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Database: PDB
Entry: 1AV4 1AVK 1AVL
LinkDB: 1AV4 1AVK 1AVL
Original site: 1AV4 1AVK 1AVL 
HEADER    OXIDOREDUCTASE                          24-SEP-97   1AV4              
TITLE     CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM        
TITLE    2 ARTHROBACTER GLOBIFORMIS IN THE HOLO-AND APO-FORMS: IMPLICATIONS FOR 
TITLE    3 THE BIOGENESIS OF TOPA QUINONE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AMINE OXIDASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AGAO;                                                       
COMPND   5 EC: 1.4.3.6                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARTHROBACTER GLOBIFORMIS;                       
SOURCE   3 ORGANISM_TAXID: 1665                                                 
KEYWDS    OXIDOREDUCTASE, COPPER CONTAINING, AMINE OXIDASE, ARTHROBACTER        
KEYWDS   2 GLOBIFORMIS                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.C.J.WILCE,J.M.GUSS,H.C.FREEMAN                                      
REVDAT   5   02-AUG-23 1AV4    1       REMARK SEQADV LINK                       
REVDAT   4   13-JUL-11 1AV4    1       VERSN                                    
REVDAT   3   24-FEB-09 1AV4    1       VERSN                                    
REVDAT   2   01-APR-03 1AV4    1       JRNL                                     
REVDAT   1   25-MAR-98 1AV4    0                                                
JRNL        AUTH   M.C.WILCE,D.M.DOOLEY,H.C.FREEMAN,J.M.GUSS,H.MATSUNAMI,       
JRNL        AUTH 2 W.S.MCINTIRE,C.E.RUGGIERO,K.TANIZAWA,H.YAMAGUCHI             
JRNL        TITL   CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE    
JRNL        TITL 2 FROM ARTHROBACTER GLOBIFORMIS IN THE HOLO AND APO FORMS:     
JRNL        TITL 3 IMPLICATIONS FOR THE BIOGENESIS OF TOPAQUINONE.              
JRNL        REF    BIOCHEMISTRY                  V.  36 16116 1997              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9405045                                                      
JRNL        DOI    10.1021/BI971797I                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 33778                          
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 SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1049                            
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.30                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3637                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE                    : 0.2990                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 121                          
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            : 4868                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 247                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.00                          
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) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.700                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.600                           
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  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  : TPQ-NEW.PAR                                    
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TPQ-NEW.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: STANDARD X-PLOR LIBRARIES USED FOR        
REMARK   3  REFINEMENT EXCEPT FOR TPQ-NEW.PAR/.TOP FOR RESIDUE TPQ 382          
REMARK   4                                                                      
REMARK   4 1AV4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171295.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : DEC-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 8.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : BENT QUARTZ CRYSTAL                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : FILM                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33778                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.000                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY                : 3.130                              
REMARK 200  R MERGE                    (I) : 0.08500                            
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) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.8                                            
REMARK 200 STARTING MODEL: PDB ENTRY 1OAC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.1                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       79.32500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.28500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       79.32500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.28500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 13530 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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 -1.000000  0.000000  0.000000      -37.18437            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       85.55903            
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     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     PRO A   629                                                      
REMARK 465     SER A   630                                                      
REMARK 465     GLN A   631                                                      
REMARK 465     SER A   632                                                      
REMARK 465     GLY A   633                                                      
REMARK 465     SER A   634                                                      
REMARK 465     HIS A   635                                                      
REMARK 465     CYS A   636                                                      
REMARK 465     HIS A   637                                                      
REMARK 465     GLY A   638                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     ARG A    49                                                      
REMARK 475     GLY A    50                                                      
REMARK 475     ALA A    51                                                      
REMARK 475     GLY A    52                                                      
REMARK 475     SER A    53                                                      
REMARK 475     GLU A    54                                                      
REMARK 475     ALA A    55                                                      
REMARK 475     GLU A    56                                                      
REMARK 475     TPQ A   382                                                      
REMARK 475     MET A   460                                                      
REMARK 475     GLY A   461                                                      
REMARK 475     PRO A   462                                                      
REMARK 475     GLY A   463                                                      
REMARK 475     ASN A   464                                                      
REMARK 475     GLN A   560                                                      
REMARK 475     HIS A   561                                                      
REMARK 475     SER A   562                                                      
REMARK 475     GLY A   563                                                      
