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Database: PDB
Entry: 6N13
LinkDB: 6N13
Original site: 6N13 
HEADER    LIGASE                                  08-NOV-18   6N13              
TITLE     UBCH7-UB COMPLEX WITH R0RBR PARKIN AND PHOSPHOUBIQUITIN               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE PARKIN;                        
COMPND   3 CHAIN: B;                                                            
COMPND   4 SYNONYM: PARKIN,PARKIN RBR E3 UBIQUITIN-PROTEIN LIGASE,PARKINSON     
COMPND   5 JUVENILE DISEASE PROTEIN 2,PARKINSON DISEASE PROTEIN 2;              
COMPND   6 EC: 2.3.2.31;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: UBIQUITIN;                                                 
COMPND  11 CHAIN: D;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 L3;                        
COMPND  15 CHAIN: C;                                                            
COMPND  16 SYNONYM: E2 UBIQUITIN-CONJUGATING ENZYME L3,L-UBC,UBCH7,UBIQUITIN    
COMPND  17 CARRIER PROTEIN L3,UBIQUITIN-CONJUGATING ENZYME E2-F1,UBIQUITIN-     
COMPND  18 PROTEIN LIGASE L3;                                                   
COMPND  19 EC: 2.3.2.23;                                                        
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MUTATION: YES;                                                       
COMPND  22 OTHER_DETAILS: GH RESIDUES AT N-TERMINUS WERE USED IN THE EXPRESSION 
COMPND  23 CONSTRUCT BUT WERE NOT INCLUDED IN THE X-RAY COORDINATES;            
COMPND  24 MOL_ID: 4;                                                           
COMPND  25 MOLECULE: PHOSPHOUBIQUITIN;                                          
COMPND  26 CHAIN: A;                                                            
COMPND  27 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRKN, PARK2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: UBB;                                                           
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: UBE2L3, UBCE7, UBCH7;                                          
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: UBC;                                                           
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    E3 ENZYME, PROTEIN DEGRADATION, MITOCHONDRIAL PROTEIN, LIGASE         
EXPDTA    SOLUTION NMR                                                          
NUMMDL    10                                                                    
AUTHOR    T.E.C.CONDOS,K.M.DUNKERLEY,E.A.FREEMAN,K.R.BARBER,J.D.AGUIRRE,        
AUTHOR   2 V.K.CHAUGULE,Y.XIAO,L.KONERMANN,H.WALDEN,G.S.SHAW                    
REVDAT   3   08-JAN-20 6N13    1       REMARK SEQADV                            
REVDAT   2   12-DEC-18 6N13    1       JRNL                                     
REVDAT   1   28-NOV-18 6N13    0                                                
JRNL        AUTH   T.E.CONDOS,K.M.DUNKERLEY,E.A.FREEMAN,K.R.BARBER,J.D.AGUIRRE, 
JRNL        AUTH 2 V.K.CHAUGULE,Y.XIAO,L.KONERMANN,H.WALDEN,G.S.SHAW            
JRNL        TITL   SYNERGISTIC RECRUITMENT OF UBCH7~UB AND PHOSPHORYLATED UBL   
JRNL        TITL 2 DOMAIN TRIGGERS PARKIN ACTIVATION.                           
JRNL        REF    EMBO J.                       V.  37       2018              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   30446597                                                     
JRNL        DOI    10.15252/EMBJ.2018100014                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.KUMAR,V.K.CHAUGULE,T.E.C.CONDOS,K.R.BARBER,C.JOHNSON,      
REMARK   1  AUTH 2 R.TOTH,R.SUNDARAMOORTHY,A.KNEBEL,G.S.SHAW,H.WALDEN           
REMARK   1  TITL   PARKIN-PHOSPHOUBIQUITIN COMPLEX REVEALS CRYPTIC              
REMARK   1  TITL 2 UBIQUITIN-BINDING SITE REQUIRED FOR RBR LIGASE ACTIVITY.     
