARK 620 5 HIS J 253   ND1 107.8  78.4  88.0 174.0                            
REMARK 620 6 GLU J 134   OE1  54.4 150.7  98.7  92.4  88.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN J 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU J 136   OE2                                                    
REMARK 620 2 GLU J 196   OE1  97.3                                              
REMARK 620 3 GLU J 203   OE1 103.6  80.3                                        
REMARK 620 4 P3S J 601   O3A 151.1 106.8  96.0                                  
REMARK 620 5 HOH J 718   O    81.8 168.2  88.4  77.8                            
REMARK 620 6 P3S J 601   NE   96.5 101.7 159.4  63.6  90.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN F 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN F 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN F 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN H 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN H 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN H 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 705                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 706                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 707                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 708                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I 709                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL J 710                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3S A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3S B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3S C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3S D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3S E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP F 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3S F 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3S G 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP H 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3S H 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP I 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3S I 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP J 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3S J 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OJW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN GLUTAMINE SYNTHETASE IN COMPLEX           
REMARK 900 WITH ADP AND PHOSPHATE                                               
DBREF  2QC8 A    5   365  UNP    P15104   GLNA_HUMAN       5    365             
DBREF  2QC8 B    5   365  UNP    P15104   GLNA_HUMAN       5    365             
DBREF  2QC8 C    5   365  UNP    P15104   GLNA_HUMAN       5    365             
DBREF  2QC8 D    5   365  UNP    P15104   GLNA_HUMAN       5    365             
DBREF  2QC8 E    5   365  UNP    P15104   GLNA_HUMAN       5    365             
DBREF  2QC8 F    5   365  UNP    P15104   GLNA_HUMAN       5    365             
DBREF  2QC8 G    5   365  UNP    P15104   GLNA_HUMAN       5    365             
DBREF  2QC8 H    5   365  UNP    P15104   GLNA_HUMAN       5    365             
DBREF  2QC8 I    5   365  UNP    P15104   GLNA_HUMAN       5    365             
DBREF  2QC8 J    5   365  UNP    P15104   GLNA_HUMAN       5    365             
SEQADV 2QC8 MET A  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS A  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS A  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS A  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS A  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS A  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS A  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER A  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER A  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY A   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 VAL A   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASP A   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU A   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY A   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 THR A   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLU A   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASN A   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU A   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 TYR A    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 PHE A    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLN A    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER A    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET A    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET B  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS B  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS B  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS B  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS B  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS B  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS B  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER B  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER B  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY B   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 VAL B   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASP B   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU B   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY B   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 THR B   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLU B   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASN B   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU B   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 TYR B    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 PHE B    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLN B    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER B    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET B    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET C  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS C  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS C  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS C  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS C  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS C  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS C  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER C  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER C  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY C   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 VAL C   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASP C   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU C   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY C   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 THR C   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLU C   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASN C   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU C   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 TYR C    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 PHE C    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLN C    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER C    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET C    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET D  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS D  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS D  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS D  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS D  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS D  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS D  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER D  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER D  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY D   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 VAL D   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASP D   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU D   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY D   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 THR D   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLU D   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASN D   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU D   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 TYR D    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 PHE D    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLN D    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER D    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET D    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET E  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS E  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS E  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS E  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS E  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS E  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS E  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER E  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER E  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY E   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 VAL E   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASP E   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU E   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY E   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 THR E   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLU E   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASN E   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU E   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 TYR E    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 PHE E    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLN E    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER E    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET E    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET F  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS F  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS F  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS F  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS F  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS F  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS F  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER F  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER F  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY F   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 VAL F   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASP F   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU F   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY F   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 THR F   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLU F   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASN F   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU F   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 TYR F    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 PHE F    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLN F    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER F    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET F    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET G  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS G  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS G  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS G  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS G  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS G  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS G  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER G  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER G  