REMARK 475     GLY A   564                                                      
REMARK 475     ALA A   565                                                      
REMARK 475     GLY A   566                                                      
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   NH1  ARG A   466     O    HOH A   689              1.61            
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   NE   ARG A   466     O    HOH A   811     2556     1.12            
REMARK 500   CZ   ARG A   466     O    HOH A   811     2556     1.53            
REMARK 500   OG   SER A   292     NH1  ARG A   466     2556     1.79            
REMARK 500   CD   ARG A   466     O    HOH A   811     2556     2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 465   C     ARG A 466   N      -0.169                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A 466   C   -  N   -  CA  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    ARG A 466   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 466   CA  -  C   -  N   ANGL. DEV. = -13.4 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    ALA A  55       94.53    -62.55                                   
REMARK 500    PHE A 142     -151.73   -127.21                                   
REMARK 500    GLU A 143       25.68    -77.59                                   
REMARK 500    LYS A 242       -7.73     85.24                                   
REMARK 500    ASP A 266      -33.51     74.23                                   
REMARK 500    PHE A 297       70.26   -111.05                                   
REMARK 500    LEU A 303       90.81     80.77                                   
REMARK 500    CYS A 315      -61.80   -102.91                                   
REMARK 500    THR A 403     -154.26   -140.78                                   
REMARK 500    ALA A 442       53.42   -146.34                                   
REMARK 500    ILE A 443       98.87    -63.62                                   
REMARK 500    ASN A 464       70.48     46.14                                   
REMARK 500    SER A 471     -154.41   -127.38                                   
REMARK 500    ASP A 488       86.46   -163.57                                   
REMARK 500    ALA A 565       -4.91    -50.46                                   
REMARK 500    ARG A 619     -176.38   -170.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 639  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 431   NE2                                                    
REMARK 620 2 HIS A 433   NE2 101.4                                              
REMARK 620 3 HIS A 592   ND1  90.3 145.4                                        
REMARK 620 4 HIS A 592   ND1 120.3  87.7  58.6                                  
REMARK 620 5 HOH A 885   O   171.1  87.2  83.6  61.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 639                  
DBREF  1AV4 A    1   638  UNP    P46881   PAOX_ARTGO       1    638             
SEQADV 1AV4 TPQ A  382  UNP  P46881    TYR   382 MODIFIED RESIDUE               
SEQRES   1 A  638  MET THR PRO SER THR ILE GLN THR ALA SER PRO PHE ARG          
SEQRES   2 A  638  LEU ALA SER ALA GLY GLU ILE SER GLU VAL GLN GLY ILE          
SEQRES   3 A  638  LEU ARG THR ALA GLY LEU LEU GLY PRO GLU LYS ARG ILE          
SEQRES   4 A  638  ALA TYR LEU GLY VAL LEU ASP PRO ALA ARG GLY ALA GLY          
SEQRES   5 A  638  SER GLU ALA GLU ASP ARG ARG PHE ARG VAL PHE ILE HIS          
SEQRES   6 A  638  ASP VAL SER GLY ALA ARG PRO GLN GLU VAL THR VAL SER          
SEQRES   7 A  638  VAL THR ASN GLY THR VAL ILE SER ALA VAL GLU LEU ASP          
SEQRES   8 A  638  THR ALA ALA THR GLY GLU LEU PRO VAL LEU GLU GLU GLU          
SEQRES   9 A  638  PHE GLU VAL VAL GLU GLN LEU LEU ALA THR ASP GLU ARG          
SEQRES  10 A  638  TRP LEU LYS ALA LEU ALA ALA ARG ASN LEU ASP VAL SER          
SEQRES  11 A  638  LYS VAL ARG VAL ALA PRO LEU SER ALA GLY VAL PHE GLU          
SEQRES  12 A  638  TYR ALA GLU GLU ARG GLY ARG ARG ILE LEU ARG GLY LEU          
SEQRES  13 A  638  ALA PHE VAL GLN ASP PHE PRO GLU ASP SER ALA TRP ALA          
SEQRES  14 A  638  HIS PRO VAL ASP GLY LEU VAL ALA TYR VAL ASP VAL VAL          
SEQRES  15 A  638  SER LYS GLU VAL THR ARG VAL ILE ASP THR GLY VAL PHE          
SEQRES  16 A  638  PRO VAL PRO ALA GLU HIS GLY ASN TYR THR ASP PRO GLU          
SEQRES  17 A  638  LEU THR GLY PRO LEU ARG THR THR GLN LYS PRO ILE SER          
SEQRES  18 A  638  ILE THR GLN PRO GLU GLY PRO SER PHE THR VAL THR GLY          
SEQRES  19 A  638  GLY ASN HIS ILE GLU TRP GLU LYS TRP SER LEU ASP VAL          
SEQRES  20 A  638  GLY PHE ASP VAL ARG GLU GLY VAL VAL LEU HIS ASN ILE          
SEQRES  21 A  638  ALA PHE ARG ASP GLY ASP ARG LEU ARG PRO ILE ILE ASN          
SEQRES  22 A  638  ARG ALA SER ILE ALA GLU MET VAL VAL PRO TYR GLY ASP          
SEQRES  23 A  638  PRO SER PRO ILE ARG SER TRP GLN ASN TYR PHE ASP THR          
SEQRES  24 A  638  GLY GLU TYR LEU VAL GLY GLN TYR ALA ASN SER LEU GLU          
SEQRES  25 A  638  LEU GLY CYS ASP CYS LEU GLY ASP ILE THR TYR LEU SER          
SEQRES  26 A  638  PRO VAL ILE SER ASP ALA PHE GLY ASN PRO ARG GLU ILE          
SEQRES  27 A  638  ARG ASN GLY ILE CYS MET HIS GLU GLU ASP TRP GLY ILE          
SEQRES  28 A  638  LEU ALA LYS HIS SER ASP LEU TRP SER GLY ILE ASN TYR          
SEQRES  29 A  638  THR ARG ARG ASN ARG ARG MET VAL ILE SER PHE PHE THR          
SEQRES  30 A  638  THR ILE GLY ASN TPQ ASP TYR GLY PHE TYR TRP TYR LEU          
SEQRES  31 A  638  TYR LEU ASP GLY THR ILE GLU PHE GLU ALA LYS ALA THR          
SEQRES  32 A  638  GLY VAL VAL PHE THR SER ALA PHE PRO GLU GLY GLY SER          
SEQRES  33 A  638  ASP ASN ILE SER GLN LEU ALA PRO GLY LEU GLY ALA PRO          
SEQRES  34 A  638  PHE HIS GLN HIS ILE PHE SER ALA ARG LEU ASP MET ALA          
SEQRES  35 A  638  ILE ASP GLY PHE THR ASN ARG VAL GLU GLU GLU ASP VAL          
SEQRES  36 A  638  VAL ARG GLN THR MET GLY PRO GLY ASN GLU ARG GLY ASN          
SEQRES  37 A  638  ALA PHE SER ARG LYS ARG THR VAL LEU THR ARG GLU SER          
SEQRES  38 A  638  GLU ALA VAL ARG GLU ALA ASP ALA ARG THR GLY ARG THR          
SEQRES  39 A  638  TRP ILE ILE SER ASN PRO GLU SER LYS ASN ARG LEU ASN          
SEQRES  40 A  638  GLU PRO VAL GLY TYR LYS LEU HIS ALA HIS ASN GLN PRO          
SEQRES  41 A  638  THR LEU LEU ALA ASP PRO GLY SER SER ILE ALA ARG ARG          
SEQRES  42 A  638  ALA ALA PHE ALA THR LYS ASP LEU TRP VAL THR ARG TYR          
SEQRES  43 A  638  ALA ASP ASP GLU ARG TYR PRO THR GLY ASP PHE VAL ASN          
SEQRES  44 A  638  GLN HIS SER GLY GLY ALA GLY LEU PRO SER TYR ILE ALA          
SEQRES  45 A  638  GLN ASP ARG ASP ILE ASP GLY GLN ASP ILE VAL VAL TRP          
SEQRES  46 A  638  HIS THR PHE GLY LEU THR HIS PHE PRO ARG VAL GLU ASP          
SEQRES  47 A  638  TRP PRO ILE MET PRO VAL ASP THR VAL GLY PHE LYS LEU          
SEQRES  48 A  638  ARG PRO GLU GLY PHE PHE ASP ARG SER PRO VAL LEU ASP          
SEQRES  49 A  638  VAL PRO ALA ASN PRO SER GLN SER GLY SER HIS CYS HIS          
SEQRES  50 A  638  GLY                                                          
MODRES 1AV4 TPQ A  382  TYR                                                     
HET    TPQ  A 382      14                                                       
HET     CU  A 639       1                                                       
HETNAM     TPQ 5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE            
HETNAM      CU COPPER (II) ION                                                  
