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Database: PDB
Entry: 4OVN
LinkDB: 4OVN
Original site: 4OVN 
HEADER    METAL BINDING PROTEIN                   10-DEC-13   4OVN              
TITLE     VOLTAGE-GATED SODIUM CHANNEL 1.5 (NAV1.5) C-TERMINAL DOMAIN IN COMPLEX
TITLE    2 WITH CALMODULIN POISED FOR ACTIVATION                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 SYNONYM: CAM;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: SODIUM CHANNEL PROTEIN TYPE 5 SUBUNIT ALPHA;               
COMPND   8 CHAIN: F, G, H, I, J;                                                
COMPND   9 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUE 1773-1929);                 
COMPND  10 SYNONYM: HH1,SODIUM CHANNEL PROTEIN CARDIAC MUSCLE SUBUNIT ALPHA,    
COMPND  11 SODIUM CHANNEL PROTEIN TYPE V SUBUNIT ALPHA,VOLTAGE-GATED SODIUM     
COMPND  12 CHANNEL SUBUNIT ALPHA NAV1.5;                                        
COMPND  13 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: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,      
SOURCE   6 CAM3, CAMC, CAMIII;                                                  
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET24;                                    
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: SCN5A;                                                         
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1                                 
KEYWDS    SCN5A, VOLTAGE GATED SODIUM CHANNEL, CALMODULIN, METAL BINDING        
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.B.GABELLI,M.A.BIANCHET,A.BOTO,J.JAKONCIC,G.F.TOMASELLI,L.M.AMZEL    
REVDAT   6   27-DEC-23 4OVN    1       LINK                                     
REVDAT   5   04-DEC-19 4OVN    1       REMARK                                   
REVDAT   4   27-SEP-17 4OVN    1       SOURCE REMARK                            
REVDAT   3   08-APR-15 4OVN    1       REMARK                                   
REVDAT   2   10-DEC-14 4OVN    1       REMARK                                   
REVDAT   1   03-DEC-14 4OVN    0                                                
JRNL        AUTH   S.B.GABELLI,A.BOTO,V.H.KUHNS,M.A.BIANCHET,F.FARINELLI,       
JRNL        AUTH 2 S.ARIPIRALA,J.YODER,J.JAKONCIC,G.F.TOMASELLI,L.M.AMZEL       
JRNL        TITL   REGULATION OF THE NAV1.5 CYTOPLASMIC DOMAIN BY CALMODULIN.   
JRNL        REF    NAT COMMUN                    V.   5  5126 2014              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   25370050                                                     
JRNL        DOI    10.1038/NCOMMS6126                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.570                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 92851                          
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) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4588                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 30                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.83                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1694                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 52.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 91                           
REMARK   3   BIN FREE R VALUE                    : 0.4318                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11669                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 53                                      
REMARK   3   SOLVENT ATOMS            : 62                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 77.01                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 93.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.480         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : NULL                              
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     4        A   148                          
REMARK   3    ORIGIN FOR THE GROUP (A):  96.0027  20.0391  14.9656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6199 T22:   0.7918                                     
REMARK   3      T33:   0.8494 T12:   0.0241                                     
REMARK   3      T13:   0.0242 T23:   0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2472 L22:   1.1519                                     
REMARK   3      L33:   1.2544 L12:  -0.1763                                     
REMARK   3      L13:  -0.3457 L23:   0.2233                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0199 S12:  -0.0536 S13:   0.3706                       
REMARK   3      S21:  -0.1441 S22:   0.0583 S23:  -0.2979                       
REMARK   3      S31:   0.0457 S32:   0.2834 S33:   0.0001                       
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 :   F  1782        F  1927                          
REMARK   3    ORIGIN FOR THE GROUP (A):  87.2731  35.1310  26.2727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6254 T22:   0.7156                                     
REMARK   3      T33:   0.9960 T12:  -0.0447                                     
REMARK   3      T13:  -0.0360 T23:  -0.0948                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5639 L22:   1.6978                                     
REMARK   3      L33:   1.2404 L12:  -0.4476                                     
REMARK   3      L13:  -0.6387 L23:   0.8350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0778 S12:  -0.0981 S13:   0.5384                       
REMARK   3      S21:   0.1282 S22:   0.1511 S23:  -0.2335                       
REMARK   3      S31:  -0.0856 S32:   0.2770 S33:  -0.0000                       
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 :   B     5        B   148                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.6924  50.6890  24.7351              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9796 T22:   0.8584                                     
REMARK   3      T33:   0.8955 T12:  -0.1064                                     
REMARK   3      T13:   0.1772 T23:  -0.0845                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3169 L22:   2.4577                                     
REMARK   3      L33:   0.2897 L12:   0.1627                                     
REMARK   3      L13:  -0.1910 L23:   0.7805                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1718 S12:   0.4368 S13:  -0.0324                       
REMARK   3      S21:  -0.4677 S22:   0.3175 S23:  -0.3596                       
REMARK   3      S31:  -0.0684 S32:   0.0466 S33:  -0.0000                       
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 :   G  1783        G  1926                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.8549  38.5329  23.8563              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8268 T22:   0.7484                                     
REMARK   3      T33:   0.6209 T12:  -0.0560                                     
REMARK   3      T13:  -0.0301 T23:  -0.0605                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2859 L22:   1.2155                                     
REMARK   3      L33:   0.5794 L12:   0.2376                                     
REMARK   3      L13:   0.1840 L23:   0.4699                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0937 S12:   0.2908 S13:   0.1375                       
REMARK   3      S21:  -0.3480 S22:   0.1304 S23:  -0.1982                       
REMARK   3      S31:  -0.0939 S32:  -0.0080 S33:  -0.0000                       
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 :   C     4        C   148                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1423  47.0720  76.5033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7894 T22:   0.7900                                     
REMARK   3      T33:   0.7351 T12:  -0.0183                                     
REMARK   3      T13:  -0.0007 T23:  -0.0674                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4464 L22:   1.6366                                     
REMARK   3      L33:   1.6185 L12:  -0.3555                                     
REMARK   3      L13:  -0.7068 L23:  -0.6544                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2538 S12:  -0.0846 S13:   0.0254                       
REMARK   3      S21:   0.1148 S22:   0.2349 S23:  -0.2133                       
REMARK   3      S31:   0.1512 S32:   0.1750 S33:  -0.0001                       
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 :   H  1778        H  1927                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.8519  49.5181  71.5899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7398 T22:   0.8518                                     
REMARK   3      T33:   0.5421 T12:  -0.1180                                     
REMARK   3      T13:  -0.0451 T23:   0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9905 L22:   1.6722                                     
REMARK   3      L33:   0.6848 L12:  -0.5253                                     
REMARK   3      L13:  -0.2055 L23:  -0.6265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1071 S12:   0.2591 S13:   0.3587                       
REMARK   3      S21:  -0.2232 S22:   0.2175 S23:   0.0072                       
REMARK   3      S31:   0.1116 S32:  -0.1132 S33:  -0.0001                       
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 :   D     4        D   148                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.5196  15.0182  43.4544              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8119 T22:   0.7112                                     
REMARK   3      T33:   0.7852 T12:  -0.0615                                     
REMARK   3      T13:  -0.0150 T23:  -0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8448 L22:   0.9999                                     
REMARK   3      L33:   1.4633 L12:  -0.4697                                     
REMARK   3      L13:   0.4363 L23:  -0.5602                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1040 S12:   0.0792 S13:  -0.1456                       
REMARK   3      S21:  -0.3489 S22:   0.1069 S23:   0.0953                       
REMARK   3      S31:   0.4328 S32:  -0.0273 S33:   0.0000                       
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 :   I  1784        I  1926                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.4434  22.6455  62.4738              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6173 T22:   0.6140                                     
REMARK   3      T33:   0.6895 T12:   0.0432                                     
REMARK   3      T13:  -0.0445 T23:  -0.0255                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7525 L22:   0.6649                                     
REMARK   3      L33:   2.4367 L12:  -0.1704                                     
REMARK   3      L13:   0.5509 L23:  -0.5404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1072 S12:  -0.1044 S13:   0.1054                       
REMARK   3      S21:   0.1740 S22:   0.1082 S23:   0.2269                       
REMARK   3      S31:   0.0936 S32:   0.1841 S33:  -0.0000                       
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 :   E     5        E   148                          