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY G   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 VAL G   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASP G   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU G   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY G   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 THR G   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLU G   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASN G   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU G   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 TYR G    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 PHE G    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLN G    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER G    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET G    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET H  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS H  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS H  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS H  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS H  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS H  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS H  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER H  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER H  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY H   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 VAL H   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASP H   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU H   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY H   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 THR H   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLU H   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASN H   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU H   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 TYR H    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 PHE H    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLN H    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER H    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET H    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET I  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS I  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS I  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS I  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS I  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS I  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS I  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER I  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER I  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY I   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 VAL I   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASP I   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU I   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY I   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 THR I   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLU I   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASN I   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU I   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 TYR I    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 PHE I    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLN I    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER I    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET I    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET J  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS J  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS J  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS J  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS J  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS J  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 HIS J  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER J  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER J  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY J   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 VAL J   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASP J   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU J   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLY J   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 THR J   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLU J   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 ASN J   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 LEU J   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 TYR J    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 PHE J    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 GLN J    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 SER J    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2QC8 MET J    4  UNP  P15104              EXPRESSION TAG                 
SEQRES   1 A  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 A  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 A  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 A  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 A  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 A  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 A  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 A  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 A  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 A  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 A  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 A  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 A  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 A  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 A  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 A  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 A  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 A  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 A  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 A  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 A  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 A  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 A  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 A  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 A  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 A  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 A  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 A  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 A  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 B  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 B  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 B  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 B  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 B  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 B  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 B  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 B  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 B  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 B  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 B  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 B  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 B  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 B  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 B  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 B  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 B  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 B  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 B  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 B  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 B  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 B  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 B  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 B  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 B  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 B  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 B  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 B  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 B  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 C  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 C  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 C  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 C  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 C  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 C  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 C  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 C  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 C  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 C  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 C  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 C  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 C  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 C  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 C  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 C  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 C  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 C  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 C  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 C  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 C  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 C  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 C  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 C  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 C  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 C  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 C  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 C  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 C  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 C  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 D  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 D  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 D  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 D  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 D  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 D  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 D  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 D  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 D  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 D  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 D  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 D  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 D  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 D  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 D  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 D  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 D  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 D  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 D  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 D  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 D  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 D  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 D  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 D  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 D  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 D  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 D  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 D  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 D  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 D  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 E  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 E  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 E  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 E  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 E  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 