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Database: PDB
Entry: 2NNX
LinkDB: 2NNX
Original site: 2NNX 
HEADER    OXIDOREDUCTASE                          24-OCT-06   2NNX              
TITLE     CRYSTAL STRUCTURE OF THE H46R, H48Q DOUBLE MUTANT OF HUMAN [CU-ZN]    
TITLE    2 SUPEROXIDE DISMUTASE                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: 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: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: EG118;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: YEP351                                    
KEYWDS    OXIDOREDUCTASE; HUMAN; CU-ZN SUPEROXIDE DISMUTASE; SUPEROXIDE         
KEYWDS   2 ACCEPTOR; FAMILIAL AMYOTROPHIC LATERAL SCLEROSIS MUTANT,             
KEYWDS   3 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.SCHUERMANN,P.J.HART                                               
REVDAT   4   13-JUL-11 2NNX    1       VERSN                                    
REVDAT   3   24-FEB-09 2NNX    1       VERSN                                    
REVDAT   2   13-FEB-07 2NNX    1       JRNL                                     
REVDAT   1   07-NOV-06 2NNX    0                                                
JRNL        AUTH   J.WANG,A.CARUANO-YZERMANS,A.RODRIGUEZ,J.P.SCHEURMANN,        
JRNL        AUTH 2 H.H.SLUNT,X.CAO,J.GITLIN,P.J.HART,D.R.BORCHELT               
JRNL        TITL   DISEASE-ASSOCIATED MUTATIONS AT COPPER LIGAND HISTIDINE      
JRNL        TITL 2 RESIDUES OF SUPEROXIDE DISMUTASE 1 DIMINISH THE BINDING OF   
JRNL        TITL 3 COPPER AND COMPROMISE DIMER STABILITY                        
JRNL        REF    J.BIOL.CHEM.                  V. 282   345 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17092942                                                     
JRNL        DOI    10.1074/JBC.M604503200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 31171                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1665                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2280                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 127                          
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4446                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 13                                      
REMARK   3   SOLVENT ATOMS            : 308                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 39.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.80000                                             
REMARK   3    B22 (A**2) : 1.24000                                              
REMARK   3    B33 (A**2) : -1.15000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.81000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.274         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.221         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.089        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4518 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6094 ; 1.378 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   608 ; 7.523 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   192 ;43.033 ;25.625       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   752 ;14.916 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;14.070 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   672 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3436 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1919 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2978 ; 0.295 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   324 ; 0.152 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     7 ; 0.112 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    37 ; 0.205 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.144 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3064 ; 0.548 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4744 ; 0.914 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1581 ; 1.501 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1350 ; 2.431 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     153      4                      
REMARK   3           1     B      1       B     153      4                      
REMARK   3           1     C      1       C     153      4                      
REMARK   3           1     D      1       D     153      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1110 ;  0.61 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1110 ;  0.49 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1110 ;  0.48 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1110 ;  0.48 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1110 ;  0.60 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1110 ;  0.52 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1110 ;  0.55 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1110 ;  0.59 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2600   0.4580  23.8170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0257 T22:  -0.0810                                     
REMARK   3      T33:  -0.0597 T12:   0.0320                                     
REMARK   3      T13:   0.0195 T23:   0.0267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0201 L22:   0.8332                                     
REMARK   3      L33:   3.0567 L12:   0.2176                                     
REMARK   3      L13:   0.4396 L23:   0.4369                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0869 S12:  -0.0590 S13:  -0.1886                       
REMARK   3      S21:   0.1299 S22:  -0.0235 S23:   0.0049                       
REMARK   3      S31:   0.3073 S32:   0.0741 S33:  -0.0634                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.3600   2.4000  -0.7540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0913 T22:  -0.0195                                     
REMARK   3      T33:  -0.0555 T12:   0.0427                                     
REMARK   3      T13:   0.0231 T23:   0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6799 L22:   1.9023                                     
REMARK   3      L33:   2.9274 L12:   0.3958                                     
