GenomeNet

Database: PDB
Entry: 3T5W
LinkDB: 3T5W
Original site: 3T5W 
HEADER    OXIDOREDUCTASE                          28-JUL-11   3T5W              
TITLE     2ME MODIFIED HUMAN SOD1                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, D, E, F, G, H, I, J, K, L, M;                           
COMPND   4 SYNONYM: COPPER ZINC SUPEROXIDE DISMUTASE, SUPEROXIDE DISMUTASE 1,   
COMPND   5 HSOD1;                                                               
COMPND   6 EC: 1.15.1.1;                                                        
COMPND   7 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: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    2ME MODIFICATION AT CYS111, OXIDOREDUCTASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.IHARA,Y.YAMAGUCHI,H.TORIGOE,S.WAKATSUKI,N.TANIGUCHI,K.SUZUKI,       
AUTHOR   2 N.FUJIWARA                                                           
REVDAT   2   03-JUL-13 3T5W    1       JRNL                                     
REVDAT   1   01-AUG-12 3T5W    0                                                
JRNL        AUTH   K.IHARA,N.FUJIWARA,Y.YAMAGUCHI,H.TORIGOE,S.WAKATSUKI,        
JRNL        AUTH 2 N.TANIGUCHI,K.SUZUKI                                         
JRNL        TITL   STRUCTURAL SWITCHING OF CU,ZN-SUPEROXIDE DISMUTASES AT LOOP  
JRNL        TITL 2 VI: INSIGHTS FROM THE CRYSTAL STRUCTURE OF                   
JRNL        TITL 3 2-MERCAPTOETHANOL-MODIFIED ENZYME                            
JRNL        REF    BIOSCI.REP.                   V.  32   539 2012              
JRNL        REFN                   ISSN 0144-8463                               
JRNL        PMID   22804629                                                     
JRNL        DOI    10.1042/BSR20120029                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 175704                         
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9252                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12534                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.50                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 683                          
REMARK   3   BIN FREE R VALUE                    : 0.3230                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13368                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 84                                      
REMARK   3   SOLVENT ATOMS            : 1746                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.55000                                             
REMARK   3    B22 (A**2) : 1.22000                                              
REMARK   3    B33 (A**2) : -0.67000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.132         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.564         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13644 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18408 ; 1.269 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1824 ; 6.209 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   576 ;37.727 ;25.625       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2208 ;13.360 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;16.697 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2016 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10344 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8940 ; 0.673 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14208 ; 1.230 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4704 ; 1.992 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4200 ; 3.365 ; 4.500       
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  : 12                                         
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     1        A   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1812  20.6740 -32.8619              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3014 T22:   0.3164                                     
REMARK   3      T33:   0.3701 T12:  -0.0080                                     
REMARK   3      T13:   0.0060 T23:  -0.0380                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2828 L22:   0.3490                                     
REMARK   3      L33:   0.4956 L12:  -0.0845                                     
REMARK   3      L13:   0.0051 L23:   0.0888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0013 S12:   0.0358 S13:  -0.0586                       
REMARK   3      S21:   0.0028 S22:  -0.0145 S23:  -0.0102                       
REMARK   3      S31:  -0.0299 S32:   0.0218 S33:   0.0132                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.8542  42.1128 -14.8219              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3232 T22:   0.3134                                     
REMARK   3      T33:   0.3414 T12:   0.0008                                     
REMARK   3      T13:  -0.0074 T23:  -0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4820 L22:   0.3622                                     
REMARK   3      L33:   0.4409 L12:  -0.0201                                     
REMARK   3      L13:  -0.1349 L23:   0.0414                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0050 S12:  -0.0123 S13:   0.0069                       
REMARK   3      S21:   0.0110 S22:   0.0003 S23:  -0.0306                       
REMARK   3      S31:  -0.0119 S32:  -0.0361 S33:   0.0047                       
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 :   D     1        D   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.7238  22.6185 -30.3196              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3070 T22:   0.3237                                     
REMARK   3      T33:   0.3556 T12:  -0.0017                                     
REMARK   3      T13:  -0.0022 T23:  -0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1156 L22:   0.7610                                     
REMARK   3      L33:   0.2549 L12:   0.0248                                     
REMARK   3      L13:  -0.0726 L23:   0.1706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0108 S12:   0.0064 S13:  -0.0066                       
REMARK   3      S21:   0.0012 S22:  -0.0125 S23:   0.0559                       
REMARK   3      S31:   0.0133 S32:  -0.0025 S33:   0.0233                       
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 :   E     1        E   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.2834  49.1757 -20.9185              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3165 T22:   0.3159                                     
REMARK   3      T33:   0.3480 T12:  -0.0148                                     
REMARK   3      T13:   0.0036 T23:  -0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4893 L22:   0.4510                                     
REMARK   3      L33:   0.3796 L12:  -0.1048                                     
REMARK   3      L13:  -0.2499 L23:  -0.0269                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0226 S12:  -0.0148 S13:   0.0283                       
REMARK   3      S21:   0.0115 S22:  -0.0091 S23:  -0.0056                       
REMARK   3      S31:  -0.0311 S32:   0.0187 S33:  -0.0136                       
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 :   F     1        F   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.3978 -10.5228 -38.5758              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3533 T22:   0.2847                                     
REMARK   3      T33:   0.3382 T12:  -0.0238                                     
REMARK   3      T13:   0.0219 T23:  -0.0389                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4980 L22:   0.7142                                     
REMARK   3      L33:   0.3416 L12:   0.0110                                     
REMARK   3      L13:   0.0237 L23:   0.0912                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0494 S12:   0.0335 S13:   0.0222                       