REMARK   3    ORIGIN FOR THE GROUP (A): 100.4409  30.0996 -35.7531              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8378 T22:   1.0931                                     
REMARK   3      T33:   0.8827 T12:  -0.0166                                     
REMARK   3      T13:   0.0193 T23:   0.2116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1343 L22:   1.7072                                     
REMARK   3      L33:   1.1196 L12:   0.9215                                     
REMARK   3      L13:   0.1301 L23:  -0.6108                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2287 S12:   0.8539 S13:   0.2898                       
REMARK   3      S21:  -0.4364 S22:   0.0820 S23:   0.1597                       
REMARK   3      S31:   0.2937 S32:   0.1849 S33:   0.0000                       
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  1776        J  1926                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.9255  18.5753 -18.9198              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6952 T22:   0.7088                                     
REMARK   3      T33:   0.6244 T12:  -0.0040                                     
REMARK   3      T13:  -0.0628 T23:   0.0200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3719 L22:   1.0020                                     
REMARK   3      L33:   1.1741 L12:   1.0955                                     
REMARK   3      L13:  -0.6613 L23:  -0.5375                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0931 S12:   0.2825 S13:  -0.0262                       
REMARK   3      S21:  -0.0528 S22:   0.1054 S23:   0.1738                       
REMARK   3      S31:   0.2563 S32:   0.0254 S33:  -0.0001                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : FLAT BULK SOLVENT MODEL                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.11                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4OVN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200030.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48516                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.798                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.3                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 58.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4K, 0.2 M MGSO4 AND 10%          
REMARK 280  GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       49.50300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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     MSE A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     LYS A   149                                                      
REMARK 465     GLU F  1773                                                      
REMARK 465     ASN F  1774                                                      
REMARK 465     PHE F  1775                                                      
REMARK 465     SER F  1776                                                      
REMARK 465     VAL F  1777                                                      
REMARK 465     ALA F  1778                                                      
REMARK 465     THR F  1779                                                      
REMARK 465     GLU F  1780                                                      
REMARK 465     GLU F  1781                                                      
REMARK 465     PHE F  1928                                                      
REMARK 465     ARG F  1929                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     LYS B   149                                                      
REMARK 465     GLU G  1773                                                      
REMARK 465     ASN G  1774                                                      
REMARK 465     PHE G  1775                                                      
REMARK 465     SER G  1776                                                      
REMARK 465     VAL G  1777                                                      
REMARK 465     ALA G  1778                                                      
REMARK 465     THR G  1779                                                      
REMARK 465     GLU G  1780                                                      
REMARK 465     GLU G  1781                                                      
REMARK 465     SER G  1782                                                      
REMARK 465     LEU G  1927                                                      
REMARK 465     PHE G  1928                                                      
REMARK 465     ARG G  1929                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ASP C     3                                                      
REMARK 465     LYS C   149                                                      
REMARK 465     GLU H  1773                                                      
REMARK 465     ASN H  1774                                                      
REMARK 465     PHE H  1775                                                      
REMARK 465     SER H  1776                                                      
REMARK 465     PHE H  1928                                                      
REMARK 465     ARG H  1929                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     ASP D     3                                                      
REMARK 465     LYS D   149                                                      
REMARK 465     GLU I  1773                                                      
REMARK 465     ASN I  1774                                                      
REMARK 465     PHE I  1775                                                      
REMARK 465     SER I  1776                                                      
REMARK 465     VAL I  1777                                                      
REMARK 465     ALA I  1778                                                      
REMARK 465     THR I  1779                                                      
REMARK 465     GLU I  1780                                                      
REMARK 465     GLU I  1781                                                      
REMARK 465     SER I  1782                                                      
REMARK 465     THR I  1783                                                      
REMARK 465     LEU I  1927                                                      
REMARK 465     PHE I  1928                                                      
REMARK 465     ARG I  1929                                                      
REMARK 465     MSE E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     ASP E     3                                                      
REMARK 465     GLN E     4                                                      
REMARK 465     LYS E   149                                                      
REMARK 465     GLU J  1773                                                      
REMARK 465     ASN J  1774                                                      
REMARK 465     PHE J  1775                                                      
REMARK 465     LEU J  1927                                                      
REMARK 465     PHE J  1928                                                      
REMARK 465     ARG J  1929                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN E   136    MG     MG E   202              1.39            
REMARK 500   OG   SER H  1925     H    PHE H  1926              1.46            
REMARK 500   O    GLU I  1823     H    ARG I  1826              1.48            
REMARK 500   OD2  ASP H  1846    HH12  ARG H  1898              1.50            
REMARK 500   O    ILE I  1827    HD22  ASN I  1831              1.51            
REMARK 500   HE   ARG A    87     OE1  GLU A   140              1.56            
REMARK 500   O    ILE D   101     H    VAL D   137              1.57            
REMARK 500   O    ILE B    10     H    LYS B    14              1.60            
REMARK 500   OG1  THR A    63     O    HOH A   301              1.68            
REMARK 500   OD1  ASP A    94     OD1  ASN A    98              2.00            
REMARK 500   O    LEU I  1854     OG1  THR I  1858              2.03            
REMARK 500   NH2  ARG A   107     OD1  ASP A   123              2.10            
REMARK 500   OD1  ASP B   130     OD1  ASP B   132              2.10            
REMARK 500   OD1  ASP E   130     OD1  ASP E   132              2.13            
REMARK 500   O    LEU J  1916     OG   SER J  1920              2.16            
REMARK 500   O    GLN A   136     O    HOH A   302              2.17            
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    PRO G1830   C   -  N   -  CD  ANGL. DEV. = -12.9 DEGREES          
REMARK 500    PRO G1891   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ASP C  21   OD1 -  CG  -  OD2 ANGL. DEV. =  20.1 DEGREES          
REMARK 500    ASP C  21   CB  -  CG  -  OD1 ANGL. DEV. =  -8.7 DEGREES          
REMARK 500    ASP C  21   CB  -  CG  -  OD2 ANGL. DEV. = -11.5 DEGREES          
REMARK 500    PRO H1824   C   -  N   -  CD  ANGL. DEV. = -15.4 DEGREES          
REMARK 500    PRO H1830   C   -  N   -  CD  ANGL. DEV. = -22.7 DEGREES          
REMARK 500    PRO I1830   C   -  N   -  CD  ANGL. DEV. = -21.4 DEGREES          
REMARK 500    PRO J1830   C   -  N   -  CD  ANGL. DEV. = -15.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A   7     -142.40   -135.77                                   
REMARK 500    SER A  82     -161.90    -71.63                                   
REMARK 500    ASP A  94       78.87   -105.70                                   
REMARK 500    GLU A 115       92.14    -64.20                                   
REMARK 500    GLN A 136      117.15   -164.56                                   
REMARK 500    MSE A 146       70.24   -102.54                                   
REMARK 500    THR A 147       37.60   -169.77                                   
REMARK 500    PRO F1785       84.44    -42.86                                   
REMARK 500    SER F1787       92.74    -57.34                                   
REMARK 500    ASP F1802       74.62   -110.15                                   
REMARK 500    SER F1812       55.01    -64.02                                   
REMARK 500    VAL F1813      -17.47    173.59                                   
REMARK 500    ALA F1820       13.08    -66.13                                   
REMARK 500    LYS F1829     -178.66    -63.29                                   
REMARK 500    PRO F1830       92.50     36.22                                   
REMARK 500    ASN F1831      -31.49   -135.08                                   
REMARK 500    LEU F1854      -74.86    -55.38                                   
REMARK 500    SER F1865      144.37   -179.43                                   
REMARK 500    ALA F1882       46.69    -84.53                                   
REMARK 500    SER F1888      101.94    -55.81                                   
REMARK 500    ILE F1892      -81.02    -84.85                                   
REMARK 500    SER F1925       67.84   -100.16                                   
REMARK 500    THR B   6     -131.86   -143.37                                   
