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    HEADER    METAL BINDING PROTEIN                   13-NOV-11   3UMI              
    TITLE     X-RAY STRUCTURE OF THE E2 DOMAIN OF THE HUMAN AMYLOID PRECURSOR       
    TITLE    2 PROTEIN (APP) IN COMPLEX WITH ZINC                                   
    COMPND    MOL_ID: 1;                                                            
    COMPND   2 MOLECULE: AMYLOID BETA A4 PROTEIN;                                   
    COMPND   3 CHAIN: A;                                                            
    COMPND   4 FRAGMENT: HUMAN AMYLOID PRECURSOR PROTEIN E2 DOMAIN;                 
    COMPND   5 ENGINEERED: YES                                                      
    SOURCE    MOL_ID: 1;                                                            
    SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
    SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
    SOURCE   4 ORGANISM_TAXID: 9606;                                                
    SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
    SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
    SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
    SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
    SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
    KEYWDS    METAL BINDING SITE, METAL BINDING, CELL SURFACE, SECRETORY PATHWAY,   
    KEYWDS   2 METAL BINDING PROTEIN                                                
    EXPDTA    X-RAY DIFFRACTION                                                     
    AUTHOR    S.O.DAHMS,I.KONNIG,D.ROESER,K.H.GUHRS,M.E.THAN                        
    REVDAT   3   08-NOV-17 3UMI    1       REMARK                                   
    REVDAT   2   22-FEB-12 3UMI    1       JRNL                                     
    REVDAT   1   25-JAN-12 3UMI    0                                                
    JRNL        AUTH   S.O.DAHMS,I.KONNIG,D.ROESER,K.H.GUHRS,M.C.MAYER,D.KADEN,     
    JRNL        AUTH 2 G.MULTHAUP,M.E.THAN                                          
    JRNL        TITL   METAL BINDING DICTATES CONFORMATION AND FUNCTION OF THE      
    JRNL        TITL 2 AMYLOID PRECURSOR PROTEIN (APP) E2 DOMAIN.                   
    JRNL        REF    J.MOL.BIOL.                   V. 416   438 2012              
    JRNL        REFN                   ISSN 0022-2836                               
    JRNL        PMID   22245578                                                     
    JRNL        DOI    10.1016/J.JMB.2011.12.057                                    
    REMARK   2                                                                      
    REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
    REMARK   3                                                                      
    REMARK   3 REFINEMENT.                                                          
    REMARK   3   PROGRAM     : CNS                                                  
    REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
    REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
    REMARK   3               : READ,RICE,SIMONSON,WARREN                            
    REMARK   3                                                                      
    REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
    REMARK   3                                                                      
    REMARK   3  DATA USED IN REFINEMENT.                                            
    REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
    REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.44                          
    REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
    REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
    REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
    REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
    REMARK   3   NUMBER OF REFLECTIONS             : 7453                           
    REMARK   3                                                                      
    REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
    REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
    REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
    REMARK   3   R VALUE            (WORKING SET) : 0.204                           
    REMARK   3   FREE R VALUE                     : 0.245                           
    REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
    REMARK   3   FREE R VALUE TEST SET COUNT      : 433                             
    REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
    REMARK   3                                                                      
    REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
    REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
    REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
    REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
    REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
    REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
    REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
    REMARK   3   BIN FREE R VALUE                    : NULL                         
    REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
    REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
    REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
    REMARK   3                                                                      
    REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
    REMARK   3   PROTEIN ATOMS            : 1534                                    
    REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
    REMARK   3   HETEROGEN ATOMS          : 13                                      
    REMARK   3   SOLVENT ATOMS            : 79                                      