REMARK   3      S21:   0.1154 S22:  -0.0588 S23:   0.0727                       
REMARK   3      S31:   0.0413 S32:   0.0006 S33:   0.0094                       
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 :   G     1        G   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.0907 -36.8038 -28.7806              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4469 T22:   0.2555                                     
REMARK   3      T33:   0.3019 T12:  -0.0829                                     
REMARK   3      T13:   0.0212 T23:  -0.0196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1582 L22:   0.8610                                     
REMARK   3      L33:   0.4902 L12:  -0.2658                                     
REMARK   3      L13:   0.1677 L23:   0.0384                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0596 S12:  -0.0255 S13:  -0.0040                       
REMARK   3      S21:   0.0832 S22:  -0.0398 S23:   0.0805                       
REMARK   3      S31:   0.0993 S32:  -0.0222 S33:  -0.0197                       
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 :   H     1        H   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.1706  -7.9051 -24.7035              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3672 T22:   0.2820                                     
REMARK   3      T33:   0.3293 T12:  -0.0203                                     
REMARK   3      T13:  -0.0267 T23:   0.0211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6794 L22:   0.6553                                     
REMARK   3      L33:   0.7429 L12:   0.4046                                     
REMARK   3      L13:  -0.0825 L23:  -0.0828                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0536 S12:  -0.0628 S13:  -0.0994                       
REMARK   3      S21:   0.0501 S22:  -0.0749 S23:  -0.0870                       
REMARK   3      S31:   0.0861 S32:  -0.0016 S33:   0.0212                       
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     1        I   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.2810 -28.2269  -6.2239              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4648 T22:   0.2661                                     
REMARK   3      T33:   0.2882 T12:  -0.0389                                     
REMARK   3      T13:  -0.0410 T23:   0.1115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7882 L22:   1.4415                                     
REMARK   3      L33:   1.0061 L12:   0.4729                                     
REMARK   3      L13:  -0.2815 L23:   0.3111                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0340 S12:  -0.1365 S13:  -0.1605                       
REMARK   3      S21:   0.2284 S22:  -0.1164 S23:  -0.0739                       
REMARK   3      S31:   0.1636 S32:   0.0787 S33:   0.0824                       
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 :   J     1        J   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5131   9.2886 -61.9096              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2990 T22:   0.3607                                     
REMARK   3      T33:   0.3101 T12:   0.0396                                     
REMARK   3      T13:  -0.0209 T23:  -0.0364                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5126 L22:   0.8147                                     
REMARK   3      L33:   0.9467 L12:   0.0941                                     
REMARK   3      L13:  -0.0995 L23:  -0.1754                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0248 S12:   0.0793 S13:  -0.0177                       
REMARK   3      S21:  -0.0445 S22:  -0.0752 S23:   0.0888                       
REMARK   3      S31:  -0.0205 S32:   0.0409 S33:   0.0504                       
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 :   K     1        K   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.5590  13.0932 -88.5014              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3797 T22:   0.5032                                     
REMARK   3      T33:   0.1525 T12:   0.0403                                     
REMARK   3      T13:  -0.0412 T23:   0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8459 L22:   0.8026                                     
REMARK   3      L33:   1.4788 L12:  -0.0635                                     
REMARK   3      L13:  -0.0017 L23:   0.3576                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0046 S12:   0.2871 S13:  -0.0639                       
REMARK   3      S21:  -0.1263 S22:  -0.0342 S23:   0.1184                       
REMARK   3      S31:  -0.2376 S32:   0.1997 S33:   0.0296                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.4377   1.9947 -53.9087              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3029 T22:   0.3898                                     
REMARK   3      T33:   0.2982 T12:   0.0240                                     
REMARK   3      T13:  -0.0050 T23:  -0.0379                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3603 L22:   0.4599                                     
REMARK   3      L33:   0.4000 L12:  -0.2258                                     
REMARK   3      L13:   0.0608 L23:   0.1105                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0446 S12:   0.3251 S13:  -0.0474                       
REMARK   3      S21:   0.0711 S22:  -0.0820 S23:   0.0074                       
REMARK   3      S31:  -0.0011 S32:   0.0186 S33:   0.0374                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M     1        M   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.1522  -2.7915 -81.0306              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1803 T22:   1.2178                                     
REMARK   3      T33:   0.0794 T12:   0.1917                                     
REMARK   3      T13:  -0.0065 T23:  -0.2001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8230 L22:   1.3527                                     
REMARK   3      L33:   1.1021 L12:  -0.6703                                     
REMARK   3      L13:   0.1029 L23:  -0.9374                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1926 S12:   1.1576 S13:  -0.1065                       
REMARK   3      S21:  -0.0708 S22:  -0.2079 S23:  -0.0101                       
REMARK   3      S31:   0.0739 S32:   0.2449 S33:   0.0153                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3T5W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-AUG-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB067076.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NUMERICAL LINK TYPE SI(111)        
REMARK 200                                   DOUBLE CRYSTAL MONOCHROMATOR,      
REMARK 200                                   DIRECT WATER COOLING USING MICRO-  
REMARK 200                                   CHANNEL (1ST CRYSTAL), INDIRECT    
REMARK 200                                   WATER COOLING (2ND CRYSTAL)        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 185279                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 118.700                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.88200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1P1V                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 300MM (NH4)2SO4, PH6.0,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       37.04300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       86.81400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       81.63850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       86.81400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.04300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.63850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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: 1860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 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: 1840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 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: 1860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, M                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    HOH A   164     O    HOH A  1746              1.82            