REMARK 500    GLU B   7     -152.93   -135.48                                   
REMARK 500    LYS B  22      -78.50    -40.43                                   
REMARK 500    GLU B  32       41.18   -103.42                                   
REMARK 500    VAL B  56      -71.33    -66.02                                   
REMARK 500    ALA B  58       35.44    -91.16                                   
REMARK 500    ASP B  79     -158.39    -96.18                                   
REMARK 500    HIS B 108      -73.58    -63.03                                   
REMARK 500    GLU B 115       80.13    -45.77                                   
REMARK 500    MSE B 145       -7.40    -58.03                                   
REMARK 500    THR B 147       20.07   -145.00                                   
REMARK 500    GLU G1784     -134.82     66.07                                   
REMARK 500    SER G1812       11.66    -67.38                                   
REMARK 500    VAL G1813       -1.38   -145.18                                   
REMARK 500    LYS G1829     -164.61    -59.06                                   
REMARK 500    PRO G1830       83.16     29.15                                   
REMARK 500    GLN G1832      -68.74    -28.12                                   
REMARK 500    SER G1844      128.02    -38.87                                   
REMARK 500    SER G1885       44.02    -86.24                                   
REMARK 500    ARG G1897       -9.40    -56.46                                   
REMARK 500    ARG G1910      -73.82    -42.78                                   
REMARK 500    GLU C   8      -42.30     64.74                                   
REMARK 500    ASP C  25       26.87   -144.75                                   
REMARK 500    GLU C  46      -19.51    -45.18                                   
REMARK 500    ASP C  57       69.56   -115.30                                   
REMARK 500    ASP C  96       29.67   -150.65                                   
REMARK 500    ASP C 132      -74.93   -114.14                                   
REMARK 500    MSE C 146       54.40    -94.69                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     114 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS F 1829     PRO F 1830                 -135.72                    
REMARK 500 LYS G 1829     PRO G 1830                 -136.09                    
REMARK 500 GLU H 1823     PRO H 1824                 -135.44                    
REMARK 500 LYS H 1829     PRO H 1830                 -129.30                    
REMARK 500 GLU I 1823     PRO I 1824                 -147.24                    
REMARK 500 LYS I 1829     PRO I 1830                 -128.82                    
REMARK 500 LYS J 1829     PRO J 1830                 -130.67                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D1113        DISTANCE =  8.89 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  21   OD1                                                    
REMARK 620 2 ASP A  23   OD1  93.5                                              
REMARK 620 3 ASP A  25   OD1  86.0  88.0                                        
REMARK 620 4 THR A  27   O    87.3 177.8  94.1                                  
REMARK 620 5 HOH A 308   O    93.8  91.5 179.4  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  57   OD1                                                    
REMARK 620 2 THR A  63   O    85.4                                              
REMARK 620 3 THR A  63   OG1  87.1  86.4                                        
REMARK 620 4 GLU A  68   OE1 177.7  96.1  94.7                                  
REMARK 620 5 HOH A 301   O    91.3 135.1  48.7  88.9                            
REMARK 620 6 HOH A 304   O    95.1 136.8 136.8  82.6  88.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  94   OD1                                                    
REMARK 620 2 ASP A  96   OD1  87.8                                              
REMARK 620 3 ASN A  98   OD1  57.7  81.1                                        
REMARK 620 4 TYR A 100   O    95.5 171.9 106.9                                  
REMARK 620 5 HOH A 306   O   167.9  95.3 134.3  79.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 204  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 130   OD1                                                    
REMARK 620 2 ASP A 132   OD1  69.4                                              
REMARK 620 3 ASP A 134   OD1  92.7  72.9                                        
REMARK 620 4 GLN A 136   O   129.5 161.1 102.7                                  
REMARK 620 5 HOH A 302   O   164.7  95.3  81.6  65.8                            
REMARK 620 6 HOH A 305   O    95.0 102.8 169.2  78.1  89.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  21   OD1                                                    
REMARK 620 2 ASP B  23   OD1  94.5                                              
REMARK 620 3 ASP B  25   OD1  89.7  83.7                                        
REMARK 620 4 ASP B  25   OD2 137.1  81.6  47.4                                  
REMARK 620 5 THR B  27   O    85.7 176.5  99.8 100.7                            
REMARK 620 6 HOH B 303   O    90.8  95.0 178.7 132.0  81.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  94   OD1                                                    
REMARK 620 2 ASP B  96   OD1  92.7                                              
REMARK 620 3 ASN B  98   OD1  87.9  91.1                                        
REMARK 620 4 TYR B 100   O    84.8 177.5  88.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 130   OD1                                                    
REMARK 620 2 ASP B 132   OD1  60.8                                              
REMARK 620 3 ASP B 134   OD1  90.9  82.6                                        
REMARK 620 4 GLN B 136   O   134.1 165.0  97.2                                  
REMARK 620 5 HOH B 302   O    94.9  96.8 172.9  81.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  21   OD1                                                    
REMARK 620 2 ASP C  23   OD1  91.2                                              
REMARK 620 3 ASP C  25   OD1  86.5  81.4                                        
REMARK 620 4 THR C  27   O    90.3 178.3  99.4                                  
REMARK 620 5 HOH C 304   O   177.7  89.2  91.3  89.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C  63   O                                                      
REMARK 620 2 THR C  63   OG1  70.4                                              
REMARK 620 3 HOH C 301   O   136.8  66.4                                        
REMARK 620 4 HOH C 302   O    79.4  74.3  89.8                                  
REMARK 620 5 HOH C 303   O   103.7 114.2  93.0 171.5                            
REMARK 620 6 HOH C 305   O   154.4 135.2  68.8 105.6  68.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  65   OD1                                                    
REMARK 620 2 ASP D  65   OD2  87.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  94   OD1                                                    
REMARK 620 2 ASP C  96   OD1  92.7                                              
REMARK 620 3 ASN C  98   OD1  84.5  83.8                                        
REMARK 620 4 TYR C 100   O    87.7 179.4  95.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 204  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 130   OD1                                                    
REMARK 620 2 ASP C 132   OD1  87.0                                              
REMARK 620 3 ASP C 134   OD1  89.5  87.8                                        
REMARK 620 4 GLN C 136   O    93.0 179.7  92.5                                  
REMARK 620 5 HOH C 306   O    90.7  91.6 179.3  88.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  21   OD1                                                    
REMARK 620 2 ASP D  23   OD1  97.1                                              
REMARK 620 3 ASP D  25   OD1  88.2  83.3                                        
REMARK 620 4 THR D  27   O    82.2 177.7  98.9                                  
REMARK 620 5 HOH D1103   O    91.4  95.3 178.5  82.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR D  63   O                                                      
REMARK 620 2 THR D  63   OG1  91.5                                              
REMARK 620 3 HOH D1101   O    73.6 165.1                                        
REMARK 620 4 HOH D1104   O   175.7  84.2 110.7                                  
REMARK 620 5 HOH D1105   O    88.9  92.2  88.0  91.5                            
REMARK 620 6 HOH D1106   O    92.2  83.8  96.2  87.2 175.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  94   OD1                                                    
REMARK 620 2 ASP D  96   OD1  90.7                                              
REMARK 620 3 ASN D  98   OD1  88.2  84.6                                        
REMARK 620 4 TYR D 100   O    88.9 179.5  95.7                                  
REMARK 620 5 HOH D1108   O   179.4  89.7  91.4  90.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 204  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 130   OD1                                                    
REMARK 620 2 ASP D 132   OD1  89.1                                              
REMARK 620 3 ASP D 134   OD1  91.9  67.3                                        
REMARK 620 4 GLN D 136   O    90.3 179.0 111.9                                  
REMARK 620 5 HOH D1102   O   179.6  91.2  88.0  89.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  94   OD1                                                    
REMARK 620 2 ASP E  96   OD1  88.6                                              
REMARK 620 3 ASN E  98   OD1  89.9  87.8                                        
REMARK 620 4 TYR E 100   O    91.6 179.4  92.7                                  
REMARK 620 5 HOH E 304   O    90.4  92.0 179.7  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 130   OD1                                                    
REMARK 620 2 ASP E 132   OD1  62.6                                              
REMARK 620 3 ASP E 134   OD1  93.3  74.4                                        
REMARK 620 4 HOH E 301   O    92.2 103.5 172.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 2101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 2101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 2101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 J 2101                
DBREF  4OVN A    1   149  UNP    P62158   CALM_HUMAN       1    149             
DBREF  4OVN F 1773  1929  UNP    Q14524   SCN5A_HUMAN   1773   1929             
DBREF  4OVN B    1   149  UNP    P62158   CALM_HUMAN       1    149             
DBREF  4OVN G 1773  1929  UNP    Q14524   SCN5A_HUMAN   1773   1929             
DBREF  4OVN C    1   149  UNP    P62158   CALM_HUMAN       1    149             
DBREF  4OVN H 1773  1929  UNP    Q14524   SCN5A_HUMAN   1773   1929             
DBREF  4OVN D    1   149  UNP    P62158   CALM_HUMAN       1    149             
DBREF  4OVN I 1773  1929  UNP    Q14524   SCN5A_HUMAN   1773   1929             
DBREF  4OVN E    1   149  UNP    P62158   CALM_HUMAN       1    149             
DBREF  4OVN J 1773  1929  UNP    Q14524   SCN5A_HUMAN   1773   1929             