    REMARK   3                                                                      
    REMARK   3  B VALUES.                                                           
    REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
    REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
    REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
    REMARK   3    B11 (A**2) : NULL                                                 
    REMARK   3    B22 (A**2) : NULL                                                 
    REMARK   3    B33 (A**2) : NULL                                                 
    REMARK   3    B12 (A**2) : NULL                                                 
    REMARK   3    B13 (A**2) : NULL                                                 
    REMARK   3    B23 (A**2) : NULL                                                 
    REMARK   3                                                                      
    REMARK   3  ESTIMATED COORDINATE ERROR.                                         
    REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
    REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
    REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
    REMARK   3                                                                      
    REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
    REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
    REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
    REMARK   3                                                                      
    REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
    REMARK   3   BOND LENGTHS                 (A) : 0.005                           
    REMARK   3   BOND ANGLES            (DEGREES) : 0.948                           
    REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
    REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
    REMARK   3                                                                      
    REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
    REMARK   3                                                                      
    REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
    REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
    REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
    REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
    REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
    REMARK   3                                                                      
    REMARK   3  BULK SOLVENT MODELING.                                              
    REMARK   3   METHOD USED : NULL                                                 
    REMARK   3   KSOL        : NULL                                                 
    REMARK   3   BSOL        : NULL                                                 
    REMARK   3                                                                      
    REMARK   3  NCS MODEL : NULL                                                    
    REMARK   3                                                                      
    REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
    REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
    REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
    REMARK   3                                                                      
    REMARK   3  PARAMETER FILE  1  : NULL                                           
    REMARK   3  TOPOLOGY FILE  1   : NULL                                           
    REMARK   3                                                                      
    REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
    REMARK   4                                                                      
    REMARK   4 3UMI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
    REMARK 100                                                                      
    REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-12.                  
    REMARK 100 THE DEPOSITION ID IS D_1000068939.                                   
    REMARK 200                                                                      
    REMARK 200 EXPERIMENTAL DETAILS                                                 
    REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
    REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-10                          
    REMARK 200  TEMPERATURE           (KELVIN) : 100                                
    REMARK 200  PH                             : 6.4                                
    REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
    REMARK 200                                                                      
    REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
    REMARK 200  RADIATION SOURCE               : BESSY                              
    REMARK 200  BEAMLINE                       : 14.2                               
    REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
    REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
    REMARK 200  WAVELENGTH OR RANGE        (A) : 1.28248                            
    REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
    REMARK 200  OPTICS                         : NULL                               
    REMARK 200                                                                      
    REMARK 200  DETECTOR TYPE                  : CCD                                
    REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
    REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
    REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
    REMARK 200                                                                      
    REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7453                               
    REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
    REMARK 200  RESOLUTION RANGE LOW       (A) : 27.440                             
    REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
    REMARK 200                                                                      
    REMARK 200 OVERALL.                                                             
    REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
    REMARK 200  DATA REDUNDANCY                : NULL                               
    REMARK 200  R MERGE                    (I) : NULL                               
    REMARK 200  R SYM                      (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
    REMARK 200                                                                      
    REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
    REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
    REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
    REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0                               
    REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
    REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
    REMARK 200  R SYM FOR SHELL            (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
    REMARK 200                                                                      
    REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
    REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
    REMARK 200 SOFTWARE USED: SHARP                                                 
    REMARK 200 STARTING MODEL: NULL                                                 
    REMARK 200                                                                      
    REMARK 200 REMARK: NULL                                                         
    REMARK 280                                                                      
    REMARK 280 CRYSTAL                                                              
    REMARK 280 SOLVENT CONTENT, VS   (%): 38.29                                     
    REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
    REMARK 280                                                                      
    REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 MM HEPES, 1 M SODIUM ACETATE, 10     
    REMARK 280  MM MGCL2, 50 MM CDSO4, PH 6.4, VAPOR DIFFUSION, SITTING DROP,       
    REMARK 280  TEMPERATURE 293K                                                    
    REMARK 290                                                                      
    REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
    REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
    REMARK 290                                                                      
    REMARK 290      SYMOP   SYMMETRY                                                
    REMARK 290     NNNMMM   OPERATOR                                                
    REMARK 290       1555   X,Y,Z                                                   
    REMARK 290       2555   -X,-Y,Z+1/2                                             
    REMARK 290       3555   -Y,X,Z+3/4                                              
    REMARK 290       4555   Y,-X,Z+1/4                                              
    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        0.00000            
    REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.21250            
    REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       94.81875            
    REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       31.60625            
    REMARK 290                                                                      
    REMARK 290 REMARK: NULL                                                         
    REMARK 300                                                                      
    REMARK 300 BIOMOLECULE: 1                                                       
    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: MONOMERIC                         
    REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
    REMARK 350 SOFTWARE USED: PISA                                                  
    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 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     MET A   294                                                      
    REMARK 465     SER A   295                                                      
    REMARK 465     THR A   296                                                      
    REMARK 465     PRO A   297                                                      
    REMARK 465     ASP A   298                                                      
    REMARK 465     ALA A   299                                                      
    REMARK 465     VAL A   300                                                      
    REMARK 465     ASP A   301                                                      
    REMARK 465     LYS A   302                                                      
    REMARK 465     TYR A   303                                                      
    REMARK 465     LEU A   304                                                      
    REMARK 465     GLU A   305                                                      
    REMARK 465     THR A   306                                                      
    REMARK 465     PRO A   307                                                      
    REMARK 465     GLY A   308                                                      
    REMARK 465     ASP A   309                                                      
    REMARK 465     LYS A   493                                                      