REMARK 500   O    HOH E   525     O    HOH E  1704              2.02            
REMARK 500   O    HOH A  1409     O    HOH A  1675              2.18            
REMARK 500   O    HIS I   110     O    HOH I  1672              2.19            
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    ASN A  65       58.73   -143.75                                   
REMARK 500    ASN B  65       59.23   -147.82                                   
REMARK 500    ALA D  55       53.90   -119.93                                   
REMARK 500    ASN D  65       61.69   -150.39                                   
REMARK 500    ALA G  55       50.53   -117.73                                   
REMARK 500    ASN G  65       57.96   -141.87                                   
REMARK 500    ASP I  90     -167.94    -75.37                                   
REMARK 500    ASN J  65       57.99   -144.46                                   
REMARK 500    ALA K  55       51.53   -119.28                                   
REMARK 500    ASN M  65       79.10   -160.83                                   
REMARK 500    ARG M  69     -162.24   -114.59                                   
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 ASN D   26     GLY D   27                 -149.27                    
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 A1654        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH F1662        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH J1726        DISTANCE =  5.75 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                              ZN J 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP J  83   OD1                                                    
REMARK 620 2 HIS J  63   ND1 100.5                                              
REMARK 620 3 HIS J  71   ND1  97.8 105.6                                        
REMARK 620 4 HIS J  80   ND1 116.7 112.8 120.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  83   OD1                                                    
REMARK 620 2 HIS A  63   ND1 105.9                                              
REMARK 620 3 HIS A  71   ND1  97.2 102.7                                        
REMARK 620 4 HIS A  80   ND1 117.0 108.5 123.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  83   OD1                                                    
REMARK 620 2 HIS D  63   ND1 104.3                                              
REMARK 620 3 HIS D  80   ND1 112.6 114.0                                        
REMARK 620 4 HIS D  71   ND1 100.6 105.2 118.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H  83   OD1                                                    
REMARK 620 2 HIS H  80   ND1 113.1                                              
REMARK 620 3 HIS H  63   ND1 102.9 112.9                                        
REMARK 620 4 HIS H  71   ND1  99.4 120.9 105.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L  83   OD1                                                    
REMARK 620 2 HIS L  63   ND1 101.6                                              
REMARK 620 3 HIS L  80   ND1 114.6 112.2                                        
REMARK 620 4 HIS L  71   ND1  98.6 106.2 121.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I  83   OD1                                                    
REMARK 620 2 HIS I  71   ND1  87.0                                              
REMARK 620 3 HIS I  80   ND1 126.3 121.7                                        
REMARK 620 4 HIS I  63   ND1  82.2 103.0 125.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP K  83   OD1                                                    
REMARK 620 2 HIS K  80   ND1 113.4                                              
REMARK 620 3 HIS K  71   ND1  94.5 117.9                                        
REMARK 620 4 HIS K  63   ND1 102.4 122.1 102.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  83   OD1                                                    
REMARK 620 2 HIS B  63   ND1 102.9                                              
REMARK 620 3 HIS B  80   ND1 114.9 113.4                                        
REMARK 620 4 HIS B  71   ND1  97.8 104.7 120.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 F 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  48   NE2                                                    
REMARK 620 2 HIS F  46   ND1 134.6                                              
REMARK 620 3 HIS F 120   NE2 121.1 104.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  83   OD1                                                    
REMARK 620 2 HIS E  63   ND1 101.6                                              
REMARK 620 3 HIS E  80   ND1 112.8 112.7                                        
REMARK 620 4 HIS E  71   ND1 100.6 105.6 121.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 D 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 120   NE2                                                    
REMARK 620 2 HIS D  48   NE2 122.0                                              
REMARK 620 3 HIS D  46   ND1  98.8 139.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 B 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  48   NE2                                                    
REMARK 620 2 HIS B 120   NE2 117.4                                              
REMARK 620 3 HIS B  46   ND1 141.6  99.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 A 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  48   NE2                                                    
REMARK 620 2 HIS A  46   ND1 140.7                                              
REMARK 620 3 HIS A 120   NE2 118.8 100.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G  83   OD1                                                    
REMARK 620 2 HIS G  63   ND1 105.5                                              
REMARK 620 3 HIS G  80   ND1 111.2 122.1                                        
REMARK 620 4 HIS G  71   ND1  99.3 104.0 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 G 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  46   ND1                                                    
REMARK 620 2 HIS G 120   NE2 101.2                                              
REMARK 620 3 HIS G  48   NE2 143.9 114.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 E 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  48   NE2                                                    
REMARK 620 2 HIS E  46   ND1 139.4                                              
REMARK 620 3 HIS E 120   NE2 119.3 100.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 J 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  48   NE2                                                    
REMARK 620 2 HIS J 120   NE2 118.2                                              
REMARK 620 3 HIS J  46   ND1 143.4  98.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  83   OD1                                                    
REMARK 620 2 HIS F  80   ND1 105.4                                              
REMARK 620 3 HIS F  63   ND1 101.2 114.2                                        
REMARK 620 4 HIS F  71   ND1  97.2 128.5 105.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 H 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  48   NE2                                                    
REMARK 620 2 HIS H 120   NE2 111.4                                              
REMARK 620 3 HIS H  46   ND1 144.1 103.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 L 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L  48   NE2                                                    
