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Database: PDB
Entry: 3KH3
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HEADER    OXIDOREDUCTASE                          30-OCT-09   3KH3              
TITLE     CRYSTAL STRUCTURE OF HUMAN CU/ZN SUPEROXIDE DISMUTASE RECOMBINANTLY   
TITLE    2 PRODUCED IN LEISHMANIA TARANTOLAE; P212121 CRYSTAL FORM CONTAINING 12
TITLE    3 CHAINS IN THE ASYMMETRIC UNIT                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 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: LEISHMANIA TARENTOLAE;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 5689;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: P10;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: CHROMOSOMAL INTEGRATION               
KEYWDS    EUKARYOTIC EXPRESSION, LEISHMANIA TARANTOLAE, AMYOTROPHIC LATERAL     
KEYWDS   2 SCLEROSIS, ANTIOXIDANT, DISEASE MUTATION, DISULFIDE BOND, METAL-     
KEYWDS   3 BINDING, NEURODEGENERATION, OXIDOREDUCTASE, PHOSPHOPROTEIN           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.M.GAZDAG,W.BLANKENFELDT                                             
REVDAT   2   01-SEP-10 3KH3    1       JRNL                                     
REVDAT   1   11-AUG-10 3KH3    0                                                
JRNL        AUTH   E.M.GAZDAG,I.C.CIRSTEA,R.BREITLING,J.LUKES,W.BLANKENFELDT,   
JRNL        AUTH 2 K.ALEXANDROV                                                 
JRNL        TITL   PURIFICATION AND CRYSTALLIZATION OF HUMAN CU/ZN SUPEROXIDE   
JRNL        TITL 2 DISMUTASE RECOMBINANTLY PRODUCED IN THE PROTOZOAN LEISHMANIA 
JRNL        TITL 3 TARENTOLAE.                                                  
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  66   871 2010              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   20693657                                                     
JRNL        DOI    10.1107/S1744309110019330                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 28597                          
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) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1446                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1993                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 107                          
REMARK   3   BIN FREE R VALUE                    : 0.3110                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13312                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.62                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.38000                                              
REMARK   3    B22 (A**2) : 4.59000                                              
REMARK   3    B33 (A**2) : -4.97000                                             
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): 0.692         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.491         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 70.354        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.862                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.811                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13552 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  8952 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18296 ; 1.173 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22042 ; 4.443 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1824 ; 6.284 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   575 ;39.026 ;25.652       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2216 ;16.443 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    47 ;10.638 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2015 ; 0.062 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15631 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2444 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8940 ; 0.147 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3900 ; 0.000 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14205 ; 0.270 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4612 ; 0.368 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4091 ; 0.651 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C E F G H I J K L           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      3       A     155      4                      
REMARK   3           1     B      3       B     155      4                      
REMARK   3           1     C      3       C     155      4                      
REMARK   3           1     E      3       E     155      4                      
REMARK   3           1     F      3       F     155      4                      
REMARK   3           1     G      3       G     155      4                      
REMARK   3           1     H      3       H     155      4                      
REMARK   3           1     I      3       I     155      4                      
REMARK   3           1     J      3       J     155      4                      
REMARK   3           1     K      3       K     155      4                      
REMARK   3           1     L      3       L     155      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1825 ; 0.030 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1825 ; 0.030 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1825 ; 0.040 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1825 ; 0.040 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):   1825 ; 0.030 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    G    (A):   1825 ; 0.040 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    H    (A):   1825 ; 0.040 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    I    (A):   1825 ; 0.030 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    J    (A):   1825 ; 0.040 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    K    (A):   1825 ; 0.040 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    L    (A):   1825 ; 0.030 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1825 ; 0.060 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1825 ; 0.080 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1825 ; 0.070 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1825 ; 0.100 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    F (A**2):   1825 ; 0.070 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    G (A**2):   1825 ; 0.080 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    H (A**2):   1825 ; 0.070 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    I (A**2):   1825 ; 0.060 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    J (A**2):   1825 ; 0.080 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    K (A**2):   1825 ; 0.090 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    L (A**2):   1825 ; 0.060 ; 2.000           
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     2        A   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.4313 -49.9097 -21.1910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4139 T22:   0.1781                                     
REMARK   3      T33:   0.3514 T12:  -0.0350                                     