E  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 E  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 E  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 E  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 E  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 E  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 E  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 E  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 E  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 E  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 E  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 E  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 E  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 E  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 E  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 E  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 E  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 E  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 E  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 E  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 E  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 E  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 E  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 E  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 E  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 F  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 F  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 F  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 F  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 F  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 F  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 F  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 F  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 F  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 F  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 F  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 F  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 F  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 F  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 F  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 F  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 F  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 F  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 F  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 F  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 F  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 F  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 F  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 F  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 F  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 F  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 F  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 F  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 F  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 F  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 G  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 G  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 G  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 G  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 G  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 G  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 G  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 G  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 G  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 G  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 G  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 G  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 G  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 G  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 G  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 G  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 G  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 G  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 G  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 G  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 G  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 G  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 G  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 G  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 G  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 G  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 G  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 G  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 G  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 G  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 H  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 H  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 H  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 H  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 H  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 H  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 H  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 H  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 H  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 H  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 H  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 H  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 H  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 H  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 H  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 H  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 H  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 H  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 H  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 H  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 H  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 H  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 H  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 H  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 H  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 H  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 H  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 H  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 H  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 H  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 I  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 I  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 I  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 I  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 I  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 I  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 I  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 I  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 I  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 I  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 I  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 I  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 I  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 I  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 I  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 I  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 I  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 I  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 I  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 I  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 I  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 I  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 I  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 I  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 I  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 I  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 I  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 I  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 I  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 I  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 J  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 J  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 J  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 J  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 J  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 J  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 J  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 J  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 J  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 J  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 J  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 J  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 J  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 J  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 J  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 J  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 J  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 J  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 J  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 J  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 J  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 J  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 J  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 J  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 J  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 J  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 J  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 J  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 J  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 J  384  CYS LEU LEU ASN GLU THR GLY                                  
HET     MN  A 401       1                                                       
HET     MN  A 402       1                                                       
HET     MN  A 403       1                                                       
HET     MN  B 401       1                                                       
HET     MN  B 402       1                                                       
HET     MN  B 403       1                                                       
HET     MN  C 401       1                                                       
HET     MN  C 402       1                                                       
HET     MN  C 403       1                                                       
HET     MN  D 401       1                                                       
HET     MN  D 402       1                                                       
HET     MN  D 403       1                                                       
HET     MN  E 401       1                                                       
HET     MN  E 402       1                                                       
HET     MN  E 403       1                                                       
HET     MN  F 401       1                                                       
HET     MN  F 402       1                                                       
HET     MN  F 403       1                                                       
HET     MN  G 401       1                                                       
HET     MN  G 402       1                                                       
HET     MN  G 403       1                                                       
HET     MN  H 401       1                                                       
HET     MN  H 402       1                                                       
HET     MN  H 403       1                                                       
HET     MN  I 401       1                                                       
