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Database: PDB
Entry: 3HFF
LinkDB: 3HFF
Original site: 3HFF 
HEADER    OXIDOREDUCTASE                          11-MAY-09   3HFF              
TITLE     MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE WITHOUT ZN LIGANDS         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CU/ZN SUPEROXIDE DISMUTASE;                                 
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21/DE3                                   
KEYWDS    OXIDOREDUCTASE, SOD1, MONOMERIC MUTANT, AMYOTROPHIC LATERAL           
KEYWDS   2 SCLEROSIS, ANTIOXIDANT, DISEASE MUTATION, DISULFIDE BOND, METAL-     
KEYWDS   3 BINDING, NEURODEGENERATION, PHOSPHOPROTEIN                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.SARABOJI,A.NORDLUND,L.LEINARTAIT,M.OLIVEBERG,D.T.LOGAN              
REVDAT   4   01-NOV-17 3HFF    1       REMARK                                   
REVDAT   3   13-JUL-11 3HFF    1       VERSN                                    
REVDAT   2   23-JUN-09 3HFF    1       JRNL                                     
REVDAT   1   16-JUN-09 3HFF    0                                                
JRNL        AUTH   A.NORDLUND,L.LEINARTAITE,K.SARABOJI,C.AISENBREY,G.GROBNER,   
JRNL        AUTH 2 P.ZETTERSTROM,J.DANIELSSON,D.T.LOGAN,M.OLIVEBERG             
JRNL        TITL   FUNCTIONAL FEATURES CAUSE MISFOLDING OF THE ALS-PROVOKING    
JRNL        TITL 2 ENZYME SOD1.                                                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 106  9667 2009              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19497878                                                     
JRNL        DOI    10.1073/PNAS.0812046106                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0044                                      
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 5250                           
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) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 559                             
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 329                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 32                           
REMARK   3   BIN FREE R VALUE                    : 0.4000                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 818                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 28                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.03000                                              
REMARK   3    B12 (A**2) : -0.01000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.355         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.263         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.217         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.876        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   828 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):   529 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1116 ; 1.397 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1310 ; 1.743 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   112 ; 6.839 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    32 ;47.527 ;26.250       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   136 ;18.798 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     2 ;21.184 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   131 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   942 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   143 ; 0.001 ; 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):   556 ; 0.624 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   246 ; 0.126 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   880 ; 1.126 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   272 ; 1.698 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   236 ; 2.874 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
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   152                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.1292 -15.9840  10.2232              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0363 T22:   0.0721                                     
REMARK   3      T33:   0.0888 T12:  -0.0429                                     
REMARK   3      T13:   0.0156 T23:  -0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2575 L22:   3.2447                                     
REMARK   3      L33:   5.6545 L12:  -0.1098                                     
REMARK   3      L13:   0.5447 L23:  -1.4004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0025 S12:  -0.1628 S13:   0.0625                       
REMARK   3      S21:  -0.0368 S22:  -0.0899 S23:  -0.1844                       
REMARK   3      S31:  -0.1830 S32:   0.2118 S33:   0.0925                       
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 3HFF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000053068.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-5                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9083                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5811                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.3500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.170                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 31.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 6000, 10% JEFFAMINE M-600 (PH    
REMARK 280  7.0), 0.1M TRIS-HCL (PH 8.0), 0.1M ZNCL2, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.13000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       96.26000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       96.26000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       48.13000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 300 REMARK: THE OLIGOMERIC STATE PREDICTED BY PISA IS A PUTATIVE DIMER.  
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       48.13000            
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     GLU A    51                                                      
REMARK 465     ASP A    52                                                      
REMARK 465     ASN A    53                                                      
REMARK 465     THR A    54                                                      
REMARK 465     ALA A    55                                                      
REMARK 465     GLY A    56                                                      
REMARK 465     CYS A    57                                                      
REMARK 465     THR A    58                                                      
REMARK 465     SER A    59                                                      
REMARK 465     ALA A    60                                                      
REMARK 465     GLY A    61                                                      
REMARK 465     PRO A    62                                                      
REMARK 465     SER A    63                                                      
REMARK 465     PHE A    64                                                      
REMARK 465     ASN A    65                                                      
REMARK 465     PRO A    66                                                      
REMARK 465     LEU A    67                                                      
REMARK 465     SER A    68                                                      
REMARK 465     ARG A    69                                                      
REMARK 465     LYS A    70                                                      