HETSYN     TPQ 5-(2-CARBOXY-2-AMINOETHYL)-4-HYDROXY-1,2-BENZOQUINONE;           
HETSYN   2 TPQ  2,4,5-TRIHYDROXYPHENYLALANINE QUINONE; TOPA QUINONE             
FORMUL   1  TPQ    C9 H9 N O5                                                   
FORMUL   2   CU    CU 2+                                                        
FORMUL   3  HOH   *247(H2 O)                                                    
HELIX    1   1 ALA A   17  THR A   29  1                                  13    
HELIX    2   2 THR A   92  THR A   95  1                                   4    
HELIX    3   3 GLU A  102  THR A  114  1                                  13    
HELIX    4   4 GLU A  116  ARG A  125  1                                  10    
HELIX    5   5 VAL A  129  LYS A  131  5                                   3    
HELIX    6   6 ALA A  167  ALA A  169  5                                   3    
HELIX    7   7 PRO A  207  THR A  210  1                                   4    
HELIX    8   8 VAL A  304  TYR A  307  5                                   4    
HELIX    9   9 GLU A  480  GLU A  482  5                                   3    
HELIX   10  10 ALA A  489  THR A  491  5                                   3    
HELIX   11  11 SER A  529  ARG A  533  1                                   5    
HELIX   12  12 ALA A  535  THR A  538  5                                   4    
HELIX   13  13 LEU A  567  GLN A  573  1                                   7    
HELIX   14  14 VAL A  596  ASP A  598  5                                   3    
SHEET    1   A 4 LYS A  37  VAL A  44  0                                        
SHEET    2   A 4 ARG A  59  ASP A  66 -1  N  HIS A  65   O  ARG A  38           
SHEET    3   A 4 GLN A  73  SER A  78 -1  N  VAL A  77   O  PHE A  60           
SHEET    4   A 4 THR A  83  GLU A  89 -1  N  VAL A  88   O  GLU A  74           
SHEET    1   B 4 VAL A 132  SER A 138  0                                        
SHEET    2   B 4 ILE A 152  VAL A 159 -1  N  PHE A 158   O  ARG A 133           
SHEET    3   B 4 LEU A 175  ASP A 180 -1  N  VAL A 179   O  LEU A 153           
SHEET    4   B 4 GLU A 185  ASP A 191 -1  N  ILE A 190   O  VAL A 176           
SHEET    1   C 4 THR A 231  THR A 233  0                                        
SHEET    2   C 4 HIS A 237  TRP A 240 -1  N  GLU A 239   O  THR A 231           
SHEET    3   C 4 TRP A 243  ASP A 250 -1  N  LEU A 245   O  ILE A 238           
SHEET    4   C 4 GLY A 254  HIS A 258 -1  N  HIS A 258   O  ASP A 246           
SHEET    1   D 5 ASN A 295  PHE A 297  0                                        
SHEET    2   D 5 GLU A 279  PRO A 283 -1  N  VAL A 282   O  TYR A 296           
SHEET    3   D 5 HIS A 431  ASP A 440 -1  N  SER A 436   O  GLU A 279           
SHEET    4   D 5 ILE A 582  HIS A 592 -1  N  HIS A 592   O  HIS A 431           
SHEET    5   D 5 LEU A 541  ARG A 545 -1  N  THR A 544   O  VAL A 583           
SHEET    1   E 5 THR A 322  LEU A 324  0                                        
SHEET    2   E 5 ILE A 342  ASP A 348 -1  N  MET A 344   O  THR A 322           
SHEET    3   E 5 ARG A 369  THR A 377 -1  N  SER A 374   O  CYS A 343           
SHEET    4   E 5 TYR A 384  TYR A 391 -1  N  LEU A 390   O  MET A 371           
SHEET    5   E 5 ILE A 396  ALA A 402 -1  N  LYS A 401   O  GLY A 385           
SHEET    1   F 2 VAL A 327  SER A 329  0                                        
SHEET    2   F 2 PRO A 335  GLU A 337 -1  N  ARG A 336   O  ILE A 328           
SHEET    1   G 3 THR A 408  ALA A 410  0                                        
SHEET    2   G 3 LEU A 426  PRO A 429 -1  N  GLY A 427   O  SER A 409           
SHEET    3   G 3 ILE A 419  ALA A 423 -1  N  ALA A 423   O  LEU A 426           
SHEET    1   H 4 PHE A 470  LEU A 477  0                                        
SHEET    2   H 4 ARG A 449  ARG A 457 -1  N  VAL A 456   O  SER A 471           
SHEET    3   H 4 THR A 494  LYS A 503 -1  N  SER A 498   O  ARG A 449           
SHEET    4   H 4 PRO A 509  LEU A 514 -1  N  LEU A 514   O  TRP A 495           
SHEET    1   I 3 ILE A 260  ASP A 264  0                                        
SHEET    2   I 3 ARG A 267  ILE A 277 -1  N  ILE A 272   O  ILE A 260           
SHEET    3   I 3 ALA A 437  MET A 441 -1  N  ASP A 440   O  ASN A 273           
SHEET    1   J 2 ILE A 351  SER A 356  0                                        
SHEET    2   J 2 ASN A 363  ARG A 367 -1  N  ARG A 366   O  LEU A 352           
SSBOND   1 CYS A  317    CYS A  343                          1555   1555  2.03  
LINK         C   ASN A 381                 N   TPQ A 382     1555   1555  1.33  
LINK         C   TPQ A 382                 N   ASP A 383     1555   1555  1.33  
LINK         NE2 HIS A 431                CU    CU A 639     1555   1555  2.08  
LINK         NE2 HIS A 433                CU    CU A 639     1555   1555  2.06  
LINK         ND1BHIS A 592                CU    CU A 639     1555   1555  2.08  
LINK         ND1AHIS A 592                CU    CU A 639     1555   1555  2.36  
LINK        CU    CU A 639                 O   HOH A 885     1555   1555  2.07  
CISPEP   1 TRP A  599    PRO A  600          0        -0.46                     
SITE     1 AC1  4 HIS A 431  HIS A 433  HIS A 592  HOH A 885                    
CRYST1  158.650   64.570   93.290  90.00 113.49  90.00 C 1 2 1       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      0.006303  0.000000  0.002739        0.00000                         
SCALE2      0.000000  0.015487  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011688        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    OXIDOREDUCTASE                          16-SEP-97   1AVK              
TITLE     CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM        
TITLE    2 ARTHROBACTER GLOBIFORMIS IN THE HOLO-AND APO-FORMS: IMPLICATIONS FOR 
TITLE    3 THE BIOGENESIS OF TOPA QUINONE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AMINE OXIDASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AGAO;                                                       
COMPND   5 EC: 1.4.3.6;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARTHROBACTER GLOBIFORMIS;                       
SOURCE   3 ORGANISM_TAXID: 1665;                                                
SOURCE   4 CELL_LINE: BL21;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PPEAO2;                                    
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: BL21                                      
KEYWDS    OXIDOREDUCTASE, COPPER CONTAINING, AMINE OXIDASE, ARTHROBACTER        
KEYWDS   2 GLOBIFORMIS, QUINONE, TPQ                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.C.J.WILCE,J.M.GUSS,H.C.FREEMAN,K.TANIZAWA,H.YAMAGUCHI               
REVDAT   5   16-NOV-11 1AVK    1       HETATM                                   
REVDAT   4   13-JUL-11 1AVK    1       VERSN                                    
REVDAT   3   24-FEB-09 1AVK    1       VERSN                                    
REVDAT   2   01-APR-03 1AVK    1       JRNL                                     
REVDAT   1   18-MAR-98 1AVK    0                                                
JRNL        AUTH   M.C.WILCE,D.M.DOOLEY,H.C.FREEMAN,J.M.GUSS,H.MATSUNAMI,       
JRNL        AUTH 2 W.S.MCINTIRE,C.E.RUGGIERO,K.TANIZAWA,H.YAMAGUCHI             
JRNL        TITL   CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE    
JRNL        TITL 2 FROM ARTHROBACTER GLOBIFORMIS IN THE HOLO AND APO FORMS:     
JRNL        TITL 3 IMPLICATIONS FOR THE BIOGENESIS OF TOPAQUINONE.              