HET     MN  I 402       1                                                       
HET     MN  I 403       1                                                       
HET     MN  J 401       1                                                       
HET     MN  J 402       1                                                       
HET     MN  J 403       1                                                       
HET     CL  B 701       1                                                       
HET     CL  C 702       1                                                       
HET     CL  A 703       1                                                       
HET     CL  D 704       1                                                       
HET     CL  B 705       1                                                       
HET     CL  F 706       1                                                       
HET     CL  G 707       1                                                       
HET     CL  G 708       1                                                       
HET     CL  I 709       1                                                       
HET     CL  J 710       1                                                       
HET    ADP  A 501      27                                                       
HET    P3S  A 601      15                                                       
HET    ADP  B 501      27                                                       
HET    P3S  B 601      15                                                       
HET    ADP  C 501      27                                                       
HET    P3S  C 601      15                                                       
HET    ADP  D 501      27                                                       
HET    P3S  D 601      15                                                       
HET    ADP  E 501      27                                                       
HET    P3S  E 601      15                                                       
HET    ADP  F 501      27                                                       
HET    P3S  F 601      15                                                       
HET    ADP  G 501      27                                                       
HET    P3S  G 601      15                                                       
HET    ADP  H 501      27                                                       
HET    P3S  H 601      15                                                       
HET    ADP  I 501      27                                                       
HET    P3S  I 601      15                                                       
HET    ADP  J 501      27                                                       
HET    P3S  J 601      15                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     P3S L-METHIONINE-S-SULFOXIMINE PHOSPHATE                             
FORMUL  11   MN    30(MN 2+)                                                    
FORMUL  41   CL    10(CL 1-)                                                    
FORMUL  51  ADP    10(C10 H15 N5 O10 P2)                                        
FORMUL  52  P3S    10(C5 H13 N2 O6 P S)                                         
FORMUL  71  HOH   *231(H2 O)                                                    
HELIX    1   1 ASN A   10  SER A   19  1                                  10    
HELIX    2   2 CYS A   53  LEU A   57  5                                   5    
HELIX    3   3 SER A   65  THR A   67  5                                   3    
HELIX    4   4 GLU A   71  ASN A   74  5                                   4    
HELIX    5   5 LEU A  113  MET A  123  1                                  11    
HELIX    6   6 VAL A  124  HIS A  128  5                                   5    
HELIX    7   7 GLY A  172  GLY A  187  1                                  16    
HELIX    8   8 ILE A  212  PHE A  232  1                                  21    
HELIX    9   9 THR A  258  GLU A  263  1                                   6    
HELIX   10  10 GLY A  266  LYS A  279  1                                  14    
HELIX   11  11 ARG A  280  TYR A  288  1                                   9    
HELIX   12  12 ASP A  295  ARG A  299  5                                   5    
HELIX   13  13 PRO A  326  LYS A  333  1                                   8    
HELIX   14  14 ASP A  347  LEU A  360  1                                  14    
HELIX   15  15 ASN B   10  LEU B   20  1                                  11    
HELIX   16  16 CYS B   53  LEU B   57  5                                   5    
HELIX   17  17 GLU B   71  ASN B   74  5                                   4    
HELIX   18  18 LEU B  113  VAL B  124  1                                  12    
HELIX   19  19 SER B  125  HIS B  128  5                                   4    
HELIX   20  20 GLY B  172  GLY B  187  1                                  16    
HELIX   21  21 ILE B  212  PHE B  232  1                                  21    
HELIX   22  22 THR B  258  GLU B  263  1                                   6    
HELIX   23  23 GLY B  266  LYS B  279  1                                  14    
HELIX   24  24 ARG B  280  TYR B  288  1                                   9    
HELIX   25  25 ASP B  295  ARG B  299  5                                   5    
HELIX   26  26 PRO B  326  LYS B  333  1                                   8    
HELIX   27  27 ASP B  347  LEU B  360  1                                  14    
HELIX   28  28 ASN C   10  SER C   19  1                                  10    
HELIX   29  29 CYS C   53  LEU C   57  5                                   5    
HELIX   30  30 GLU C   71  ASN C   74  5                                   4    
HELIX   31  31 LEU C  113  MET C  123  1                                  11    
HELIX   32  32 VAL C  124  HIS C  128  5                                   5    
HELIX   33  33 GLY C  172  GLY C  187  1                                  16    
HELIX   34  34 ILE C  212  GLY C  233  1                                  22    
HELIX   35  35 THR C  258  GLU C  263  1                                   6    
HELIX   36  36 GLY C  266  LYS C  279  1                                  14    
HELIX   37  37 ARG C  280  TYR C  288  1                                   9    
HELIX   38  38 ASP C  295  ARG C  299  5                                   5    
HELIX   39  39 PRO C  326  LYS C  333  1                                   8    
HELIX   40  40 ASP C  347  LEU C  360  1                                  14    
HELIX   41  41 ASN D   10  MET D   18  1                                   9    
HELIX   42  42 CYS D   53  LEU D   57  5                                   5    
HELIX   43  43 GLU D   71  ASN D   74  5                                   4    
HELIX   44  44 LEU D  113  VAL D  124  1                                  12    
HELIX   45  45 SER D  125  HIS D  128  5                                   4    
HELIX   46  46 GLY D  172  GLY D  187  1                                  16    
HELIX   47  47 ILE D  212  PHE D  232  1                                  21    
HELIX   48  48 THR D  258  GLU D  263  1                                   6    
HELIX   49  49 GLY D  266  LYS D  279  1                                  14    
HELIX   50  50 ARG D  280  TYR D  288  1                                   9    
HELIX   51  51 ASP D  295  ARG D  299  5                                   5    
HELIX   52  52 PRO D  326  LYS D  333  1                                   8    
HELIX   53  53 ASP D  347  LEU D  360  1                                  14    
HELIX   54  54 ASN E   10  SER E   19  1                                  10    
HELIX   55  55 CYS E   53  LEU E   57  5                                   5    
HELIX   56  56 GLU E   71  ASN E   74  5                                   4    
HELIX   57  57 LEU E  113  VAL E  124  1                                  12    
HELIX   58  58 SER E  125  HIS E  128  5                                   4    
HELIX   59  59 GLY E  172  GLY E  187  1                                  16    
HELIX   60  60 ILE E  212  PHE E  232  1                                  21    
HELIX   61  61 THR E  258  GLU E  263  1                                   6    
HELIX   62  62 GLY E  266  SER E  278  1                                  13    
HELIX   63  63 ARG E  280  TYR E  288  1                                   9    
HELIX   64  64 ASP E  295  ARG E  299  5                                   5    
HELIX   65  65 PRO E  326  LYS E  333  1                                   8    
HELIX   66  66 ASP E  347  LEU E  360  1                                  14    
HELIX   67  67 ASN F   10  SER F   19  1                                  10    
HELIX   68  68 CYS F   53  LEU F   57  5                                   5    
HELIX   69  69 SER F   65  THR F   67  5                                   3    
HELIX   70  70 GLU F   71  ASN F   74  5                                   4    
HELIX   71  71 LEU F  113  MET F  123  1                                  11    
HELIX   72  72 VAL F  124  HIS F  128  5                                   5    
HELIX   73  73 GLY F  172  GLY F  187  1                                  16    
HELIX   74  74 ILE F  212  GLY F  233  1                                  22    
HELIX   75  75 THR F  258  GLU F  263  1                                   6    
HELIX   76  76 GLY F  266  LYS F  279  1                                  14    
HELIX   77  77 ARG F  280  TYR F  288  1                                   9    
HELIX   78  78 GLY F  293  ARG F  298  1                                   6    
HELIX   79  79 PRO F  326  LYS F  333  1                                   8    
HELIX   80  80 ASP F  347  LEU F  360  1                                  14    
HELIX   81  81 ASN G   10  SER G   19  1                                  10    
HELIX   82  82 CYS G   53  LEU G   57  5                                   5    
HELIX   83  83 GLU G   71  ASN G   74  5                                   4    
HELIX   84  84 LEU G  113  VAL G  124  1                                  12    
HELIX   85  85 SER G  125  HIS G  128  5                                   4    
HELIX   86  86 GLY G  172  GLY G  187  1                                  16    
HELIX   87  87 ILE G  212  GLY G  233  1                                  22    
HELIX   88  88 THR G  258  GLU G  263  1                                   6    
HELIX   89  89 GLY G  266  LYS G  279  1                                  14    
HELIX   90  90 ARG G  280  TYR G  288  1                                   9    
HELIX   91  91 ASP G  295  ARG G  299  5                                   5    
HELIX   92  92 PRO G  326  LYS G  333  1                                   8    
HELIX   93  93 ASP G  347  LEU G  360  1                                  14    
HELIX   94  94 ASN H   10  SER H   19  1                                  10    
HELIX   95  95 CYS H   53  LEU H   57  5                                   5    
HELIX   96  96 GLU H   71  ASN H   74  5                                   4    
HELIX   97  97 LEU H  113  VAL H  124  1                                  12    
HELIX   98  98 SER H  125  HIS H  128  5                                   4    
HELIX   99  99 GLY H  172  GLY H  187  1                                  16    
HELIX  100 100 ILE H  212  PHE H  232  1                                  21    
HELIX  101 101 THR H  258  GLU H  263  1                                   6    
HELIX  102 102 GLY H  266  LYS H  279  1                                  14    
HELIX  103 103 ARG H  280  TYR H  288  1                                   9    
HELIX  104 104 ASP H  295  ARG H  299  5                                   5    
HELIX  105 105 PRO H  326  GLU H  332  1                                   7    
HELIX  106 106 ASP H  347  LEU H  360  1                                  14    
HELIX  107 107 ASN I   10  SER I   19  1                                  10    
HELIX  108 108 CYS I   53  LEU I   57  5                                   5    