REMARK   3      L13:   0.4335 L23:   0.9078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0763 S12:   0.1125 S13:  -0.0457                       
REMARK   3      S21:  -0.1406 S22:  -0.1049 S23:   0.1008                       
REMARK   3      S31:  -0.0962 S32:  -0.1808 S33:   0.0286                       
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     1        C   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.6280  31.4060  -0.6940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1060 T22:   0.0070                                     
REMARK   3      T33:  -0.0126 T12:   0.0575                                     
REMARK   3      T13:   0.0345 T23:   0.0633                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8193 L22:   1.6340                                     
REMARK   3      L33:   3.6040 L12:  -0.0898                                     
REMARK   3      L13:   0.1430 L23:  -0.7602                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0256 S12:   0.1990 S13:   0.0747                       
REMARK   3      S21:  -0.0360 S22:   0.0550 S23:   0.1367                       
REMARK   3      S31:  -0.1420 S32:  -0.2700 S33:  -0.0806                       
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     1        D   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6640  29.4450  23.4520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0629 T22:  -0.0851                                     
REMARK   3      T33:  -0.0557 T12:   0.0076                                     
REMARK   3      T13:   0.0610 T23:   0.0239                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9478 L22:   1.6374                                     
REMARK   3      L33:   2.4682 L12:   0.1015                                     
REMARK   3      L13:   0.5529 L23:   0.4112                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0307 S12:  -0.1189 S13:   0.0781                       
REMARK   3      S21:   0.0558 S22:   0.0003 S23:  -0.0180                       
REMARK   3      S31:  -0.1481 S32:   0.0728 S33:  -0.0311                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2NNX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB040092.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : CONFOCAL OPTICS                    
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32846                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.53100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1AZV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 550MME, 0.1M MES, 0.01M ZINC     
REMARK 280  SULFATE, PH 5.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       31.77450            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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: 1830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -169.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1 -1.000000  0.000000  0.000000      -37.37431            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000       31.77450            
REMARK 350   BIOMT3   1  0.000000  0.000000 -1.000000       76.45928            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -76.47100            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -31.77450            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, B                                  
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -141.0 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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -76.47100            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       31.77450            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -171.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, C                                  
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -37.37431            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       31.77450            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       76.45928            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ACE A     0                                                      
REMARK 465     ACE C     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    THR B   2   N   -  CA  -  CB  ANGL. DEV. =  12.6 DEGREES          
REMARK 500    ARG D  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  90     -169.69    -78.05                                   
REMARK 500    THR B   2      -31.94   -165.06                                   
REMARK 500    SER B  59        6.50    -69.73                                   
REMARK 500    ASN B  65       57.51   -149.86                                   
REMARK 500    THR C   2      -40.68   -130.42                                   
REMARK 500    ASN C  26       -3.42     70.99                                   
REMARK 500    ASN C  65       59.53   -151.47                                   
REMARK 500    ASN D  65       59.04   -151.25                                   
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 ALA B    1     THR B    2                  -97.95                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP D 109        24.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  83   OD1                                                    
REMARK 620 2 HIS A  63   ND1 107.7                                              
REMARK 620 3 HIS A  80   ND1 119.8 107.8                                        
REMARK 620 4 HIS A  71   ND1  96.5 103.3 120.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  63   ND1                                                    
REMARK 620 2 HIS B  71   ND1 101.9                                              
REMARK 620 3 ASP B  83   OD1 108.2  98.0                                        
REMARK 620 4 HIS B  80   ND1 111.0 125.3 110.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  71   ND1                                                    
REMARK 620 2 ASP C  83   OD1 102.7                                              
REMARK 620 3 HIS C  63   ND1 100.7 106.4                                        
REMARK 620 4 HIS C  80   ND1 119.9 116.6 108.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  80   ND1                                                    