REMARK   3      T13:  -0.0667 T23:   0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2744 L22:   7.2183                                     
REMARK   3      L33:   3.7510 L12:   0.7487                                     
REMARK   3      L13:   0.3096 L23:   0.1411                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1558 S12:  -0.0448 S13:  -0.5022                       
REMARK   3      S21:   0.7686 S22:  -0.0308 S23:  -0.2409                       
REMARK   3      S31:   0.4991 S32:   0.1612 S33:  -0.1251                       
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     2        B   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9960 -23.2487 -30.3087              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0521 T22:   0.2187                                     
REMARK   3      T33:   0.1735 T12:  -0.0983                                     
REMARK   3      T13:  -0.0167 T23:   0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1522 L22:   7.2689                                     
REMARK   3      L33:   3.1711 L12:  -0.9171                                     
REMARK   3      L13:   0.4097 L23:  -0.7853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1215 S12:  -0.0481 S13:  -0.1694                       
REMARK   3      S21:   0.1525 S22:  -0.1554 S23:  -0.1793                       
REMARK   3      S31:  -0.1192 S32:   0.1804 S33:   0.0339                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.7635   8.2147 -24.7897              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7980 T22:   0.2997                                     
REMARK   3      T33:   0.3946 T12:  -0.2973                                     
REMARK   3      T13:   0.2961 T23:  -0.1415                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9731 L22:   8.2655                                     
REMARK   3      L33:   7.4126 L12:   4.1013                                     
REMARK   3      L13:   0.5654 L23:   0.8692                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.3358 S12:  -0.7736 S13:   0.6771                       
REMARK   3      S21:   1.5519 S22:  -1.1060 S23:   0.5968                       
REMARK   3      S31:  -0.5194 S32:  -0.0183 S33:  -0.2298                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.5329  29.4846  -7.0148              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8306 T22:   0.7554                                     
REMARK   3      T33:   0.9753 T12:  -0.7285                                     
REMARK   3      T13:   0.5790 T23:  -0.6373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4899 L22:   1.8470                                     
REMARK   3      L33:   2.4108 L12:   0.5688                                     
REMARK   3      L13:  -1.4693 L23:  -1.9231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3452 S12:  -0.4842 S13:   0.9601                       
REMARK   3      S21:   0.8305 S22:  -0.0927 S23:   0.1022                       
REMARK   3      S31:  -0.6618 S32:   0.0694 S33:  -0.2525                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     2        E   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1561   1.1889 -81.9817              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5932 T22:   1.9314                                     
REMARK   3      T33:   0.3790 T12:   0.1944                                     
REMARK   3      T13:  -0.1393 T23:   0.1829                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8288 L22:   4.8750                                     
REMARK   3      L33:   6.8400 L12:   0.6980                                     
REMARK   3      L13:   0.8190 L23:  -0.7047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1499 S12:   1.7489 S13:   0.5114                       
REMARK   3      S21:  -0.7859 S22:  -0.0060 S23:   0.3482                       
REMARK   3      S31:  -0.5637 S32:  -0.9815 S33:  -0.1439                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     2        F   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0676  -2.9103 -54.3841              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0942 T22:   0.4460                                     
REMARK   3      T33:   0.2699 T12:   0.0973                                     
REMARK   3      T13:  -0.0879 T23:  -0.0472                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7782 L22:   4.0620                                     
REMARK   3      L33:   7.4643 L12:   0.0312                                     
REMARK   3      L13:  -1.3737 L23:  -1.5419                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1908 S12:   0.9023 S13:   0.2463                       
REMARK   3      S21:  -0.1229 S22:  -0.1887 S23:   0.1255                       
REMARK   3      S31:  -0.3568 S32:  -0.0593 S33:  -0.0021                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     2        G   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.8071 -45.7141 -58.8609              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9679 T22:   0.3148                                     
REMARK   3      T33:   0.5406 T12:   0.2679                                     
REMARK   3      T13:  -0.2116 T23:  -0.0870                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7988 L22:   7.1795                                     
REMARK   3      L33:   5.2668 L12:  -1.0241                                     
REMARK   3      L13:  -0.5424 L23:  -0.2508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2991 S12:   0.2318 S13:   0.3372                       
REMARK   3      S21:  -1.3705 S22:  -0.2947 S23:   0.4657                       
REMARK   3      S31:  -0.6551 S32:  -0.2638 S33:  -0.0044                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     2        H   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.8359 -72.4777 -49.3801              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2917 T22:   0.1758                                     
REMARK   3      T33:   0.2744 T12:   0.1320                                     
REMARK   3      T13:  -0.1746 T23:  -0.1223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7682 L22:   7.8526                                     
REMARK   3      L33:   4.0150 L12:   1.2791                                     
REMARK   3      L13:  -0.6031 L23:   0.4899                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2017 S12:   0.0302 S13:  -0.0697                       
REMARK   3      S21:  -0.7080 S22:  -0.3597 S23:   0.3328                       
REMARK   3      S31:  -0.3704 S32:  -0.1084 S33:   0.1580                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     2        I   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.1661-126.2632 -72.3537              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3979 T22:   0.1912                                     
REMARK   3      T33:   0.3902 T12:   0.0320                                     