JRNL        REF    BIOCHEMISTRY                  V.  36 16116 1997              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9405045                                                      
JRNL        DOI    10.1021/BI971797I                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 39585                          
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 SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1707                            
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.30                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2909                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3030                       
REMARK   3   BIN FREE R VALUE                    : 0.3630                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 141                          
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            : 4866                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 204                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.00                          
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) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.70                            
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  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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AVK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : DEC-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 6.8                                
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 RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PROCESS                            
REMARK 200  DATA SCALING SOFTWARE          : PROCESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39585                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.3                               
REMARK 200  DATA REDUNDANCY                : 1.500                              
REMARK 200  R MERGE                    (I) : 0.06100                            
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) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: HOLO-AGAO                                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.8                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       79.36000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.30000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       79.36000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.30000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 13260 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 -1.000000  0.000000  0.000000      -35.44465            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       86.29427            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 827  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 818  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 832  LIES ON A SPECIAL POSITION.                          
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     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     PRO A   629                                                      
REMARK 465     SER A   630                                                      
REMARK 465     GLN A   631                                                      
REMARK 465     SER A   632                                                      
REMARK 465     GLY A   633                                                      
REMARK 465     SER A   634                                                      
REMARK 465     HIS A   635                                                      
REMARK 465     CYS A   636                                                      
REMARK 465     HIS A   637                                                      
REMARK 465     GLY A   638                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     GLY A   50                                                       
REMARK 475     ALA A   51                                                       
REMARK 475     GLY A   52                                                       
REMARK 475     SER A   53                                                       
REMARK 475     GLU A   54                                                       
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   NH2  ARG A   466     O    HOH A   660              1.25            
REMARK 500   CZ   ARG A   466     O    HOH A   660              1.34            
REMARK 500   NE   ARG A   466     O    HOH A   660              1.98            
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   OG   SER A   292     NH1  ARG A   466     2556     1.49            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    PRO A 462   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    GLU A 465   N   -  CA  -  C   ANGL. DEV. = -21.5 DEGREES          
REMARK 500    ARG A 466   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 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    LEU A  33       61.81   -106.96                                   
REMARK 500    ALA A  51       13.47    -69.29                                   
REMARK 500    ALA A  55      129.80    101.00                                   
REMARK 500    PHE A 142     -146.08   -127.80                                   
REMARK 500    TYR A 144       95.26    -42.74                                   
REMARK 500    TYR A 204        3.46    -64.73                                   
REMARK 500    ASN A 236       19.03   -147.03                                   
REMARK 500    LYS A 242       -4.65     80.13                                   
REMARK 500    ASP A 266       46.46   -108.58                                   
REMARK 500    ILE A 271      -55.34   -125.65                                   
REMARK 500    ARG A 291       -3.53   -141.95                                   
REMARK 500    PHE A 297       73.40   -109.63                                   
REMARK 500    LEU A 303       95.32     68.35                                   
REMARK 500    CYS A 315      -60.41    -96.94                                   
REMARK 500    ASP A 330     -169.62    -75.94                                   
REMARK 500    ALA A 428      107.02   -160.47                                   
REMARK 500    ALA A 442       52.33   -146.53                                   
REMARK 500    ILE A 443       97.64    -64.14                                   
REMARK 500    PRO A 462      -73.17    -71.53                                   
REMARK 500    ARG A 466      -25.78     82.28                                   
REMARK 500    SER A 471     -158.00   -130.19                                   
REMARK 500    ASP A 488       84.64   -158.18                                   