    REMARK 465     GLU A   494                                                      
    REMARK 465     GLN A   495                                                      
    REMARK 465     ASN A   496                                                      
    REMARK 465     TYR A   497                                                      
    REMARK 465     SER A   498                                                      
    REMARK 465     ASP A   499                                                      
    REMARK 465     ASP A   500                                                      
    REMARK 465     ILE A   501                                                      
    REMARK 465     GLU A   502                                                      
    REMARK 465     GLY A   503                                                      
    REMARK 465     ARG A   504                                                      
    REMARK 480                                                                      
    REMARK 480 ZERO OCCUPANCY ATOM                                                  
    REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
    REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
    REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
    REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
    REMARK 480   M RES C SSEQI ATOMS                                                
    REMARK 480     GLU A  310   N    CB   CG   CD   OE1  OE2                        
    REMARK 480     ASN A  311   CG   OD1  ND2                                       
    REMARK 480     GLU A  312   CG   CD   OE1  OE2                                  
    REMARK 480     HIS A  313   CG   ND1  CD2  CE1  NE2                             
    REMARK 480     HIS A  315   CG   ND1  CD2  CE1  NE2                             
    REMARK 480     LYS A  318   CE   NZ                                             
    REMARK 480     GLU A  324   CD   OE1  OE2                                       
    REMARK 480     ARG A  328   CD   NE   CZ   NH1  NH2                             
    REMARK 480     GLN A  333   OE1  NE2                                            
    REMARK 480     GLU A  337   OE1  OE2                                            
    REMARK 480     GLU A  339   CG   CD   OE1  OE2                                  
    REMARK 480     GLU A  342   OE1  OE2                                            
    REMARK 480     ARG A  343   CG   CD   NE   CZ   NH1  NH2                        
    REMARK 480     GLN A  344   CD   OE1  NE2                                       
    REMARK 480     LYS A  346   CG   CD   CE   NZ                                   
    REMARK 480     ASN A  347   CG   OD1  ND2                                       
    REMARK 480     LEU A  348   CG   CD1  CD2                                       
    REMARK 480     LYS A  350   CG   CD   CE   NZ                                   
    REMARK 480     ASP A  352   CG   OD1  OD2                                       
    REMARK 480     LYS A  353   CE   NZ                                             
    REMARK 480     LYS A  354   CG   CD   CE   NZ                                   
    REMARK 480     GLN A  358   OE1  NE2                                            
    REMARK 480     LYS A  363   CE   NZ                                             
    REMARK 480     GLN A  376   CD   OE1  NE2                                       
    REMARK 480     GLU A  380   OE1  OE2                                            
    REMARK 480     ARG A  393   NE   CZ   NH1  NH2                                  
    REMARK 480     LYS A  420   NZ                                                  
    REMARK 480     LYS A  428   CD   CE   NZ                                        
    REMARK 480     GLN A  431   OE1  NE2                                            
    REMARK 480     LYS A  435   CD   CE   NZ                                        
    REMARK 480     ARG A  452   NE   CZ   NH1  NH2                                  
    REMARK 480     GLN A  454   CD   OE1  NE2                                       
    REMARK 480     ARG A  460   CZ   NH1  NH2                                       
    REMARK 480     GLU A  464   CD   OE1  OE2                                       
    REMARK 480     GLN A  468   CD   OE1  NE2                                       
    REMARK 480     GLN A  492   CD   OE1  NE2                                       
    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   NE2  HIS A   458    CD     CD A     2              2.12            
    REMARK 500   OD1  ASP A   429    CD     CD A     2              2.17            
    REMARK 500                                                                      
    REMARK 500 REMARK: NULL                                                         
    REMARK 500                                                                      
    REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
    REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
    REMARK 500                                                                      
    REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
    REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
    REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
    REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
    REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
    REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
    REMARK 500                                                                      
    REMARK 500 DISTANCE CUTOFF:                                                     
    REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
    REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
    REMARK 500                                                                      
    REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
    REMARK 500   OD1  ASP A   392    CD     CD A     5     1655     2.06            
    REMARK 500  CD     CD A     4     O    HOH A   748     1455     2.10            
    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    GLN A 344       32.95    -81.65                                   
    REMARK 500    ALA A 345       11.06   -154.61                                   
    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   1  ZN                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 HIS A 432   NE2                                                    
    REMARK 620 2 HOH A  79   O   116.2                                              
    REMARK 620 3 HIS A 382   NE2 113.2 103.7                                        
    REMARK 620 4 HIS A 436   NE2  86.7 128.0 108.6                                  
    REMARK 620 N                    1     2     3                                   
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                              CD A   5  CD                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 HIS A 327   NE2                                                    
    REMARK 620 2 HOH A 711   O   116.3                                              
    REMARK 620 3 GLU A 368   OE2  88.3 134.5                                        
    REMARK 620 4 GLU A 368   OE1 105.8  80.7  55.1                                  
    REMARK 620 N                    1     2     3                                   
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                              CD A   6  CD                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 ACT A 601   O                                                      
    REMARK 620 2 GLU A 365   OE1  77.8                                              
    REMARK 620 3 GLU A 362   OE1 166.9  90.4                                        
    REMARK 620 4 ACT A 601   OXT  55.2 109.8 125.6                                  
    REMARK 620 N                    1     2     3                                   
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                              CD A   3  CD                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 ASP A 444   OD2                                                    
    REMARK 620 2 HOH A 732   O    98.7                                              
    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 ACT A 601                 
    REMARK 800                                                                      
    REMARK 800 SITE_IDENTIFIER: AC2                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1                    
    REMARK 800                                                                      
    REMARK 800 SITE_IDENTIFIER: AC3                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 2                    
    REMARK 800                                                                      
    REMARK 800 SITE_IDENTIFIER: AC4                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 3                    
    REMARK 800                                                                      
    REMARK 800 SITE_IDENTIFIER: AC5                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 4                    
    REMARK 800                                                                      
    REMARK 800 SITE_IDENTIFIER: AC6                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 5                    
    REMARK 800                                                                      
    REMARK 800 SITE_IDENTIFIER: AC7                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 6                    
    REMARK 800                                                                      
    REMARK 800 SITE_IDENTIFIER: AC8                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 7                    
    REMARK 800                                                                      
    REMARK 800 SITE_IDENTIFIER: AC9                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 8                    
    REMARK 800                                                                      
    REMARK 800 SITE_IDENTIFIER: BC1                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 9                    
    REMARK 900                                                                      
    REMARK 900 RELATED ENTRIES                                                      
    REMARK 900 RELATED ID: 3UMH   RELATED DB: PDB                                   
    REMARK 900 RELATED ID: 3UMK   RELATED DB: PDB                                   
    DBREF  3UMI A  295   500  UNP    P05067   A4_HUMAN       370    575             
    SEQADV 3UMI MET A  294  UNP  P05067              INITIATING METHIONINE          
    SEQADV 3UMI ILE A  501  UNP  P05067              EXPRESSION TAG                 
    SEQADV 3UMI GLU A  502  UNP  P05067              EXPRESSION TAG                 
    SEQADV 3UMI GLY A  503  UNP  P05067              EXPRESSION TAG                 
    SEQADV 3UMI ARG A  504  UNP  P05067              EXPRESSION TAG                 
    SEQRES   1 A  211  MET SER THR PRO ASP ALA VAL ASP LYS TYR LEU GLU THR          
    SEQRES   2 A  211  PRO GLY ASP GLU ASN GLU HIS ALA HIS PHE GLN LYS ALA          
    SEQRES   3 A  211  LYS GLU ARG LEU GLU ALA LYS HIS ARG GLU ARG MET SER          
    SEQRES   4 A  211  GLN VAL MET ARG GLU TRP GLU GLU ALA GLU ARG GLN ALA          
    SEQRES   5 A  211  LYS ASN LEU PRO LYS ALA ASP LYS LYS ALA VAL ILE GLN          
    SEQRES   6 A  211  HIS PHE GLN GLU LYS VAL GLU SER LEU GLU GLN GLU ALA          