REMARK   1  REF    NAT. STRUCT. MOL. BIOL.       V.  24   475 2017              
REMARK   1  REFN                   ESSN 1545-9985                               
REMARK   1  PMID   28414322                                                     
REMARK   1  DOI    10.1038/NSMB.3400                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : HADDOCK                                              
REMARK   3   AUTHORS     : BONVIN                                               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6N13 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237885.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 7                                  
REMARK 210  IONIC STRENGTH                 : 50                                 
REMARK 210  PRESSURE                       : AMBIENT ATM                        
REMARK 210  SAMPLE CONTENTS                : 0.11 MM [U-13C; U-15N; U-2H]       
REMARK 210                                   UBCH7, 0.11 MM [U-13C; U-15N; U-   
REMARK 210                                   2H] UBIQUITIN, 0.11 MM [U-2H]      
REMARK 210                                   PARKIN -RESIDUES 144-465           
REMARK 210                                   COMPRISING THE RING0-RING1-IBR     
REMARK 210                                   AND RING2(RCAT) DOMAINS, 0.11 MM   
REMARK 210                                   [U-2H] PHOSPHORYLATED UBIQUITIN,   
REMARK 210                                   90% H2O/10% D2O                    
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC                     
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ                            
REMARK 210  SPECTROMETER MODEL             : INOVA                              
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NMRVIEW, NMRPIPE, PYMOL 2.0.0      
REMARK 210   METHOD USED                   : SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 1000                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 10                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST         
REMARK 210                                   ENERGY                             
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, C, A                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465   MODELS 1-10                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     GLY C   499                                                      
REMARK 465     HIS C   500                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
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   C    GLY D   776     CE   LYS C   586              2.08            
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  2 CYS B 436   CB    CYS B 436   SG     -0.118                       
REMARK 500  2 GLY D 776   C     GLY D 776   O       0.108                       
REMARK 500  6 GLY D 776   C     GLY D 776   O       0.105                       
REMARK 500  7 GLY D 776   C     GLY D 776   O       0.104                       
REMARK 500  8 GLY D 776   C     GLY D 776   O       0.102                       
REMARK 500  9 CYS B 436   CB    CYS B 436   SG     -0.103                       
REMARK 500 10 GLY D 776   C     GLY D 776   O       0.098                       
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  1 ARG B 156   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  1 ARG B 163   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500  1 CYS B 169   CA  -  CB  -  SG  ANGL. DEV. =   7.8 DEGREES          
REMARK 500  1 ARG B 170   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  1 ARG B 191   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500  1 ARG B 234   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500  1 CYS B 238   CA  -  CB  -  SG  ANGL. DEV. =   7.3 DEGREES          
REMARK 500  1 ARG B 245   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  1 ARG B 256   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500  1 ARG B 271   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  1 ARG B 275   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  1 ARG B 305   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  1 ARG B 314   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  1 ARG B 334   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  1 ARG B 348   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  1 ARG B 366   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  1 ARG B 392   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  1 ARG B 396   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500  1 ARG B 402   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  1 ARG B 420   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  1 CYS B 421   N   -  CA  -  CB  ANGL. DEV. =  13.2 DEGREES          
REMARK 500  1 CYS B 421   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES          
REMARK 500  1 ARG B 442   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  1 ARG B 455   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  1 ARG D 742   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  1 ARG D 754   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  1 ARG D 772   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  1 ARG D 772   O   -  C   -  N   ANGL. DEV. =  12.5 DEGREES          
REMARK 500  1 ARG D 774   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500  1 ARG C 505   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  1 ARG C 506   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500  1 ARG C 515   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  1 ARG C 523   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  1 ARG C 552   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  1 ARG C 622   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500  1 ARG C 633   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500  1 ARG C 651   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500  1 ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  1 ARG A  54   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500  1 ARG A  72   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500  1 ARG A  74   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500  2 ARG B 156   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  2 ARG B 163   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  2 CYS B 169   CA  -  CB  -  SG  ANGL. DEV. =   9.7 DEGREES          
REMARK 500  2 ARG B 170   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  2 ARG B 191   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500  2 ARG B 234   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500  2 ARG B 245   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  2 ARG B 256   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500  2 ARG B 271   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     413 ANGLE DEVIATIONS.                             