REMARK   3      T13:   0.0712 T23:  -0.1226                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3934 L22:   4.4077                                     
REMARK   3      L33:   5.1304 L12:   1.1024                                     
REMARK   3      L13:   2.0547 L23:   1.4769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0676 S12:   0.2312 S13:  -0.3905                       
REMARK   3      S21:  -0.1605 S22:  -0.0648 S23:  -0.1320                       
REMARK   3      S31:   0.7952 S32:   0.0384 S33:  -0.0028                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     2        J   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7888-104.3244 -54.6040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0031 T22:   0.1188                                     
REMARK   3      T33:   0.3528 T12:   0.0096                                     
REMARK   3      T13:  -0.0167 T23:  -0.0682                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3692 L22:   4.4276                                     
REMARK   3      L33:   5.8625 L12:  -0.7387                                     
REMARK   3      L13:   0.3815 L23:   2.3823                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0318 S12:  -0.0969 S13:   0.0174                       
REMARK   3      S21:  -0.0600 S22:  -0.0480 S23:  -0.1752                       
REMARK   3      S31:  -0.0627 S32:   0.2816 S33:   0.0163                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K     2        K   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3584 -97.9055   1.6761              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6855 T22:   1.4958                                     
REMARK   3      T33:   0.3328 T12:  -0.0340                                     
REMARK   3      T13:   0.0007 T23:   0.2584                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2207 L22:   4.2830                                     
REMARK   3      L33:   7.1028 L12:   0.9784                                     
REMARK   3      L13:  -1.3866 L23:  -0.8843                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0246 S12:  -1.5516 S13:  -0.5334                       
REMARK   3      S21:   0.8752 S22:  -0.2963 S23:  -0.1015                       
REMARK   3      S31:   0.6845 S32:   0.9814 S33:   0.3209                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     2        L   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1565 -93.0065 -25.2774              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1773 T22:   0.4100                                     
REMARK   3      T33:   0.2611 T12:  -0.1199                                     
REMARK   3      T13:   0.0519 T23:  -0.0512                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3295 L22:   3.5343                                     
REMARK   3      L33:   7.6604 L12:  -0.2018                                     
REMARK   3      L13:   1.5269 L23:  -1.2132                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1032 S12:  -0.4247 S13:  -0.2909                       
REMARK   3      S21:   0.3294 S22:  -0.2509 S23:   0.1062                       
REMARK   3      S31:   0.1552 S32:   0.3157 S33:   0.1477                       
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:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3   U VALUES: RESIDUAL ONLY                                            
REMARK   4                                                                      
REMARK   4 3KH3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-NOV-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055984.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.2-5.2                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9797                             
REMARK 200  MONOCHROMATOR                  : SI(111) MONOCHROMATOR              
REMARK 200  OPTICS                         : SI(111)                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28607                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.18900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21-25% (W/V) PEG4000, 0.1 M NAOAC, PH    
REMARK 280  4.2-5.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K            
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       37.75000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       87.49000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       83.30500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       87.49000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.75000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       83.30500            
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: 1600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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: 1560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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: 1340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 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: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 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: 1470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 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: 1340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL E  95    CG1  CG2                                            
REMARK 470     ARG K  70    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP E    84    ZN     ZN E   156              1.69            
REMARK 500   O    LYS D    10     O    CYS D   147              2.02            
REMARK 500   O    PHE D    51     OG1  THR D   117              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CD1  TRP A    33     OE1  GLU I   133     2545     2.05            
REMARK 500   CB   PRO F    14     OE1  GLU H    41     3554     2.17            
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    ALA A  56       47.66   -102.28                                   
REMARK 500    LYS A  92      -64.15    -18.56                                   
REMARK 500    SER A  99       86.86   -151.39                                   
REMARK 500    ALA B  56       49.52   -105.90                                   
REMARK 500    LYS B  92      -65.03    -15.81                                   
REMARK 500    SER B  99       88.99   -151.10                                   
REMARK 500    ALA C  56       52.13   -102.99                                   
REMARK 500    LYS C  92      -62.80    -18.00                                   
REMARK 500    SER C  99       82.21   -152.33                                   
REMARK 500    LYS D  10     -168.96    -65.68                                   
REMARK 500    ASP D  12       31.90   -143.32                                   
REMARK 500    PRO D  14       33.27    -99.97                                   
REMARK 500    VAL D  32      103.69   -170.92                                   
REMARK 500    SER D  35     -177.39    162.20                                   
REMARK 500    ILE D  36       85.33   -158.26                                   
REMARK 500    THR D  40     -128.59    -81.39                                   