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    SER A 562        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1AVK A    1   638  UNP    P46881   PAOX_ARTGO       1    638             
SEQRES   1 A  638  MET THR PRO SER THR ILE GLN THR ALA SER PRO PHE ARG          
SEQRES   2 A  638  LEU ALA SER ALA GLY GLU ILE SER GLU VAL GLN GLY ILE          
SEQRES   3 A  638  LEU ARG THR ALA GLY LEU LEU GLY PRO GLU LYS ARG ILE          
SEQRES   4 A  638  ALA TYR LEU GLY VAL LEU ASP PRO ALA ARG GLY ALA GLY          
SEQRES   5 A  638  SER GLU ALA GLU ASP ARG ARG PHE ARG VAL PHE ILE HIS          
SEQRES   6 A  638  ASP VAL SER GLY ALA ARG PRO GLN GLU VAL THR VAL SER          
SEQRES   7 A  638  VAL THR ASN GLY THR VAL ILE SER ALA VAL GLU LEU ASP          
SEQRES   8 A  638  THR ALA ALA THR GLY GLU LEU PRO VAL LEU GLU GLU GLU          
SEQRES   9 A  638  PHE GLU VAL VAL GLU GLN LEU LEU ALA THR ASP GLU ARG          
SEQRES  10 A  638  TRP LEU LYS ALA LEU ALA ALA ARG ASN LEU ASP VAL SER          
SEQRES  11 A  638  LYS VAL ARG VAL ALA PRO LEU SER ALA GLY VAL PHE GLU          
SEQRES  12 A  638  TYR ALA GLU GLU ARG GLY ARG ARG ILE LEU ARG GLY LEU          
SEQRES  13 A  638  ALA PHE VAL GLN ASP PHE PRO GLU ASP SER ALA TRP ALA          
SEQRES  14 A  638  HIS PRO VAL ASP GLY LEU VAL ALA TYR VAL ASP VAL VAL          
SEQRES  15 A  638  SER LYS GLU VAL THR ARG VAL ILE ASP THR GLY VAL PHE          
SEQRES  16 A  638  PRO VAL PRO ALA GLU HIS GLY ASN TYR THR ASP PRO GLU          
SEQRES  17 A  638  LEU THR GLY PRO LEU ARG THR THR GLN LYS PRO ILE SER          
SEQRES  18 A  638  ILE THR GLN PRO GLU GLY PRO SER PHE THR VAL THR GLY          
SEQRES  19 A  638  GLY ASN HIS ILE GLU TRP GLU LYS TRP SER LEU ASP VAL          
SEQRES  20 A  638  GLY PHE ASP VAL ARG GLU GLY VAL VAL LEU HIS ASN ILE          
SEQRES  21 A  638  ALA PHE ARG ASP GLY ASP ARG LEU ARG PRO ILE ILE ASN          
SEQRES  22 A  638  ARG ALA SER ILE ALA GLU MET VAL VAL PRO TYR GLY ASP          
SEQRES  23 A  638  PRO SER PRO ILE ARG SER TRP GLN ASN TYR PHE ASP THR          
SEQRES  24 A  638  GLY GLU TYR LEU VAL GLY GLN TYR ALA ASN SER LEU GLU          
SEQRES  25 A  638  LEU GLY CYS ASP CYS LEU GLY ASP ILE THR TYR LEU SER          
SEQRES  26 A  638  PRO VAL ILE SER ASP ALA PHE GLY ASN PRO ARG GLU ILE          
SEQRES  27 A  638  ARG ASN GLY ILE CYS MET HIS GLU GLU ASP TRP GLY ILE          
SEQRES  28 A  638  LEU ALA LYS HIS SER ASP LEU TRP SER GLY ILE ASN TYR          
SEQRES  29 A  638  THR ARG ARG ASN ARG ARG MET VAL ILE SER PHE PHE THR          
SEQRES  30 A  638  THR ILE GLY ASN TYR ASP TYR GLY PHE TYR TRP TYR LEU          
SEQRES  31 A  638  TYR LEU ASP GLY THR ILE GLU PHE GLU ALA LYS ALA THR          
SEQRES  32 A  638  GLY VAL VAL PHE THR SER ALA PHE PRO GLU GLY GLY SER          
SEQRES  33 A  638  ASP ASN ILE SER GLN LEU ALA PRO GLY LEU GLY ALA PRO          
SEQRES  34 A  638  PHE HIS GLN HIS ILE PHE SER ALA ARG LEU ASP MET ALA          
SEQRES  35 A  638  ILE ASP GLY PHE THR ASN ARG VAL GLU GLU GLU ASP VAL          
SEQRES  36 A  638  VAL ARG GLN THR MET GLY PRO GLY ASN GLU ARG GLY ASN          
SEQRES  37 A  638  ALA PHE SER ARG LYS ARG THR VAL LEU THR ARG GLU SER          
SEQRES  38 A  638  GLU ALA VAL ARG GLU ALA ASP ALA ARG THR GLY ARG THR          
SEQRES  39 A  638  TRP ILE ILE SER ASN PRO GLU SER LYS ASN ARG LEU ASN          
SEQRES  40 A  638  GLU PRO VAL GLY TYR LYS LEU HIS ALA HIS ASN GLN PRO          
SEQRES  41 A  638  THR LEU LEU ALA ASP PRO GLY SER SER ILE ALA ARG ARG          
SEQRES  42 A  638  ALA ALA PHE ALA THR LYS ASP LEU TRP VAL THR ARG TYR          
SEQRES  43 A  638  ALA ASP ASP GLU ARG TYR PRO THR GLY ASP PHE VAL ASN          
SEQRES  44 A  638  GLN HIS SER GLY GLY ALA GLY LEU PRO SER TYR ILE ALA          
SEQRES  45 A  638  GLN ASP ARG ASP ILE ASP GLY GLN ASP ILE VAL VAL TRP          
SEQRES  46 A  638  HIS THR PHE GLY LEU THR HIS PHE PRO ARG VAL GLU ASP          
SEQRES  47 A  638  TRP PRO ILE MET PRO VAL ASP THR VAL GLY PHE LYS LEU          
SEQRES  48 A  638  ARG PRO GLU GLY PHE PHE ASP ARG SER PRO VAL LEU ASP          
SEQRES  49 A  638  VAL PRO ALA ASN PRO SER GLN SER GLY SER HIS CYS HIS          
SEQRES  50 A  638  GLY                                                          
FORMUL   2  HOH   *204(H2 O)                                                    
HELIX    1   1 ALA A   17  THR A   29  1                                  13    
HELIX    2   2 THR A   92  THR A   95  1                                   4    
HELIX    3   3 GLU A  102  PHE A  105  1                                   4    
HELIX    4   4 VAL A  107  THR A  114  1                                   8    
HELIX    5   5 GLU A  116  ALA A  123  1                                   8    
HELIX    6   6 VAL A  129  LYS A  131  5                                   3    
HELIX    7   7 ALA A  167  ALA A  169  5                                   3    
HELIX    8   8 PRO A  207  THR A  210  1                                   4    
HELIX    9   9 VAL A  304  TYR A  307  5                                   4    
HELIX   10  10 GLU A  480  GLU A  482  5                                   3    
HELIX   11  11 ALA A  489  THR A  491  5                                   3    
HELIX   12  12 SER A  529  ARG A  533  1                                   5    
HELIX   13  13 ALA A  535  THR A  538  5                                   4    
HELIX   14  14 LEU A  567  GLN A  573  1                                   7    
HELIX   15  15 VAL A  596  ASP A  598  5                                   3    
SHEET    1   A 4 LYS A  37  VAL A  44  0                                        
SHEET    2   A 4 ARG A  59  ASP A  66 -1  N  HIS A  65   O  ARG A  38           
SHEET    3   A 4 GLN A  73  SER A  78 -1  N  VAL A  77   O  PHE A  60           
SHEET    4   A 4 THR A  83  GLU A  89 -1  N  VAL A  88   O  GLU A  74           
SHEET    1   B 4 VAL A 132  SER A 138  0                                        
SHEET    2   B 4 ILE A 152  VAL A 159 -1  N  PHE A 158   O  ARG A 133           
SHEET    3   B 4 LEU A 175  ASP A 180 -1  N  VAL A 179   O  LEU A 153           
SHEET    4   B 4 GLU A 185  ASP A 191 -1  N  ILE A 190   O  VAL A 176           
SHEET    1   C 4 THR A 231  THR A 233  0                                        
SHEET    2   C 4 HIS A 237  TRP A 240 -1  N  GLU A 239   O  THR A 231           
SHEET    3   C 4 TRP A 243  ASP A 250 -1  N  LEU A 245   O  ILE A 238           
SHEET    4   C 4 GLY A 254  HIS A 258 -1  N  HIS A 258   O  ASP A 246           
SHEET    1   D 5 ASN A 295  PHE A 297  0                                        
SHEET    2   D 5 GLU A 279  PRO A 283 -1  N  VAL A 282   O  TYR A 296           
SHEET    3   D 5 HIS A 431  ASP A 440 -1  N  SER A 436   O  GLU A 279           
SHEET    4   D 5 ILE A 582  HIS A 592 -1  N  HIS A 592   O  HIS A 431           
SHEET    5   D 5 LEU A 541  ARG A 545 -1  N  THR A 544   O  VAL A 583           