SEQRES   1 A  149  MSE ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 A  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 A  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MSE ARG SER          
SEQRES   4 A  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MSE          
SEQRES   5 A  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 A  149  PHE PRO GLU PHE LEU THR MSE MSE ALA ARG LYS MSE LYS          
SEQRES   7 A  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 A  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 A  149  GLU LEU ARG HIS VAL MSE THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 A  149  THR ASP GLU GLU VAL ASP GLU MSE ILE ARG GLU ALA ASP          
SEQRES  11 A  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 A  149  GLN MSE MSE THR ALA LYS                                      
SEQRES   1 F  157  GLU ASN PHE SER VAL ALA THR GLU GLU SER THR GLU PRO          
SEQRES   2 F  157  LEU SER GLU ASP ASP PHE ASP MSE PHE TYR GLU ILE TRP          
SEQRES   3 F  157  GLU LYS PHE ASP PRO GLU ALA THR GLN PHE ILE GLU TYR          
SEQRES   4 F  157  SER VAL LEU SER ASP PHE ALA ASP ALA LEU SER GLU PRO          
SEQRES   5 F  157  LEU ARG ILE ALA LYS PRO ASN GLN ILE SER LEU ILE ASN          
SEQRES   6 F  157  MSE ASP LEU PRO MSE VAL SER GLY ASP ARG ILE HIS CYS          
SEQRES   7 F  157  MSE ASP ILE LEU PHE ALA PHE THR LYS ARG VAL LEU GLY          
SEQRES   8 F  157  GLU SER GLY GLU MSE ASP ALA LEU LYS ILE GLN MSE GLU          
SEQRES   9 F  157  GLU LYS PHE MSE ALA ALA ASN PRO SER LYS ILE SER TYR          
SEQRES  10 F  157  GLU PRO ILE THR THR THR LEU ARG ARG LYS HIS GLU GLU          
SEQRES  11 F  157  VAL SER ALA MSE VAL ILE GLN ARG ALA PHE ARG ARG HIS          
SEQRES  12 F  157  LEU LEU GLN ARG SER LEU LYS HIS ALA SER PHE LEU PHE          
SEQRES  13 F  157  ARG                                                          
SEQRES   1 B  149  MSE ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 B  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 B  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MSE ARG SER          
SEQRES   4 B  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MSE          
SEQRES   5 B  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 B  149  PHE PRO GLU PHE LEU THR MSE MSE ALA ARG LYS MSE LYS          
SEQRES   7 B  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 B  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 B  149  GLU LEU ARG HIS VAL MSE THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 B  149  THR ASP GLU GLU VAL ASP GLU MSE ILE ARG GLU ALA ASP          
SEQRES  11 B  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 B  149  GLN MSE MSE THR ALA LYS                                      
SEQRES   1 G  157  GLU ASN PHE SER VAL ALA THR GLU GLU SER THR GLU PRO          
SEQRES   2 G  157  LEU SER GLU ASP ASP PHE ASP MSE PHE TYR GLU ILE TRP          
SEQRES   3 G  157  GLU LYS PHE ASP PRO GLU ALA THR GLN PHE ILE GLU TYR          
SEQRES   4 G  157  SER VAL LEU SER ASP PHE ALA ASP ALA LEU SER GLU PRO          
SEQRES   5 G  157  LEU ARG ILE ALA LYS PRO ASN GLN ILE SER LEU ILE ASN          
SEQRES   6 G  157  MSE ASP LEU PRO MSE VAL SER GLY ASP ARG ILE HIS CYS          
SEQRES   7 G  157  MSE ASP ILE LEU PHE ALA PHE THR LYS ARG VAL LEU GLY          
SEQRES   8 G  157  GLU SER GLY GLU MSE ASP ALA LEU LYS ILE GLN MSE GLU          
SEQRES   9 G  157  GLU LYS PHE MSE ALA ALA ASN PRO SER LYS ILE SER TYR          
SEQRES  10 G  157  GLU PRO ILE THR THR THR LEU ARG ARG LYS HIS GLU GLU          
SEQRES  11 G  157  VAL SER ALA MSE VAL ILE GLN ARG ALA PHE ARG ARG HIS          
SEQRES  12 G  157  LEU LEU GLN ARG SER LEU LYS HIS ALA SER PHE LEU PHE          
SEQRES  13 G  157  ARG                                                          
SEQRES   1 C  149  MSE ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 C  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 C  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MSE ARG SER          
SEQRES   4 C  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MSE          
SEQRES   5 C  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 C  149  PHE PRO GLU PHE LEU THR MSE MSE ALA ARG LYS MSE LYS          
SEQRES   7 C  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 C  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 C  149  GLU LEU ARG HIS VAL MSE THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 C  149  THR ASP GLU GLU VAL ASP GLU MSE ILE ARG GLU ALA ASP          
SEQRES  11 C  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 C  149  GLN MSE MSE THR ALA LYS                                      
SEQRES   1 H  157  GLU ASN PHE SER VAL ALA THR GLU GLU SER THR GLU PRO          
SEQRES   2 H  157  LEU SER GLU ASP ASP PHE ASP MSE PHE TYR GLU ILE TRP          
SEQRES   3 H  157  GLU LYS PHE ASP PRO GLU ALA THR GLN PHE ILE GLU TYR          
SEQRES   4 H  157  SER VAL LEU SER ASP PHE ALA ASP ALA LEU SER GLU PRO          
SEQRES   5 H  157  LEU ARG ILE ALA LYS PRO ASN GLN ILE SER LEU ILE ASN          
SEQRES   6 H  157  MSE ASP LEU PRO MSE VAL SER GLY ASP ARG ILE HIS CYS          
SEQRES   7 H  157  MSE ASP ILE LEU PHE ALA PHE THR LYS ARG VAL LEU GLY          
SEQRES   8 H  157  GLU SER GLY GLU MSE ASP ALA LEU LYS ILE GLN MSE GLU          
SEQRES   9 H  157  GLU LYS PHE MSE ALA ALA ASN PRO SER LYS ILE SER TYR          
SEQRES  10 H  157  GLU PRO ILE THR THR THR LEU ARG ARG LYS HIS GLU GLU          
SEQRES  11 H  157  VAL SER ALA MSE VAL ILE GLN ARG ALA PHE ARG ARG HIS          
SEQRES  12 H  157  LEU LEU GLN ARG SER LEU LYS HIS ALA SER PHE LEU PHE          
SEQRES  13 H  157  ARG                                                          
SEQRES   1 D  149  MSE ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 D  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 D  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MSE ARG SER          
SEQRES   4 D  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MSE          
SEQRES   5 D  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 D  149  PHE PRO GLU PHE LEU THR MSE MSE ALA ARG LYS MSE LYS          
SEQRES   7 D  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 D  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 D  149  GLU LEU ARG HIS VAL MSE THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 D  149  THR ASP GLU GLU VAL ASP GLU MSE ILE ARG GLU ALA ASP          
SEQRES  11 D  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 D  149  GLN MSE MSE THR ALA LYS                                      
SEQRES   1 I  157  GLU ASN PHE SER VAL ALA THR GLU GLU SER THR GLU PRO          
SEQRES   2 I  157  LEU SER GLU ASP ASP PHE ASP MSE PHE TYR GLU ILE TRP          
SEQRES   3 I  157  GLU LYS PHE ASP PRO GLU ALA THR GLN PHE ILE GLU TYR          
SEQRES   4 I  157  SER VAL LEU SER ASP PHE ALA ASP ALA LEU SER GLU PRO          
SEQRES   5 I  157  LEU ARG ILE ALA LYS PRO ASN GLN ILE SER LEU ILE ASN          
SEQRES   6 I  157  MSE ASP LEU PRO MSE VAL SER GLY ASP ARG ILE HIS CYS          
SEQRES   7 I  157  MSE ASP ILE LEU PHE ALA PHE THR LYS ARG VAL LEU GLY          
SEQRES   8 I  157  GLU SER GLY GLU MSE ASP ALA LEU LYS ILE GLN MSE GLU          
SEQRES   9 I  157  GLU LYS PHE MSE ALA ALA ASN PRO SER LYS ILE SER TYR          
SEQRES  10 I  157  GLU PRO ILE THR THR THR LEU ARG ARG LYS HIS GLU GLU          
SEQRES  11 I  157  VAL SER ALA MSE VAL ILE GLN ARG ALA PHE ARG ARG HIS          
SEQRES  12 I  157  LEU LEU GLN ARG SER LEU LYS HIS ALA SER PHE LEU PHE          
SEQRES  13 I  157  ARG                                                          
SEQRES   1 E  149  MSE ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 E  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 E  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MSE ARG SER          
SEQRES   4 E  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MSE          
SEQRES   5 E  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 E  149  PHE PRO GLU PHE LEU THR MSE MSE ALA ARG LYS MSE LYS          
SEQRES   7 E  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 E  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 E  149  GLU LEU ARG HIS VAL MSE THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 E  149  THR ASP GLU GLU VAL ASP GLU MSE ILE ARG GLU ALA ASP          
SEQRES  11 E  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 E  149  GLN MSE MSE THR ALA LYS                                      
SEQRES   1 J  157  GLU ASN PHE SER VAL ALA THR GLU GLU SER THR GLU PRO          
SEQRES   2 J  157  LEU SER GLU ASP ASP PHE ASP MSE PHE TYR GLU ILE TRP          
SEQRES   3 J  157  GLU LYS PHE ASP PRO GLU ALA THR GLN PHE ILE GLU TYR          
SEQRES   4 J  157  SER VAL LEU SER ASP PHE ALA ASP ALA LEU SER GLU PRO          
SEQRES   5 J  157  LEU ARG ILE ALA LYS PRO ASN GLN ILE SER LEU ILE ASN          
SEQRES   6 J  157  MSE ASP LEU PRO MSE VAL SER GLY ASP ARG ILE HIS CYS          
SEQRES   7 J  157  MSE ASP ILE LEU PHE ALA PHE THR LYS ARG VAL LEU GLY          
SEQRES   8 J  157  GLU SER GLY GLU MSE ASP ALA LEU LYS ILE GLN MSE GLU          
SEQRES   9 J  157  GLU LYS PHE MSE ALA ALA ASN PRO SER LYS ILE SER TYR          
SEQRES  10 J  157  GLU PRO ILE THR THR THR LEU ARG ARG LYS HIS GLU GLU          
SEQRES  11 J  157  VAL SER ALA MSE VAL ILE GLN ARG ALA PHE ARG ARG HIS          
SEQRES  12 J  157  LEU LEU GLN ARG SER LEU LYS HIS ALA SER PHE LEU PHE          
SEQRES  13 J  157  ARG                                                          
MODRES 4OVN MSE A   37  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE A   52  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE A   72  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE A   73  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE A   77  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE A  110  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE A  125  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE A  145  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE A  146  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE F 1793  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE F 1838  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE F 1842  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE F 1851  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE F 1868  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE F 1875  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE F 1880  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE F 1906  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE B   37  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE B   52  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE B   72  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE B   73  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE B   77  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE B  110  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE B  125  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE B  145  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE B  146  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE G 1793  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE G 1838  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE G 1842  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE G 1851  