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  1 PRO B 153       49.68    -96.38                                   
REMARK 500  1 THR B 168      -60.60    -91.04                                   
REMARK 500  1 CYS B 201       93.53   -171.07                                   
REMARK 500  1 ALA B 214      -58.72   -145.89                                   
REMARK 500  1 ASN B 235       60.52     69.94                                   
REMARK 500  1 ARG B 256      109.54     74.18                                   
REMARK 500  1 ARG B 275       79.93     60.99                                   
REMARK 500  1 TYR B 285       78.97   -113.68                                   
REMARK 500  1 LYS B 299       57.97   -101.38                                   
REMARK 500  1 GLU B 300      103.67   -168.03                                   
REMARK 500  1 PRO B 333       30.82    -89.87                                   
REMARK 500  1 CYS B 337      -68.18   -127.84                                   
REMARK 500  1 CYS B 352       89.93    -65.75                                   
REMARK 500  1 LEU B 358      -78.16     67.87                                   
REMARK 500  1 CYS B 360       56.69   -177.25                                   
REMARK 500  1 PHE B 362      107.19   -161.71                                   
REMARK 500  1 LYS B 369       64.38     63.16                                   
REMARK 500  1 THR B 387      -71.19     69.46                                   
REMARK 500  1 ALA B 401       63.66   -105.62                                   
REMARK 500  1 ALA B 405      -79.74   -117.59                                   
REMARK 500  1 ALA B 406      -75.41     54.95                                   
REMARK 500  1 LYS B 408       77.05     68.73                                   
REMARK 500  1 LYS B 413       58.99   -152.15                                   
REMARK 500  1 THR B 414      -57.49   -137.91                                   
REMARK 500  1 CYS B 421      -55.58    128.32                                   
REMARK 500  1 HIS B 422       63.02     65.54                                   
REMARK 500  1 CYS B 441      -78.77    -78.04                                   
REMARK 500  1 ARG B 442       87.85     52.14                                   
REMARK 500  1 THR D 709       57.23   -107.63                                   
REMARK 500  1 PRO D 738      -32.81    -39.82                                   
REMARK 500  1 GLN D 740       57.73   -103.88                                   
REMARK 500  1 ASN D 760       85.59     72.75                                   
REMARK 500  1 LYS C 520      -66.31     70.52                                   
REMARK 500  1 PRO C 545       45.95    -97.37                                   
REMARK 500  1 PRO C 562       40.16    -97.69                                   
REMARK 500  1 LYS C 571       54.50   -109.81                                   
REMARK 500  1 LEU C 621      -60.91   -109.23                                   
REMARK 500  1 ASN A  60       86.29     71.48                                   
REMARK 500  2 PRO B 153       46.76    -99.13                                   
REMARK 500  2 THR B 173       57.04   -146.87                                   
REMARK 500  2 CYS B 201      108.32   -168.63                                   
REMARK 500  2 PRO B 202       45.42    -97.36                                   
REMARK 500  2 ARG B 256       88.32     68.32                                   
REMARK 500  2 GLN B 282       55.48   -108.86                                   
REMARK 500  2 LEU B 283      -58.47   -160.11                                   
REMARK 500  2 PRO B 333       74.07    -63.02                                   
REMARK 500  2 PRO B 335      105.10    -47.01                                   
REMARK 500  2 LEU B 358      -63.79     73.81                                   
REMARK 500  2 LYS B 369       61.19     60.56                                   
REMARK 500  2 CYS B 377      -80.54    -98.01                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     365 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY B  152     PRO B  153          1       -41.61                    