HELIX  109 109 GLU I   71  ASN I   74  5                                   4    
HELIX  110 110 LEU I  113  MET I  123  1                                  11    
HELIX  111 111 VAL I  124  HIS I  128  5                                   5    
HELIX  112 112 GLY I  172  GLY I  187  1                                  16    
HELIX  113 113 ILE I  212  GLY I  233  1                                  22    
HELIX  114 114 THR I  258  GLU I  263  1                                   6    
HELIX  115 115 GLY I  266  LYS I  279  1                                  14    
HELIX  116 116 ARG I  280  TYR I  288  1                                   9    
HELIX  117 117 ASP I  295  ARG I  299  5                                   5    
HELIX  118 118 PRO I  326  LYS I  333  1                                   8    
HELIX  119 119 ASP I  347  LEU I  360  1                                  14    
HELIX  120 120 ASN J   10  SER J   19  1                                  10    
HELIX  121 121 CYS J   53  LEU J   57  5                                   5    
HELIX  122 122 SER J   65  THR J   67  5                                   3    
HELIX  123 123 GLU J   71  ASN J   74  5                                   4    
HELIX  124 124 LEU J  113  MET J  123  1                                  11    
HELIX  125 125 VAL J  124  HIS J  128  5                                   5    
HELIX  126 126 GLY J  172  GLY J  187  1                                  16    
HELIX  127 127 ILE J  212  PHE J  232  1                                  21    
HELIX  128 128 THR J  258  GLU J  263  1                                   6    
HELIX  129 129 GLY J  266  LYS J  279  1                                  14    
HELIX  130 130 ARG J  280  TYR J  288  1                                   9    
HELIX  131 131 GLY J  293  ARG J  298  1                                   6    
HELIX  132 132 PRO J  326  LYS J  333  1                                   8    
HELIX  133 133 ASP J  347  LEU J  360  1                                  14    
SHEET    1   A 9 TRP A  60  ASP A  63  0                                        
SHEET    2   A 9 ASP A  76  ARG A  86 -1  O  LEU A  79   N  TRP A  60           
SHEET    3   A 9 LYS A  95  PHE A 102 -1  O  LEU A  96   N  PHE A  85           
SHEET    4   A 9 VAL A  26  ILE A  33  1  N  ILE A  31   O  VAL A  97           
SHEET    5   A 9 LEU A  40  LEU A  47 -1  O  LEU A  47   N  VAL A  26           
SHEET    6   A 9 ILE B 190  ALA B 195 -1  O  ALA B 191   N  THR A  46           
SHEET    7   A 9 GLN B 201  GLU B 210 -1  O  GLN B 205   N  GLY B 192           
SHEET    8   A 9 TRP B 130  MET B 140 -1  N  MET B 133   O  ILE B 206           
SHEET    9   A 9 ILE B 235  THR B 237 -1  O  ILE B 235   N  MET B 140           
SHEET    1   B12 TRP A  60  ASP A  63  0                                        
SHEET    2   B12 ASP A  76  ARG A  86 -1  O  LEU A  79   N  TRP A  60           
SHEET    3   B12 LYS A  95  PHE A 102 -1  O  LEU A  96   N  PHE A  85           
SHEET    4   B12 VAL A  26  ILE A  33  1  N  ILE A  31   O  VAL A  97           
SHEET    5   B12 LEU A  40  LEU A  47 -1  O  LEU A  47   N  VAL A  26           
SHEET    6   B12 ILE B 190  ALA B 195 -1  O  ALA B 191   N  THR A  46           
SHEET    7   B12 GLN B 201  GLU B 210 -1  O  GLN B 205   N  GLY B 192           
SHEET    8   B12 TRP B 130  MET B 140 -1  N  MET B 133   O  ILE B 206           
SHEET    9   B12 CYS B 252  SER B 257 -1  O  ASN B 255   N  GLY B 132           
SHEET   10   B12 PHE B 337  ASP B 339 -1  O  ASP B 339   N  THR B 254           
SHEET   11   B12 ILE B 323  ILE B 325 -1  N  ARG B 324   O  GLU B 338           
SHEET   12   B12 ALA B 314  VAL B 316  1  N  GLY B 315   O  ILE B 325           
SHEET    1   C 6 ILE A 235  THR A 237  0                                        
SHEET    2   C 6 TRP A 130  MET A 140 -1  N  MET A 140   O  ILE A 235           
SHEET    3   C 6 CYS A 252  SER A 257 -1  O  ASN A 255   N  GLY A 132           
SHEET    4   C 6 PHE A 337  ASP A 339 -1  O  ASP A 339   N  THR A 254           
SHEET    5   C 6 ILE A 323  ILE A 325 -1  N  ARG A 324   O  GLU A 338           
SHEET    6   C 6 ALA A 314  VAL A 316  1  N  GLY A 315   O  ILE A 325           
SHEET    1   D 9 ILE A 235  THR A 237  0                                        
SHEET    2   D 9 TRP A 130  MET A 140 -1  N  MET A 140   O  ILE A 235           
SHEET    3   D 9 GLN A 201  GLU A 210 -1  O  TRP A 202   N  TYR A 137           
SHEET    4   D 9 ILE A 190  ALA A 195 -1  N  ALA A 191   O  GLN A 205           
SHEET    5   D 9 LEU E  40  LEU E  47 -1  O  THR E  46   N  ALA A 191           
SHEET    6   D 9 VAL E  26  ILE E  33 -1  N  TRP E  32   O  ARG E  41           
SHEET    7   D 9 LYS E  95  PHE E 102  1  O  VAL E  97   N  ILE E  31           
SHEET    8   D 9 ASP E  76  ARG E  86 -1  N  PHE E  85   O  LEU E  96           
SHEET    9   D 9 TRP E  60  ASP E  63 -1  N  TRP E  60   O  LEU E  79           
SHEET    1   E 9 TRP B  60  ASP B  63  0                                        
SHEET    2   E 9 ASP B  76  ARG B  86 -1  O  LEU B  79   N  TRP B  60           
SHEET    3   E 9 LYS B  95  PHE B 102 -1  O  LEU B  96   N  PHE B  85           
SHEET    4   E 9 VAL B  26  ILE B  33  1  N  ILE B  31   O  VAL B  97           
SHEET    5   E 9 LEU B  40  LEU B  47 -1  O  LYS B  43   N  TYR B  30           
SHEET    6   E 9 ILE C 190  ALA C 195 -1  O  ALA C 191   N  THR B  46           
SHEET    7   E 9 GLN C 201  GLU C 210 -1  O  GLN C 205   N  ALA C 191           
SHEET    8   E 9 TRP C 130  MET C 140 -1  N  TYR C 137   O  TRP C 202           
SHEET    9   E 9 ILE C 235  THR C 237 -1  O  ILE C 235   N  MET C 140           
SHEET    1   F12 TRP B  60  ASP B  63  0                                        
SHEET    2   F12 ASP B  76  ARG B  86 -1  O  LEU B  79   N  TRP B  60           
SHEET    3   F12 LYS B  95  PHE B 102 -1  O  LEU B  96   N  PHE B  85           
SHEET    4   F12 VAL B  26  ILE B  33  1  N  ILE B  31   O  VAL B  97           
SHEET    5   F12 LEU B  40  LEU B  47 -1  O  LYS B  43   N  TYR B  30           
SHEET    6   F12 ILE C 190  ALA C 195 -1  O  ALA C 191   N  THR B  46           
SHEET    7   F12 GLN C 201  GLU C 210 -1  O  GLN C 205   N  ALA C 191           
SHEET    8   F12 TRP C 130  MET C 140 -1  N  TYR C 137   O  TRP C 202           
SHEET    9   F12 CYS C 252  SER C 257 -1  O  ASN C 255   N  GLY C 132           
SHEET   10   F12 PHE C 337  ASP C 339 -1  O  ASP C 339   N  THR C 254           
SHEET   11   F12 ILE C 323  ILE C 325 -1  N  ARG C 324   O  GLU C 338           
SHEET   12   F12 ALA C 314  VAL C 316  1  N  GLY C 315   O  ILE C 325           
SHEET    1   G 9 TRP C  60  ASP C  63  0                                        
SHEET    2   G 9 ASP C  76  ARG C  86 -1  O  LEU C  79   N  TRP C  60           
SHEET    3   G 9 LYS C  95  PHE C 102 -1  O  LEU C  98   N  ALA C  82           
SHEET    4   G 9 VAL C  26  ILE C  33  1  N  ILE C  31   O  CYS C  99           
SHEET    5   G 9 LEU C  40  LEU C  47 -1  O  LYS C  43   N  TYR C  30           
SHEET    6   G 9 ILE D 190  ALA D 195 -1  O  ALA D 191   N  THR C  46           
SHEET    7   G 9 GLN D 201  GLU D 210 -1  O  GLN D 205   N  GLY D 192           
SHEET    8   G 9 TRP D 130  MET D 140 -1  N  PHE D 131   O  CYS D 209           
SHEET    9   G 9 ILE D 235  THR D 237 -1  O  ILE D 235   N  MET D 140           
SHEET    1   H12 TRP C  60  ASP C  63  0                                        
SHEET    2   H12 ASP C  76  ARG C  86 -1  O  LEU C  79   N  TRP C  60           
SHEET    3   H12 LYS C  95  PHE C 102 -1  O  LEU C  98   N  ALA C  82           
SHEET    4   H12 VAL C  26  ILE C  33  1  N  ILE C  31   O  CYS C  99           
SHEET    5   H12 LEU C  40  LEU C  47 -1  O  LYS C  43   N  TYR C  30           
SHEET    6   H12 ILE D 190  ALA D 195 -1  O  ALA D 191   N  THR C  46           
SHEET    7   H12 GLN D 201  GLU D 210 -1  O  GLN D 205   N  GLY D 192           
SHEET    8   H12 TRP D 130  MET D 140 -1  N  PHE D 131   O  CYS D 209           
SHEET    9   H12 CYS D 252  SER D 257 -1  O  ASN D 255   N  GLY D 132           
SHEET   10   H12 PHE D 337  ASP D 339 -1  O  ASP D 339   N  THR D 254           
SHEET   11   H12 ILE D 323  ILE D 325 -1  N  ARG D 324   O  GLU D 338           
SHEET   12   H12 ALA D 314  VAL D 316  1  N  GLY D 315   O  ILE D 323           
SHEET    1   I 9 TRP D  60  ASP D  63  0                                        
SHEET    2   I 9 ASP D  76  ARG D  86 -1  O  LEU D  79   N  TRP D  60           
SHEET    3   I 9 LYS D  95  PHE D 102 -1  O  LEU D  98   N  ALA D  82           
SHEET    4   I 9 VAL D  26  ILE D  33  1  N  MET D  29   O  LYS D  95           
SHEET    5   I 9 LEU D  40  LEU D  47 -1  O  LYS D  43   N  TYR D  30           
SHEET    6   I 9 ILE E 190  ALA E 195 -1  O  ALA E 191   N  THR D  46           
SHEET    7   I 9 GLN E 201  GLU E 210 -1  O  GLN E 205   N  ALA E 191           
SHEET    8   I 9 TRP E 130  MET E 140 -1  N  PHE E 131   O  CYS E 209           
SHEET    9   I 9 ILE E 235  THR E 237 -1  O  ILE E 235   N  MET E 140           
SHEET    1   J12 TRP D  60  ASP D  63  0                                        
SHEET    2   J12 ASP D  76  ARG D  86 -1  O  LEU D  79   N  TRP D  60           
SHEET    3   J12 LYS D  95  PHE D 102 -1  O  LEU D  98   N  ALA D  82           
SHEET    4   J12 VAL D  26  ILE D  33  1  N  MET D  29   O  LYS D  95           
SHEET    5   J12 LEU D  40  LEU D  47 -1  O  LYS D  43   N  TYR D  30           
SHEET    6   J12 ILE E 190  ALA E 195 -1  O  ALA E 191   N  THR D  46           
SHEET    7   J12 GLN E 201  GLU E 210 -1  O  GLN E 205   N  ALA E 191           
SHEET    8   J12 TRP E 130  MET E 140 -1  N  PHE E 131   O  CYS E 209           
SHEET    9   J12 THR E 254  SER E 257 -1  O  ASN E 255   N  GLY E 132           
SHEET   10   J12 PHE E 337  ASP E 339 -1  O  ASP E 339   N  THR E 254           
SHEET   11   J12 ILE E 323  ILE E 325 -1  N  ARG E 324   O  GLU E 338           
SHEET   12   J12 ALA E 314  VAL E 316  1  N  GLY E 315   O  ILE E 325           
SHEET    1   K 9 TRP F  60  ASP F  63  0                                        
SHEET    2   K 9 ASP F  76  ARG F  86 -1  O  LEU F  79   N  TRP F  60           
SHEET    3   K 9 LYS F  95  PHE F 102 -1  O  LEU F  98   N  ALA F  83           
SHEET    4   K 9 VAL F  26  ILE F  33  1  N  ILE F  31   O  VAL F  97           
SHEET    5   K 9 LEU F  40  LEU F  47 -1  O  LYS F  43   N  TYR F  30           
SHEET    6   K 9 ILE G 190  ALA G 195 -1  O  ALA G 191   N  THR F  46           
SHEET    7   K 9 GLN G 201  GLU G 210 -1  O  GLN G 205   N  GLY G 192           
SHEET    8   K 9 TRP G 130  GLY G 141 -1  N  TYR G 137   O  TRP G 202           
SHEET    9   K 9 VAL G 234  THR G 237 -1  O  ILE G 235   N  MET G 140           
SHEET    1   L12 TRP F  60  ASP F  63  0                                        
SHEET    2   L12 ASP F  76  ARG F  86 -1  O  LEU F  79   N  TRP F  60           
SHEET    3   L12 LYS F  95  PHE F 102 -1  O  LEU F  98   N  ALA F  83           
SHEET    4   L12 VAL F  26  ILE F  33  1  N  ILE F  31   O  VAL F  97           
SHEET    5   L12 LEU F  40  LEU F  47 -1  O  LYS F  43   N  TYR F  30           
SHEET    6   L12 ILE G 190  ALA G 195 -1  O  ALA G 191   N  THR F  46           
SHEET    7   L12 GLN G 201  GLU G 210 -1  O  GLN G 205   N  GLY G 192           
SHEET    8   L12 TRP G 130  GLY G 141 -1  N  TYR G 137   O  TRP G 202           
SHEET    9   L12 CYS G 252  SER G 257 -1  O  SER G 257   N  TRP G 130           
SHEET   10   L12 PHE G 337  ASP G 339 -1  O  ASP G 339   N  THR G 254           
SHEET   11   L12 ILE G 323  ILE G 325 -1  N  ARG G 324   O  GLU G 338           
SHEET   12   L12 ALA G 314  VAL G 316  1  N  GLY G 315   O  ILE G 325           
SHEET    1   M 6 ILE F 235  THR F 237  0                                        
SHEET    2   M 6 TRP F 130  MET F 140 -1  N  THR F 138   O  THR F 237           
SHEET    3   M 6 CYS F 252  SER F 257 -1  O  ASN F 255   N  GLY F 132           
SHEET    4   M 6 PHE F 337  ASP F 339 -1  O  ASP F 339   N  THR F 254           