REMARK 620 2 HIS L 120   NE2 115.4                                              
REMARK 620 3 HIS L  46   ND1 141.3 102.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 I 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  48   NE2                                                    
REMARK 620 2 HIS I 120   NE2 106.8                                              
REMARK 620 3 HIS I  46   ND1 151.0 101.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN M 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS M  80   ND1                                                    
REMARK 620 2 ASP M  83   OD1 143.5                                              
REMARK 620 3 HIS M  63   ND1 119.9  86.2                                        
REMARK 620 4 HIS M  71   ND1 107.4  92.4  97.3                                  
REMARK 620 5 ASP M  83   OD2  93.8  53.0 137.5  96.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 K 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  48   NE2                                                    
REMARK 620 2 HIS K  46   ND1 147.7                                              
REMARK 620 3 HIS K 120   NE2 112.4  99.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 M 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS M  48   NE2                                                    
REMARK 620 2 HIS M  46   ND1 156.4                                              
REMARK 620 3 HIS M 120   NE2 109.2  94.1                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 D 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 E 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 F 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 G 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 H 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 I 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 J 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 K 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 K 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 L 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 M 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN M 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 400                 
DBREF  3T5W A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3T5W B    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3T5W D    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3T5W E    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3T5W F    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3T5W G    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3T5W H    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3T5W I    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3T5W J    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3T5W K    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3T5W L    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3T5W M    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQRES   1 A  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS CME ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 B  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 B  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 B  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 B  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 B  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 B  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 B  153  SER LEU SER GLY ASP HIS CME ILE ILE GLY ARG THR LEU          
SEQRES  10 B  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 B  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 B  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 D  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 D  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 D  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 D  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 D  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 D  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 D  153  SER LEU SER GLY ASP HIS CME ILE ILE GLY ARG THR LEU          
SEQRES  10 D  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 D  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 D  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 E  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 E  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 E  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 E  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 E  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 E  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 E  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 E  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 E  153  SER LEU SER GLY ASP HIS CME ILE ILE GLY ARG THR LEU          
SEQRES  10 E  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 E  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 E  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 F  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 F  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 F  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 F  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 F  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 F  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 F  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 F  153  SER LEU SER GLY ASP HIS CME ILE ILE GLY ARG THR LEU          
SEQRES  10 F  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 F  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 F  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 G  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 G  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 G  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 G  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 G  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 G  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 G  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 G  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 G  153  SER LEU SER GLY ASP HIS CME ILE ILE GLY ARG THR LEU          
SEQRES  10 G  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 G  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 G  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 H  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 H  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 H  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 H  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 H  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 H  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 H  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 H  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 H  153  SER LEU SER GLY ASP HIS CME ILE ILE GLY ARG THR LEU          
SEQRES  10 H  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 H  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 H  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 I  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 I  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 I  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 I  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 I  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 I  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 I  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 I  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 I  153  SER LEU SER GLY ASP HIS CME ILE ILE GLY ARG THR LEU          
SEQRES  10 I  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 I  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 I  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 J  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 J  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 J  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 J  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 J  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 J  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 J  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 J  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 J  153  SER LEU SER GLY ASP HIS CME ILE ILE GLY ARG THR LEU          