SHEET    1   E 5 THR A 322  LEU A 324  0                                        
SHEET    2   E 5 ILE A 342  ASP A 348 -1  N  MET A 344   O  THR A 322           
SHEET    3   E 5 ARG A 369  ILE A 379 -1  N  SER A 374   O  CYS A 343           
SHEET    4   E 5 TYR A 382  TYR A 391 -1  N  LEU A 390   O  MET A 371           
SHEET    5   E 5 ILE A 396  GLY A 404 -1  N  THR A 403   O  ASP A 383           
SHEET    1   F 2 VAL A 327  SER A 329  0                                        
SHEET    2   F 2 PRO A 335  GLU A 337 -1  N  ARG A 336   O  ILE A 328           
SHEET    1   G 4 PHE A 470  LEU A 477  0                                        
SHEET    2   G 4 ARG A 449  ARG A 457 -1  N  VAL A 456   O  SER A 471           
SHEET    3   G 4 THR A 494  LYS A 503 -1  N  SER A 498   O  ARG A 449           
SHEET    4   G 4 PRO A 509  LEU A 514 -1  N  LEU A 514   O  TRP A 495           
SHEET    1   H 3 ILE A 260  ARG A 263  0                                        
SHEET    2   H 3 LEU A 268  ILE A 277 -1  N  ILE A 272   O  ILE A 260           
SHEET    3   H 3 ALA A 437  MET A 441 -1  N  ASP A 440   O  ASN A 273           
SHEET    1   I 2 ILE A 351  SER A 356  0                                        
SHEET    2   I 2 ASN A 363  ARG A 367 -1  N  ARG A 366   O  LEU A 352           
SHEET    1   J 2 ILE A 419  ALA A 423  0                                        
SHEET    2   J 2 LEU A 426  PRO A 429 -1  N  ALA A 428   O  SER A 420           
SSBOND   1 CYS A  317    CYS A  343                          1555   1555  2.02  
CISPEP   1 TRP A  599    PRO A  600          0         0.88                     
CRYST1  158.720   64.600   93.290  90.00 112.33  90.00 C 1 2 1       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      0.006300  0.000000  0.002588        0.00000                         
SCALE2      0.000000  0.015480  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011588        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    OXIDOREDUCTASE                          17-SEP-97   1AVL              
TITLE     CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM        
TITLE    2 ARTHROBACTER GLOBIFORMIS IN THE HOLO-AND APO-FORMS: IMPLICATIONS FOR 
TITLE    3 THE BIOGENESIS OF TOPA QUINONE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AMINE OXIDASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AGAO;                                                       
COMPND   5 EC: 1.4.3.6                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARTHROBACTER GLOBIFORMIS;                       
SOURCE   3 ORGANISM_TAXID: 1665                                                 
KEYWDS    OXIDOREDUCTASE, COPPER CONTAINING, AMINE OXIDASE, ARTHROBACTER        
KEYWDS   2 GLOBIFORMIS                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.C.J.WILCE,J.M.GUSS,H.C.FREEMAN                                      
REVDAT   4   13-JUL-11 1AVL    1       VERSN                                    
REVDAT   3   24-FEB-09 1AVL    1       VERSN                                    
REVDAT   2   01-APR-03 1AVL    1       JRNL                                     
REVDAT   1   18-MAR-98 1AVL    0                                                
JRNL        AUTH   M.C.WILCE,D.M.DOOLEY,H.C.FREEMAN,J.M.GUSS,H.MATSUNAMI,       
JRNL        AUTH 2 W.S.MCINTIRE,C.E.RUGGIERO,K.TANIZAWA,H.YAMAGUCHI             
JRNL        TITL   CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE    
JRNL        TITL 2 FROM ARTHROBACTER GLOBIFORMIS IN THE HOLO AND APO FORMS:     
JRNL        TITL 3 IMPLICATIONS FOR THE BIOGENESIS OF TOPAQUINONE.              
JRNL        REF    BIOCHEMISTRY                  V.  36 16116 1997              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9405045                                                      
JRNL        DOI    10.1021/BI971797I                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 19006                          
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 SET) : 0.150                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 590                             
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.90                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 19006                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1690                       
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 48                           
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            : 4868                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 121                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.00                          
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) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.80                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.70                            
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) : 2.880 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.010 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.450 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.550 ; 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: STANDARD X-PLOR LIBRARIES                 
REMARK   4                                                                      
REMARK   4 1AVL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : DEC-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 8.7                                
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 RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19006                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08200                            
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) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.21000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.8                                            
REMARK 200 STARTING MODEL: HOLO-ACTIVE FORM                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.7                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       79.10000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.05000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       79.10000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.05000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 13460 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 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 -1.000000  0.000000  0.000000      -35.85067            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       85.70379            
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     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     PRO A   629                                                      
REMARK 465     SER A   630                                                      
REMARK 465     GLN A   631                                                      