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE G 1868  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE G 1875  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE G 1880  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE G 1906  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE C   37  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE C   52  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE C   72  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE C   73  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE C   77  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE C  110  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE C  125  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE C  145  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE C  146  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE H 1793  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE H 1838  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE H 1842  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE H 1851  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE H 1868  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE H 1875  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE H 1880  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE H 1906  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE D   37  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE D   52  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE D   72  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE D   73  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE D   77  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE D  110  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE D  125  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE D  145  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE D  146  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE I 1793  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE I 1838  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE I 1842  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE I 1851  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE I 1868  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE I 1875  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE I 1880  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE I 1906  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE E   37  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE E   52  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE E   72  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE E   73  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE E   77  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE E  110  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE E  125  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE E  145  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE E  146  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE J 1793  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE J 1838  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE J 1842  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE J 1851  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE J 1868  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE J 1875  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE J 1880  MET  MODIFIED RESIDUE                                   
MODRES 4OVN MSE J 1906  MET  MODIFIED RESIDUE                                   
HET    MSE  A  37      17                                                       
HET    MSE  A  52      17                                                       
HET    MSE  A  72      17                                                       
HET    MSE  A  73      17                                                       
HET    MSE  A  77      17                                                       
HET    MSE  A 110      17                                                       
HET    MSE  A 125      17                                                       
HET    MSE  A 145      17                                                       
HET    MSE  A 146      17                                                       
HET    MSE  F1793      17                                                       
HET    MSE  F1838      17                                                       
HET    MSE  F1842      17                                                       
HET    MSE  F1851      17                                                       
HET    MSE  F1868      17                                                       
HET    MSE  F1875      17                                                       
HET    MSE  F1880      17                                                       
HET    MSE  F1906      17                                                       
HET    MSE  B  37      17                                                       
HET    MSE  B  52      17                                                       
HET    MSE  B  72      17                                                       
HET    MSE  B  73      17                                                       
HET    MSE  B  77      17                                                       
HET    MSE  B 110      17                                                       
HET    MSE  B 125      17                                                       
HET    MSE  B 145      17                                                       
HET    MSE  B 146      17                                                       
HET    MSE  G1793      17                                                       
HET    MSE  G1838      17                                                       
HET    MSE  G1842      17                                                       
HET    MSE  G1851      17                                                       
HET    MSE  G1868      17                                                       
HET    MSE  G1875      17                                                       
HET    MSE  G1880      17                                                       
HET    MSE  G1906      17                                                       
HET    MSE  C  37      17                                                       
HET    MSE  C  52      17                                                       
HET    MSE  C  72      17                                                       
HET    MSE  C  73      17                                                       
HET    MSE  C  77      17                                                       
HET    MSE  C 110      17                                                       
HET    MSE  C 125      17                                                       
HET    MSE  C 145      17                                                       
HET    MSE  C 146      17                                                       
HET    MSE  H1793      17                                                       
HET    MSE  H1838      17                                                       
HET    MSE  H1842      17                                                       
HET    MSE  H1851      17                                                       
HET    MSE  H1868      17                                                       
HET    MSE  H1875      17                                                       
HET    MSE  H1880      17                                                       
HET    MSE  H1906      17                                                       
HET    MSE  D  37      17                                                       
HET    MSE  D  52      17                                                       
HET    MSE  D  72      17                                                       
HET    MSE  D  73      17                                                       
HET    MSE  D  77      17                                                       
HET    MSE  D 110      17                                                       
HET    MSE  D 125      17                                                       
HET    MSE  D 145      17                                                       
HET    MSE  D 146      17                                                       
HET    MSE  I1793      17                                                       
HET    MSE  I1838      17                                                       
HET    MSE  I1842      17                                                       
HET    MSE  I1851      17                                                       
HET    MSE  I1868      17                                                       
HET    MSE  I1875      17                                                       
HET    MSE  I1880      17                                                       
HET    MSE  I1906      17                                                       
HET    MSE  E  37      17                                                       
HET    MSE  E  52      17                                                       
HET    MSE  E  72      17                                                       
HET    MSE  E  73      17                                                       
HET    MSE  E  77      17                                                       
HET    MSE  E 110      17                                                       
HET    MSE  E 125      17                                                       
HET    MSE  E 145      17                                                       
HET    MSE  E 146      17                                                       
HET    MSE  J1793      17                                                       
HET    MSE  J1838      17                                                       
HET    MSE  J1842      17                                                       
HET    MSE  J1851      17                                                       
HET    MSE  J1868      17                                                       
HET    MSE  J1875      17                                                       
HET    MSE  J1880      17                                                       
HET    MSE  J1906      17                                                       
HET     MG  A 201       1                                                       
HET     MG  A 202       1                                                       
HET     MG  A 203       1                                                       
HET     MG  A 204       1                                                       
HET    SO4  A 205       5                                                       
HET    SO4  F2101       5                                                       
HET     MG  B 201       1                                                       
HET     MG  B 202       1                                                       
HET     MG  B 203       1                                                       
HET    PO4  B 204       5                                                       
HET    SO4  G2101       5                                                       
HET     MG  C 201       1                                                       