REMARK 500    ASP D  53       71.41   -152.79                                   
REMARK 500    LEU D  68      -71.02    -96.81                                   
REMARK 500    SER D  69       33.63    158.30                                   
REMARK 500    HIS D  72      150.61    -47.74                                   
REMARK 500    VAL D  82       -7.64    -54.83                                   
REMARK 500    VAL D  95       60.70   -108.03                                   
REMARK 500    SER D  99       59.46   -161.69                                   
REMARK 500    LEU D 107       54.93   -105.93                                   
REMARK 500    SER D 108      151.43    178.74                                   
REMARK 500    CYS D 112      105.11    -40.48                                   
REMARK 500    LYS D 137      -55.08   -144.49                                   
REMARK 500    ALA E  56       50.08   -101.04                                   
REMARK 500    LYS E  92      -65.73    -17.13                                   
REMARK 500    VAL E  95     -154.66     85.87                                   
REMARK 500    SER E  99       87.64   -152.13                                   
REMARK 500    ALA F  56       47.39    -99.00                                   
REMARK 500    LYS F  92      -64.41    -16.13                                   
REMARK 500    SER F  99       88.12   -151.27                                   
REMARK 500    ALA G  56       48.71   -103.50                                   
REMARK 500    LYS G  92      -64.16    -17.65                                   
REMARK 500    SER G  99       87.32   -151.62                                   
REMARK 500    ALA H  56       47.69   -102.01                                   
REMARK 500    LYS H  92      -64.65    -18.45                                   
REMARK 500    SER H  99       89.59   -152.75                                   
REMARK 500    ALA I  56       48.79   -102.35                                   
REMARK 500    LYS I  92      -64.17    -17.35                                   
REMARK 500    SER I  99       86.59   -151.34                                   
REMARK 500    ALA J  56       47.07   -101.09                                   
REMARK 500    LYS J  92      -64.12    -17.61                                   
REMARK 500    SER J  99       87.65   -153.62                                   
REMARK 500    ALA K  56       48.60   -101.10                                   
REMARK 500    LYS K  92      -65.02    -16.38                                   
REMARK 500    SER K  99       86.52   -153.85                                   
REMARK 500    ALA L  56       48.66   -102.15                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL E   95     ALA E   96                  -46.39                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  49   NE2                                                    
REMARK 620 2 HIS A 121   NE2  96.4                                              
REMARK 620 3 HIS A  47   ND1 144.2 100.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  64   ND1                                                    
REMARK 620 2 HIS A  72   ND1 107.3                                              
REMARK 620 3 HIS A  81   ND1 122.4 118.6                                        
REMARK 620 4 ASP A  84   OD1  90.1  91.2 120.0                                  
REMARK 620 5 ASP A  84   OD2 141.7  72.2  86.9  52.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  47   ND1                                                    
REMARK 620 2 HIS B 121   NE2 104.5                                              
REMARK 620 3 HIS B  49   NE2 145.6  95.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  64   ND1                                                    
REMARK 620 2 HIS B  72   ND1 113.0                                              
REMARK 620 3 HIS B  81   ND1 114.6 114.7                                        
REMARK 620 4 ASP B  84   OD1  94.1 101.9 116.2                                  
REMARK 620 5 ASP B  84   OD2 148.8  72.9  87.4  55.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  47   ND1                                                    
REMARK 620 2 HIS C 121   NE2 108.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  64   ND1                                                    
REMARK 620 2 HIS C  72   ND1 107.7                                              
REMARK 620 3 HIS C  81   ND1 111.4 124.6                                        
REMARK 620 4 ASP C  84   OD1  86.8 102.3 117.4                                  
REMARK 620 5 ASP C  84   OD2 143.5  76.2  93.4  57.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU E 155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  47   ND1                                                    
REMARK 620 2 HIS E  49   NE2 146.5                                              
REMARK 620 3 HIS E 121   NE2  98.2  88.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  81   ND1                                                    
REMARK 620 2 ASP E  84   OD2 116.5                                              
REMARK 620 3 HIS E  72   ND1 113.0  79.7                                        
REMARK 620 4 HIS E  64   ND1 101.8 141.6  83.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  47   ND1                                                    
REMARK 620 2 HIS F 121   NE2 108.2                                              
REMARK 620 3 HIS F  49   NE2 148.8  95.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  64   ND1                                                    
REMARK 620 2 HIS F  72   ND1 115.3                                              
REMARK 620 3 HIS F  81   ND1 110.5 126.4                                        
REMARK 620 4 ASP F  84   OD1  81.9 103.5 109.2                                  
REMARK 620 5 ASP F  84   OD2 136.9  74.9  90.3  55.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU G 155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  47   ND1                                                    
REMARK 620 2 HIS G 121   NE2 109.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  64   ND1                                                    
REMARK 620 2 HIS G  72   ND1 102.4                                              
REMARK 620 3 HIS G  81   ND1 119.8 116.9                                        
REMARK 620 4 ASP G  84   OD1  89.8  91.4 129.8                                  
REMARK 620 5 ASP G  84   OD2 143.8  70.6  93.6  55.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU H 155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  47   ND1                                                    
REMARK 620 2 HIS H 121   NE2 105.4                                              
REMARK 620 3 HIS H  49   NE2 142.5  91.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  64   ND1                                                    
REMARK 620 2 HIS H  72   ND1 113.3                                              
REMARK 620 3 HIS H  81   ND1 115.3 128.0                                        