    SEQRES   7 A  211  ALA ASN GLU ARG GLN GLN LEU VAL GLU THR HIS MET ALA          
    SEQRES   8 A  211  ARG VAL GLU ALA MET LEU ASN ASP ARG ARG ARG LEU ALA          
    SEQRES   9 A  211  LEU GLU ASN TYR ILE THR ALA LEU GLN ALA VAL PRO PRO          
    SEQRES  10 A  211  ARG PRO ARG HIS VAL PHE ASN MET LEU LYS LYS TYR VAL          
    SEQRES  11 A  211  ARG ALA GLU GLN LYS ASP ARG GLN HIS THR LEU LYS HIS          
    SEQRES  12 A  211  PHE GLU HIS VAL ARG MET VAL ASP PRO LYS LYS ALA ALA          
    SEQRES  13 A  211  GLN ILE ARG SER GLN VAL MET THR HIS LEU ARG VAL ILE          
    SEQRES  14 A  211  TYR GLU ARG MET ASN GLN SER LEU SER LEU LEU TYR ASN          
    SEQRES  15 A  211  VAL PRO ALA VAL ALA GLU GLU ILE GLN ASP GLU VAL ASP          
    SEQRES  16 A  211  GLU LEU LEU GLN LYS GLU GLN ASN TYR SER ASP ASP ILE          
    SEQRES  17 A  211  GLU GLY ARG                                                  
    HET    ACT  A 601       4                                                       
    HET     ZN  A   1       1                                                       
    HET     CD  A   2       2                                                       
    HET     CD  A   3       1                                                       
    HET     CD  A   4       1                                                       
    HET     CD  A   5       1                                                       
    HET     CD  A   6       1                                                       
    HET     CD  A   7       1                                                       
    HET     CD  A   8       1                                                       
    HET     CD  A   9       1                                                       
    HETNAM     ACT ACETATE ION                                                      
    HETNAM      ZN ZINC ION                                                         
    HETNAM      CD CADMIUM ION                                                      
    FORMUL   2  ACT    C2 H3 O2 1-                                                  
    FORMUL   3   ZN    ZN 2+                                                        
    FORMUL   4   CD    8(CD 2+)                                                     
    FORMUL  12  HOH   *79(H2 O)                                                     
    HELIX    1   1 GLU A  310  GLN A  344  1                                  35    
    HELIX    2   2 PRO A  349  GLN A  406  1                                  58    
    HELIX    3   3 ARG A  411  ASP A  444  1                                  34    
    HELIX    4   4 ASP A  444  SER A  471  1                                  28    
    HELIX    5   5 LEU A  472  ASN A  475  5                                   4    
    HELIX    6   6 VAL A  476  LEU A  491  1                                  16    
    LINK         NE2 HIS A 432                ZN    ZN A   1     1555   1555  1.96  
    LINK        ZN    ZN A   1                 O   HOH A  79     1555   1555  2.00  
    LINK         NE2 HIS A 382                ZN    ZN A   1     1555   1555  2.03  
    LINK         ND1 HIS A 359                CD    CD A   8     1555   1555  2.05  
    LINK         NE2 HIS A 436                ZN    ZN A   1     1555   1555  2.08  
    LINK         NE2 HIS A 327                CD    CD A   5     1555   1555  2.10  
    LINK        CD    CD A   5                 O   HOH A 711     1555   1555  2.13  
    LINK         OD1 ASP A 488                CD    CD A   7     1555   1555  2.17  
    LINK         O   ACT A 601                CD    CD A   6     1555   1555  2.21  
    LINK         NE2 HIS A 439                CD    CD A   4     1555   1555  2.22  
    LINK         OE2 GLU A 321                CD    CD A   9     1555   1555  2.24  
    LINK         OD2 ASP A 444                CD    CD A   3     1555   1555  2.25  
    LINK         OE1 GLU A 365                CD    CD A   6     1555   1555  2.29  
    LINK         OE2 GLU A 368                CD    CD A   5     1555   1555  2.32  
    LINK         OE1 GLU A 368                CD    CD A   5     1555   1555  2.42  
    LINK         OE1 GLU A 362                CD    CD A   6     1555   1555  2.45  
    LINK        CD    CD A   3                 O   HOH A 732     1555   1555  2.45  
    LINK         OXT ACT A 601                CD    CD A   6     1555   1555  2.49  
    CISPEP   1 VAL A  408    PRO A  409          0         0.05                     
    SITE     1 AC1  4  CD A   6  GLU A 362  GLU A 365  HOH A 767                    
    SITE     1 AC2  4 HOH A  79  HIS A 382  HIS A 432  HIS A 436                    
    SITE     1 AC3  5 HOH A  33  GLU A 387  ASN A 391  ASP A 429                    
    SITE     2 AC3  5 HIS A 458                                                     
    SITE     1 AC4  2 ASP A 444  HOH A 732                                          
    SITE     1 AC5  4 GLU A 399  HIS A 439  HOH A 747  HOH A 748                    
    SITE     1 AC6  4 HIS A 327  GLU A 368  ASP A 392  HOH A 711                    
    SITE     1 AC7  3 GLU A 362  GLU A 365  ACT A 601                               
    SITE     1 AC8  3 GLU A 329  GLN A 484  ASP A 488                               
    SITE     1 AC9  1 HIS A 359                                                     
    SITE     1 BC1  2 GLU A 321  ASN A 400                                          
    CRYST1   39.757   39.757  126.425  90.00  90.00  90.00 P 43          4          
    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      0.025153  0.000000  0.000000        0.00000                         
    SCALE2      0.000000  0.025153  0.000000        0.00000                         
    SCALE3      0.000000  0.000000  0.007910        0.00000                         