SEQRES  10 J  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 J  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 J  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 K  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 K  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 K  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 K  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 K  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 K  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 K  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 K  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 K  153  SER LEU SER GLY ASP HIS CME ILE ILE GLY ARG THR LEU          
SEQRES  10 K  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 K  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 K  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 L  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 L  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 L  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 L  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 L  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 L  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 L  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 L  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 L  153  SER LEU SER GLY ASP HIS CME ILE ILE GLY ARG THR LEU          
SEQRES  10 L  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 L  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 L  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 M  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 M  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 M  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 M  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 M  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 M  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 M  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 M  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 M  153  SER LEU SER GLY ASP HIS CME ILE ILE GLY ARG THR LEU          
SEQRES  10 M  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 M  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 M  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
MODRES 3T5W CME A  111  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 3T5W CME B  111  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 3T5W CME D  111  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 3T5W CME E  111  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 3T5W CME F  111  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 3T5W CME G  111  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 3T5W CME H  111  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 3T5W CME I  111  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 3T5W CME J  111  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 3T5W CME K  111  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 3T5W CME L  111  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 3T5W CME M  111  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
HET    CME  A 111      10                                                       
HET    CME  B 111      10                                                       
HET    CME  D 111      10                                                       
HET    CME  E 111      10                                                       
HET    CME  F 111      10                                                       
HET    CME  G 111      10                                                       
HET    CME  H 111      10                                                       
HET    CME  I 111      10                                                       
HET    CME  J 111      10                                                       
HET    CME  K 111      10                                                       
HET    CME  L 111      10                                                       
HET    CME  M 111      10                                                       
HET    CU1  A 200       1                                                       
HET     ZN  A 300       1                                                       
HET    SO4  A 400       5                                                       
HET    CU1  B 200       1                                                       
HET     ZN  B 300       1                                                       
HET    SO4  B 400       5                                                       
HET    CU1  D 200       1                                                       
HET     ZN  D 300       1                                                       
HET    SO4  D 400       5                                                       
HET    CU1  E 200       1                                                       
HET     ZN  E 300       1                                                       
HET    SO4  E 400       5                                                       
HET    CU1  F 200       1                                                       
HET     ZN  F 300       1                                                       
HET    SO4  F 400       5                                                       
HET    CU1  G 200       1                                                       
HET     ZN  G 300       1                                                       
HET    SO4  G 400       5                                                       
HET    CU1  H 200       1                                                       
HET     ZN  H 300       1                                                       
HET    SO4  H 400       5                                                       
HET    CU1  I 200       1                                                       
HET     ZN  I 300       1                                                       
HET    SO4  I 400       5                                                       
HET    CU1  J 200       1                                                       
HET     ZN  J 300       1                                                       
HET    SO4  J 400       5                                                       
HET    CU1  K 200       1                                                       
HET     ZN  K 300       1                                                       
HET    SO4  K 400       5                                                       
HET    CU1  L 200       1                                                       
HET     ZN  L 300       1                                                       
HET    SO4  L 400       5                                                       
HET    CU1  M 200       1                                                       
HET     ZN  M 300       1                                                       
HET    SO4  M 400       5                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     CU1 COPPER (I) ION                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  CME    12(C5 H11 N O3 S2)                                           
FORMUL  13  CU1    12(CU 1+)                                                    
FORMUL  14   ZN    12(ZN 2+)                                                    
FORMUL  15  SO4    12(O4 S 2-)                                                  
FORMUL  49  HOH   *1746(H2 O)                                                   
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 SER A  107  CME A  111  5                                   5    
HELIX    3   3 GLU A  132  LYS A  136  5                                   5    