HET     MG  C 202       1                                                       
HET     MG  C 203       1                                                       
HET     MG  C 204       1                                                       
HET    PO4  C 205       5                                                       
HET     MG  C 206       1                                                       
HET    SO4  H2101       5                                                       
HET     MG  D 201       1                                                       
HET     MG  D 202       1                                                       
HET     MG  D 203       1                                                       
HET     MG  D 204       1                                                       
HET     MG  E 201       1                                                       
HET     MG  E 202       1                                                       
HET    SO4  J2101       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   1  MSE    85(C5 H11 N O2 SE)                                           
FORMUL  11   MG    18(MG 2+)                                                    
FORMUL  15  SO4    5(O4 S 2-)                                                   
FORMUL  20  PO4    2(O4 P 3-)                                                   
FORMUL  36  HOH   *62(H2 O)                                                     
HELIX    1 AA1 GLU A    8  ASP A   21  1                                  14    
HELIX    2 AA2 THR A   30  SER A   39  1                                  10    
HELIX    3 AA3 THR A   45  ASP A   57  1                                  13    
HELIX    4 AA4 PHE A   66  ASP A   79  1                                  14    
HELIX    5 AA5 GLU A   83  VAL A   92  1                                  10    
HELIX    6 AA6 SER A  102  LEU A  113  1                                  12    
HELIX    7 AA7 THR A  118  ASP A  130  1                                  13    
HELIX    8 AA8 TYR A  139  GLN A  144  1                                   6    
HELIX    9 AA9 ASP F 1790  ASP F 1802  1                                  13    
HELIX   10 AB1 VAL F 1813  ALA F 1820  1                                   8    
HELIX   11 AB2 ASN F 1831  MSE F 1838  1                                   8    
HELIX   12 AB3 CYS F 1850  GLY F 1863  1                                  14    
HELIX   13 AB4 GLU F 1867  ALA F 1882  1                                  16    
HELIX   14 AB5 LEU F 1896  SER F 1925  1                                  30    
HELIX   15 AB6 GLN B    9  ASP B   21  1                                  13    
HELIX   16 AB7 LEU B   33  LEU B   40  1                                   8    
HELIX   17 AB8 THR B   45  ASP B   51  1                                   7    
HELIX   18 AB9 PHE B   66  LEU B   70  1                                   5    
HELIX   19 AC1 MSE B   72  MSE B   77  1                                   6    
HELIX   20 AC2 SER B   82  ASP B   94  1                                  13    
HELIX   21 AC3 ALA B  103  LEU B  113  1                                  11    
HELIX   22 AC4 THR B  118  ASP B  130  1                                  13    
HELIX   23 AC5 ASN B  138  MSE B  145  1                                   8    
HELIX   24 AC6 SER G 1787  ASP G 1802  1                                  16    
HELIX   25 AC7 VAL G 1813  LEU G 1821  1                                   9    
HELIX   26 AC8 ASN G 1831  ASN G 1837  1                                   7    
HELIX   27 AC9 CYS G 1850  GLY G 1863  1                                  14    
HELIX   28 AD1 GLU G 1867  ASN G 1883  1                                  17    
HELIX   29 AD2 THR G 1895  PHE G 1926  1                                  32    
HELIX   30 AD3 GLU C    8  ASP C   21  1                                  14    
HELIX   31 AD4 GLU C   32  SER C   39  1                                   8    
HELIX   32 AD5 ALA C   47  ASP C   57  1                                  11    
HELIX   33 AD6 PHE C   66  ASP C   79  1                                  14    
HELIX   34 AD7 SER C   82  VAL C   92  1                                  11    
HELIX   35 AD8 ALA C  103  LEU C  113  1                                  11    
HELIX   36 AD9 THR C  118  ASP C  130  1                                  13    
HELIX   37 AE1 TYR C  139  MSE C  146  1                                   8    
HELIX   38 AE2 SER H 1787  ASP H 1802  1                                  16    
HELIX   39 AE3 VAL H 1813  LEU H 1821  1                                   9    
HELIX   40 AE4 ASN H 1831  ASP H 1839  1                                   9    
HELIX   41 AE5 CYS H 1850  GLY H 1863  1                                  14    
HELIX   42 AE6 GLU H 1867  ASN H 1883  1                                  17    
HELIX   43 AE7 THR H 1895  ALA H 1924  1                                  30    
HELIX   44 AE8 GLU D    8  ASP D   21  1                                  14    
HELIX   45 AE9 LYS D   31  LEU D   40  1                                  10    
HELIX   46 AF1 THR D   45  ASP D   57  1                                  13    
HELIX   47 AF2 PHE D   66  ASP D   79  1                                  14    
HELIX   48 AF3 ASP D   81  VAL D   92  1                                  12    
HELIX   49 AF4 ALA D  103  LEU D  113  1                                  11    
HELIX   50 AF5 THR D  118  ASP D  130  1                                  13    
HELIX   51 AF6 TYR D  139  MSE D  145  1                                   7    
HELIX   52 AF7 SER I 1787  ASP I 1802  1                                  16    
HELIX   53 AF8 VAL I 1813  LEU I 1821  1                                   9    
HELIX   54 AF9 ASN I 1831  ASN I 1837  1                                   7    
HELIX   55 AG1 CYS I 1850  GLY I 1863  1                                  14    
HELIX   56 AG2 SER I 1865  ALA I 1882  1                                  18    
HELIX   57 AG3 THR I 1895  HIS I 1923  1                                  29    
HELIX   58 AG4 GLN E    9  PHE E   20  1                                  12    
HELIX   59 AG5 THR E   30  SER E   39  1                                  10    
HELIX   60 AG6 ALA E   47  ASP E   51  5                                   5    
HELIX   61 AG7 PHE E   66  LYS E   76  1                                  11    
HELIX   62 AG8 GLU E   83  PHE E   93  1                                  11    
HELIX   63 AG9 SER E  102  THR E  111  1                                  10    
HELIX   64 AH1 THR E  118  ASP E  130  1                                  13    
HELIX   65 AH2 TYR E  139  MSE E  146  1                                   8    
HELIX   66 AH3 SER J 1787  ASP J 1802  1                                  16    
HELIX   67 AH4 VAL J 1813  LEU J 1821  1                                   9    
HELIX   68 AH5 ASN J 1831  MSE J 1838  1                                   8    
HELIX   69 AH6 CYS J 1850  GLY J 1863  1                                  14    
HELIX   70 AH7 SER J 1865  ALA J 1882  1                                  18    
HELIX   71 AH8 THR J 1895  ALA J 1924  1                                  30    
SHEET    1 AA1 2 THR A  27  THR A  29  0                                        
SHEET    2 AA1 2 THR A  63  ASP A  65 -1  O  ILE A  64   N  ILE A  28           
SHEET    1 AA2 2 TYR A 100  ILE A 101  0                                        
SHEET    2 AA2 2 VAL A 137  ASN A 138 -1  O  VAL A 137   N  ILE A 101           
SHEET    1 AA3 2 PHE F1808  GLU F1810  0                                        
SHEET    2 AA3 2 ARG F1847  HIS F1849 -1  O  ILE F1848   N  ILE F1809           
SHEET    1 AA4 2 PRO F1841  VAL F1843  0                                        
SHEET    2 AA4 2 PRO F1891  THR F1894 -1  O  ILE F1892   N  MSE F1842           
SHEET    1 AA5 2 THR B  27  THR B  29  0                                        
SHEET    2 AA5 2 THR B  63  ASP B  65 -1  O  ILE B  64   N  ILE B  28           
SHEET    1 AA6 2 ILE B 101  SER B 102  0                                        
SHEET    2 AA6 2 GLN B 136  VAL B 137 -1  O  VAL B 137   N  ILE B 101           
SHEET    1 AA7 4 PHE G1808  GLU G1810  0                                        
SHEET    2 AA7 4 ARG G1847  HIS G1849 -1  O  ILE G1848   N  ILE G1809           
SHEET    3 AA7 4 PRO G1841  VAL G1843 -1  N  VAL G1843   O  ARG G1847           
SHEET    4 AA7 4 PRO G1891  THR G1894 -1  O  THR G1893   N  MSE G1842           
SHEET    1 AA8 2 THR C  27  THR C  29  0                                        
SHEET    2 AA8 2 THR C  63  ASP C  65 -1  O  ILE C  64   N  ILE C  28           
SHEET    1 AA9 2 TYR C 100  SER C 102  0                                        
SHEET    2 AA9 2 GLN C 136  ASN C 138 -1  O  VAL C 137   N  ILE C 101           
SHEET    1 AB1 2 PHE H1808  GLU H1810  0                                        
SHEET    2 AB1 2 ARG H1847  HIS H1849 -1  O  ILE H1848   N  ILE H1809           
SHEET    1 AB2 2 PRO H1841  MSE H1842  0                                        
SHEET    2 AB2 2 THR H1893  THR H1894 -1  O  THR H1893   N  MSE H1842           
SHEET    1 AB3 2 THR D  27  THR D  29  0                                        
SHEET    2 AB3 2 THR D  63  ASP D  65 -1  O  ILE D  64   N  ILE D  28           
SHEET    1 AB4 2 TYR D 100  SER D 102  0                                        
SHEET    2 AB4 2 GLN D 136  ASN D 138 -1  O  VAL D 137   N  ILE D 101           
SHEET    1 AB5 2 PHE I1808  GLU I1810  0                                        
SHEET    2 AB5 2 ARG I1847  HIS I1849 -1  O  ILE I1848   N  ILE I1809           
SHEET    1 AB6 2 PRO I1841  VAL I1843  0                                        
SHEET    2 AB6 2 PRO I1891  THR I1894 -1  O  ILE I1892   N  MSE I1842           
SHEET    1 AB7 2 THR E  27  ILE E  28  0                                        
SHEET    2 AB7 2 ILE E  64  ASP E  65 -1  O  ILE E  64   N  ILE E  28           
SHEET    1 AB8 2 TYR E 100  ILE E 101  0                                        
SHEET    2 AB8 2 VAL E 137  ASN E 138 -1  O  VAL E 137   N  ILE E 101           
SHEET    1 AB9 2 PHE J1808  GLU J1810  0                                        
SHEET    2 AB9 2 ARG J1847  HIS J1849 -1  O  ILE J1848   N  ILE J1809           
SHEET    1 AC1 2 PRO J1841  VAL J1843  0                                        
SHEET    2 AC1 2 PRO J1891  THR J1894 -1  O  ILE J1892   N  MSE J1842           
LINK         C   VAL A  36                 N   MSE A  37     1555   1555  1.33  
LINK         C   MSE A  37                 N   ARG A  38     1555   1555  1.33  
LINK         C   ASP A  51                 N   MSE A  52     1555   1555  1.33  
LINK         C   MSE A  52                 N   ILE A  53     1555   1555  1.33  
LINK         C   THR A  71                 N   MSE A  72     1555   1555  1.33  
LINK         C   MSE A  72                 N   MSE A  73     1555   1555  1.33  
LINK         C   MSE A  73                 N   ALA A  74     1555   1555  1.33  
LINK         C   LYS A  76                 N   MSE A  77     1555   1555  1.34  
LINK         C   MSE A  77                 N   LYS A  78     1555   1555  1.33  
LINK         C   VAL A 109                 N   MSE A 110     1555   1555  1.33  
LINK         C   MSE A 110                 N   THR A 111     1555   1555  1.32  
LINK         C   GLU A 124                 N   MSE A 125     1555   1555  1.32  
LINK         C   MSE A 125                 N   ILE A 126     1555   1555  1.33  