    3D molecular view of vibration

    Displacement vectors
    Display
    Animation
    Display

    Still image of displacement vectors and GIF animation


    Mode 1

    Time-average properties and properties of the 10 lowest-frequency modes

    Fluctuation of atoms:
    Time average and for the 3 lowest-frequency modes.
    Fluctuation of dihedral angles:
    Time average and for the 3 lowest-frequency modes.
    Fluctuation of atomsFluctuation of dihedral angles

    Correlations between fluctuations of atoms

    Mode 1
    Correlations between fluctuations of atoms - Mode 1
    Time Average
    Time Average
    Distance map
    Distance map

    Calculation note

    PDB file name : pdb3umi.ent

    Chains and HETATMs selected: 
      ATOM        A

    The following atoms are removed from PDB data on concern that they may have 
    abnormally large fluctuations, because they interact with few atoms.
      ATOM    296  CG  ARG A 343     -95.333 -14.745 -13.552  0.00 64.64           C  
      ATOM    297  CD  ARG A 343     -95.034 -14.676 -12.055  0.00 64.25           C  
      ATOM    298  NE  ARG A 343     -95.640 -13.509 -11.418  0.00 63.94           N  
      ATOM    299  CZ  ARG A 343     -96.054 -13.470 -10.154  0.00 63.79           C  
      ATOM    300  NH1 ARG A 343     -95.939 -14.541  -9.379  0.00 63.70           N  
      ATOM    301  NH2 ARG A 343     -96.579 -12.356  -9.662  0.00 63.70           N  
      ATOM    353  CG  LYS A 350     -99.503 -24.353 -27.881  0.00 68.36           C  
      ATOM    354  CD  LYS A 350    -100.435 -25.326 -28.571  0.00 66.64           C  
      ATOM    355  CE  LYS A 350     -99.799 -26.693 -28.720  0.00 65.57           C  
      ATOM    356  NZ  LYS A 350    -100.701 -27.674 -29.385  0.00 64.57           N  
      ATOM    384  CG  LYS A 354     -94.083 -25.640 -28.793  0.00 59.47           C  
      ATOM    385  CD  LYS A 354     -95.004 -26.112 -29.924  0.00 59.56           C  
      ATOM    386  CE  LYS A 354     -94.541 -27.402 -30.597  0.00 59.61           C  
      ATOM    387  NZ  LYS A 354     -95.484 -27.791 -31.696  0.00 59.62           N  
      ATOM    865  CG  ARG A 413     -29.120 -44.890   4.285  1.00 29.37           C  
      ATOM    866  CD  ARG A 413     -29.858 -45.907   5.110  1.00 41.00           C  
      ATOM    867  NE  ARG A 413     -30.123 -45.421   6.461  1.00 46.32           N  
      ATOM    868  CZ  ARG A 413     -30.371 -46.216   7.495  1.00 42.13           C  
      ATOM    869  NH1 ARG A 413     -30.609 -45.701   8.692  1.00 47.95           N  
      ATOM    870  NH2 ARG A 413     -30.365 -47.529   7.332  1.00 40.34           N  
      ATOM   1061  CG  LYS A 435     -56.178 -40.514 -11.621  1.00 36.91           C  
      ATOM   1062  CD  LYS A 435     -55.639 -39.718 -10.441  0.00 34.93           C  
      ATOM   1063  CE  LYS A 435     -56.759 -39.090  -9.630  0.00 35.56           C  
      ATOM   1064  NZ  LYS A 435     -56.230 -38.284  -8.494  0.00 35.45           N  
      ATOM   1158  CG  LYS A 446     -67.210 -44.119 -28.495  1.00 38.81           C  
      ATOM   1159  CD  LYS A 446     -68.490 -43.574 -29.110  1.00 44.38           C  
      ATOM   1160  CE  LYS A 446     -69.540 -44.664 -29.227  1.00 48.05           C  
      ATOM   1161  NZ  LYS A 446     -70.892 -44.112 -29.530  1.00 56.06           N  

    = Normal mode analysis calculation =

    No. of modes used in the calculation : All modes.

    Parameters of potential energies:
      1-4 and 1-5 non-bonded interactions: E(d) = A*exp(-d(PDB)**2/B**2)(d-d(PDB))**2.
      Loop-closing potential:              E(d) = A*(d-d(PDB))**2.
        for a disulfide bond and one of the bonds in the DNA and RNA sugar ring.
      where d and d(PDB) are distances between atoms in calculation and in PDB data, 
      respectively.

      Interaction type   A       B      Cutoff distance (A)
        1-4             1.00    5.00      100.00
        1-5             1.00    5.00      100.00
        Loop-closing  100.00

    Temperature adjustment by magnitude of fluctuation:
      Set to mean displacements of atoms       0.500 A

    Animation
      No. of frames: 11
      Mean displacements (A):    0.50

    Displacement vector
      Mean length of vectors (A):    3.00