HELIX    4   4 ALA B   55  GLY B   61  5                                   7    
HELIX    5   5 GLU B  133  GLY B  138  1                                   6    
HELIX    6   6 ALA D   55  GLY D   61  5                                   7    
HELIX    7   7 SER D  107  CME D  111  5                                   5    
HELIX    8   8 GLU D  133  GLY D  138  1                                   6    
HELIX    9   9 ALA E   55  GLY E   61  5                                   7    
HELIX   10  10 GLU E  133  GLY E  138  1                                   6    
HELIX   11  11 ALA F   55  GLY F   61  5                                   7    
HELIX   12  12 SER F  107  CME F  111  5                                   5    
HELIX   13  13 GLU F  133  GLY F  138  1                                   6    
HELIX   14  14 ALA G   55  GLY G   61  5                                   7    
HELIX   15  15 GLU G  133  GLY G  138  1                                   6    
HELIX   16  16 CYS H   57  GLY H   61  5                                   5    
HELIX   17  17 SER H  107  CME H  111  5                                   5    
HELIX   18  18 ALA I   55  GLY I   61  5                                   7    
HELIX   19  19 ASN I  131  LYS I  136  5                                   6    
HELIX   20  20 ALA J   55  GLY J   61  5                                   7    
HELIX   21  21 GLU J  132  LYS J  136  5                                   5    
HELIX   22  22 ALA K   55  GLY K   61  5                                   7    
HELIX   23  23 ALA L   55  GLY L   61  5                                   7    
HELIX   24  24 SER L  107  CME L  111  5                                   5    
HELIX   25  25 GLU L  133  GLY L  138  1                                   6    
HELIX   26  26 CYS M   57  GLY M   61  5                                   5    
HELIX   27  27 ASN M  131  THR M  137  1                                   7    
SHEET    1   A 5 ALA A  95  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  ILE A  35   O  ALA A  95           
SHEET    3   A 5 GLN A  15  GLN A  22 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 THR A   2  LEU A   8 -1  N  LEU A   8   O  GLY A  16           
SHEET    5   A 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1   B 4 ASP A  83  ALA A  89  0                                        
SHEET    2   B 4 GLY A  41  HIS A  48 -1  N  GLY A  41   O  ALA A  89           
SHEET    3   B 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4   B 4 ARG A 143  VAL A 148 -1  O  GLY A 147   N  LEU A 117           
SHEET    1   C 5 ALA B  95  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  LYS B  36 -1  N  ILE B  35   O  ALA B  95           
SHEET    3   C 5 GLN B  15  GLN B  22 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 THR B   2  LYS B   9 -1  N  LEU B   8   O  GLY B  16           
SHEET    5   C 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  HIS B  48 -1  N  GLY B  41   O  ALA B  89           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  GLY B 147   N  LEU B 117           
SHEET    1   E 5 ALA D  95  ASP D 101  0                                        
SHEET    2   E 5 VAL D  29  LYS D  36 -1  N  VAL D  31   O  ILE D  99           
SHEET    3   E 5 GLN D  15  GLN D  22 -1  N  ASN D  19   O  TRP D  32           
SHEET    4   E 5 THR D   2  LEU D   8 -1  N  LEU D   8   O  GLY D  16           
SHEET    5   E 5 GLY D 150  ALA D 152 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   F 4 ASP D  83  ALA D  89  0                                        
SHEET    2   F 4 GLY D  41  HIS D  48 -1  N  GLY D  41   O  ALA D  89           
SHEET    3   F 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4   F 4 ARG D 143  VAL D 148 -1  O  GLY D 147   N  LEU D 117           
SHEET    1   G 5 ALA E  95  ASP E 101  0                                        
SHEET    2   G 5 VAL E  29  LYS E  36 -1  N  VAL E  29   O  ASP E 101           
SHEET    3   G 5 GLN E  15  GLN E  22 -1  N  GLN E  15   O  LYS E  36           
SHEET    4   G 5 THR E   2  LYS E   9 -1  N  THR E   2   O  GLN E  22           
SHEET    5   G 5 GLY E 150  ILE E 151 -1  O  GLY E 150   N  VAL E   5           
SHEET    1   H 4 ASP E  83  ALA E  89  0                                        
SHEET    2   H 4 GLY E  41  HIS E  48 -1  N  GLY E  41   O  ALA E  89           
SHEET    3   H 4 THR E 116  HIS E 120 -1  O  THR E 116   N  HIS E  48           
SHEET    4   H 4 ARG E 143  VAL E 148 -1  O  GLY E 147   N  LEU E 117           
SHEET    1   I 5 ALA F  95  ASP F 101  0                                        
SHEET    2   I 5 VAL F  29  LYS F  36 -1  N  VAL F  31   O  ILE F  99           
SHEET    3   I 5 GLN F  15  GLN F  22 -1  N  ASN F  19   O  TRP F  32           
SHEET    4   I 5 THR F   2  LEU F   8 -1  N  THR F   2   O  GLN F  22           
SHEET    5   I 5 GLY F 150  ALA F 152 -1  O  GLY F 150   N  VAL F   5           
SHEET    1   J 4 ASP F  83  ALA F  89  0                                        
SHEET    2   J 4 GLY F  41  HIS F  48 -1  N  HIS F  43   O  VAL F  87           
SHEET    3   J 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4   J 4 ARG F 143  VAL F 148 -1  O  GLY F 147   N  LEU F 117           
SHEET    1   K 5 ALA G  95  ASP G 101  0                                        
SHEET    2   K 5 VAL G  29  LYS G  36 -1  N  VAL G  29   O  ASP G 101           
SHEET    3   K 5 GLN G  15  GLN G  22 -1  N  ASN G  19   O  TRP G  32           
SHEET    4   K 5 THR G   2  LYS G   9 -1  N  LEU G   8   O  GLY G  16           
SHEET    5   K 5 GLY G 150  ALA G 152 -1  O  GLY G 150   N  VAL G   5           
SHEET    1   L 4 ASP G  83  ALA G  89  0                                        
SHEET    2   L 4 GLY G  41  HIS G  48 -1  N  GLY G  41   O  ALA G  89           
SHEET    3   L 4 THR G 116  HIS G 120 -1  O  THR G 116   N  HIS G  48           
SHEET    4   L 4 ARG G 143  VAL G 148 -1  O  GLY G 147   N  LEU G 117           
SHEET    1   M 5 ALA H  95  ASP H 101  0                                        
SHEET    2   M 5 VAL H  29  LYS H  36 -1  N  VAL H  31   O  ILE H  99           
SHEET    3   M 5 GLN H  15  GLN H  22 -1  N  GLN H  15   O  LYS H  36           
SHEET    4   M 5 THR H   2  LYS H   9 -1  N  LEU H   8   O  GLY H  16           
SHEET    5   M 5 GLY H 150  ALA H 152 -1  O  GLY H 150   N  VAL H   5           
SHEET    1   N 4 ASP H  83  ALA H  89  0                                        
SHEET    2   N 4 GLY H  41  HIS H  48 -1  N  GLY H  41   O  ALA H  89           
SHEET    3   N 4 THR H 116  HIS H 120 -1  O  THR H 116   N  HIS H  48           
SHEET    4   N 4 ARG H 143  VAL H 148 -1  O  GLY H 147   N  LEU H 117           
SHEET    1   O 5 ALA I  95  ASP I 101  0                                        
SHEET    2   O 5 VAL I  29  LYS I  36 -1  N  VAL I  31   O  ILE I  99           
SHEET    3   O 5 GLN I  15  GLN I  22 -1  N  GLN I  15   O  LYS I  36           
SHEET    4   O 5 THR I   2  LEU I   8 -1  N  LEU I   8   O  GLY I  16           
SHEET    5   O 5 GLY I 150  ILE I 151 -1  O  GLY I 150   N  VAL I   5           
SHEET    1   P 4 ASP I  83  ALA I  89  0                                        
SHEET    2   P 4 GLY I  41  HIS I  48 -1  N  GLY I  41   O  ALA I  89           
SHEET    3   P 4 THR I 116  HIS I 120 -1  O  THR I 116   N  HIS I  48           
SHEET    4   P 4 ARG I 143  VAL I 148 -1  O  GLY I 147   N  LEU I 117           
SHEET    1   Q 5 ALA J  95  ASP J 101  0                                        
SHEET    2   Q 5 VAL J  29  LYS J  36 -1  N  VAL J  31   O  ILE J  99           
SHEET    3   Q 5 GLN J  15  GLN J  22 -1  N  ASN J  19   O  TRP J  32           
SHEET    4   Q 5 THR J   2  LEU J   8 -1  N  ALA J   4   O  PHE J  20           
SHEET    5   Q 5 GLY J 150  ILE J 151 -1  O  GLY J 150   N  VAL J   5           
SHEET    1   R 4 ASP J  83  ALA J  89  0                                        
SHEET    2   R 4 GLY J  41  HIS J  48 -1  N  GLY J  41   O  ALA J  89           
SHEET    3   R 4 THR J 116  HIS J 120 -1  O  THR J 116   N  HIS J  48           