REMARK 500 GLY B  179     PRO B  180          1      -112.39                    
REMARK 500 SER B  198     PRO B  199          1      -124.45                    
REMARK 500 CYS B  436     PRO B  437          1      -145.95                    
REMARK 500 LEU D  773     ARG D  774          1       145.32                    
REMARK 500 GLU A   18     PRO A   19          1       147.70                    
REMARK 500 SER B  246     PRO B  247          4       -30.08                    
REMARK 500 SER B  246     PRO B  247          7       -33.61                    
REMARK 500 LEU B  358     GLY B  359          7       143.53                    
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  1 TYR B 147         0.10    SIDE CHAIN                              
REMARK 500  1 TYR C 546         0.08    SIDE CHAIN                              
REMARK 500  2 TYR B 285         0.10    SIDE CHAIN                              
REMARK 500  2 TYR B 315         0.12    SIDE CHAIN                              
REMARK 500  2 ARG D 754         0.08    SIDE CHAIN                              
REMARK 500  2 ARG C 505         0.08    SIDE CHAIN                              
REMARK 500  2 ARG C 506         0.09    SIDE CHAIN                              
REMARK 500  3 TYR B 285         0.10    SIDE CHAIN                              
REMARK 500  3 TYR B 315         0.13    SIDE CHAIN                              
REMARK 500  3 ARG B 334         0.09    SIDE CHAIN                              
REMARK 500  3 ARG B 348         0.09    SIDE CHAIN                              
REMARK 500  3 ARG B 392         0.08    SIDE CHAIN                              
REMARK 500  3 ARG D 754         0.09    SIDE CHAIN                              
REMARK 500  3 ARG C 506         0.08    SIDE CHAIN                              
REMARK 500  4 TYR B 285         0.10    SIDE CHAIN                              
REMARK 500  4 TYR B 315         0.11    SIDE CHAIN                              
REMARK 500  4 ARG D 742         0.09    SIDE CHAIN                              
REMARK 500  4 ARG D 754         0.09    SIDE CHAIN                              
REMARK 500  4 ARG C 506         0.09    SIDE CHAIN                              
REMARK 500  4 ARG C 651         0.08    SIDE CHAIN                              
REMARK 500  5 TYR B 285         0.09    SIDE CHAIN                              
REMARK 500  5 TYR B 315         0.11    SIDE CHAIN                              
REMARK 500  5 ARG B 334         0.08    SIDE CHAIN                              
REMARK 500  5 ARG C 505         0.08    SIDE CHAIN                              
REMARK 500  5 ARG C 506         0.08    SIDE CHAIN                              
REMARK 500  5 ARG C 523         0.09    SIDE CHAIN                              
REMARK 500  6 TYR B 285         0.09    SIDE CHAIN                              
REMARK 500  6 TYR B 315         0.13    SIDE CHAIN                              
REMARK 500  6 ARG B 348         0.08    SIDE CHAIN                              
REMARK 500  6 ARG D 754         0.08    SIDE CHAIN                              
REMARK 500  6 ARG C 506         0.08    SIDE CHAIN                              
REMARK 500  7 TYR B 285         0.10    SIDE CHAIN                              
REMARK 500  7 TYR B 315         0.12    SIDE CHAIN                              
REMARK 500  7 TYR B 318         0.09    SIDE CHAIN                              
REMARK 500  7 ARG B 392         0.08    SIDE CHAIN                              
REMARK 500  7 ARG D 754         0.07    SIDE CHAIN                              
REMARK 500  7 ARG C 506         0.08    SIDE CHAIN                              
REMARK 500  7 ARG C 523         0.09    SIDE CHAIN                              
REMARK 500  8 TYR B 285         0.09    SIDE CHAIN                              
REMARK 500  8 TYR B 315         0.11    SIDE CHAIN                              
REMARK 500  8 ARG B 392         0.08    SIDE CHAIN                              
REMARK 500  8 ARG D 754         0.07    SIDE CHAIN                              
REMARK 500  8 ARG C 506         0.08    SIDE CHAIN                              
REMARK 500  9 TYR B 285         0.07    SIDE CHAIN                              
REMARK 500  9 TYR B 315         0.10    SIDE CHAIN                              