REMARK 620 4 ASP H  84   OD1  82.8  95.7 107.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU I 155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  47   ND1                                                    
REMARK 620 2 HIS I 121   NE2 107.2                                              
REMARK 620 3 HIS I  49   NE2 141.0  91.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  64   ND1                                                    
REMARK 620 2 HIS I  72   ND1 106.6                                              
REMARK 620 3 HIS I  81   ND1 113.2 125.3                                        
REMARK 620 4 ASP I  84   OD1  84.7 100.1 119.1                                  
REMARK 620 5 ASP I  84   OD2 141.2  77.7  92.4  56.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU J 155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  47   ND1                                                    
REMARK 620 2 HIS J 121   NE2 105.9                                              
REMARK 620 3 HIS J  49   NE2 146.2  90.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  64   ND1                                                    
REMARK 620 2 HIS J  72   ND1 111.0                                              
REMARK 620 3 HIS J  81   ND1 115.6 121.5                                        
REMARK 620 4 ASP J  84   OD1  84.8 100.7 116.5                                  
REMARK 620 5 ASP J  84   OD2 140.4  74.0  90.4  56.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU K 155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  47   ND1                                                    
REMARK 620 2 HIS K 121   NE2  98.7                                              
REMARK 620 3 HIS K  49   NE2 134.7  87.4                                        
REMARK 620 4 HIS K  64   NE2  95.6 139.1 108.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  64   ND1                                                    
REMARK 620 2 HIS K  72   ND1 106.6                                              
REMARK 620 3 HIS K  81   ND1 126.7 125.2                                        
REMARK 620 4 ASP K  84   OD1  71.9  81.0 102.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU L 155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L  47   ND1                                                    
REMARK 620 2 HIS L  49   NE2 158.8                                              
REMARK 620 3 HIS L 121   NE2  99.5  95.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L  64   ND1                                                    
REMARK 620 2 HIS L  72   ND1 112.6                                              
REMARK 620 3 HIS L  81   ND1 113.0 112.5                                        
REMARK 620 4 ASP L  84   OD1  95.2 105.8 116.5                                  
REMARK 620 5 ASP L  84   OD2 150.7  73.1  88.9  56.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  81   ND1                                                    
REMARK 620 2 ASP D  84   OD1 125.8                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU E 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU G 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU H 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU I 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU J 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU K 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU L 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 157                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KH4   RELATED DB: PDB                                   
REMARK 900 P6522 CRYSTAL FORM                                                   
DBREF  3KH3 A    2   154  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH3 B    2   154  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH3 C    2   154  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH3 D    2   154  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH3 E    2   154  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH3 F    2   154  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH3 G    2   154  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH3 H    2   154  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH3 I    2   154  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH3 J    2   154  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH3 K    2   154  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3KH3 L    2   154  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 CYS 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 CYS 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 C  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 C  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 C  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 C  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 C  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 C  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 C  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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                      
HET     CU  A 155       1                                                       
HET     ZN  A 156       1                                                       
HET     CU  B 155       1                                                       
HET     ZN  B 156       1                                                       
HET     CU  C 155       1                                                       
HET     ZN  C 156       1                                                       
HET     CU  D 155       1                                                       
HET     ZN  D 156       1                                                       
HET     CU  E 155       1                                                       
HET     ZN  E 156       1                                                       
HET     CU  F 155       1                                                       
HET     ZN  F 156       1                                                       
HET     CU  G 155       1                                                       
HET     ZN  G 156       1                                                       
HET     CU  H 155       1                                                       
HET     ZN  H 156       1                                                       
HET     CU  I 155       1                                                       
HET     ZN  I 156       1                                                       
HET     CU  J 155       1                                                       
HET     ZN  J 156       1                                                       
HET     CU  K 155       1                                                       
HET     ZN  K 156       1                                                       
HET     CU  L 155       1                                                       
HET     ZN  L 156       1                                                       
HET    SO4  B   1       5                                                       
HET    SO4  J 157       5                                                       
