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Database: PDB
Entry: 5K1C
LinkDB: 5K1C
Original site: 5K1C 
HEADER    HYDROLASE                               18-MAY-16   5K1C              
TITLE     CRYSTAL STRUCTURE OF THE UAF1/WDR20/USP12 COMPLEX                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 12;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 16-370;                                           
COMPND   5 SYNONYM: DEUBIQUITINATING ENZYME 12,UBIQUITIN THIOESTERASE 12,       
COMPND   6 UBIQUITIN-HYDROLYZING ENZYME 1,UBIQUITIN-SPECIFIC-PROCESSING PROTEASE
COMPND   7 12;                                                                  
COMPND   8 EC: 3.4.19.12;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: WD REPEAT-CONTAINING PROTEIN 48;                           
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: RESIDUES 1-563;                                            
COMPND  14 SYNONYM: USP1-ASSOCIATED FACTOR 1,WD REPEAT ENDOSOMAL PROTEIN,P80;   
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: WD REPEAT-CONTAINING PROTEIN 20;                           
COMPND  18 CHAIN: C;                                                            
COMPND  19 SYNONYM: PROTEIN DMR;                                                
COMPND  20 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: USP12, UBH1, USP12L1;                                          
SOURCE   6 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM;       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 274590;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: WDR48, KIAA1449, UAF1;                                         
SOURCE  13 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM;       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 274590;                                     
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: WDR20;                                                         
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 83333                                       
KEYWDS    WD40 REPEAT DOMAIN, WDR20, USP12, UAF1, WDR48, DEUBIQUITINATING       
KEYWDS   2 ENZYME, UBIQUITIN-SPECIFIC PROTEASE, USP1-ASSOCIATED FACTOR 1,       
KEYWDS   3 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,A.D.D'ANDREA,N.ZHENG                                             
REVDAT   2   10-AUG-16 5K1C    1       JRNL                                     
REVDAT   1   20-JUL-16 5K1C    0                                                
JRNL        AUTH   H.LI,K.S.LIM,H.KIM,T.R.HINDS,U.JO,H.MAO,C.E.WELLER,J.SUN,    
JRNL        AUTH 2 C.CHATTERJEE,A.D.D'ANDREA,N.ZHENG                            
JRNL        TITL   ALLOSTERIC ACTIVATION OF UBIQUITIN-SPECIFIC PROTEASES BY     
JRNL        TITL 2 BETA-PROPELLER PROTEINS UAF1 AND WDR20.                      
JRNL        REF    MOL.CELL                      V.  63   249 2016              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   27373336                                                     
JRNL        DOI    10.1016/J.MOLCEL.2016.05.031                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0131                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 58534                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3014                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4263                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.46                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 209                          
REMARK   3   BIN FREE R VALUE                    : 0.4080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9541                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 17                                      
REMARK   3   SOLVENT ATOMS            : 75                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 97.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.17000                                             
REMARK   3    B22 (A**2) : -0.17000                                             
REMARK   3    B33 (A**2) : 0.55000                                              
REMARK   3    B12 (A**2) : -0.09000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.492         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.338         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.923                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9779 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9054 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13291 ; 1.737 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20776 ; 3.832 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1212 ; 8.651 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   444 ;37.818 ;24.009       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1572 ;17.288 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    56 ;16.421 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1504 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11081 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2299 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4885 ; 6.633 ; 9.901       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4883 ; 6.630 ; 9.900       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6084 ;10.259 ;14.821       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  6085 ;10.258 ;14.822       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4894 ; 7.166 ;10.186       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4894 ; 7.165 ;10.186       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  7208 ;11.188 ;15.151       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10639 ;15.640 ;77.888       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 10640 ;15.639 ;77.889       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5K1C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221579.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58534                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 11.30                              
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : 0.10900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5K16, 5K19 AND 5K1A                                  
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, 1.3 M AMMONIUM PHOSPHATE      
REMARK 280  DIBASIC, PH 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  277.0K                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.60633            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      149.21267            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      111.90950            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      186.51583            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       37.30317            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       74.60633            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      149.21267            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      186.51583            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      111.90950            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       37.30317            
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     ASN A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     LEU A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     LYS A    25                                                      
REMARK 465     GLU A    26                                                      
REMARK 465     ILE A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     GLN A    31                                                      
REMARK 465     PHE A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     VAL A    34                                                      
REMARK 465     ASN A    35                                                      
REMARK 465     GLU A    36                                                      