REMARK 500  9 TYR B 318         0.08    SIDE CHAIN                              
REMARK 500  9 ARG D 754         0.08    SIDE CHAIN                              
REMARK 500  9 ARG C 506         0.08    SIDE CHAIN                              
REMARK 500 10 TYR B 285         0.10    SIDE CHAIN                              
REMARK 500 10 TYR B 315         0.11    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 PLANE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 508  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 150   SG                                                     
REMARK 620 2 CYS B 154   SG  103.7                                              
REMARK 620 3 CYS B 212   SG  110.9 121.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 166   SG                                                     
REMARK 620 2 CYS B 169   SG  101.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 505  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 238   SG                                                     
REMARK 620 2 CYS B 260   SG  101.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 253   SG                                                     
REMARK 620 2 HIS B 257   ND1 112.5                                              
REMARK 620 3 CYS B 289   SG  108.6 107.4                                        
REMARK 620 4 CYS B 293   SG  115.3 109.3 103.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 506  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 352   SG                                                     
REMARK 620 2 LEU B 358   O   104.4                                              
REMARK 620 3 CYS B 360   SG  107.2 107.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 449   SG                                                     
REMARK 620 2 CYS B 457   SG  117.6                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 508                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 27664   RELATED DB: BMRB                                 
REMARK 900 RELATED ID: 5N2W   RELATED DB: PDB                                   
REMARK 900 PARKIN+PHOSPHOUBIQUITIN                                              
REMARK 900 RELATED ID: 4Q5E   RELATED DB: PDB                                   
REMARK 900 UBCH7                                                                
REMARK 900 RELATED ID: 1UBQ   RELATED DB: PDB                                   
REMARK 900 UBIQUITIN                                                            
DBREF  6N13 A    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
DBREF  6N13 B  144   465  UNP    O60260   PRKN_HUMAN     144    465             
DBREF  6N13 C  501   654  UNP    P68036   UB2L3_HUMAN      1    154             
DBREF  6N13 D  701   776  UNP    P0CG47   UBB_HUMAN        1     76             
SEQADV 6N13 CYS B  347  UNP  O60260    GLN   347 ENGINEERED MUTATION            
SEQADV 6N13 GLY C  499  UNP  P68036              EXPRESSION TAG                 
SEQADV 6N13 HIS C  500  UNP  P68036              EXPRESSION TAG                 
SEQADV 6N13 SER C  517  UNP  P68036    CYS    17 ENGINEERED MUTATION            
SEQADV 6N13 LYS C  586  UNP  P68036    CYS    86 ENGINEERED MUTATION            
SEQADV 6N13 SER C  637  UNP  P68036    CYS   137 ENGINEERED MUTATION            
SEQRES   1 B  322  ASN SER PHE TYR VAL TYR CYS LYS GLY PRO CYS GLN ARG          
SEQRES   2 B  322  VAL GLN PRO GLY LYS LEU ARG VAL GLN CYS SER THR CYS          
SEQRES   3 B  322  ARG GLN ALA THR LEU THR LEU THR GLN GLY PRO SER CYS          
SEQRES   4 B  322  TRP ASP ASP VAL LEU ILE PRO ASN ARG MET SER GLY GLU          
SEQRES   5 B  322  CYS GLN SER PRO HIS CYS PRO GLY THR SER ALA GLU PHE          
SEQRES   6 B  322  PHE PHE LYS CYS GLY ALA HIS PRO THR SER ASP LYS GLU          
SEQRES   7 B  322  THR SER VAL ALA LEU HIS LEU ILE ALA THR ASN SER ARG          
SEQRES   8 B  322  ASN ILE THR CYS ILE THR CYS THR ASP VAL ARG SER PRO          
SEQRES   9 B  322  VAL LEU VAL PHE GLN CYS ASN SER ARG HIS VAL ILE CYS          
SEQRES  10 B  322  LEU ASP CYS PHE HIS LEU TYR CYS VAL THR ARG LEU ASN          
SEQRES  11 B  322  ASP ARG GLN PHE VAL HIS ASP PRO GLN LEU GLY TYR SER          
SEQRES  12 B  322  LEU PRO CYS VAL ALA GLY CYS PRO ASN SER LEU ILE LYS          