HET    SO4  B 157       5                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL  13   CU    12(CU 2+)                                                    
FORMUL  14   ZN    12(ZN 2+)                                                    
FORMUL  37  SO4    3(O4 S 2-)                                                   
HELIX    1   1 CYS A   58  GLY A   62  5                                   5    
HELIX    2   2 GLU A  133  LYS A  137  5                                   5    
HELIX    3   3 CYS B   58  GLY B   62  5                                   5    
HELIX    4   4 GLU B  133  LYS B  137  5                                   5    
HELIX    5   5 CYS C   58  GLY C   62  5                                   5    
HELIX    6   6 GLU C  133  LYS C  137  5                                   5    
HELIX    7   7 GLY D   57  GLY D   62  1                                   6    
HELIX    8   8 ALA E   56  GLY E   62  5                                   7    
HELIX    9   9 GLU E  133  LYS E  137  5                                   5    
HELIX   10  10 CYS F   58  GLY F   62  5                                   5    
HELIX   11  11 GLU F  133  LYS F  137  5                                   5    
HELIX   12  12 CYS G   58  GLY G   62  5                                   5    
HELIX   13  13 GLU G  133  LYS G  137  5                                   5    
HELIX   14  14 CYS H   58  GLY H   62  5                                   5    
HELIX   15  15 GLU H  133  LYS H  137  5                                   5    
HELIX   16  16 CYS I   58  GLY I   62  5                                   5    
HELIX   17  17 GLU I  133  LYS I  137  5                                   5    
HELIX   18  18 ALA J   56  GLY J   62  5                                   7    
HELIX   19  19 GLU J  133  LYS J  137  5                                   5    
HELIX   20  20 CYS K   58  GLY K   62  5                                   5    
HELIX   21  21 GLU K  133  LYS K  137  5                                   5    
HELIX   22  22 CYS L   58  GLY L   62  5                                   5    
HELIX   23  23 GLU L  133  LYS L  137  5                                   5    
SHEET    1   A 5 ALA A  96  ASP A 102  0                                        
SHEET    2   A 5 VAL A  30  LYS A  37 -1  N  ILE A  36   O  ALA A  96           
SHEET    3   A 5 GLN A  16  GLN A  23 -1  N  ASN A  20   O  TRP A  33           
SHEET    4   A 5 THR A   3  LEU A   9 -1  N  ALA A   5   O  PHE A  21           
SHEET    5   A 5 GLY A 151  ILE A 152 -1  O  GLY A 151   N  VAL A   6           
SHEET    1   B 4 ASP A  84  ALA A  90  0                                        
SHEET    2   B 4 GLY A  42  HIS A  49 -1  N  GLY A  42   O  ALA A  90           
SHEET    3   B 4 THR A 117  HIS A 121 -1  O  THR A 117   N  HIS A  49           
SHEET    4   B 4 ARG A 144  VAL A 149 -1  O  GLY A 148   N  LEU A 118           
SHEET    1   C 5 ALA B  96  ASP B 102  0                                        
SHEET    2   C 5 VAL B  30  LYS B  37 -1  N  ILE B  36   O  ALA B  96           
SHEET    3   C 5 GLN B  16  GLN B  23 -1  N  ASN B  20   O  TRP B  33           
SHEET    4   C 5 THR B   3  LEU B   9 -1  N  ALA B   5   O  PHE B  21           
SHEET    5   C 5 GLY B 151  ILE B 152 -1  O  GLY B 151   N  VAL B   6           
SHEET    1   D 4 ASP B  84  ALA B  90  0                                        
SHEET    2   D 4 GLY B  42  HIS B  49 -1  N  GLY B  42   O  ALA B  90           
SHEET    3   D 4 THR B 117  HIS B 121 -1  O  THR B 117   N  HIS B  49           
SHEET    4   D 4 ARG B 144  VAL B 149 -1  O  GLY B 148   N  LEU B 118           
SHEET    1   E 5 ALA C  96  ASP C 102  0                                        
SHEET    2   E 5 VAL C  30  LYS C  37 -1  N  VAL C  30   O  ASP C 102           
SHEET    3   E 5 GLN C  16  GLN C  23 -1  N  ASN C  20   O  TRP C  33           
SHEET    4   E 5 THR C   3  LEU C   9 -1  N  ALA C   5   O  PHE C  21           
SHEET    5   E 5 GLY C 151  ILE C 152 -1  O  GLY C 151   N  VAL C   6           
SHEET    1   F 4 ASP C  84  ALA C  90  0                                        
SHEET    2   F 4 GLY C  42  HIS C  49 -1  N  GLY C  42   O  ALA C  90           
SHEET    3   F 4 THR C 117  HIS C 121 -1  O  THR C 117   N  HIS C  49           
SHEET    4   F 4 ARG C 144  VAL C 149 -1  O  ALA C 146   N  VAL C 120           
SHEET    1   G 3 ILE D  18  PHE D  21  0                                        
SHEET    2   G 3 ALA D   5  VAL D   8 -1  N  ALA D   5   O  PHE D  21           
SHEET    3   G 3 ILE D 150  ILE D 152 -1  O  GLY D 151   N  VAL D   6           
SHEET    1   H 3 ASP D  84  ALA D  90  0                                        
SHEET    2   H 3 GLY D  42  HIS D  49 -1  N  GLY D  42   O  ALA D  90           
SHEET    3   H 3 THR D 117  VAL D 120 -1  O  THR D 117   N  HIS D  49           
SHEET    1   I 5 ASP E  97  ASP E 102  0                                        
SHEET    2   I 5 VAL E  30  LYS E  37 -1  N  VAL E  30   O  ASP E 102           
SHEET    3   I 5 GLN E  16  GLN E  23 -1  N  ASN E  20   O  TRP E  33           
SHEET    4   I 5 LYS E   4  LEU E   9 -1  N  ALA E   5   O  PHE E  21           
SHEET    5   I 5 GLY E 151  ILE E 152 -1  O  GLY E 151   N  VAL E   6           
SHEET    1   J 4 ASP E  84  ALA E  90  0                                        
SHEET    2   J 4 GLY E  42  HIS E  49 -1  N  GLY E  42   O  ALA E  90           
SHEET    3   J 4 THR E 117  HIS E 121 -1  O  THR E 117   N  HIS E  49           
SHEET    4   J 4 ARG E 144  VAL E 149 -1  O  GLY E 148   N  LEU E 118           
SHEET    1   K 5 ALA F  96  ASP F 102  0                                        
SHEET    2   K 5 VAL F  30  LYS F  37 -1  N  ILE F  36   O  ALA F  96           
SHEET    3   K 5 GLN F  16  GLN F  23 -1  N  ASN F  20   O  TRP F  33           
SHEET    4   K 5 THR F   3  LEU F   9 -1  N  ALA F   5   O  PHE F  21           
SHEET    5   K 5 GLY F 151  ILE F 152 -1  O  GLY F 151   N  VAL F   6           
SHEET    1   L 4 ASP F  84  ALA F  90  0                                        
SHEET    2   L 4 GLY F  42  HIS F  49 -1  N  GLY F  42   O  ALA F  90           
SHEET    3   L 4 THR F 117  HIS F 121 -1  O  THR F 117   N  HIS F  49           
SHEET    4   L 4 ARG F 144  VAL F 149 -1  O  ALA F 146   N  VAL F 120           
SHEET    1   M 5 ALA G  96  ASP G 102  0                                        
SHEET    2   M 5 VAL G  30  LYS G  37 -1  N  ILE G  36   O  ALA G  96           
SHEET    3   M 5 GLN G  16  GLN G  23 -1  N  ASN G  20   O  TRP G  33           
SHEET    4   M 5 THR G   3  LEU G   9 -1  N  CYS G   7   O  ILE G  19           
SHEET    5   M 5 GLY G 151  ILE G 152 -1  O  GLY G 151   N  VAL G   6           
SHEET    1   N 4 ASP G  84  ALA G  90  0                                        
SHEET    2   N 4 GLY G  42  HIS G  49 -1  N  GLY G  42   O  ALA G  90           
SHEET    3   N 4 THR G 117  HIS G 121 -1  O  THR G 117   N  HIS G  49           
SHEET    4   N 4 ARG G 144  VAL G 149 -1  O  GLY G 148   N  LEU G 118           
SHEET    1   O 5 ALA H  96  ASP H 102  0                                        