SHEET    5   M 6 ILE F 323  ILE F 325 -1  N  ARG F 324   O  GLU F 338           
SHEET    6   M 6 ALA F 314  VAL F 316  1  N  GLY F 315   O  ILE F 325           
SHEET    1   N 9 ILE F 235  THR F 237  0                                        
SHEET    2   N 9 TRP F 130  MET F 140 -1  N  THR F 138   O  THR F 237           
SHEET    3   N 9 GLN F 201  GLU F 210 -1  O  CYS F 209   N  PHE F 131           
SHEET    4   N 9 ILE F 190  ALA F 195 -1  N  ALA F 191   O  GLN F 205           
SHEET    5   N 9 LEU J  40  LEU J  47 -1  O  THR J  46   N  ALA F 191           
SHEET    6   N 9 VAL J  26  ILE J  33 -1  N  VAL J  26   O  LEU J  47           
SHEET    7   N 9 LYS J  95  PHE J 102  1  O  VAL J  97   N  ILE J  31           
SHEET    8   N 9 ASP J  76  ARG J  86 -1  N  PHE J  85   O  LEU J  96           
SHEET    9   N 9 TRP J  60  ASP J  63 -1  N  TRP J  60   O  LEU J  79           
SHEET    1   O 9 TRP G  60  ASP G  63  0                                        
SHEET    2   O 9 ASP G  76  ARG G  86 -1  O  MET G  77   N  PHE G  62           
SHEET    3   O 9 LYS G  95  PHE G 102 -1  O  LEU G  98   N  ALA G  83           
SHEET    4   O 9 VAL G  26  ILE G  33  1  N  ILE G  31   O  VAL G  97           
SHEET    5   O 9 LEU G  40  LEU G  47 -1  O  LEU G  47   N  VAL G  26           
SHEET    6   O 9 ILE H 190  ALA H 195 -1  O  ALA H 191   N  THR G  46           
SHEET    7   O 9 GLN H 201  GLU H 210 -1  O  GLN H 205   N  GLY H 192           
SHEET    8   O 9 TRP H 130  MET H 140 -1  N  PHE H 131   O  CYS H 209           
SHEET    9   O 9 ILE H 235  THR H 237 -1  O  ILE H 235   N  MET H 140           
SHEET    1   P12 TRP G  60  ASP G  63  0                                        
SHEET    2   P12 ASP G  76  ARG G  86 -1  O  MET G  77   N  PHE G  62           
SHEET    3   P12 LYS G  95  PHE G 102 -1  O  LEU G  98   N  ALA G  83           
SHEET    4   P12 VAL G  26  ILE G  33  1  N  ILE G  31   O  VAL G  97           
SHEET    5   P12 LEU G  40  LEU G  47 -1  O  LEU G  47   N  VAL G  26           
SHEET    6   P12 ILE H 190  ALA H 195 -1  O  ALA H 191   N  THR G  46           
SHEET    7   P12 GLN H 201  GLU H 210 -1  O  GLN H 205   N  GLY H 192           
SHEET    8   P12 TRP H 130  MET H 140 -1  N  PHE H 131   O  CYS H 209           
SHEET    9   P12 CYS H 252  SER H 257 -1  O  ASN H 255   N  GLY H 132           
SHEET   10   P12 PHE H 337  ASP H 339 -1  O  ASP H 339   N  THR H 254           
SHEET   11   P12 ILE H 323  ILE H 325 -1  N  ARG H 324   O  GLU H 338           
SHEET   12   P12 ALA H 314  VAL H 316  1  N  GLY H 315   O  ILE H 325           
SHEET    1   Q 9 TRP H  60  ASP H  63  0                                        
SHEET    2   Q 9 ASP H  76  ARG H  86 -1  O  LEU H  79   N  TRP H  60           
SHEET    3   Q 9 LYS H  95  PHE H 102 -1  O  LEU H  98   N  ALA H  83           
SHEET    4   Q 9 VAL H  26  ILE H  33  1  N  ILE H  31   O  VAL H  97           
SHEET    5   Q 9 LEU H  40  LEU H  47 -1  O  LEU H  47   N  VAL H  26           
SHEET    6   Q 9 ILE I 190  ALA I 195 -1  O  ALA I 191   N  THR H  46           
SHEET    7   Q 9 GLN I 201  GLU I 210 -1  O  GLN I 205   N  ALA I 191           
SHEET    8   Q 9 TRP I 130  MET I 140 -1  N  PHE I 131   O  CYS I 209           
SHEET    9   Q 9 ILE I 235  THR I 237 -1  O  THR I 237   N  THR I 138           
SHEET    1   R12 TRP H  60  ASP H  63  0                                        
SHEET    2   R12 ASP H  76  ARG H  86 -1  O  LEU H  79   N  TRP H  60           
SHEET    3   R12 LYS H  95  PHE H 102 -1  O  LEU H  98   N  ALA H  83           
SHEET    4   R12 VAL H  26  ILE H  33  1  N  ILE H  31   O  VAL H  97           
SHEET    5   R12 LEU H  40  LEU H  47 -1  O  LEU H  47   N  VAL H  26           
SHEET    6   R12 ILE I 190  ALA I 195 -1  O  ALA I 191   N  THR H  46           
SHEET    7   R12 GLN I 201  GLU I 210 -1  O  GLN I 205   N  ALA I 191           
SHEET    8   R12 TRP I 130  MET I 140 -1  N  PHE I 131   O  CYS I 209           
SHEET    9   R12 CYS I 252  SER I 257 -1  O  ASN I 255   N  GLY I 132           
SHEET   10   R12 PHE I 337  ASP I 339 -1  O  ASP I 339   N  THR I 254           
SHEET   11   R12 ILE I 323  ILE I 325 -1  N  ARG I 324   O  GLU I 338           
SHEET   12   R12 ALA I 314  VAL I 316  1  N  GLY I 315   O  ILE I 325           
SHEET    1   S 9 TRP I  60  ASP I  63  0                                        
SHEET    2   S 9 ASP I  76  ARG I  86 -1  O  LEU I  79   N  TRP I  60           
SHEET    3   S 9 LYS I  95  PHE I 102 -1  O  LEU I  98   N  ALA I  83           
SHEET    4   S 9 VAL I  26  ILE I  33  1  N  ILE I  31   O  VAL I  97           
SHEET    5   S 9 LEU I  40  LEU I  47 -1  O  LYS I  43   N  TYR I  30           
SHEET    6   S 9 ILE J 190  ALA J 195 -1  O  THR J 193   N  THR I  44           
SHEET    7   S 9 GLN J 201  GLU J 210 -1  O  GLN J 205   N  ALA J 191           
SHEET    8   S 9 TRP J 130  GLY J 141 -1  N  PHE J 131   O  CYS J 209           
SHEET    9   S 9 VAL J 234  THR J 237 -1  O  ILE J 235   N  MET J 140           
SHEET    1   T12 TRP I  60  ASP I  63  0                                        
SHEET    2   T12 ASP I  76  ARG I  86 -1  O  LEU I  79   N  TRP I  60           
SHEET    3   T12 LYS I  95  PHE I 102 -1  O  LEU I  98   N  ALA I  83           
SHEET    4   T12 VAL I  26  ILE I  33  1  N  ILE I  31   O  VAL I  97           
SHEET    5   T12 LEU I  40  LEU I  47 -1  O  LYS I  43   N  TYR I  30           
SHEET    6   T12 ILE J 190  ALA J 195 -1  O  THR J 193   N  THR I  44           
SHEET    7   T12 GLN J 201  GLU J 210 -1  O  GLN J 205   N  ALA J 191           
SHEET    8   T12 TRP J 130  GLY J 141 -1  N  PHE J 131   O  CYS J 209           
SHEET    9   T12 THR J 254  SER J 257 -1  O  ASN J 255   N  GLY J 132           
SHEET   10   T12 PHE J 337  ASP J 339 -1  O  ASP J 339   N  THR J 254           
SHEET   11   T12 ILE J 323  ILE J 325 -1  N  ARG J 324   O  GLU J 338           
SHEET   12   T12 ALA J 314  VAL J 316  1  N  GLY J 315   O  ILE J 325           
SSBOND   1 CYS A   53    CYS C   53                          1555   4455  1.99  
SSBOND   2 CYS F   53    CYS H   53                          1555   4454  2.02  
LINK         OE1 GLU A 134                MN    MN A 403     1555   1555  2.15  
LINK         OE1 GLU A 134                MN    MN A 402     1555   1555  2.34  
LINK         OE2 GLU A 134                MN    MN A 402     1555   1555  2.48  
LINK         OE2 GLU A 136                MN    MN A 401     1555   1555  2.08  
LINK         OE1 GLU A 196                MN    MN A 401     1555   1555  2.17  
LINK         OE1 GLU A 203                MN    MN A 401     1555   1555  2.01  
LINK         OE2 GLU A 203                MN    MN A 403     1555   1555  2.17  
LINK         OE2 GLU A 338                MN    MN A 402     1555   1555  1.99  
LINK         OE1 GLU B 134                MN    MN B 403     1555   1555  2.29  
LINK         OE1 GLU B 134                MN    MN B 402     1555   1555  2.23  
LINK         OE2 GLU B 134                MN    MN B 402     1555   1555  2.31  
LINK         OE2 GLU B 136                MN    MN B 401     1555   1555  2.10  
LINK         OE1 GLU B 196                MN    MN B 401     1555   1555  2.20  
LINK         OE1 GLU B 203                MN    MN B 401     1555   1555  1.99  
LINK         OE2 GLU B 203                MN    MN B 403     1555   1555  2.14  
LINK         OE2 GLU B 338                MN    MN B 402     1555   1555  1.96  
LINK         OE1 GLU C 134                MN    MN C 402     1555   1555  2.41  
LINK         OE1 GLU C 134                MN    MN C 403     1555   1555  1.96  
LINK         OE2 GLU C 134                MN    MN C 402     1555   1555  2.31  
LINK         OE2 GLU C 136                MN    MN C 401     1555   1555  2.08  
LINK         OE1 GLU C 196                MN    MN C 401     1555   1555  2.15  
LINK         OE1 GLU C 203                MN    MN C 401     1555   1555  2.00  
LINK         OE2 GLU C 203                MN    MN C 403     1555   1555  2.27  
LINK         OE2 GLU C 338                MN    MN C 402     1555   1555  1.95  
LINK         OE1 GLU D 134                MN    MN D 402     1555   1555  2.38  
LINK         OE1 GLU D 134                MN    MN D 403     1555   1555  2.12  
LINK         OE2 GLU D 134                MN    MN D 402     1555   1555  2.25  
LINK         OE2 GLU D 136                MN    MN D 401     1555   1555  2.18  
LINK         OE1 GLU D 196                MN    MN D 401     1555   1555  2.27  
LINK         OE1 GLU D 203                MN    MN D 401     1555   1555  2.20  
LINK         OE2 GLU D 203                MN    MN D 403     1555   1555  2.18  
LINK         OE2 GLU D 338                MN    MN D 402     1555   1555  2.05  
LINK         OE1 GLU E 134                MN    MN E 402     1555   1555  2.46  
LINK         OE1 GLU E 134                MN    MN E 403     1555   1555  2.22  
LINK         OE2 GLU E 134                MN    MN E 402     1555   1555  2.37  
LINK         OE2 GLU E 136                MN    MN E 401     1555   1555  2.12  
LINK         OE1 GLU E 196                MN    MN E 401     1555   1555  2.11  
LINK         OE1 GLU E 203                MN    MN E 401     1555   1555  2.10  
LINK         OE2 GLU E 203                MN    MN E 403     1555   1555  2.26  
LINK         OE2 GLU E 338                MN    MN E 402     1555   1555  2.06  
LINK         OE1 GLU F 134                MN    MN F 403     1555   1555  2.14  
LINK         OE1 GLU F 134                MN    MN F 402     1555   1555  2.49  
LINK         OE2 GLU F 134                MN    MN F 402     1555   1555  2.40  
LINK         OE2 GLU F 136                MN    MN F 401     1555   1555  2.19  
LINK         OE1 GLU F 196                MN    MN F 401     1555   1555  2.14  
LINK         OE1 GLU F 203                MN    MN F 401     1555   1555  2.13  
LINK         OE2 GLU F 203                MN    MN F 403     1555   1555  2.18  
LINK         OE2 GLU F 338                MN    MN F 402     1555   1555  1.85  
LINK         OE1 GLU G 134                MN    MN G 402     1555   1555  2.36  
LINK         OE1 GLU G 134                MN    MN G 403     1555   1555  2.34  
LINK         OE2 GLU G 134                MN    MN G 402     1555   1555  2.33  
LINK         OE2 GLU G 136                MN    MN G 401     1555   1555  2.27  
LINK         OE1 GLU G 196                MN    MN G 401     1555   1555  2.31  
LINK         OE1 GLU G 203                MN    MN G 401     1555   1555  2.08  
LINK         OE2 GLU G 203                MN    MN G 403     1555   1555  2.14  
LINK         OE2 GLU G 338                MN    MN G 402     1555   1555  2.05  
LINK         OE1 GLU H 134                MN    MN H 402     1555   1555  2.39  
LINK         OE1 GLU H 134                MN    MN H 403     1555   1555  2.14  
LINK         OE2 GLU H 134                MN    MN H 402     1555   1555  2.15  
LINK         OE2 GLU H 136                MN    MN H 401     1555   1555  2.16  
LINK         OE1 GLU H 196                MN    MN H 401     1555   1555  2.22  
LINK         OE1 GLU H 203                MN    MN H 401     1555   1555  2.03  
LINK         OE2 GLU H 203                MN    MN H 403     1555   1555  2.27  
LINK         OE2 GLU H 338                MN    MN H 402     1555   1555  2.13  
LINK         OE1 GLU I 134                MN    MN I 402     1555   1555  2.40  
LINK         OE1 GLU I 134                MN    MN I 403     1555   1555  2.05  
LINK         OE2 GLU I 134                MN    MN I 402     1555   1555  2.33  
LINK         OE2 GLU I 136                MN    MN I 401     1555   1555  2.26  
LINK         OE1 GLU I 196                MN    MN I 401     1555   1555  2.38  
LINK         OE1 GLU I 203                MN    MN I 401     1555   1555  2.04  
LINK         OE2 GLU I 203                MN    MN I 403     1555   1555  2.22  
LINK         OE2 GLU I 338                MN    MN I 402     1555   1555  1.95  
LINK         OE1 GLU J 134                MN    MN J 403     1555   1555  2.18  