REMARK 465     SER A   632                                                      
REMARK 465     GLY A   633                                                      
REMARK 465     SER A   634                                                      
REMARK 465     HIS A   635                                                      
REMARK 465     CYS A   636                                                      
REMARK 465     HIS A   637                                                      
REMARK 465     GLY A   638                                                      
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   OG   SER A   292     NH1  ARG A   466     2556     1.82            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 465   C     ARG A 466   N      -0.197                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A 466   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 466   C   -  N   -  CA  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    ARG A 466   CA  -  C   -  N   ANGL. DEV. = -12.6 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    LEU A  33       65.81   -115.95                                   
REMARK 500    ALA A  51       31.85    -82.10                                   
REMARK 500    ALA A  55       87.98    -61.96                                   
REMARK 500    PHE A 142     -141.08   -123.81                                   
REMARK 500    LYS A 242      -12.28     78.96                                   
REMARK 500    ASP A 266      -38.47     75.12                                   
REMARK 500    ILE A 271      -52.24   -124.98                                   
REMARK 500    PRO A 289       -9.02    -58.66                                   
REMARK 500    PHE A 297       68.30   -112.48                                   
REMARK 500    LEU A 303       93.22     68.09                                   
REMARK 500    CYS A 315      -60.38    -96.77                                   
REMARK 500    ALA A 442       56.37   -144.12                                   
REMARK 500    ILE A 443       98.28    -67.41                                   
REMARK 500    ASN A 464       65.50     31.90                                   
REMARK 500    SER A 471     -161.80   -127.56                                   
REMARK 500    ASP A 488       82.89   -159.10                                   
REMARK 500    GLU A 550       70.53   -103.12                                   
REMARK 500    ALA A 565      -15.52    -48.48                                   
REMARK 500    ALA A 627       63.98   -112.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 296         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG A 466         10.30                                           
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    GLU A 465        23.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 744        DISTANCE =  5.93 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 639  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 592   ND1                                                    
REMARK 620 2 TPQ A 382   O4  109.2                                              
REMARK 620 3 HIS A 433   NE2 145.5 103.6                                        
REMARK 620 4 HIS A 431   NE2  89.3  72.8  90.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 639                  
DBREF  1AVL A    1   638  UNP    P46881   PAOX_ARTGO       1    638             
SEQADV 1AVL TPQ A  382  UNP  P46881    TYR   382 MODIFIED RESIDUE               
SEQRES   1 A  638  MET THR PRO SER THR ILE GLN THR ALA SER PRO PHE ARG          
SEQRES   2 A  638  LEU ALA SER ALA GLY GLU ILE SER GLU VAL GLN GLY ILE          
SEQRES   3 A  638  LEU ARG THR ALA GLY LEU LEU GLY PRO GLU LYS ARG ILE          
SEQRES   4 A  638  ALA TYR LEU GLY VAL LEU ASP PRO ALA ARG GLY ALA GLY          
SEQRES   5 A  638  SER GLU ALA GLU ASP ARG ARG PHE ARG VAL PHE ILE HIS          
SEQRES   6 A  638  ASP VAL SER GLY ALA ARG PRO GLN GLU VAL THR VAL SER          
SEQRES   7 A  638  VAL THR ASN GLY THR VAL ILE SER ALA VAL GLU LEU ASP          
SEQRES   8 A  638  THR ALA ALA THR GLY GLU LEU PRO VAL LEU GLU GLU GLU          
SEQRES   9 A  638  PHE GLU VAL VAL GLU GLN LEU LEU ALA THR ASP GLU ARG          
SEQRES  10 A  638  TRP LEU LYS ALA LEU ALA ALA ARG ASN LEU ASP VAL SER          
SEQRES  11 A  638  LYS VAL ARG VAL ALA PRO LEU SER ALA GLY VAL PHE GLU          
SEQRES  12 A  638  TYR ALA GLU GLU ARG GLY ARG ARG ILE LEU ARG GLY LEU          
SEQRES  13 A  638  ALA PHE VAL GLN ASP PHE PRO GLU ASP SER ALA TRP ALA          
SEQRES  14 A  638  HIS PRO VAL ASP GLY LEU VAL ALA TYR VAL ASP VAL VAL          
SEQRES  15 A  638  SER LYS GLU VAL THR ARG VAL ILE ASP THR GLY VAL PHE          
SEQRES  16 A  638  PRO VAL PRO ALA GLU HIS GLY ASN TYR THR ASP PRO GLU          
SEQRES  17 A  638  LEU THR GLY PRO LEU ARG THR THR GLN LYS PRO ILE SER          
SEQRES  18 A  638  ILE THR GLN PRO GLU GLY PRO SER PHE THR VAL THR GLY          
SEQRES  19 A  638  GLY ASN HIS ILE GLU TRP GLU LYS TRP SER LEU ASP VAL          
SEQRES  20 A  638  GLY PHE ASP VAL ARG GLU GLY VAL VAL LEU HIS ASN ILE          
SEQRES  21 A  638  ALA PHE ARG ASP GLY ASP ARG LEU ARG PRO ILE ILE ASN          
SEQRES  22 A  638  ARG ALA SER ILE ALA GLU MET VAL VAL PRO TYR GLY ASP          
SEQRES  23 A  638  PRO SER PRO ILE ARG SER TRP GLN ASN TYR PHE ASP THR          
SEQRES  24 A  638  GLY GLU TYR LEU VAL GLY GLN TYR ALA ASN SER LEU GLU          
SEQRES  25 A  638  LEU GLY CYS ASP CYS LEU GLY ASP ILE THR TYR LEU SER          
SEQRES  26 A  638  PRO VAL ILE SER ASP ALA PHE GLY ASN PRO ARG GLU ILE          
SEQRES  27 A  638  ARG ASN GLY ILE CYS MET HIS GLU GLU ASP TRP GLY ILE          
SEQRES  28 A  638  LEU ALA LYS HIS SER ASP LEU TRP SER GLY ILE ASN TYR          
SEQRES  29 A  638  THR ARG ARG ASN ARG ARG MET VAL ILE SER PHE PHE THR          
SEQRES  30 A  638  THR ILE GLY ASN TPQ ASP TYR GLY PHE TYR TRP TYR LEU          
SEQRES  31 A  638  TYR LEU ASP GLY THR ILE GLU PHE GLU ALA LYS ALA THR          
SEQRES  32 A  638  GLY VAL VAL PHE THR SER ALA PHE PRO GLU GLY GLY SER          
SEQRES  33 A  638  ASP ASN ILE SER GLN LEU ALA PRO GLY LEU GLY ALA PRO          
SEQRES  34 A  638  PHE HIS GLN HIS ILE PHE SER ALA ARG LEU ASP MET ALA          
SEQRES  35 A  638  ILE ASP GLY PHE THR ASN ARG VAL GLU GLU GLU ASP VAL          
SEQRES  36 A  638  VAL ARG GLN THR MET GLY PRO GLY ASN GLU ARG GLY ASN          
SEQRES  37 A  638  ALA PHE SER ARG LYS ARG THR VAL LEU THR ARG GLU SER          
SEQRES  38 A  638  GLU ALA VAL ARG GLU ALA ASP ALA ARG THR GLY ARG THR          
SEQRES  39 A  638  TRP ILE ILE SER ASN PRO GLU SER LYS ASN ARG LEU ASN          
SEQRES  40 A  638  GLU PRO VAL GLY TYR LYS LEU HIS ALA HIS ASN GLN PRO          
SEQRES  41 A  638  THR LEU LEU ALA ASP PRO GLY SER SER ILE ALA ARG ARG          