SHEET    4   R 4 ARG J 143  VAL J 148 -1  O  GLY J 147   N  LEU J 117           
SHEET    1   S 5 ALA K  95  ASP K 101  0                                        
SHEET    2   S 5 VAL K  29  LYS K  36 -1  N  ILE K  35   O  ALA K  95           
SHEET    3   S 5 GLN K  15  GLN K  22 -1  N  ASN K  19   O  TRP K  32           
SHEET    4   S 5 THR K   2  LEU K   8 -1  N  LEU K   8   O  GLY K  16           
SHEET    5   S 5 GLY K 150  ILE K 151 -1  O  GLY K 150   N  VAL K   5           
SHEET    1   T 4 ASP K  83  ALA K  89  0                                        
SHEET    2   T 4 GLY K  41  HIS K  48 -1  N  HIS K  43   O  VAL K  87           
SHEET    3   T 4 THR K 116  HIS K 120 -1  O  THR K 116   N  HIS K  48           
SHEET    4   T 4 ARG K 143  VAL K 148 -1  O  ALA K 145   N  VAL K 119           
SHEET    1   U 5 ALA L  95  ASP L 101  0                                        
SHEET    2   U 5 VAL L  29  LYS L  36 -1  N  VAL L  29   O  ASP L 101           
SHEET    3   U 5 GLN L  15  GLN L  22 -1  N  ASN L  19   O  TRP L  32           
SHEET    4   U 5 THR L   2  LEU L   8 -1  N  ALA L   4   O  PHE L  20           
SHEET    5   U 5 GLY L 150  ILE L 151 -1  O  GLY L 150   N  VAL L   5           
SHEET    1   V 4 ASP L  83  ALA L  89  0                                        
SHEET    2   V 4 GLY L  41  HIS L  48 -1  N  GLY L  41   O  ALA L  89           
SHEET    3   V 4 THR L 116  HIS L 120 -1  O  THR L 116   N  HIS L  48           
SHEET    4   V 4 ARG L 143  VAL L 148 -1  O  ALA L 145   N  VAL L 119           
SHEET    1   W 5 ALA M  95  ILE M  99  0                                        
SHEET    2   W 5 LYS M  30  LYS M  36 -1  N  ILE M  35   O  ALA M  95           
SHEET    3   W 5 GLN M  15  GLN M  22 -1  N  ASN M  19   O  TRP M  32           
SHEET    4   W 5 THR M   2  LEU M   8 -1  N  ALA M   4   O  PHE M  20           
SHEET    5   W 5 GLY M 150  ILE M 151 -1  O  GLY M 150   N  VAL M   5           
SHEET    1   X 4 ASP M  83  ALA M  89  0                                        
SHEET    2   X 4 GLY M  41  HIS M  48 -1  N  GLY M  41   O  ALA M  89           
SHEET    3   X 4 THR M 116  HIS M 120 -1  O  THR M 116   N  HIS M  48           
SHEET    4   X 4 ARG M 143  VAL M 148 -1  O  ALA M 145   N  VAL M 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.10  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.09  
SSBOND   3 CYS D   57    CYS D  146                          1555   1555  2.10  
SSBOND   4 CYS E   57    CYS E  146                          1555   1555  2.09  
SSBOND   5 CYS F   57    CYS F  146                          1555   1555  2.04  
SSBOND   6 CYS G   57    CYS G  146                          1555   1555  2.05  
SSBOND   7 CYS H   57    CYS H  146                          1555   1555  2.04  
SSBOND   8 CYS I   57    CYS I  146                          1555   1555  2.05  
SSBOND   9 CYS J   57    CYS J  146                          1555   1555  2.04  
SSBOND  10 CYS K   57    CYS K  146                          1555   1555  2.05  
SSBOND  11 CYS L   57    CYS L  146                          1555   1555  2.04  
SSBOND  12 CYS M   57    CYS M  146                          1555   1555  2.04  
LINK         C   HIS A 110                 N   CME A 111     1555   1555  1.34  
LINK         C   CME A 111                 N   ILE A 112     1555   1555  1.32  
LINK         C   HIS B 110                 N   CME B 111     1555   1555  1.33  
LINK         C   CME B 111                 N   ILE B 112     1555   1555  1.34  
LINK         C   HIS D 110                 N   CME D 111     1555   1555  1.33  
LINK         C   CME D 111                 N   ILE D 112     1555   1555  1.33  
LINK         C   HIS E 110                 N   CME E 111     1555   1555  1.33  
LINK         C   CME E 111                 N   ILE E 112     1555   1555  1.33  
LINK         C   HIS F 110                 N   CME F 111     1555   1555  1.34  
LINK         C   CME F 111                 N   ILE F 112     1555   1555  1.34  
LINK         C   HIS G 110                 N   CME G 111     1555   1555  1.33  
LINK         C   CME G 111                 N   ILE G 112     1555   1555  1.33  
LINK         C   HIS H 110                 N   CME H 111     1555   1555  1.34  
LINK         C   CME H 111                 N   ILE H 112     1555   1555  1.33  
LINK         C   HIS I 110                 N   CME I 111     1555   1555  1.33  
LINK         C   CME I 111                 N   ILE I 112     1555   1555  1.33  
LINK         C   HIS J 110                 N   CME J 111     1555   1555  1.34  
LINK         C   CME J 111                 N   ILE J 112     1555   1555  1.33  
LINK         C   HIS K 110                 N   CME K 111     1555   1555  1.33  
LINK         C   CME K 111                 N   ILE K 112     1555   1555  1.33  
LINK         C   HIS L 110                 N   CME L 111     1555   1555  1.34  
LINK         C   CME L 111                 N   ILE L 112     1555   1555  1.33  
LINK         C   HIS M 110                 N   CME M 111     1555   1555  1.34  
LINK         C   CME M 111                 N   ILE M 112     1555   1555  1.34  
LINK         OD1 ASP J  83                ZN    ZN J 300     1555   1555  1.94  
LINK         OD1 ASP A  83                ZN    ZN A 300     1555   1555  1.94  
LINK         OD1 ASP D  83                ZN    ZN D 300     1555   1555  1.95  
LINK         OD1 ASP H  83                ZN    ZN H 300     1555   1555  1.96  
LINK         OD1 ASP L  83                ZN    ZN L 300     1555   1555  1.97  
LINK         OD1 ASP I  83                ZN    ZN I 300     1555   1555  1.98  
LINK         OD1 ASP K  83                ZN    ZN K 300     1555   1555  2.00  
LINK         OD1 ASP B  83                ZN    ZN B 300     1555   1555  2.00  
LINK         NE2 HIS F  48                CU   CU1 F 200     1555   1555  2.01  
LINK         OD1 ASP E  83                ZN    ZN E 300     1555   1555  2.01  
LINK         NE2 HIS D 120                CU   CU1 D 200     1555   1555  2.02  
LINK         NE2 HIS B  48                CU   CU1 B 200     1555   1555  2.02  
LINK         NE2 HIS A  48                CU   CU1 A 200     1555   1555  2.02  
LINK         OD1 ASP G  83                ZN    ZN G 300     1555   1555  2.02  
LINK         ND1 HIS G  46                CU   CU1 G 200     1555   1555  2.02  
LINK         NE2 HIS E  48                CU   CU1 E 200     1555   1555  2.03  
LINK         NE2 HIS G 120                CU   CU1 G 200     1555   1555  2.03  
LINK         ND1 HIS A  46                CU   CU1 A 200     1555   1555  2.03  
LINK         NE2 HIS D  48                CU   CU1 D 200     1555   1555  2.04  
LINK         ND1 HIS D  46                CU   CU1 D 200     1555   1555  2.04  
LINK         NE2 HIS J  48                CU   CU1 J 200     1555   1555  2.04  
LINK         OD1 ASP F  83                ZN    ZN F 300     1555   1555  2.05  
LINK         ND1 HIS E  46                CU   CU1 E 200     1555   1555  2.05  
LINK         NE2 HIS H  48                CU   CU1 H 200     1555   1555  2.05  
LINK         NE2 HIS E 120                CU   CU1 E 200     1555   1555  2.05  
LINK         NE2 HIS B 120                CU   CU1 B 200     1555   1555  2.05  
LINK         NE2 HIS H 120                CU   CU1 H 200     1555   1555  2.05  
LINK         NE2 HIS G  48                CU   CU1 G 200     1555   1555  2.06  
LINK         NE2 HIS L  48                CU   CU1 L 200     1555   1555  2.06  
LINK         NE2 HIS I  48                CU   CU1 I 200     1555   1555  2.06  
LINK         ND1 HIS K  80                ZN    ZN K 300     1555   1555  2.06  
LINK         ND1 HIS F  46                CU   CU1 F 200     1555   1555  2.06  
LINK         ND1 HIS M  80                ZN    ZN M 300     1555   1555  2.06  
LINK         ND1 HIS A  63                ZN    ZN A 300     1555   1555  2.06  
LINK         ND1 HIS L  63                ZN    ZN L 300     1555   1555  2.06  
LINK         ND1 HIS H  46                CU   CU1 H 200     1555   1555  2.07  