LINK         OE2 GLU J 134                MN    MN J 402     1555   1555  2.32  
LINK         OE2 GLU J 136                MN    MN J 401     1555   1555  2.04  
LINK         OE1 GLU J 196                MN    MN J 401     1555   1555  2.48  
LINK         OE1 GLU J 203                MN    MN J 401     1555   1555  2.10  
LINK         OE2 GLU J 203                MN    MN J 403     1555   1555  2.31  
LINK         OE2 GLU J 338                MN    MN J 402     1555   1555  2.12  
LINK        MN    MN A 401                 O3A P3S A 601     1555   1555  2.40  
LINK        MN    MN A 401                 O   HOH A 704     1555   1555  2.05  
LINK        MN    MN A 402                 O3B ADP A 501     1555   1555  2.09  
LINK        MN    MN A 402                 O2A P3S A 601     1555   1555  2.00  
LINK        MN    MN A 403                 O   HOH A 729     1555   1555  2.06  
LINK        MN    MN A 403                 O1B ADP A 501     1555   1555  2.07  
LINK        MN    MN A 403                 O3A P3S A 601     1555   1555  1.99  
LINK        MN    MN A 403                 O2A ADP A 501     1555   1555  2.02  
LINK        MN    MN B 401                 O3A P3S B 601     1555   1555  2.26  
LINK        MN    MN B 401                 O   HOH B 744     1555   1555  2.13  
LINK        MN    MN B 402                 O2A P3S B 601     1555   1555  2.10  
LINK        MN    MN B 402                 O2B ADP B 501     1555   1555  2.07  
LINK        MN    MN B 403                 O3A P3S B 601     1555   1555  1.94  
LINK        MN    MN B 403                 O2A ADP B 501     1555   1555  2.12  
LINK        MN    MN B 403                 O   HOH B 741     1555   1555  2.42  
LINK        MN    MN B 403                 O3B ADP B 501     1555   1555  2.04  
LINK        MN    MN C 401                 O   HOH C 740     1555   1555  2.17  
LINK        MN    MN C 401                 O3A P3S C 601     1555   1555  2.07  
LINK        MN    MN C 402                 O2B ADP C 501     1555   1555  2.13  
LINK        MN    MN C 402                 O2A P3S C 601     1555   1555  2.01  
LINK        MN    MN C 403                 O3B ADP C 501     1555   1555  2.26  
LINK        MN    MN C 403                 O3A P3S C 601     1555   1555  2.19  
LINK        MN    MN C 403                 O   HOH C 738     1555   1555  2.27  
LINK        MN    MN C 403                 O2A ADP C 501     1555   1555  2.21  
LINK        MN    MN D 401                 O3A P3S D 601     1555   1555  2.21  
LINK        MN    MN D 402                 O2A P3S D 601     1555   1555  2.16  
LINK        MN    MN D 402                 O2B ADP D 501     1555   1555  2.27  
LINK        MN    MN D 403                 O3A P3S D 601     1555   1555  1.93  
LINK        MN    MN D 403                 O2A ADP D 501     1555   1555  2.14  
LINK        MN    MN D 403                 O3B ADP D 501     1555   1555  2.01  
LINK        MN    MN D 403                 O   HOH D 747     1555   1555  2.42  
LINK        MN    MN E 401                 O3A P3S E 601     1555   1555  2.14  
LINK        MN    MN E 401                 O   HOH E 629     1555   1555  2.10  
LINK        MN    MN E 402                 O2A P3S E 601     1555   1555  2.11  
LINK        MN    MN E 402                 O2B ADP E 501     1555   1555  2.10  
LINK        MN    MN E 403                 O3A P3S E 601     1555   1555  2.10  
LINK        MN    MN E 403                 O3B ADP E 501     1555   1555  2.03  
LINK        MN    MN E 403                 O   HOH E 627     1555   1555  2.17  
LINK        MN    MN E 403                 O2A ADP E 501     1555   1555  2.28  
LINK        MN    MN F 402                 O2B ADP F 501     1555   1555  2.12  
LINK        MN    MN F 402                 O2A P3S F 601     1555   1555  2.44  
LINK        MN    MN F 403                 O   HOH F 717     1555   1555  1.88  
LINK        MN    MN F 403                 O2A ADP F 501     1555   1555  2.21  
LINK        MN    MN F 403                 O3B ADP F 501     1555   1555  2.01  
LINK        MN    MN F 403                 O3A P3S F 601     1555   1555  1.87  
LINK        MN    MN G 402                 O2B ADP G 501     1555   1555  2.21  
LINK        MN    MN G 402                 O2A P3S G 601     1555   1555  2.21  
LINK        MN    MN G 403                 O2A ADP G 501     1555   1555  2.23  
LINK        MN    MN G 403                 O3B ADP G 501     1555   1555  1.92  
LINK        MN    MN G 403                 O3A P3S G 601     1555   1555  2.00  
LINK        MN    MN H 401                 O   HOH H 609     1555   1555  2.35  
LINK        MN    MN H 401                 O3A P3S H 601     1555   1555  2.22  
LINK        MN    MN H 402                 O2B ADP H 501     1555   1555  2.25  
LINK        MN    MN H 402                 O2A P3S H 601     1555   1555  2.02  
LINK        MN    MN H 403                 O3B ADP H 501     1555   1555  2.26  
LINK        MN    MN H 403                 O2A ADP H 501     1555   1555  2.25  
LINK        MN    MN H 403                 O   HOH H 608     1555   1555  1.90  
LINK        MN    MN H 403                 O3A P3S H 601     1555   1555  2.17  
LINK        MN    MN I 401                 O3A P3S I 601     1555   1555  2.25  
LINK        MN    MN I 402                 O2B ADP I 501     1555   1555  2.26  
LINK        MN    MN I 402                 O2A P3S I 601     1555   1555  2.42  
LINK        MN    MN I 403                 O   HOH I 718     1555   1555  2.19  
LINK        MN    MN I 403                 O2A ADP I 501     1555   1555  2.25  
LINK        MN    MN I 403                 O3B ADP I 501     1555   1555  2.00  
LINK        MN    MN I 403                 O3A P3S I 601     1555   1555  1.99  
LINK        MN    MN J 401                 O3A P3S J 601     1555   1555  2.25  
LINK        MN    MN J 401                 O   HOH J 718     1555   1555  2.14  
LINK        MN    MN J 402                 O2A P3S J 601     1555   1555  2.34  
LINK        MN    MN J 402                 O3B ADP J 501     1555   1555  2.16  
LINK        MN    MN J 403                 O   HOH J 717     1555   1555  2.08  
LINK        MN    MN J 403                 O2A ADP J 501     1555   1555  2.33  
LINK        MN    MN J 403                 O1B ADP J 501     1555   1555  2.02  
LINK        MN    MN J 403                 O3A P3S J 601     1555   1555  2.02  
LINK        MN    MN A 401                 NE  P3S A 601     1555   1555  2.22  
LINK        MN    MN A 402                 ND1 HIS A 253     1555   1555  2.41  
LINK        MN    MN B 401                 NE  P3S B 601     1555   1555  2.36  
LINK        MN    MN B 402                 ND1 HIS B 253     1555   1555  2.34  
LINK        MN    MN C 401                 NE  P3S C 601     1555   1555  2.71  
LINK        MN    MN C 402                 ND1 HIS C 253     1555   1555  2.31  
LINK        MN    MN D 401                 NE  P3S D 601     1555   1555  2.31  
LINK        MN    MN D 402                 ND1 HIS D 253     1555   1555  2.37  
LINK        MN    MN E 401                 NE  P3S E 601     1555   1555  2.51  
LINK        MN    MN E 402                 ND1 HIS E 253     1555   1555  2.25  
LINK        MN    MN F 401                 NE  P3S F 601     1555   1555  2.32  
LINK        MN    MN F 401                 O3A P3S F 601     1555   1555  2.56  
LINK        MN    MN F 402                 ND1 HIS F 253     1555   1555  2.26  
LINK        MN    MN G 401                 NE  P3S G 601     1555   1555  2.30  
LINK        MN    MN G 401                 O3A P3S G 601     1555   1555  2.57  
LINK        MN    MN G 402                 ND1 HIS G 253     1555   1555  2.53  
LINK        MN    MN H 401                 NE  P3S H 601     1555   1555  2.56  
LINK        MN    MN H 402                 ND1 HIS H 253     1555   1555  2.17  
LINK        MN    MN I 401                 NE  P3S I 601     1555   1555  2.48  
LINK        MN    MN I 402                 ND1 HIS I 253     1555   1555  2.32  
LINK        MN    MN J 401                 NE  P3S J 601     1555   1555  2.49  
LINK        MN    MN J 402                 ND1 HIS J 253     1555   1555  2.17  
LINK        MN    MN J 402                 OE1 GLU J 134     1555   1555  2.57  
CISPEP   1 ASP A   92    PRO A   93          0        16.56                     
CISPEP   2 GLY A  207    PRO A  208          0        -1.59                     
CISPEP   3 ASP B   92    PRO B   93          0        13.15                     
CISPEP   4 GLY B  207    PRO B  208          0        -3.46                     
CISPEP   5 ASP C   92    PRO C   93          0        15.89                     
CISPEP   6 GLY C  207    PRO C  208          0        -3.97                     
CISPEP   7 ASP D   92    PRO D   93          0        16.78                     
CISPEP   8 GLY D  207    PRO D  208          0       -10.47                     
CISPEP   9 ASP E   92    PRO E   93          0        22.04                     
CISPEP  10 GLY E  207    PRO E  208          0        -6.74                     
CISPEP  11 ASP F   92    PRO F   93          0        14.75                     
CISPEP  12 GLY F  207    PRO F  208          0        -4.04                     
CISPEP  13 ASP G   92    PRO G   93          0        15.58                     
CISPEP  14 GLY G  207    PRO G  208          0        -2.75                     
CISPEP  15 ASP H   92    PRO H   93          0        22.67                     
CISPEP  16 GLY H  207    PRO H  208          0        -1.96                     
CISPEP  17 ASP I   92    PRO I   93          0        21.59                     
CISPEP  18 GLY I  207    PRO I  208          0        -5.35                     
CISPEP  19 ASP J   92    PRO J   93          0        20.72                     
CISPEP  20 GLY J  207    PRO J  208          0        -3.20                     
SITE     1 AC1  6 GLU A 136  GLU A 196  GLU A 203   MN A 403                    
SITE     2 AC1  6 P3S A 601  HOH A 704                                          
SITE     1 AC2  6 GLU A 134  HIS A 253  GLU A 338  ARG A 340                    
SITE     2 AC2  6 ADP A 501  P3S A 601                                          
SITE     1 AC3  6 GLU A 134  GLU A 203   MN A 401  ADP A 501                    
SITE     2 AC3  6 P3S A 601  HOH A 729                                          
SITE     1 AC4  6 GLU B 136  GLU B 196  GLU B 203   MN B 403                    
SITE     2 AC4  6 P3S B 601  HOH B 744                                          
SITE     1 AC5  7 GLU B 134  HIS B 253  GLU B 338  ARG B 340                    
SITE     2 AC5  7  MN B 403  ADP B 501  P3S B 601                               
SITE     1 AC6  7 GLU B 134  GLU B 203   MN B 401   MN B 402                    
SITE     2 AC6  7 ADP B 501  P3S B 601  HOH B 741                               
SITE     1 AC7  6 GLU C 136  GLU C 196  GLU C 203   MN C 403                    
SITE     2 AC7  6 P3S C 601  HOH C 740                                          
SITE     1 AC8  6 GLU C 134  HIS C 253  GLU C 338  ARG C 340                    
SITE     2 AC8  6 ADP C 501  P3S C 601                                          
SITE     1 AC9  6 GLU C 134  GLU C 203   MN C 401  ADP C 501                    
SITE     2 AC9  6 P3S C 601  HOH C 738                                          
SITE     1 BC1  5 GLU D 136  GLU D 196  GLU D 203   MN D 403                    
SITE     2 BC1  5 P3S D 601                                                     
SITE     1 BC2  5 GLU D 134  HIS D 253  GLU D 338  ADP D 501                    
SITE     2 BC2  5 P3S D 601                                                     
SITE     1 BC3  6 GLU D 134  GLU D 203   MN D 401  ADP D 501                    
SITE     2 BC3  6 P3S D 601  HOH D 747                                          
SITE     1 BC4  5 GLU E 136  GLU E 196  GLU E 203  P3S E 601                    
SITE     2 BC4  5 HOH E 629                                                     
SITE     1 BC5  6 GLU E 134  HIS E 253  GLU E 338  ARG E 340                    