REMARK 620 2 HIS D  71   ND1 125.9                                              
REMARK 620 3 HIS D  63   ND1 110.8 101.5                                        
REMARK 620 4 ASP D  83   OD1 113.2  98.3 104.6                                  
REMARK 620 N                    1     2     3                                   
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 HOH D1054   O                                                      
REMARK 620 2 GLU D  77   OE1 132.7                                              
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 ZN 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 ZN 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 ZN 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 ZN 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 SO4 D 991                 
DBREF  2NNX A    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2NNX B    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2NNX C    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2NNX D    1   153  UNP    P00441   SODC_HUMAN       1    153             
SEQADV 2NNX ARG A   46  UNP  P00441    HIS    46 ENGINEERED                     
SEQADV 2NNX GLN A   48  UNP  P00441    HIS    48 ENGINEERED                     
SEQADV 2NNX ARG B   46  UNP  P00441    HIS    46 ENGINEERED                     
SEQADV 2NNX GLN B   48  UNP  P00441    HIS    48 ENGINEERED                     
SEQADV 2NNX ARG C   46  UNP  P00441    HIS    46 ENGINEERED                     
SEQADV 2NNX GLN C   48  UNP  P00441    HIS    48 ENGINEERED                     
SEQADV 2NNX ARG D   46  UNP  P00441    HIS    46 ENGINEERED                     
SEQADV 2NNX GLN D   48  UNP  P00441    HIS    48 ENGINEERED                     
SEQRES   1 A  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 A  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 A  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 A  154  THR GLU GLY LEU HIS GLY PHE ARG VAL GLN GLU PHE GLY          
SEQRES   5 A  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 A  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 A  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 A  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 A  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 A  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 A  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 A  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 B  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 B  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 B  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 B  154  THR GLU GLY LEU HIS GLY PHE ARG VAL GLN GLU PHE GLY          
SEQRES   5 B  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 B  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 B  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 B  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 B  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 B  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 B  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 B  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 C  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 C  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 C  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 C  154  THR GLU GLY LEU HIS GLY PHE ARG VAL GLN GLU PHE GLY          
SEQRES   5 C  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 C  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 C  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 C  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 C  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 C  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 C  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 C  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 D  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 D  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 D  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 D  154  THR GLU GLY LEU HIS GLY PHE ARG VAL GLN GLU PHE GLY          
SEQRES   5 D  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 D  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 D  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 D  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 D  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 D  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 D  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 D  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
HET    ACE  B   0       3                                                       
HET    ACE  D   0       3                                                       
HET     ZN  A 155       1                                                       
HET     ZN  A 156       1                                                       
HET     ZN  B 155       1                                                       
HET     ZN  B 156       1                                                       
HET     ZN  C 155       1                                                       
HET     ZN  C 156       1                                                       
HET     ZN  D 155       1                                                       
HET     ZN  D 156       1                                                       
HET    SO4  D 991       5                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  ACE    2(C2 H4 O)                                                   
FORMUL   5   ZN    8(ZN 2+)                                                     
FORMUL  13  SO4    O4 S 2-                                                      
FORMUL  14  HOH   *308(H2 O)                                                    
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 SER A  107  CYS A  111  5                                   5    
HELIX    3   3 ASN A  131  THR A  137  1                                   7    
HELIX    4   4 CYS B   57  GLY B   61  5                                   5    
HELIX    5   5 SER B  107  CYS B  111  5                                   5    