SEQRES  13 B  322  GLU LEU HIS HIS PHE ARG ILE LEU GLY GLU GLU GLN TYR          
SEQRES  14 B  322  ASN ARG TYR GLN GLN TYR GLY ALA GLU GLU CYS VAL LEU          
SEQRES  15 B  322  GLN MET GLY GLY VAL LEU CYS PRO ARG PRO GLY CYS GLY          
SEQRES  16 B  322  ALA GLY LEU LEU PRO GLU PRO ASP CYS ARG LYS VAL THR          
SEQRES  17 B  322  CYS GLU GLY GLY ASN GLY LEU GLY CYS GLY PHE ALA PHE          
SEQRES  18 B  322  CYS ARG GLU CYS LYS GLU ALA TYR HIS GLU GLY GLU CYS          
SEQRES  19 B  322  SER ALA VAL PHE GLU ALA SER GLY THR THR THR GLN ALA          
SEQRES  20 B  322  TYR ARG VAL ASP GLU ARG ALA ALA GLU GLN ALA ARG TRP          
SEQRES  21 B  322  GLU ALA ALA SER LYS GLU THR ILE LYS LYS THR THR LYS          
SEQRES  22 B  322  PRO CYS PRO ARG CYS HIS VAL PRO VAL GLU LYS ASN GLY          
SEQRES  23 B  322  GLY CYS MET HIS MET LYS CYS PRO GLN PRO GLN CYS ARG          
SEQRES  24 B  322  LEU GLU TRP CYS TRP ASN CYS GLY CYS GLU TRP ASN ARG          
SEQRES  25 B  322  VAL CYS MET GLY ASP HIS TRP PHE ASP VAL                      
SEQRES   1 D   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 D   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 D   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 D   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 D   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 D   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 C  156  GLY HIS MET ALA ALA SER ARG ARG LEU MET LYS GLU LEU          
SEQRES   2 C  156  GLU GLU ILE ARG LYS SER GLY MET LYS ASN PHE ARG ASN          
SEQRES   3 C  156  ILE GLN VAL ASP GLU ALA ASN LEU LEU THR TRP GLN GLY          
SEQRES   4 C  156  LEU ILE VAL PRO ASP ASN PRO PRO TYR ASP LYS GLY ALA          
SEQRES   5 C  156  PHE ARG ILE GLU ILE ASN PHE PRO ALA GLU TYR PRO PHE          
SEQRES   6 C  156  LYS PRO PRO LYS ILE THR PHE LYS THR LYS ILE TYR HIS          
SEQRES   7 C  156  PRO ASN ILE ASP GLU LYS GLY GLN VAL LYS LEU PRO VAL          
SEQRES   8 C  156  ILE SER ALA GLU ASN TRP LYS PRO ALA THR LYS THR ASP          
SEQRES   9 C  156  GLN VAL ILE GLN SER LEU ILE ALA LEU VAL ASN ASP PRO          
SEQRES  10 C  156  GLN PRO GLU HIS PRO LEU ARG ALA ASP LEU ALA GLU GLU          
SEQRES  11 C  156  TYR SER LYS ASP ARG LYS LYS PHE SER LYS ASN ALA GLU          
SEQRES  12 C  156  GLU PHE THR LYS LYS TYR GLY GLU LYS ARG PRO VAL ASP          
SEQRES   1 A   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 A   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 A   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 A   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 A   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SEP          
SEQRES   6 A   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
MODRES 6N13 SEP A   65  SER  MODIFIED RESIDUE                                   
HET    SEP  A  65      11                                                       
HET     ZN  B 501       1                                                       
HET     ZN  B 502       1                                                       
HET     ZN  B 503       1                                                       
HET     ZN  B 504       1                                                       
HET     ZN  B 505       1                                                       
HET     ZN  B 506       1                                                       
HET     ZN  B 507       1                                                       
HET     ZN  B 508       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM      ZN ZINC ION                                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   4  SEP    C3 H8 N O6 P                                                 
FORMUL   5   ZN    8(ZN 2+)                                                     
HELIX    1 AA1 CYS B  182  ILE B  188  1                                   7    
HELIX    2 AA2 LEU B  261  ARG B  275  1                                  15    
HELIX    3 AA3 GLU B  300  LEU B  307  5                                   8    
HELIX    4 AA4 GLY B  308  GLY B  328  1                                  21    
HELIX    5 AA5 ASP B  394  ALA B  401  1                                   8    
HELIX    6 AA6 ASN B  454  HIS B  461  1                                   8    