SITE     2 BC5  6 ADP E 501  P3S E 601                                          
SITE     1 BC6  5 GLU E 134  GLU E 203  ADP E 501  P3S E 601                    
SITE     2 BC6  5 HOH E 627                                                     
SITE     1 BC7  5 GLU F 136  GLU F 196  GLU F 203   MN F 403                    
SITE     2 BC7  5 P3S F 601                                                     
SITE     1 BC8  6 GLU F 134  HIS F 253  GLU F 338  ARG F 340                    
SITE     2 BC8  6 ADP F 501  P3S F 601                                          
SITE     1 BC9  6 GLU F 134  GLU F 203   MN F 401  ADP F 501                    
SITE     2 BC9  6 P3S F 601  HOH F 717                                          
SITE     1 CC1  5 GLU G 136  GLU G 196  GLU G 203   MN G 403                    
SITE     2 CC1  5 P3S G 601                                                     
SITE     1 CC2  5 GLU G 134  HIS G 253  GLU G 338  ADP G 501                    
SITE     2 CC2  5 P3S G 601                                                     
SITE     1 CC3  5 GLU G 134  GLU G 203   MN G 401  ADP G 501                    
SITE     2 CC3  5 P3S G 601                                                     
SITE     1 CC4  6 GLU H 136  GLU H 196  GLU H 203   MN H 403                    
SITE     2 CC4  6 P3S H 601  HOH H 609                                          
SITE     1 CC5  6 GLU H 134  HIS H 253  GLU H 338   MN H 403                    
SITE     2 CC5  6 ADP H 501  P3S H 601                                          
SITE     1 CC6  7 GLU H 134  GLU H 203   MN H 401   MN H 402                    
SITE     2 CC6  7 ADP H 501  P3S H 601  HOH H 608                               
SITE     1 CC7  5 GLU I 136  GLU I 196  GLU I 203   MN I 403                    
SITE     2 CC7  5 P3S I 601                                                     
SITE     1 CC8  6 GLU I 134  HIS I 253  GLU I 338  ARG I 340                    
SITE     2 CC8  6 ADP I 501  P3S I 601                                          
SITE     1 CC9  6 GLU I 134  GLU I 203   MN I 401  ADP I 501                    
SITE     2 CC9  6 P3S I 601  HOH I 718                                          
SITE     1 DC1  6 GLU J 136  GLU J 196  GLU J 203   MN J 403                    
SITE     2 DC1  6 P3S J 601  HOH J 718                                          
SITE     1 DC2  5 GLU J 134  HIS J 253  GLU J 338  ADP J 501                    
SITE     2 DC2  5 P3S J 601                                                     
SITE     1 DC3  6 GLU J 134  GLU J 203   MN J 401  ADP J 501                    
SITE     2 DC3  6 P3S J 601  HOH J 717                                          
SITE     1 DC4  3 MET B  29  THR B  44  THR C 193                               
SITE     1 DC5  4 MET C  29  THR C  44  THR D 193  HOH D 731                    
SITE     1 DC6  3 THR A 193  MET E  29  THR E  44                               
SITE     1 DC7  2 THR D  44  THR E 193                                          
SITE     1 DC8  3 MET A  29  THR A  44  THR B 193                               
SITE     1 DC9  2 THR F 193  THR J  44                                          
SITE     1 EC1  2 THR F  44  THR G 193                                          
SITE     1 EC2  4 MET G  29  LYS G  43  THR G  44  THR H 193                    
SITE     1 EC3  2 THR H  44  THR I 193                                          
SITE     1 EC4  2 THR I  44  THR J 193                                          
SITE     1 EC5 20 TRP A 130  GLY A 132  GLU A 134  GLU A 203                    
SITE     2 EC5 20 GLN A 205  GLY A 207  PRO A 208  ASN A 255                    
SITE     3 EC5 20 SER A 257  ARG A 262  ARG A 319  ARG A 324                    
SITE     4 EC5 20 TYR A 336  GLU A 338   MN A 402   MN A 403                    
SITE     5 EC5 20 P3S A 601  HOH A 729  HOH A 730  HOH A 731                    
SITE     1 EC6 20 GLU A 134  GLU A 136  GLU A 196  GLU A 203                    
SITE     2 EC6 20 GLY A 249  HIS A 253  ARG A 299  GLU A 305                    
SITE     3 EC6 20 THR A 306  ARG A 319  GLU A 338  ARG A 340                    
SITE     4 EC6 20  MN A 401   MN A 402   MN A 403  ADP A 501                    
SITE     5 EC6 20 HOH A 704  HOH A 729  HOH A 733  ASP E  63                    
SITE     1 EC7 19 HOH A 732  TRP B 130  GLY B 132  GLU B 134                    
SITE     2 EC7 19 GLU B 203  GLN B 205  ILE B 206  GLY B 207                    
SITE     3 EC7 19 PRO B 208  ASN B 255  SER B 257  ARG B 319                    
SITE     4 EC7 19 ARG B 324  TYR B 336  GLU B 338   MN B 402                    
SITE     5 EC7 19  MN B 403  P3S B 601  HOH B 742                               
SITE     1 EC8 20 ASP A  63  GLU B 134  GLU B 136  TYR B 162                    
SITE     2 EC8 20 GLU B 196  GLU B 203  GLY B 249  HIS B 253                    
SITE     3 EC8 20 ARG B 299  GLU B 305  THR B 306  ARG B 319                    
SITE     4 EC8 20 GLU B 338  ARG B 340   MN B 401   MN B 402                    
SITE     5 EC8 20  MN B 403  ADP B 501  HOH B 718  HOH B 744                    
SITE     1 EC9 19 TRP C 130  GLY C 132  GLU C 134  GLU C 203                    
SITE     2 EC9 19 GLN C 205  GLY C 207  PRO C 208  ASN C 255                    
SITE     3 EC9 19 SER C 257  ARG C 324  TYR C 336  GLU C 338                    
SITE     4 EC9 19  MN C 402   MN C 403  P3S C 601  HOH C 709                    
SITE     5 EC9 19 HOH C 736  HOH C 738  HOH C 739                               
SITE     1 FC1 21 ASP B  63  GLU C 134  GLU C 136  TYR C 162                    
SITE     2 FC1 21 GLU C 196  GLU C 203  GLY C 249  HIS C 253                    
SITE     3 FC1 21 ARG C 299  GLU C 305  THR C 306  ARG C 319                    
SITE     4 FC1 21 GLU C 338  ARG C 340   MN C 401   MN C 402                    
SITE     5 FC1 21  MN C 403  ADP C 501  HOH C 704  HOH C 730                    
SITE     6 FC1 21 HOH C 740                                                     
SITE     1 FC2 18 HOH C 707  TRP D 130  GLY D 132  GLU D 134                    
SITE     2 FC2 18 GLU D 203  GLN D 205  GLY D 207  PRO D 208                    
SITE     3 FC2 18 ASN D 255  SER D 257  ARG D 319  ARG D 324                    
SITE     4 FC2 18 TYR D 336  GLU D 338   MN D 402   MN D 403                    
SITE     5 FC2 18 P3S D 601  HOH D 747                                          
SITE     1 FC3 18 ASP C  63  GLU D 134  GLU D 136  GLU D 196                    
SITE     2 FC3 18 GLU D 203  GLY D 249  HIS D 253  ARG D 299                    
SITE     3 FC3 18 GLU D 305  THR D 306  ARG D 319  GLU D 338                    
SITE     4 FC3 18 ARG D 340   MN D 401   MN D 402   MN D 403                    
SITE     5 FC3 18 ADP D 501  HOH D 711                                          
SITE     1 FC4 20 HOH D 749  TRP E 130  GLY E 132  GLU E 134                    
SITE     2 FC4 20 GLU E 203  GLN E 205  GLY E 207  PRO E 208                    
SITE     3 FC4 20 ASN E 255  SER E 257  ARG E 319  ARG E 324                    
SITE     4 FC4 20 TYR E 336  GLU E 338   MN E 402   MN E 403                    
SITE     5 FC4 20 P3S E 601  HOH E 624  HOH E 627  HOH E 628                    
SITE     1 FC5 18 ASP D  63  GLU E 134  GLU E 136  GLU E 196                    
SITE     2 FC5 18 GLU E 203  GLY E 249  HIS E 253  ARG E 299                    
SITE     3 FC5 18 GLU E 305  THR E 306  ARG E 319  GLU E 338                    
SITE     4 FC5 18 ARG E 340   MN E 401   MN E 402   MN E 403                    
SITE     5 FC5 18 ADP E 501  HOH E 629                                          
SITE     1 FC6 20 TRP F 130  GLY F 132  GLU F 134  ALA F 191                    
SITE     2 FC6 20 GLU F 203  GLN F 205  ILE F 206  GLY F 207                    
SITE     3 FC6 20 PRO F 208  ASN F 255  SER F 257  ARG F 319                    
SITE     4 FC6 20 ARG F 324  TYR F 336  GLU F 338   MN F 402                    
SITE     5 FC6 20  MN F 403  P3S F 601  HOH F 717  HOH F 718                    
SITE     1 FC7 18 GLU F 134  GLU F 136  GLU F 196  GLU F 203                    
SITE     2 FC7 18 GLY F 249  HIS F 253  ARG F 299  GLU F 305                    
SITE     3 FC7 18 THR F 306  ARG F 319  ARG F 340   MN F 401                    
SITE     4 FC7 18  MN F 402   MN F 403  ADP F 501  HOH F 712                    
SITE     5 FC7 18 HOH F 717  ASP J  63                                          
SITE     1 FC8 18 TRP G 130  GLY G 132  GLU G 134  ALA G 191                    
SITE     2 FC8 18 GLU G 203  GLN G 205  ILE G 206  GLY G 207                    
SITE     3 FC8 18 PRO G 208  ASN G 255  SER G 257  ARG G 319                    
SITE     4 FC8 18 ARG G 324  TYR G 336  GLU G 338   MN G 402                    
SITE     5 FC8 18  MN G 403  P3S G 601                                          
SITE     1 FC9 18 ASP F  63  GLU G 134  GLU G 136  GLU G 196                    
SITE     2 FC9 18 GLU G 203  ASN G 248  GLY G 249  HIS G 253                    
SITE     3 FC9 18 ARG G 299  GLU G 305  THR G 306  ARG G 319                    
SITE     4 FC9 18 GLU G 338  ARG G 340   MN G 401   MN G 402                    
SITE     5 FC9 18  MN G 403  ADP G 501                                          
SITE     1 GC1 17 GLY H 132  GLU H 134  ALA H 191  GLU H 203                    
SITE     2 GC1 17 GLN H 205  GLY H 207  PRO H 208  ASN H 255                    
SITE     3 GC1 17 SER H 257  ARG H 319  ARG H 324  TYR H 336                    
SITE     4 GC1 17 GLU H 338   MN H 402   MN H 403  P3S H 601                    
SITE     5 GC1 17 HOH H 608                                                     
SITE     1 GC2 18 ASP G  63  GLU H 134  GLU H 136  TYR H 162                    
SITE     2 GC2 18 GLU H 196  GLU H 203  GLY H 249  HIS H 253                    
SITE     3 GC2 18 ARG H 299  GLU H 305  ARG H 319  GLU H 338                    
SITE     4 GC2 18 ARG H 340   MN H 401   MN H 402   MN H 403                    
SITE     5 GC2 18 ADP H 501  HOH H 608                                          
SITE     1 GC3 19 TRP I 130  GLY I 132  GLU I 134  GLU I 203                    
SITE     2 GC3 19 GLN I 205  ILE I 206  GLY I 207  PRO I 208                    
SITE     3 GC3 19 ASN I 255  SER I 257  ARG I 319  ARG I 324                    
SITE     4 GC3 19 TYR I 336  GLU I 338   MN I 402   MN I 403                    
SITE     5 GC3 19 P3S I 601  HOH I 718  HOH I 719                               
SITE     1 GC4 19 ASP H  63  GLU I 134  GLU I 136  GLU I 196                    
SITE     2 GC4 19 GLU I 203  ASN I 248  GLY I 249  GLY I 251                    
SITE     3 GC4 19 HIS I 253  ARG I 299  GLU I 305  ARG I 319                    
SITE     4 GC4 19 ARG I 324  GLU I 338  ARG I 340   MN I 401                    
SITE     5 GC4 19  MN I 402   MN I 403  ADP I 501                               
SITE     1 GC5 18 TRP J 130  GLY J 132  GLU J 134  ALA J 191                    
SITE     2 GC5 18 GLU J 203  GLN J 205  GLY J 207  PRO J 208                    
SITE     3 GC5 18 ASN J 255  SER J 257  ARG J 319  ARG J 324                    
SITE     4 GC5 18 TYR J 336  GLU J 338   MN J 402   MN J 403                    
SITE     5 GC5 18 P3S J 601  HOH J 717                                          
SITE     1 GC6 20 ASP I  63  GLU J 134  GLU J 136  TYR J 162                    
SITE     2 GC6 20 GLU J 196  GLU J 203  GLY J 249  HIS J 253                    
SITE     3 GC6 20 ARG J 299  GLU J 305  THR J 306  ARG J 319                    
SITE     4 GC6 20 GLU J 338  ARG J 340   MN J 401   MN J 402                    
SITE     5 GC6 20  MN J 403  ADP J 501  HOH J 714  HOH J 718                    
CRYST1  181.210  126.080  188.170  90.00  92.14  90.00 C 1 2 1      40          
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      0.005518  0.000000  0.000206        0.00000                         
SCALE2      0.000000  0.007931  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005318        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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