LINK         C   GLN A 144                 N   MSE A 145     1555   1555  1.32  
LINK         C   MSE A 145                 N   MSE A 146     1555   1555  1.33  
LINK         C   MSE A 146                 N   THR A 147     1555   1555  1.32  
LINK         C   ASP F1792                 N   MSE F1793     1555   1555  1.33  
LINK         C   MSE F1793                 N   PHE F1794     1555   1555  1.33  
LINK         C   ASN F1837                 N   MSE F1838     1555   1555  1.33  
LINK         C   MSE F1838                 N   ASP F1839     1555   1555  1.33  
LINK         C   PRO F1841                 N   MSE F1842     1555   1555  1.32  
LINK         C   MSE F1842                 N   VAL F1843     1555   1555  1.33  
LINK         C   CYS F1850                 N   MSE F1851     1555   1555  1.33  
LINK         C   MSE F1851                 N   ASP F1852     1555   1555  1.33  
LINK         C   GLU F1867                 N   MSE F1868     1555   1555  1.34  
LINK         C   MSE F1868                 N   ASP F1869     1555   1555  1.33  
LINK         C   GLN F1874                 N   MSE F1875     1555   1555  1.33  
LINK         C   MSE F1875                 N   GLU F1876     1555   1555  1.33  
LINK         C   PHE F1879                 N   MSE F1880     1555   1555  1.33  
LINK         C   MSE F1880                 N   ALA F1881     1555   1555  1.33  
LINK         C   ALA F1905                 N   MSE F1906     1555   1555  1.33  
LINK         C   MSE F1906                 N   VAL F1907     1555   1555  1.33  
LINK         C   VAL B  36                 N   MSE B  37     1555   1555  1.33  
LINK         C   MSE B  37                 N   ARG B  38     1555   1555  1.33  
LINK         C   ASP B  51                 N   MSE B  52     1555   1555  1.33  
LINK         C   MSE B  52                 N   ILE B  53     1555   1555  1.33  
LINK         C   THR B  71                 N   MSE B  72     1555   1555  1.33  
LINK         C   MSE B  72                 N   MSE B  73     1555   1555  1.34  
LINK         C   MSE B  73                 N   ALA B  74     1555   1555  1.33  
LINK         C   LYS B  76                 N   MSE B  77     1555   1555  1.34  
LINK         C   MSE B  77                 N   LYS B  78     1555   1555  1.33  
LINK         C   VAL B 109                 N   MSE B 110     1555   1555  1.33  
LINK         C   MSE B 110                 N   THR B 111     1555   1555  1.34  
LINK         C   GLU B 124                 N   MSE B 125     1555   1555  1.33  
LINK         C   MSE B 125                 N   ILE B 126     1555   1555  1.33  
LINK         C   GLN B 144                 N   MSE B 145     1555   1555  1.33  
LINK         C   MSE B 145                 N   MSE B 146     1555   1555  1.33  
LINK         C   MSE B 146                 N   THR B 147     1555   1555  1.33  
LINK         C   ASP G1792                 N   MSE G1793     1555   1555  1.32  
LINK         C   MSE G1793                 N   PHE G1794     1555   1555  1.33  
LINK         C   ASN G1837                 N   MSE G1838     1555   1555  1.33  
LINK         C   MSE G1838                 N   ASP G1839     1555   1555  1.33  
LINK         C   PRO G1841                 N   MSE G1842     1555   1555  1.32  
LINK         C   MSE G1842                 N   VAL G1843     1555   1555  1.33  
LINK         C   CYS G1850                 N   MSE G1851     1555   1555  1.32  
LINK         C   MSE G1851                 N   ASP G1852     1555   1555  1.33  
LINK         C   GLU G1867                 N   MSE G1868     1555   1555  1.33  
LINK         C   MSE G1868                 N   ASP G1869     1555   1555  1.33  
LINK         C   GLN G1874                 N   MSE G1875     1555   1555  1.33  
LINK         C   MSE G1875                 N   GLU G1876     1555   1555  1.33  
LINK         C   PHE G1879                 N   MSE G1880     1555   1555  1.33  
LINK         C   MSE G1880                 N   ALA G1881     1555   1555  1.33  
LINK         C   ALA G1905                 N   MSE G1906     1555   1555  1.33  
LINK         C   MSE G1906                 N   VAL G1907     1555   1555  1.34  
LINK         C   VAL C  36                 N   MSE C  37     1555   1555  1.32  
LINK         C   MSE C  37                 N   ARG C  38     1555   1555  1.33  
LINK         C   ASP C  51                 N   MSE C  52     1555   1555  1.33  
LINK         C   MSE C  52                 N   ILE C  53     1555   1555  1.33  
LINK         C   THR C  71                 N   MSE C  72     1555   1555  1.33  
LINK         C   MSE C  72                 N   MSE C  73     1555   1555  1.33  
LINK         C   MSE C  73                 N   ALA C  74     1555   1555  1.33  
LINK         C   LYS C  76                 N   MSE C  77     1555   1555  1.33  
LINK         C   MSE C  77                 N   LYS C  78     1555   1555  1.33  
LINK         C   VAL C 109                 N   MSE C 110     1555   1555  1.33  
LINK         C   MSE C 110                 N   THR C 111     1555   1555  1.33  
LINK         C   GLU C 124                 N   MSE C 125     1555   1555  1.33  
LINK         C   MSE C 125                 N   ILE C 126     1555   1555  1.32  
LINK         C   GLN C 144                 N   MSE C 145     1555   1555  1.33  
LINK         C   MSE C 145                 N   MSE C 146     1555   1555  1.33  
LINK         C   MSE C 146                 N   THR C 147     1555   1555  1.33  
LINK         C   ASP H1792                 N   MSE H1793     1555   1555  1.33  
LINK         C   MSE H1793                 N   PHE H1794     1555   1555  1.33  
LINK         C   ASN H1837                 N   MSE H1838     1555   1555  1.33  
LINK         C   MSE H1838                 N   ASP H1839     1555   1555  1.33  
LINK         C   PRO H1841                 N   MSE H1842     1555   1555  1.33  
LINK         C   MSE H1842                 N   VAL H1843     1555   1555  1.33  
LINK         C   CYS H1850                 N   MSE H1851     1555   1555  1.33  
LINK         C   MSE H1851                 N   ASP H1852     1555   1555  1.33  
LINK         C   GLU H1867                 N   MSE H1868     1555   1555  1.33  
LINK         C   MSE H1868                 N   ASP H1869     1555   1555  1.33  
LINK         C   GLN H1874                 N   MSE H1875     1555   1555  1.33  
LINK         C   MSE H1875                 N   GLU H1876     1555   1555  1.33  
LINK         C   PHE H1879                 N   MSE H1880     1555   1555  1.34  
LINK         C   MSE H1880                 N   ALA H1881     1555   1555  1.33  
LINK         C   ALA H1905                 N   MSE H1906     1555   1555  1.33  
LINK         C   MSE H1906                 N   VAL H1907     1555   1555  1.32  
LINK         C   VAL D  36                 N   MSE D  37     1555   1555  1.32  
LINK         C   MSE D  37                 N   ARG D  38     1555   1555  1.33  
LINK         C   ASP D  51                 N   MSE D  52     1555   1555  1.33  
LINK         C   MSE D  52                 N   ILE D  53     1555   1555  1.33  
LINK         C   THR D  71                 N   MSE D  72     1555   1555  1.33  
LINK         C   MSE D  72                 N   MSE D  73     1555   1555  1.33  
LINK         C   MSE D  73                 N   ALA D  74     1555   1555  1.33  
LINK         C   LYS D  76                 N   MSE D  77     1555   1555  1.33  
LINK         C   MSE D  77                 N   LYS D  78     1555   1555  1.33  
LINK         C   VAL D 109                 N   MSE D 110     1555   1555  1.33  
LINK         C   MSE D 110                 N   THR D 111     1555   1555  1.33  
LINK         C   GLU D 124                 N   MSE D 125     1555   1555  1.33  
LINK         C   MSE D 125                 N   ILE D 126     1555   1555  1.32  
LINK         C   GLN D 144                 N   MSE D 145     1555   1555  1.33  
LINK         C   MSE D 145                 N   MSE D 146     1555   1555  1.33  
LINK         C   MSE D 146                 N   THR D 147     1555   1555  1.34  
LINK         C   ASP I1792                 N   MSE I1793     1555   1555  1.33  
LINK         C   MSE I1793                 N   PHE I1794     1555   1555  1.33  
LINK         C   ASN I1837                 N   MSE I1838     1555   1555  1.33  
LINK         C   MSE I1838                 N   ASP I1839     1555   1555  1.33  
LINK         C   PRO I1841                 N   MSE I1842     1555   1555  1.32  
LINK         C   MSE I1842                 N   VAL I1843     1555   1555  1.32  
LINK         C   CYS I1850                 N   MSE I1851     1555   1555  1.33  
LINK         C   MSE I1851                 N   ASP I1852     1555   1555  1.33  
LINK         C   GLU I1867                 N   MSE I1868     1555   1555  1.33  
LINK         C   MSE I1868                 N   ASP I1869     1555   1555  1.33  
LINK         C   GLN I1874                 N   MSE I1875     1555   1555  1.33  
LINK         C   MSE I1875                 N   GLU I1876     1555   1555  1.33  
LINK         C   PHE I1879                 N   MSE I1880     1555   1555  1.32  
LINK         C   MSE I1880                 N   ALA I1881     1555   1555  1.33  
LINK         C   ALA I1905                 N   MSE I1906     1555   1555  1.33  
LINK         C   MSE I1906                 N   VAL I1907     1555   1555  1.33  
LINK         C   VAL E  36                 N   MSE E  37     1555   1555  1.33  
LINK         C   MSE E  37                 N   ARG E  38     1555   1555  1.33  
LINK         C   ASP E  51                 N   MSE E  52     1555   1555  1.33  
LINK         C   MSE E  52                 N   ILE E  53     1555   1555  1.33  
LINK         C   THR E  71                 N   MSE E  72     1555   1555  1.33  
LINK         C   MSE E  72                 N   MSE E  73     1555   1555  1.33  
LINK         C   MSE E  73                 N   ALA E  74     1555   1555  1.33  
LINK         C   LYS E  76                 N   MSE E  77     1555   1555  1.33  
LINK         C   MSE E  77                 N   LYS E  78     1555   1555  1.34  
LINK         C   VAL E 109                 N   MSE E 110     1555   1555  1.34  
LINK         C   MSE E 110                 N   THR E 111     1555   1555  1.33  
LINK         C   GLU E 124                 N   MSE E 125     1555   1555  1.33  
LINK         C   MSE E 125                 N   ILE E 126     1555   1555  1.33  
LINK         C   GLN E 144                 N   MSE E 145     1555   1555  1.33  
LINK         C   MSE E 145                 N   MSE E 146     1555   1555  1.33  
LINK         C   MSE E 146                 N   THR E 147     1555   1555  1.33  
LINK         C   ASP J1792                 N   MSE J1793     1555   1555  1.33  
LINK         C   MSE J1793                 N   PHE J1794     1555   1555  1.32  
LINK         C   ASN J1837                 N   MSE J1838     1555   1555  1.33  
LINK         C   MSE J1838                 N   ASP J1839     1555   1555  1.34  
LINK         C   PRO J1841                 N   MSE J1842     1555   1555  1.32  
LINK         C   MSE J1842                 N   VAL J1843     1555   1555  1.34  
LINK         C   CYS J1850                 N   MSE J1851     1555   1555  1.32  
LINK         C   MSE J1851                 N   ASP J1852     1555   1555  1.33  
LINK         C   GLU J1867                 N   MSE J1868     1555   1555  1.33  
LINK         C   MSE J1868                 N   ASP J1869     1555   1555  1.33  