HELIX    6   6 GLU B  132  LYS B  136  5                                   5    
HELIX    7   7 GLY C   56  GLY C   61  5                                   6    
HELIX    8   8 CYS D   57  GLY D   61  5                                   5    
HELIX    9   9 SER D  107  CYS D  111  5                                   5    
SHEET    1   A 5 ALA A  95  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  VAL A  29   O  ASP A 101           
SHEET    3   A 5 GLN A  15  GLN A  22 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 THR A   2  LEU A   8 -1  N  CYS A   6   O  ILE A  18           
SHEET    5   A 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1   B 4 ASP A  83  ALA A  89  0                                        
SHEET    2   B 4 GLY A  41  GLN A  48 -1  N  GLY A  41   O  ALA A  89           
SHEET    3   B 4 THR A 116  HIS A 120 -1  O  THR A 116   N  GLN A  48           
SHEET    4   B 4 ARG A 143  VAL A 148 -1  O  LEU A 144   N  VAL A 119           
SHEET    1   C 5 ALA B  95  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  LYS B  36 -1  N  ILE B  35   O  ALA B  95           
SHEET    3   C 5 GLN B  15  GLU B  21 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 LYS B   3  LYS B   9 -1  N  LEU B   8   O  GLY B  16           
SHEET    5   C 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  GLN B  48 -1  N  GLY B  41   O  ALA B  89           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  THR B 116   N  GLN B  48           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  LEU B 144   N  VAL B 119           
SHEET    1   E 5 ALA C  95  ASP C 101  0                                        
SHEET    2   E 5 VAL C  29  LYS C  36 -1  N  VAL C  29   O  ASP C 101           
SHEET    3   E 5 GLN C  15  GLU C  21 -1  N  ASN C  19   O  TRP C  32           
SHEET    4   E 5 LYS C   3  LYS C   9 -1  N  CYS C   6   O  ILE C  18           
SHEET    5   E 5 GLY C 150  ILE C 151 -1  O  GLY C 150   N  VAL C   5           
SHEET    1   F 4 ASP C  83  ALA C  89  0                                        
SHEET    2   F 4 GLY C  41  GLN C  48 -1  N  GLY C  41   O  ALA C  89           
SHEET    3   F 4 THR C 116  HIS C 120 -1  O  THR C 116   N  GLN C  48           
SHEET    4   F 4 ARG C 143  VAL C 148 -1  O  LEU C 144   N  VAL C 119           
SHEET    1   G 5 ALA D  95  ASP D 101  0                                        
SHEET    2   G 5 VAL D  29  LYS D  36 -1  N  GLY D  33   O  VAL D  97           
SHEET    3   G 5 GLN D  15  GLU D  21 -1  N  ASN D  19   O  TRP D  32           
SHEET    4   G 5 LYS D   3  LEU D   8 -1  N  ALA D   4   O  PHE D  20           
SHEET    5   G 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   H 4 ASP D  83  ALA D  89  0                                        
SHEET    2   H 4 GLY D  41  GLN D  48 -1  N  GLY D  41   O  ALA D  89           
SHEET    3   H 4 THR D 116  HIS D 120 -1  O  THR D 116   N  GLN D  48           
SHEET    4   H 4 ARG D 143  VAL D 148 -1  O  LEU D 144   N  VAL D 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.08  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.08  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.07  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.07  
LINK         C   ACE B   0                 N   ALA B   1     1555   1555  1.32  
LINK         C   ACE D   0                 N   ALA D   1     1555   1555  1.34  
LINK        ZN    ZN A 155                 OD1 ASP A  83     1555   1555  1.93  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  2.21  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  2.07  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  2.12  
LINK        ZN    ZN A 156                 OE2 GLU A  77     1555   1555  1.88  
LINK        ZN    ZN B 155                 ND1 HIS B  63     1555   1555  2.19  
LINK        ZN    ZN B 155                 ND1 HIS B  71     1555   1555  2.17  
LINK        ZN    ZN B 155                 OD1 ASP B  83     1555   1555  1.84  
LINK        ZN    ZN B 155                 ND1 HIS B  80     1555   1555  2.03  
LINK        ZN    ZN B 156                 OE2 GLU B  77     1555   1555  2.48  
LINK        ZN    ZN C 155                 ND1 HIS C  71     1555   1555  2.21  
LINK        ZN    ZN C 155                 OD1 ASP C  83     1555   1555  1.86  
LINK        ZN    ZN C 155                 ND1 HIS C  63     1555   1555  2.19  
LINK        ZN    ZN C 155                 ND1 HIS C  80     1555   1555  2.10  
LINK        ZN    ZN C 156                 OE2 GLU C  77     1555   1555  2.00  
LINK        ZN    ZN D 155                 ND1 HIS D  80     1555   1555  2.07  
LINK        ZN    ZN D 155                 ND1 HIS D  71     1555   1555  2.14  
LINK        ZN    ZN D 155                 ND1 HIS D  63     1555   1555  2.23  
LINK        ZN    ZN D 155                 OD1 ASP D  83     1555   1555  1.98  
LINK        ZN    ZN D 156                 O   HOH D1054     1555   1555  2.26  
LINK        ZN    ZN D 156                 OE1 GLU D  77     1555   1555  2.29  
CISPEP   1 ALA C    1    THR C    2          0       -16.71                     
SITE     1 AC1  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC2  1 GLU A  77                                                     
SITE     1 AC3  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC4  1 GLU B  77                                                     
SITE     1 AC5  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 AC6  1 GLU C  77                                                     
SITE     1 AC7  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 AC8  2 GLU D  77  HOH D1054                                          
SITE     1 AC9  7 ARG D  46  HIS D  63  HIS D 120  THR D 137                    
SITE     2 AC9  7 ARG D 143  HOH D1018  HOH D1040                               
CRYST1   76.471   63.549   85.105  90.00 116.05  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013077  0.000000  0.006392        0.00000                         
SCALE2      0.000000  0.015736  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013079        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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