LINK         NE2 HIS K  48                CU   CU1 K 200     1555   1555  2.07  
LINK         NE2 HIS A 120                CU   CU1 A 200     1555   1555  2.07  
LINK         ND1 HIS F  80                ZN    ZN F 300     1555   1555  2.07  
LINK         NE2 HIS F 120                CU   CU1 F 200     1555   1555  2.07  
LINK         ND1 HIS E  63                ZN    ZN E 300     1555   1555  2.08  
LINK         NE2 HIS J 120                CU   CU1 J 200     1555   1555  2.08  
LINK         NE2 HIS L 120                CU   CU1 L 200     1555   1555  2.08  
LINK         ND1 HIS B  63                ZN    ZN B 300     1555   1555  2.08  
LINK         NE2 HIS I 120                CU   CU1 I 200     1555   1555  2.08  
LINK         ND1 HIS D  63                ZN    ZN D 300     1555   1555  2.08  
LINK         ND1 HIS J  46                CU   CU1 J 200     1555   1555  2.08  
LINK         ND1 HIS L  46                CU   CU1 L 200     1555   1555  2.08  
LINK         ND1 HIS H  80                ZN    ZN H 300     1555   1555  2.08  
LINK         ND1 HIS B  46                CU   CU1 B 200     1555   1555  2.09  
LINK         ND1 HIS K  46                CU   CU1 K 200     1555   1555  2.09  
LINK         ND1 HIS J  63                ZN    ZN J 300     1555   1555  2.09  
LINK         ND1 HIS E  80                ZN    ZN E 300     1555   1555  2.09  
LINK         ND1 HIS F  63                ZN    ZN F 300     1555   1555  2.09  
LINK         ND1 HIS I  46                CU   CU1 I 200     1555   1555  2.10  
LINK         ND1 HIS H  63                ZN    ZN H 300     1555   1555  2.11  
LINK         ND1 HIS B  80                ZN    ZN B 300     1555   1555  2.11  
LINK         NE2 HIS M  48                CU   CU1 M 200     1555   1555  2.11  
LINK         ND1 HIS A  71                ZN    ZN A 300     1555   1555  2.11  
LINK         ND1 HIS L  80                ZN    ZN L 300     1555   1555  2.11  
LINK         ND1 HIS E  71                ZN    ZN E 300     1555   1555  2.11  
LINK         ND1 HIS G  63                ZN    ZN G 300     1555   1555  2.11  
LINK         ND1 HIS D  80                ZN    ZN D 300     1555   1555  2.11  
LINK         ND1 HIS A  80                ZN    ZN A 300     1555   1555  2.12  
LINK         ND1 HIS B  71                ZN    ZN B 300     1555   1555  2.12  
LINK         ND1 HIS H  71                ZN    ZN H 300     1555   1555  2.12  
LINK         ND1 HIS D  71                ZN    ZN D 300     1555   1555  2.12  
LINK         ND1 HIS J  71                ZN    ZN J 300     1555   1555  2.12  
LINK         ND1 HIS G  80                ZN    ZN G 300     1555   1555  2.13  
LINK         NE2 HIS K 120                CU   CU1 K 200     1555   1555  2.13  
LINK         ND1 HIS L  71                ZN    ZN L 300     1555   1555  2.13  
LINK         ND1 HIS F  71                ZN    ZN F 300     1555   1555  2.13  
LINK         ND1 HIS J  80                ZN    ZN J 300     1555   1555  2.15  
LINK         ND1 HIS K  71                ZN    ZN K 300     1555   1555  2.15  
LINK         ND1 HIS K  63                ZN    ZN K 300     1555   1555  2.15  
LINK         ND1 HIS M  46                CU   CU1 M 200     1555   1555  2.16  
LINK         OD1 ASP M  83                ZN    ZN M 300     1555   1555  2.16  
LINK         ND1 HIS I  71                ZN    ZN I 300     1555   1555  2.16  
LINK         ND1 HIS G  71                ZN    ZN G 300     1555   1555  2.16  
LINK         ND1 HIS I  80                ZN    ZN I 300     1555   1555  2.17  
LINK         ND1 HIS I  63                ZN    ZN I 300     1555   1555  2.18  
LINK         NE2 HIS M 120                CU   CU1 M 200     1555   1555  2.21  
LINK         ND1 HIS M  63                ZN    ZN M 300     1555   1555  2.31  
LINK         ND1 HIS M  71                ZN    ZN M 300     1555   1555  2.36  
LINK         OD2 ASP M  83                ZN    ZN M 300     1555   1555  2.65  
SITE     1 AC1  4 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     1 AC2  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC3 10 GLU A 133  THR A 137  ASN A 139  ALA A 140                    
SITE     2 AC3 10 GLY A 141  HOH A 170  HOH A 779  HOH A1035                    
SITE     3 AC3 10 HOH A1109  HOH A1579                                          
SITE     1 AC4  4 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 AC5  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC6  7 GLU B 133  THR B 137  ASN B 139  GLY B 141                    
SITE     2 AC6  7 HOH B 171  HOH B 482  HOH B1055                               
SITE     1 AC7  4 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     1 AC8  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 AC9  8 GLU D 133  THR D 137  ASN D 139  GLY D 141                    
SITE     2 AC9  8 HOH D 182  HOH D 608  HOH D 824  HOH D1058                    
SITE     1 BC1  4 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     1 BC2  5 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     2 BC2  5 LYS E 136                                                     
SITE     1 BC3  7 GLU E 133  THR E 137  ASN E 139  GLY E 141                    
SITE     2 BC3  7 HOH E 187  HOH E 460  HOH E1164                               
SITE     1 BC4  4 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     1 BC5  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC6  6 GLU F 133  THR F 137  ASN F 139  ALA F 140                    
SITE     2 BC6  6 GLY F 141  HOH F 274                                          
SITE     1 BC7  4 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     1 BC8  4 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     1 BC9  8 GLU G 133  THR G 137  ASN G 139  ALA G 140                    
SITE     2 BC9  8 GLY G 141  HOH G 857  HOH G 883  HOH G1243                    
SITE     1 CC1  4 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     1 CC2  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 CC3  6 GLU H 133  THR H 137  ASN H 139  GLY H 141                    
SITE     2 CC3  6 HOH H 750  HOH H1048                                          
SITE     1 CC4  4 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     1 CC5  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 CC6  5 GLU I 133  THR I 137  ASN I 139  ALA I 140                    
SITE     2 CC6  5 GLY I 141                                                     
SITE     1 CC7  4 HIS J  46  HIS J  48  HIS J  63  HIS J 120                    
SITE     1 CC8  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
SITE     1 CC9  8 GLU J 133  THR J 137  ASN J 139  ALA J 140                    
SITE     2 CC9  8 GLY J 141  HOH J 391  HOH J1378  HOH J1547                    
SITE     1 DC1  4 HIS K  46  HIS K  48  HIS K  63  HIS K 120                    
SITE     1 DC2  4 HIS K  63  HIS K  71  HIS K  80  ASP K  83                    
SITE     1 DC3  5 GLU K 133  THR K 137  ASN K 139  ALA K 140                    
SITE     2 DC3  5 GLY K 141                                                     
SITE     1 DC4  4 HIS L  46  HIS L  48  HIS L  63  HIS L 120                    
SITE     1 DC5  4 HIS L  63  HIS L  71  HIS L  80  ASP L  83                    
SITE     1 DC6  8 LYS L 122  GLU L 133  THR L 137  ASN L 139                    
SITE     2 DC6  8 ALA L 140  GLY L 141  HOH L 162  HOH L 527                    
SITE     1 DC7  4 HIS M  46  HIS M  48  HIS M  63  HIS M 120                    
SITE     1 DC8  4 HIS M  63  HIS M  71  HIS M  80  ASP M  83                    
SITE     1 DC9  5 GLU M 133  THR M 137  ASN M 139  ALA M 140                    
SITE     2 DC9  5 GLY M 141                                                     
CRYST1   74.086  163.277  173.628  90.00  90.00  90.00 P 21 21 21   48          
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      0.013498  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006125  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005759        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system