LINK         C   GLN J1874                 N   MSE J1875     1555   1555  1.33  
LINK         C   MSE J1875                 N   GLU J1876     1555   1555  1.33  
LINK         C   PHE J1879                 N   MSE J1880     1555   1555  1.33  
LINK         C   MSE J1880                 N   ALA J1881     1555   1555  1.32  
LINK         C   ALA J1905                 N   MSE J1906     1555   1555  1.34  
LINK         C   MSE J1906                 N   VAL J1907     1555   1555  1.33  
LINK         OD1 ASP A  21                MG    MG A 201     1555   1555  2.07  
LINK         OD1 ASP A  23                MG    MG A 201     1555   1555  2.06  
LINK         OD1 ASP A  25                MG    MG A 201     1555   1555  2.07  
LINK         O   THR A  27                MG    MG A 201     1555   1555  2.06  
LINK         OD1 ASP A  57                MG    MG A 202     1555   1555  2.09  
LINK         O   THR A  63                MG    MG A 202     1555   1555  2.08  
LINK         OG1 THR A  63                MG    MG A 202     1555   1555  2.08  
LINK         OE1 GLU A  68                MG    MG A 202     1555   1555  2.30  
LINK         OD1 ASP A  94                MG    MG A 203     1555   1555  2.08  
LINK         OD1 ASP A  96                MG    MG A 203     1555   1555  2.06  
LINK         OD1 ASN A  98                MG    MG A 203     1555   1555  2.07  
LINK         O   TYR A 100                MG    MG A 203     1555   1555  2.04  
LINK         OD1 ASP A 130                MG    MG A 204     1555   1555  2.07  
LINK         OD1 ASP A 132                MG    MG A 204     1555   1555  2.07  
LINK         OD1 ASP A 134                MG    MG A 204     1555   1555  2.05  
LINK         O   GLN A 136                MG    MG A 204     1555   1555  1.99  
LINK        MG    MG A 201                 O   HOH A 308     1555   1555  1.98  
LINK        MG    MG A 202                 O   HOH A 301     1555   1555  1.99  
LINK        MG    MG A 202                 O   HOH A 304     1555   1555  2.07  
LINK        MG    MG A 203                 O   HOH A 306     1555   1555  1.94  
LINK        MG    MG A 204                 O   HOH A 302     1555   1555  2.00  
LINK        MG    MG A 204                 O   HOH A 305     1555   1555  2.01  
LINK         OD1 ASP B  21                MG    MG B 201     1555   1555  2.09  
LINK         OD1 ASP B  23                MG    MG B 201     1555   1555  2.07  
LINK         OD1 ASP B  25                MG    MG B 201     1555   1555  2.08  
LINK         OD2 ASP B  25                MG    MG B 201     1555   1555  2.99  
LINK         O   THR B  27                MG    MG B 201     1555   1555  2.07  
LINK         OD1 ASP B  94                MG    MG B 202     1555   1555  2.04  
LINK         OD1 ASP B  96                MG    MG B 202     1555   1555  2.06  
LINK         OD1 ASN B  98                MG    MG B 202     1555   1555  2.04  
LINK         O   TYR B 100                MG    MG B 202     1555   1555  2.05  
LINK         OD1 ASP B 130                MG    MG B 203     1555   1555  2.07  
LINK         OD1 ASP B 132                MG    MG B 203     1555   1555  2.07  
LINK         OD1 ASP B 134                MG    MG B 203     1555   1555  2.07  
LINK         O   GLN B 136                MG    MG B 203     1555   1555  2.04  
LINK        MG    MG B 201                 O   HOH B 303     1555   1555  2.11  
LINK        MG    MG B 203                 O   HOH B 302     1555   1555  2.06  
LINK         OD1 ASP C  21                MG    MG C 201     1555   1555  2.09  
LINK         OD1 ASP C  23                MG    MG C 201     1555   1555  2.07  
LINK         OD1 ASP C  25                MG    MG C 201     1555   1555  2.05  
LINK         O   THR C  27                MG    MG C 201     1555   1555  2.07  
LINK         O   THR C  63                MG    MG C 202     1555   1555  2.06  
LINK         OG1 THR C  63                MG    MG C 202     1555   1555  2.10  
LINK         OD1 ASP C  65                MG    MG C 206     1555   1555  2.54  
LINK         OD1 ASP C  94                MG    MG C 203     1555   1555  2.07  
LINK         OD1 ASP C  96                MG    MG C 203     1555   1555  2.07  
LINK         OD1 ASN C  98                MG    MG C 203     1555   1555  2.03  
LINK         O   TYR C 100                MG    MG C 203     1555   1555  2.06  
LINK         OD1 ASP C 130                MG    MG C 204     1555   1555  2.08  
LINK         OD1 ASP C 132                MG    MG C 204     1555   1555  2.07  
LINK         OD1 ASP C 134                MG    MG C 204     1555   1555  2.06  
LINK         O   GLN C 136                MG    MG C 204     1555   1555  2.09  
LINK        MG    MG C 201                 O   HOH C 304     1555   1555  2.02  
LINK        MG    MG C 202                 O   HOH C 301     1555   1555  1.99  
LINK        MG    MG C 202                 O   HOH C 302     1555   1555  1.98  
LINK        MG    MG C 202                 O   HOH C 303     1555   1555  2.07  
LINK        MG    MG C 202                 O   HOH C 305     1555   1555  2.07  
LINK        MG    MG C 204                 O   HOH C 306     1555   1555  2.11  
LINK        MG    MG C 206                 OD2 ASP D  65     2646   1555  2.23  
LINK         OD1 ASP D  21                MG    MG D 201     1555   1555  2.07  
LINK         OD1 ASP D  23                MG    MG D 201     1555   1555  2.06  
LINK         OD1 ASP D  25                MG    MG D 201     1555   1555  2.07  
LINK         O   THR D  27                MG    MG D 201     1555   1555  2.06  
LINK         O   THR D  63                MG    MG D 202     1555   1555  2.07  
LINK         OG1 THR D  63                MG    MG D 202     1555   1555  2.06  
LINK         OD1 ASP D  94                MG    MG D 203     1555   1555  2.06  
LINK         OD1 ASP D  96                MG    MG D 203     1555   1555  2.07  
LINK         OD1 ASN D  98                MG    MG D 203     1555   1555  2.07  
LINK         O   TYR D 100                MG    MG D 203     1555   1555  2.07  
LINK         OD1 ASP D 130                MG    MG D 204     1555   1555  2.07  
LINK         OD1 ASP D 132                MG    MG D 204     1555   1555  2.08  
LINK         OD1 ASP D 134                MG    MG D 204     1555   1555  2.06  
LINK         O   GLN D 136                MG    MG D 204     1555   1555  2.06  
LINK        MG    MG D 201                 O   HOH D1103     1555   1555  2.07  
LINK        MG    MG D 202                 O   HOH D1101     1555   1555  1.98  
LINK        MG    MG D 202                 O   HOH D1104     1555   1555  2.07  
LINK        MG    MG D 202                 O   HOH D1105     1555   1555  1.98  
LINK        MG    MG D 202                 O   HOH D1106     1555   1555  2.24  
LINK        MG    MG D 203                 O   HOH D1108     1555   1555  2.10  
LINK        MG    MG D 204                 O   HOH D1102     1555   1555  2.10  
LINK         OD1 ASP E  94                MG    MG E 201     1555   1555  2.08  
LINK         OD1 ASP E  96                MG    MG E 201     1555   1555  2.07  
LINK         OD1 ASN E  98                MG    MG E 201     1555   1555  2.08  
LINK         O   TYR E 100                MG    MG E 201     1555   1555  2.07  
LINK         OD1 ASP E 130                MG    MG E 202     1555   1555  2.05  
LINK         OD1 ASP E 132                MG    MG E 202     1555   1555  2.06  
LINK         OD1 ASP E 134                MG    MG E 202     1555   1555  2.12  
LINK        MG    MG E 201                 O   HOH E 304     1555   1555  2.02  
LINK        MG    MG E 202                 O   HOH E 301     1555   1555  1.99  
CISPEP   1 ALA J 1778    THR J 1779          0         6.66                     
SITE     1 AC1  5 ASP A  21  ASP A  23  ASP A  25  THR A  27                    
SITE     2 AC1  5 HOH A 308                                                     
SITE     1 AC2  5 ASP A  57  THR A  63  GLU A  68  HOH A 301                    
SITE     2 AC2  5 HOH A 304                                                     
SITE     1 AC3  5 ASP A  94  ASP A  96  ASN A  98  TYR A 100                    
SITE     2 AC3  5 HOH A 306                                                     
SITE     1 AC4  6 ASP A 130  ASP A 132  ASP A 134  GLN A 136                    
SITE     2 AC4  6 HOH A 302  HOH A 305                                          
SITE     1 AC5  2 HIS A 108  ASN A 112                                          
SITE     1 AC6  3 ARG A 127  ARG F1919  HIS F1923                               
SITE     1 AC7  5 ASP B  21  ASP B  23  ASP B  25  THR B  27                    
SITE     2 AC7  5 HOH B 303                                                     
SITE     1 AC8  4 ASP B  94  ASP B  96  ASN B  98  TYR B 100                    
SITE     1 AC9  5 ASP B 130  ASP B 132  ASP B 134  GLN B 136                    
SITE     2 AC9  5 HOH B 302                                                     
SITE     1 AD1  2 HIS B 108  ASN B 112                                          
SITE     1 AD2  2 ARG G1826  ALA G1828                                          
SITE     1 AD3  5 ASP C  21  ASP C  23  ASP C  25  THR C  27                    
SITE     2 AD3  5 HOH C 304                                                     
SITE     1 AD4  6 THR C  63  GLU C  68  HOH C 301  HOH C 302                    
SITE     2 AD4  6 HOH C 303  HOH C 305                                          
SITE     1 AD5  4 ASP C  94  ASP C  96  ASN C  98  TYR C 100                    
SITE     1 AD6  5 ASP C 130  ASP C 132  ASP C 134  GLN C 136                    
SITE     2 AD6  5 HOH C 306                                                     
SITE     1 AD7  2 HIS C 108  ASN C 112                                          
SITE     1 AD8  1 ASP C  65                                                     
SITE     1 AD9  3 ARG C 127  ARG H1919  HIS H1923                               
SITE     1 AE1  5 ASP D  21  ASP D  23  ASP D  25  THR D  27                    
SITE     2 AE1  5 HOH D1103                                                     
SITE     1 AE2  5 THR D  63  HOH D1101  HOH D1104  HOH D1105                    
SITE     2 AE2  5 HOH D1106                                                     
SITE     1 AE3  5 ASP D  94  ASP D  96  ASN D  98  TYR D 100                    
SITE     2 AE3  5 HOH D1108                                                     
SITE     1 AE4  5 ASP D 130  ASP D 132  ASP D 134  GLN D 136                    
SITE     2 AE4  5 HOH D1102                                                     
SITE     1 AE5  5 ASP E  94  ASP E  96  ASN E  98  TYR E 100                    
SITE     2 AE5  5 HOH E 304                                                     
SITE     1 AE6  6 ASP E 130  ASP E 132  ASP E 134  GLN E 136                    
SITE     2 AE6  6 VAL E 137  HOH E 301                                          
SITE     1 AE7  2 ARG J1919  HIS J1923                                          
CRYST1  106.128   99.006  109.281  90.00 106.11  90.00 P 1 21 1     10          
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      0.009423  0.000000  0.002722        0.00000                         
SCALE2      0.000000  0.010100  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009525        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system