HELIX    7 AA7 THR D  722  GLU D  734  1                                  13    
HELIX    8 AA8 PRO D  737  ASP D  739  5                                   3    
HELIX    9 AA9 THR D  755  ASN D  760  1                                   6    
HELIX   10 AB1 ALA C  502  GLY C  518  1                                  17    
HELIX   11 AB2 LYS C  600  ASP C  614  1                                  15    
HELIX   12 AB3 ARG C  622  ASP C  632  1                                  11    
HELIX   13 AB4 ASP C  632  GLY C  648  1                                  17    
HELIX   14 AB5 THR A   22  GLU A   34  1                                  13    
HELIX   15 AB6 THR A   55  ASN A   60  1                                   6    
SHEET    1 AA1 4 ALA B 206  CYS B 212  0                                        
SHEET    2 AA1 4 VAL B 157  CYS B 166 -1  N  GLN B 165   O  GLU B 207           
SHEET    3 AA1 4 TYR B 147  TYR B 149 -1  N  VAL B 148   O  GLN B 158           
SHEET    4 AA1 4 VAL B 224  LEU B 226 -1  O  LEU B 226   N  TYR B 147           
SHEET    1 AA2 2 LEU B 174  LEU B 176  0                                        
SHEET    2 AA2 2 GLY B 194  CYS B 196 -1  O  GLU B 195   N  THR B 175           
SHEET    1 AA3 2 VAL B 248  VAL B 250  0                                        
SHEET    2 AA3 2 VAL B 258  CYS B 260 -1  O  ILE B 259   N  LEU B 249           
SHEET    1 AA4 2 VAL B 278  HIS B 279  0                                        
SHEET    2 AA4 2 TYR B 285  SER B 286 -1  O  SER B 286   N  VAL B 278           
SHEET    1 AA5 2 VAL B 350  THR B 351  0                                        
SHEET    2 AA5 2 ALA B 363  PHE B 364 -1  O  PHE B 364   N  VAL B 350           
SHEET    1 AA6 2 THR B 415  PRO B 417  0                                        
SHEET    2 AA6 2 PRO B 424  GLU B 426 -1  O  VAL B 425   N  LYS B 416           
SHEET    1 AA7 2 HIS B 433  LYS B 435  0                                        
SHEET    2 AA7 2 GLU B 444  CYS B 446 -1  O  TRP B 445   N  MET B 434           
SHEET    1 AA8 4 ILE D 713  GLU D 716  0                                        
SHEET    2 AA8 4 GLN D 702  LYS D 706 -1  N  VAL D 705   O  ILE D 713           
SHEET    3 AA8 4 THR D 766  LEU D 771  1  O  LEU D 767   N  LYS D 706           
SHEET    4 AA8 4 GLN D 741  ILE D 744 -1  N  ARG D 742   O  VAL D 770           
SHEET    1 AA9 4 PHE C 522  VAL C 527  0                                        
SHEET    2 AA9 4 THR C 534  ILE C 539 -1  O  LEU C 538   N  ARG C 523           
SHEET    3 AA9 4 PHE C 551  ASN C 556 -1  O  ILE C 553   N  GLY C 537           
SHEET    4 AA9 4 LYS C 567  PHE C 570 -1  O  THR C 569   N  GLU C 554           
SHEET    1 AB1 5 THR A  12  GLU A  16  0                                        
SHEET    2 AB1 5 GLN A   2  LYS A   6 -1  N  VAL A   5   O  ILE A  13           
SHEET    3 AB1 5 THR A  66  LEU A  71  1  N  LEU A  67   O  LYS A   6           
SHEET    4 AB1 5 GLN A  41  PHE A  45 -1  N  ARG A  42   O  VAL A  70           
SHEET    5 AB1 5 LYS A  48  GLN A  49 -1  O  LYS A  48   N  PHE A  45           
LINK         SG  CYS B 150                ZN    ZN B 508     1555   1555  1.92  
LINK         SG  CYS B 154                ZN    ZN B 508     1555   1555  1.96  
LINK         SG  CYS B 166                ZN    ZN B 504     1555   1555  1.96  
LINK         SG  CYS B 169                ZN    ZN B 504     1555   1555  1.98  
LINK         SG  CYS B 212                ZN    ZN B 508     1555   1555  1.92  
LINK         SG  CYS B 238                ZN    ZN B 505     1555   1555  2.00  
LINK         SG  CYS B 253                ZN    ZN B 501     1555   1555  1.97  
LINK         ND1 HIS B 257                ZN    ZN B 501     1555   1555  1.77  
LINK         SG  CYS B 260                ZN    ZN B 505     1555   1555  1.95  
LINK         SG  CYS B 289                ZN    ZN B 501     1555   1555  1.98  
LINK         SG  CYS B 293                ZN    ZN B 501     1555   1555  1.94  
LINK         SG  CYS B 352                ZN    ZN B 506     1555   1555  1.90  
LINK         O   LEU B 358                ZN    ZN B 506     1555   1555  1.71  
LINK         SG  CYS B 360                ZN    ZN B 506     1555   1555  1.95  
LINK         SG  CYS B 377                ZN    ZN B 502     1555   1555  1.94  