SEQRES  42 A  638  ALA ALA PHE ALA THR LYS ASP LEU TRP VAL THR ARG TYR          
SEQRES  43 A  638  ALA ASP ASP GLU ARG TYR PRO THR GLY ASP PHE VAL ASN          
SEQRES  44 A  638  GLN HIS SER GLY GLY ALA GLY LEU PRO SER TYR ILE ALA          
SEQRES  45 A  638  GLN ASP ARG ASP ILE ASP GLY GLN ASP ILE VAL VAL TRP          
SEQRES  46 A  638  HIS THR PHE GLY LEU THR HIS PHE PRO ARG VAL GLU ASP          
SEQRES  47 A  638  TRP PRO ILE MET PRO VAL ASP THR VAL GLY PHE LYS LEU          
SEQRES  48 A  638  ARG PRO GLU GLY PHE PHE ASP ARG SER PRO VAL LEU ASP          
SEQRES  49 A  638  VAL PRO ALA ASN PRO SER GLN SER GLY SER HIS CYS HIS          
SEQRES  50 A  638  GLY                                                          
MODRES 1AVL TPQ A  382  TYR                                                     
HET    TPQ  A 382      14                                                       
HET     CU  A 639       1                                                       
HETNAM     TPQ 5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE            
HETNAM      CU COPPER (II) ION                                                  
HETSYN     TPQ 5-(2-CARBOXY-2-AMINOETHYL)-4-HYDROXY-1,2-BENZOQUINONE;           
HETSYN   2 TPQ  2,4,5-TRIHYDROXYPHENYLALANINE QUINONE; TOPA QUINONE             
FORMUL   1  TPQ    C9 H9 N O5                                                   
FORMUL   2   CU    CU 2+                                                        
FORMUL   3  HOH   *121(H2 O)                                                    
HELIX    1   1 ALA A   17  THR A   29  1                                  13    
HELIX    2   2 THR A   92  THR A   95  1                                   4    
HELIX    3   3 GLU A  102  THR A  114  1                                  13    
HELIX    4   4 GLU A  116  ARG A  125  1                                  10    
HELIX    5   5 VAL A  129  LYS A  131  5                                   3    
HELIX    6   6 ALA A  145  GLU A  147  5                                   3    
HELIX    7   7 ALA A  167  ALA A  169  5                                   3    
HELIX    8   8 PRO A  207  THR A  210  1                                   4    
HELIX    9   9 ASP A  298  TYR A  302  1                                   5    
HELIX   10  10 VAL A  304  TYR A  307  5                                   4    
HELIX   11  11 GLU A  480  GLU A  482  5                                   3    
HELIX   12  12 ALA A  489  THR A  491  5                                   3    
HELIX   13  13 SER A  529  ARG A  533  1                                   5    
HELIX   14  14 ALA A  535  THR A  538  5                                   4    
HELIX   15  15 LEU A  567  GLN A  573  1                                   7    
HELIX   16  16 VAL A  596  ASP A  598  5                                   3    
SHEET    1   A 4 LYS A  37  VAL A  44  0                                        
SHEET    2   A 4 ARG A  59  ASP A  66 -1  N  HIS A  65   O  ARG A  38           
SHEET    3   A 4 GLN A  73  SER A  78 -1  N  VAL A  77   O  PHE A  60           
SHEET    4   A 4 THR A  83  GLU A  89 -1  N  VAL A  88   O  GLU A  74           
SHEET    1   B 4 VAL A 132  SER A 138  0                                        
SHEET    2   B 4 ILE A 152  VAL A 159 -1  N  PHE A 158   O  ARG A 133           
SHEET    3   B 4 LEU A 175  ASP A 180 -1  N  VAL A 179   O  LEU A 153           
SHEET    4   B 4 GLU A 185  ASP A 191 -1  N  ILE A 190   O  VAL A 176           
SHEET    1   C 4 THR A 231  THR A 233  0                                        
SHEET    2   C 4 HIS A 237  TRP A 240 -1  N  GLU A 239   O  THR A 231           
SHEET    3   C 4 TRP A 243  ASP A 250 -1  N  LEU A 245   O  ILE A 238           
SHEET    4   C 4 GLY A 254  HIS A 258 -1  N  HIS A 258   O  ASP A 246           
SHEET    1   D 5 ASN A 295  PHE A 297  0                                        
SHEET    2   D 5 GLU A 279  PRO A 283 -1  N  VAL A 282   O  TYR A 296           
SHEET    3   D 5 HIS A 431  ASP A 440 -1  N  SER A 436   O  GLU A 279           
SHEET    4   D 5 ILE A 582  HIS A 592 -1  N  HIS A 592   O  HIS A 431           
SHEET    5   D 5 LEU A 541  ARG A 545 -1  N  THR A 544   O  VAL A 583           
SHEET    1   E10 THR A 322  LEU A 324  0                                        
SHEET    2   E10 ILE A 342  ASP A 348 -1  N  MET A 344   O  THR A 322           
SHEET    3   E10 ARG A 369  THR A 377 -1  N  SER A 374   O  CYS A 343           
SHEET    4   E10 TYR A 384  TYR A 391 -1  N  LEU A 390   O  MET A 371           
SHEET    5   E10 ILE A 396  ALA A 402 -1  N  LYS A 401   O  GLY A 385           
SHEET    6   E10 ASP A 605  PRO A 613 -1  N  LEU A 611   O  ILE A 396           
SHEET    7   E10 PRO A 509  ALA A 516 -1  N  HIS A 515   O  LYS A 610           
SHEET    8   E10 THR A 494  LYS A 503 -1  N  SER A 502   O  VAL A 510           
SHEET    9   E10 ARG A 449  ARG A 457 -1  N  GLU A 453   O  THR A 494           
SHEET   10   E10 PHE A 470  LEU A 477 -1  N  LEU A 477   O  VAL A 450           
SHEET    1   F 2 VAL A 327  SER A 329  0                                        
SHEET    2   F 2 PRO A 335  GLU A 337 -1  N  ARG A 336   O  ILE A 328           
SHEET    1   G 3 ILE A 260  ASP A 264  0                                        
SHEET    2   G 3 ARG A 267  ILE A 277 -1  N  ILE A 272   O  ILE A 260           
SHEET    3   G 3 ALA A 437  MET A 441 -1  N  ASP A 440   O  ASN A 273           
SHEET    1   H 2 ILE A 351  SER A 356  0                                        
SHEET    2   H 2 ASN A 363  ARG A 367 -1  N  ARG A 366   O  LEU A 352           
SHEET    1   I 2 ILE A 419  ALA A 423  0                                        
SHEET    2   I 2 LEU A 426  PRO A 429 -1  N  ALA A 428   O  SER A 420           
SSBOND   1 CYS A  317    CYS A  343                          1555   1555  2.02  
LINK         N   TPQ A 382                 C   ASN A 381     1555   1555  1.33  
LINK         C   TPQ A 382                 N   ASP A 383     1555   1555  1.35  
LINK        CU    CU A 639                 ND1AHIS A 592     1555   1555  2.27  
LINK        CU    CU A 639                 O4  TPQ A 382     1555   1555  2.44  
LINK        CU    CU A 639                 NE2 HIS A 433     1555   1555  2.13  
LINK        CU    CU A 639                 NE2 HIS A 431     1555   1555  2.02  
CISPEP   1 TRP A  599    PRO A  600          0        -0.06                     
SITE     1 AC1  4 TPQ A 382  HIS A 431  HIS A 433  HIS A 592                    
CRYST1  158.200   64.100   92.900  90.00 112.70  90.00 C 1 2 1       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      0.006321  0.000000  0.002644        0.00000                         
SCALE2      0.000000  0.015601  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011668        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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