SHEET    2   O 5 VAL H  30  LYS H  37 -1  N  ILE H  36   O  ALA H  96           
SHEET    3   O 5 GLN H  16  GLN H  23 -1  N  ASN H  20   O  TRP H  33           
SHEET    4   O 5 LYS H   4  LEU H   9 -1  N  ALA H   5   O  PHE H  21           
SHEET    5   O 5 GLY H 151  ILE H 152 -1  O  GLY H 151   N  VAL H   6           
SHEET    1   P 4 ASP H  84  ALA H  90  0                                        
SHEET    2   P 4 GLY H  42  HIS H  49 -1  N  GLY H  42   O  ALA H  90           
SHEET    3   P 4 THR H 117  HIS H 121 -1  O  THR H 117   N  HIS H  49           
SHEET    4   P 4 ARG H 144  VAL H 149 -1  O  GLY H 148   N  LEU H 118           
SHEET    1   Q 5 ALA I  96  ASP I 102  0                                        
SHEET    2   Q 5 VAL I  30  LYS I  37 -1  N  VAL I  30   O  ASP I 102           
SHEET    3   Q 5 GLN I  16  GLN I  23 -1  N  ASN I  20   O  TRP I  33           
SHEET    4   Q 5 THR I   3  LEU I   9 -1  N  ALA I   5   O  PHE I  21           
SHEET    5   Q 5 GLY I 151  ILE I 152 -1  O  GLY I 151   N  VAL I   6           
SHEET    1   R 4 ASP I  84  ALA I  90  0                                        
SHEET    2   R 4 GLY I  42  HIS I  49 -1  N  GLY I  42   O  ALA I  90           
SHEET    3   R 4 THR I 117  HIS I 121 -1  O  THR I 117   N  HIS I  49           
SHEET    4   R 4 ARG I 144  VAL I 149 -1  O  GLY I 148   N  LEU I 118           
SHEET    1   S 5 ALA J  96  ASP J 102  0                                        
SHEET    2   S 5 VAL J  30  LYS J  37 -1  N  VAL J  30   O  ASP J 102           
SHEET    3   S 5 GLN J  16  GLN J  23 -1  N  ASN J  20   O  TRP J  33           
SHEET    4   S 5 THR J   3  LEU J   9 -1  N  CYS J   7   O  ILE J  19           
SHEET    5   S 5 GLY J 151  ILE J 152 -1  O  GLY J 151   N  VAL J   6           
SHEET    1   T 4 ASP J  84  ALA J  90  0                                        
SHEET    2   T 4 GLY J  42  HIS J  49 -1  N  GLY J  42   O  ALA J  90           
SHEET    3   T 4 THR J 117  HIS J 121 -1  O  THR J 117   N  HIS J  49           
SHEET    4   T 4 ARG J 144  VAL J 149 -1  O  GLY J 148   N  LEU J 118           
SHEET    1   U 5 ALA K  96  ASP K 102  0                                        
SHEET    2   U 5 VAL K  30  LYS K  37 -1  N  ILE K  36   O  ALA K  96           
SHEET    3   U 5 GLN K  16  GLN K  23 -1  N  ASN K  20   O  TRP K  33           
SHEET    4   U 5 THR K   3  LEU K   9 -1  N  CYS K   7   O  ILE K  19           
SHEET    5   U 5 GLY K 151  ILE K 152 -1  O  GLY K 151   N  VAL K   6           
SHEET    1   V 4 ASP K  84  ALA K  90  0                                        
SHEET    2   V 4 GLY K  42  HIS K  49 -1  N  GLY K  42   O  ALA K  90           
SHEET    3   V 4 THR K 117  HIS K 121 -1  O  THR K 117   N  HIS K  49           
SHEET    4   V 4 ARG K 144  VAL K 149 -1  O  GLY K 148   N  LEU K 118           
SHEET    1   W 5 ALA L  96  ASP L 102  0                                        
SHEET    2   W 5 VAL L  30  LYS L  37 -1  N  ILE L  36   O  ALA L  96           
SHEET    3   W 5 GLN L  16  GLN L  23 -1  N  ASN L  20   O  TRP L  33           
SHEET    4   W 5 THR L   3  LEU L   9 -1  N  ALA L   5   O  PHE L  21           
SHEET    5   W 5 GLY L 151  ILE L 152 -1  O  GLY L 151   N  VAL L   6           
SHEET    1   X 4 ASP L  84  ALA L  90  0                                        
SHEET    2   X 4 GLY L  42  HIS L  49 -1  N  GLY L  42   O  ALA L  90           
SHEET    3   X 4 THR L 117  HIS L 121 -1  O  THR L 117   N  HIS L  49           
SHEET    4   X 4 ARG L 144  VAL L 149 -1  O  GLY L 148   N  LEU L 118           
SSBOND   1 CYS A   58    CYS A  147                          1555   1555  2.03  
SSBOND   2 CYS B   58    CYS B  147                          1555   1555  2.03  
SSBOND   3 CYS C   58    CYS C  147                          1555   1555  2.02  
SSBOND   4 CYS D   58    CYS D  147                          1555   1555  2.07  
SSBOND   5 CYS E   58    CYS E  147                          1555   1555  2.06  
SSBOND   6 CYS F   58    CYS F  147                          1555   1555  2.01  
SSBOND   7 CYS G   58    CYS G  147                          1555   1555  2.06  
SSBOND   8 CYS H   58    CYS H  147                          1555   1555  2.03  
SSBOND   9 CYS I   58    CYS I  147                          1555   1555  2.02  
SSBOND  10 CYS J   58    CYS J  147                          1555   1555  2.02  
SSBOND  11 CYS K   58    CYS K  147                          1555   1555  2.06  
SSBOND  12 CYS L   58    CYS L  147                          1555   1555  2.03  
LINK         NE2 HIS A  49                CU  A CU A 155     1555   1555  2.36  
LINK         ND1 HIS A  64                ZN    ZN A 156     1555   1555  1.99  
LINK         ND1 HIS A  72                ZN    ZN A 156     1555   1555  2.16  
LINK         ND1 HIS A  81                ZN    ZN A 156     1555   1555  1.95  
LINK         OD1 ASP A  84                ZN    ZN A 156     1555   1555  1.87  
LINK         NE2 HIS A 121                CU  A CU A 155     1555   1555  2.38  
LINK         ND1 HIS B  47                CU  A CU B 155     1555   1555  2.33  
LINK         ND1 HIS B  64                ZN    ZN B 156     1555   1555  2.00  
LINK         ND1 HIS B  72                ZN    ZN B 156     1555   1555  2.04  
LINK         ND1 HIS B  81                ZN    ZN B 156     1555   1555  2.10  
LINK         NE2 HIS B 121                CU  A CU B 155     1555   1555  2.29  
LINK         ND1 HIS C  47                CU  A CU C 155     1555   1555  2.03  
LINK         ND1 HIS C  64                ZN    ZN C 156     1555   1555  2.17  
LINK         ND1 HIS C  72                ZN    ZN C 156     1555   1555  1.99  
LINK         ND1 HIS C  81                ZN    ZN C 156     1555   1555  2.03  
LINK         OD1 ASP C  84                ZN    ZN C 156     1555   1555  1.82  
LINK         NE2 HIS D  49                CU  A CU D 155     1555   1555  2.11  
LINK         ND1 HIS E  47                CU  A CU E 155     1555   1555  2.28  
LINK         ND1 HIS E  81                ZN    ZN E 156     1555   1555  1.87  
LINK         OD2 ASP E  84                ZN    ZN E 156     1555   1555  2.06  
LINK         ND1 HIS F  47                CU  A CU F 155     1555   1555  2.26  
LINK         ND1 HIS F  64                ZN    ZN F 156     1555   1555  2.15  
LINK         ND1 HIS F  72                ZN    ZN F 156     1555   1555  1.83  
LINK         ND1 HIS F  81                ZN    ZN F 156     1555   1555  2.07  
LINK         OD1 ASP F  84                ZN    ZN F 156     1555   1555  1.95  
LINK         NE2 HIS F 121                CU  A CU F 155     1555   1555  2.23  
LINK         ND1 HIS G  47                CU  A CU G 155     1555   1555  2.20  
LINK         ND1 HIS G  64                ZN    ZN G 156     1555   1555  2.11  
LINK         ND1 HIS G  72                ZN    ZN G 156     1555   1555  2.25  
LINK         ND1 HIS G  81                ZN    ZN G 156     1555   1555  1.94  
LINK         OD1 ASP G  84                ZN    ZN G 156     1555   1555  1.80  
LINK         NE2 HIS G 121                CU  A CU G 155     1555   1555  2.33  
LINK         ND1 HIS H  47                CU  A CU H 155     1555   1555  2.28  