LINK         SG  CYS B 421                ZN    ZN B 507     1555   1555  1.90  
LINK         SG  CYS B 449                ZN    ZN B 503     1555   1555  1.93  
LINK         SG  CYS B 457                ZN    ZN B 503     1555   1555  1.97  
LINK         C   GLY D 776                 NZ  LYS C 586     1555   1555  1.40  
LINK         C   GLU A  64                 N   SEP A  65     1555   1555  1.32  
LINK         C   SEP A  65                 N   THR A  66     1555   1555  1.32  
CISPEP   1 SER B  246    PRO B  247          1       -15.31                     
CISPEP   2 PRO C  544    PRO C  545          1       -15.58                     
CISPEP   3 TYR C  561    PRO C  562          1         3.45                     
CISPEP   4 GLY B  152    PRO B  153          2       -20.39                     
CISPEP   5 SER B  246    PRO B  247          2        -4.98                     
CISPEP   6 PRO C  544    PRO C  545          2       -14.14                     
CISPEP   7 TYR C  561    PRO C  562          2        -2.06                     
CISPEP   8 GLY B  152    PRO B  153          3        -9.50                     
CISPEP   9 SER B  246    PRO B  247          3        -7.39                     
CISPEP  10 PRO C  544    PRO C  545          3       -11.99                     
CISPEP  11 TYR C  561    PRO C  562          3        -4.49                     
CISPEP  12 GLY B  152    PRO B  153          4        -9.27                     
CISPEP  13 PRO C  544    PRO C  545          4        -8.29                     
CISPEP  14 TYR C  561    PRO C  562          4        -6.70                     
CISPEP  15 GLY B  152    PRO B  153          5       -14.33                     
CISPEP  16 SER B  246    PRO B  247          5        -5.01                     
CISPEP  17 PRO C  544    PRO C  545          5       -16.96                     
CISPEP  18 TYR C  561    PRO C  562          5        -5.80                     
CISPEP  19 GLY B  152    PRO B  153          6        -9.14                     
CISPEP  20 SER B  246    PRO B  247          6        -3.52                     
CISPEP  21 PRO C  544    PRO C  545          6        -9.22                     
CISPEP  22 TYR C  561    PRO C  562          6        -5.62                     
CISPEP  23 GLY B  152    PRO B  153          7       -18.88                     
CISPEP  24 PRO C  544    PRO C  545          7       -19.01                     
CISPEP  25 TYR C  561    PRO C  562          7        -2.83                     
CISPEP  26 GLY B  152    PRO B  153          8       -10.58                     
CISPEP  27 SER B  246    PRO B  247          8       -29.64                     
CISPEP  28 PRO C  544    PRO C  545          8       -19.80                     
CISPEP  29 TYR C  561    PRO C  562          8        -4.95                     
CISPEP  30 GLY B  152    PRO B  153          9       -23.03                     
CISPEP  31 SER B  246    PRO B  247          9        -3.68                     
CISPEP  32 PRO C  544    PRO C  545          9       -16.76                     
CISPEP  33 TYR C  561    PRO C  562          9         0.96                     
CISPEP  34 GLY B  152    PRO B  153         10       -10.49                     
CISPEP  35 SER B  246    PRO B  247         10        -4.59                     
CISPEP  36 PRO C  544    PRO C  545         10       -13.98                     
CISPEP  37 TYR C  561    PRO C  562         10        -1.17                     
SITE     1 AC1  4 CYS B 253  HIS B 257  CYS B 289  CYS B 293                    
SITE     1 AC2  3 GLU B 370  HIS B 373  CYS B 377                               
SITE     1 AC3  2 CYS B 449  CYS B 457                                          
SITE     1 AC4  4 CYS B 166  CYS B 169  CYS B 196  CYS B 201                    
SITE     1 AC5  4 CYS B 238  CYS B 241  CYS B 260  CYS B 263                    
SITE     1 AC6  5 CYS B 337  CYS B 352  LEU B 358  GLY B 359                    
SITE     2 AC6  5 CYS B 360                                                     
SITE     1 AC7  4 CYS B 418  ARG B 420  CYS B 421  CYS B 436                    
SITE     1 AC8  4 CYS B 150  CYS B 154  CYS B 212  HIS B 215                    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system