REMARK 465     SER A    71                                                      
REMARK 465     GLY A    72                                                      
REMARK 465     GLY A    73                                                      
REMARK 465     PRO A    74                                                      
REMARK 465     LYS A    75                                                      
REMARK 465     ASP A    76                                                      
REMARK 465     GLU A    77                                                      
REMARK 465     GLU A    78                                                      
REMARK 465     ARG A    79                                                      
REMARK 465     SER A    80                                                      
REMARK 465     GLU A   132                                                      
REMARK 465     GLU A   133                                                      
REMARK 465     SER A   134                                                      
REMARK 465     THR A   135                                                      
REMARK 465     LYS A   136                                                      
REMARK 465     THR A   137                                                      
REMARK 465     GLY A   138                                                      
REMARK 465     GLN A   153                                                      
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     LYS A 122    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HIS A   110     O    HOH A   224              2.13            
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    HIS A 110       50.16   -118.07                                   
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 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A   1   N                                                      
REMARK 620 2 ALA A   1   O    77.7                                              
REMARK 620 3 HOH A 206   O    87.1 163.7                                        
REMARK 620 4 HOH A 209   O   108.8  94.6  95.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A 120   NE2  98.8                                              
REMARK 620 3 HOH A 211   O    95.7 104.8                                        
REMARK 620 N                    1     2                                         
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  90   OD2                                                    
REMARK 620 2 HOH A 208   O   111.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 159  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 125   OD2                                                    
REMARK 620 2 HOH A 219   O   114.5                                              
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 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 158                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 159                  
DBREF  3HFF A    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 3HFF ALA A    6  UNP  P00441    CYS     7 ENGINEERED                     
SEQADV 3HFF GLU A   50  UNP  P00441    PHE    51 ENGINEERED                     
SEQADV 3HFF GLU A   51  UNP  P00441    GLY    52 ENGINEERED                     
SEQADV 3HFF SER A   63  UNP  P00441    HIS    64 ENGINEERED                     
SEQADV 3HFF SER A   71  UNP  P00441    HIS    72 ENGINEERED                     
SEQADV 3HFF SER A   80  UNP  P00441    HIS    81 ENGINEERED                     
SEQADV 3HFF SER A   83  UNP  P00441    ASP    84 ENGINEERED                     
SEQADV 3HFF ALA A  111  UNP  P00441    CYS   112 ENGINEERED                     
SEQRES   1 A  153  ALA THR LYS ALA VAL ALA 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 GLU GLU ASP          
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO SER PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS SER GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG SER VAL GLY SER 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 ALA 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                      
HET     ZN  A 154       1                                                       
HET     ZN  A 155       1                                                       
HET     ZN  A 156       1                                                       
HET     ZN  A 158       1                                                       
HET     ZN  A 159       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    5(ZN 2+)                                                     
FORMUL   7  HOH   *28(H2 O)                                                     
SHEET    1   A 8 GLY A  82  ALA A  89  0                                        
SHEET    2   A 8 GLY A  41  VAL A  47 -1  N  GLY A  41   O  ALA A  89           
SHEET    3   A 8 THR A 116  HIS A 120 -1  O  HIS A 120   N  GLY A  44           
SHEET    4   A 8 ARG A 143  VAL A 148 -1  O  GLY A 147   N  LEU A 117           
SHEET    5   A 8 THR A   2  GLY A  10 -1  N  LYS A   9   O  CYS A 146           
SHEET    6   A 8 GLN A  15  GLN A  22 -1  O  GLY A  16   N  LEU A   8           
SHEET    7   A 8 VAL A  29  LYS A  36 -1  O  TRP A  32   N  ASN A  19           
SHEET    8   A 8 ALA A  95  ASP A 101 -1  O  VAL A  97   N  GLY A  33           
SHEET    1   B 6 GLY A  82  ALA A  89  0                                        
SHEET    2   B 6 GLY A  41  VAL A  47 -1  N  GLY A  41   O  ALA A  89           
SHEET    3   B 6 THR A 116  HIS A 120 -1  O  HIS A 120   N  GLY A  44           
SHEET    4   B 6 ARG A 143  VAL A 148 -1  O  GLY A 147   N  LEU A 117           
SHEET    5   B 6 THR A   2  GLY A  10 -1  N  LYS A   9   O  CYS A 146           
SHEET    6   B 6 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
LINK         N   ALA A   1                ZN    ZN A 156     1555   1555  2.23  
LINK         O   ALA A   1                ZN    ZN A 156     1555   1555  2.23  
LINK         ND1 HIS A  46                ZN    ZN A 154     1555   1555  1.98  
LINK         OD2 ASP A  90                ZN    ZN A 155     1555   1555  1.81  
LINK         NE2 HIS A 110                ZN    ZN A 158     1555   1555  2.06  
LINK         NE2 HIS A 120                ZN    ZN A 154     1555   1555  1.95  
LINK         OD2 ASP A 125                ZN    ZN A 159     1555   1555  1.99  
LINK        ZN    ZN A 154                 O   HOH A 211     1555   1555  2.13  
LINK        ZN    ZN A 155                 O   HOH A 208     1555   1555  2.35  
LINK        ZN    ZN A 156                 O   HOH A 206     1555   1555  2.15  
LINK        ZN    ZN A 156                 O   HOH A 209     1555   1555  2.32  
LINK        ZN    ZN A 159                 O   HOH A 219     1555   1555  1.90  
SITE     1 AC1  4 HIS A  46  HIS A 120  HOH A 211  HOH A 212                    
SITE     1 AC2  5 ASP A  90  ASP A  92  HOH A 204  HOH A 207                    
SITE     2 AC2  5 HOH A 208                                                     
SITE     1 AC3  4 ALA A   1  ASP A  96  HOH A 206  HOH A 209                    
SITE     1 AC4  4 ASP A  11  HIS A 110  HOH A 220  HOH A 222                    
SITE     1 AC5  3 ASP A 125  HOH A 216  HOH A 219                               
CRYST1   36.670   36.670  144.390  90.00  90.00 120.00 P 31 2 1      6          
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      0.027270  0.015744  0.000000        0.00000                         
SCALE2      0.000000  0.031489  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006926        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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