LINK         ND1 HIS H  64                ZN    ZN H 156     1555   1555  2.10  
LINK         ND1 HIS H  72                ZN    ZN H 156     1555   1555  1.91  
LINK         ND1 HIS H  81                ZN    ZN H 156     1555   1555  2.04  
LINK         OD1 ASP H  84                ZN    ZN H 156     1555   1555  2.03  
LINK         NE2 HIS H 121                CU  A CU H 155     1555   1555  2.37  
LINK         ND1 HIS I  47                CU  A CU I 155     1555   1555  2.26  
LINK         ND1 HIS I  64                ZN    ZN I 156     1555   1555  2.17  
LINK         ND1 HIS I  72                ZN    ZN I 156     1555   1555  2.01  
LINK         ND1 HIS I  81                ZN    ZN I 156     1555   1555  1.98  
LINK         OD1 ASP I  84                ZN    ZN I 156     1555   1555  1.88  
LINK         NE2 HIS I 121                CU  A CU I 155     1555   1555  2.35  
LINK         ND1 HIS J  47                CU  A CU J 155     1555   1555  2.18  
LINK         ND1 HIS J  64                ZN    ZN J 156     1555   1555  2.11  
LINK         ND1 HIS J  72                ZN    ZN J 156     1555   1555  2.01  
LINK         ND1 HIS J  81                ZN    ZN J 156     1555   1555  1.99  
LINK         OD1 ASP J  84                ZN    ZN J 156     1555   1555  1.83  
LINK         NE2 HIS J 121                CU  A CU J 155     1555   1555  2.39  
LINK         ND1 HIS K  47                CU  A CU K 155     1555   1555  2.35  
LINK         ND1 HIS K  64                ZN    ZN K 156     1555   1555  2.11  
LINK         ND1 HIS K  72                ZN    ZN K 156     1555   1555  2.12  
LINK         ND1 HIS K  81                ZN    ZN K 156     1555   1555  1.87  
LINK         ND1 HIS L  47                CU  A CU L 155     1555   1555  2.29  
LINK         NE2 HIS L  49                CU  A CU L 155     1555   1555  2.30  
LINK         ND1 HIS L  64                ZN    ZN L 156     1555   1555  2.00  
LINK         ND1 HIS L  72                ZN    ZN L 156     1555   1555  2.01  
LINK         ND1 HIS L  81                ZN    ZN L 156     1555   1555  2.15  
LINK         OD1 ASP L  84                ZN    ZN L 156     1555   1555  1.70  
LINK         OD1 ASP B  84                ZN    ZN B 156     1555   1555  1.73  
LINK         ND1 HIS E  72                ZN    ZN E 156     1555   1555  2.40  
LINK         ND1 HIS D  81                ZN    ZN D 156     1555   1555  2.43  
LINK         ND1 HIS A  47                CU  A CU A 155     1555   1555  2.44  
LINK         NE2 HIS B  49                CU  A CU B 155     1555   1555  2.45  
LINK         NE2 HIS E  49                CU  A CU E 155     1555   1555  2.46  
LINK         NE2 HIS C 121                CU  A CU C 155     1555   1555  2.47  
LINK         NE2 HIS F  49                CU  A CU F 155     1555   1555  2.48  
LINK         OD1 ASP D  84                ZN    ZN D 156     1555   1555  2.48  
LINK         OD1 ASP K  84                ZN    ZN K 156     1555   1555  2.49  
LINK         NE2 HIS L 121                CU  A CU L 155     1555   1555  2.51  
LINK         OD2 ASP C  84                ZN    ZN C 156     1555   1555  2.51  
LINK         OD2 ASP I  84                ZN    ZN I 156     1555   1555  2.52  
LINK         NE2 HIS K 121                CU  A CU K 155     1555   1555  2.52  
LINK         OD2 ASP F  84                ZN    ZN F 156     1555   1555  2.54  
LINK         OD2 ASP L  84                ZN    ZN L 156     1555   1555  2.55  
LINK         NE2 HIS H  49                CU  A CU H 155     1555   1555  2.55  
LINK         OD2 ASP J  84                ZN    ZN J 156     1555   1555  2.56  
LINK         NE2 HIS J  49                CU  A CU J 155     1555   1555  2.56  
LINK         OD2 ASP B  84                ZN    ZN B 156     1555   1555  2.59  
LINK         NE2 HIS I  49                CU  A CU I 155     1555   1555  2.59  
LINK         NE2 HIS E 121                CU  A CU E 155     1555   1555  2.60  
LINK         OD2 ASP G  84                ZN    ZN G 156     1555   1555  2.61  
LINK         NE2 HIS K  49                CU  A CU K 155     1555   1555  2.62  
LINK         ND1 HIS E  64                ZN    ZN E 156     1555   1555  2.64  
LINK         NE2 HIS K  64                CU  A CU K 155     1555   1555  2.66  
LINK         OD2 ASP A  84                ZN    ZN A 156     1555   1555  2.70  
CISPEP   1 GLY D   13    PRO D   14          0       -14.19                     
SITE     1 AC1  4 HIS A  47  HIS A  49  HIS A  64  HIS A 121                    
SITE     1 AC2  4 HIS A  64  HIS A  72  HIS A  81  ASP A  84                    
SITE     1 AC3  4 HIS B  47  HIS B  49  HIS B  64  HIS B 121                    
SITE     1 AC4  4 HIS B  64  HIS B  72  HIS B  81  ASP B  84                    
SITE     1 AC5  4 HIS C  47  HIS C  49  HIS C  64  HIS C 121                    
SITE     1 AC6  4 HIS C  64  HIS C  72  HIS C  81  ASP C  84                    
SITE     1 AC7  4 HIS D  47  HIS D  49  VAL D 119  HIS D 121                    
SITE     1 AC8  4 HIS D  64  HIS D  72  HIS D  81  ASP D  84                    
SITE     1 AC9  4 HIS E  47  HIS E  49  HIS E  64  HIS E 121                    
SITE     1 BC1  4 HIS E  64  HIS E  72  HIS E  81  ASP E  84                    
SITE     1 BC2  4 HIS F  47  HIS F  49  HIS F  64  HIS F 121                    
SITE     1 BC3  5 HIS F  64  HIS F  72  HIS F  81  ASP F  84                    
SITE     2 BC3  5 LYS F 137                                                     
SITE     1 BC4  4 HIS G  47  HIS G  49  HIS G  64  HIS G 121                    
SITE     1 BC5  4 HIS G  64  HIS G  72  HIS G  81  ASP G  84                    
SITE     1 BC6  4 HIS H  47  HIS H  49  HIS H  64  HIS H 121                    
SITE     1 BC7  5 HIS H  64  HIS H  72  HIS H  81  ASP H  84                    
SITE     2 BC7  5 LYS H 137                                                     
SITE     1 BC8  4 HIS I  47  HIS I  49  HIS I  64  HIS I 121                    
SITE     1 BC9  4 HIS I  64  HIS I  72  HIS I  81  ASP I  84                    
SITE     1 CC1  4 HIS J  47  HIS J  49  HIS J  64  HIS J 121                    
SITE     1 CC2  4 HIS J  64  HIS J  72  HIS J  81  ASP J  84                    
SITE     1 CC3  4 HIS K  47  HIS K  49  HIS K  64  HIS K 121                    
SITE     1 CC4  5 HIS K  64  HIS K  72  HIS K  81  ASP K  84                    
SITE     2 CC4  5 LYS K 137                                                     
SITE     1 CC5  4 HIS L  47  HIS L  49  HIS L  64  HIS L 121                    
SITE     1 CC6  4 HIS L  64  HIS L  72  HIS L  81  ASP L  84                    
SITE     1 CC7  3 LYS B 129  LYS C 129  LYS F 129                               
SITE     1 CC8  3 LYS H 129  LYS J 129  LYS L 129                               
SITE     1 CC9  4 HIS B  49  HIS B 121  THR B 138  ARG B 144                    
CRYST1   75.500  166.610  174.980  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      0.013245  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006002  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005715        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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