REMARK 465     LYS A    71                                                      
REMARK 465     SER A    72                                                      
REMARK 465     GLN A    73                                                      
REMARK 465     PRO A    74                                                      
REMARK 465     ARG A    75                                                      
REMARK 465     LYS A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     GLU A    78                                                      
REMARK 465     LYS A    95                                                      
REMARK 465     LYS A    96                                                      
REMARK 465     LYS A    97                                                      
REMARK 465     VAL A    98                                                      
REMARK 465     GLY A    99                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     GLN A   149                                                      
REMARK 465     ASN A   150                                                      
REMARK 465     GLY A   151                                                      
REMARK 465     ARG A   152                                                      
REMARK 465     LEU A   153                                                      
REMARK 465     PRO A   154                                                      
REMARK 465     ASN A   155                                                      
REMARK 465     GLY A   156                                                      
REMARK 465     ASN A   157                                                      
REMARK 465     ILE A   158                                                      
REMARK 465     ASP A   159                                                      
REMARK 465     ASN A   160                                                      
REMARK 465     GLU A   161                                                      
REMARK 465     ASN A   162                                                      
REMARK 465     ASN A   163                                                      
REMARK 465     ASN A   164                                                      
REMARK 465     SER A   165                                                      
REMARK 465     THR A   166                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     ASN B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     ARG B   333                                                      
REMARK 465     ALA B   334                                                      
REMARK 465     SER B   335                                                      
REMARK 465     GLY B   336                                                      
REMARK 465     ASP B   337                                                      
REMARK 465     TYR B   338                                                      
REMARK 465     ASP B   339                                                      
REMARK 465     ASN B   340                                                      
REMARK 465     ASP B   341                                                      
REMARK 465     CYS B   342                                                      
REMARK 465     THR B   343                                                      
REMARK 465     VAL B   479                                                      
REMARK 465     ASN B   480                                                      
REMARK 465     PRO B   481                                                      
REMARK 465     MET B   482                                                      
REMARK 465     ASP B   483                                                      
REMARK 465     GLU B   484                                                      
REMARK 465     GLU B   485                                                      
REMARK 465     GLU B   486                                                      
REMARK 465     ASN B   487                                                      
REMARK 465     GLU B   488                                                      
REMARK 465     VAL B   489                                                      
REMARK 465     ASN B   490                                                      
REMARK 465     HIS B   491                                                      
REMARK 465     VAL B   492                                                      
REMARK 465     ASN B   493                                                      
REMARK 465     GLY B   494                                                      
REMARK 465     GLU B   495                                                      
REMARK 465     GLN B   496                                                      
REMARK 465     ARG B   499                                                      
REMARK 465     VAL B   500                                                      
REMARK 465     PRO B   560                                                      
REMARK 465     LYS B   561                                                      
REMARK 465     PHE B   562                                                      
REMARK 465     ASN B   563                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     GLU C     9                                                      
REMARK 465     MET C    10                                                      
REMARK 465     VAL C   319                                                      
REMARK 465     GLU C   320                                                      
REMARK 465     GLU C   321                                                      
REMARK 465     GLY C   322                                                      
REMARK 465     ASP C   323                                                      
REMARK 465     PRO C   324                                                      
REMARK 465     MET C   325                                                      
REMARK 465     GLU C   326                                                      
REMARK 465     PHE C   327                                                      
REMARK 465     SER C   328                                                      
REMARK 465     GLY C   329                                                      
REMARK 465     SER C   330                                                      
REMARK 465     ASP C   331                                                      
REMARK 465     GLU C   332                                                      
REMARK 465     ASP C   333                                                      
REMARK 465     PHE C   334                                                      
REMARK 465     GLN C   335                                                      
REMARK 465     ASP C   336                                                      
REMARK 465     LEU C   337                                                      
REMARK 465     LEU C   338                                                      
REMARK 465     HIS C   339                                                      
REMARK 465     PHE C   340                                                      
REMARK 465     GLY C   341                                                      
REMARK 465     ARG C   342                                                      
REMARK 465     ASP C   343                                                      
REMARK 465     ARG C   344                                                      
REMARK 465     ALA C   345                                                      
REMARK 465     ASN C   346                                                      
REMARK 465     SER C   347                                                      
REMARK 465     THR C   348                                                      
REMARK 465     GLN C   349                                                      
REMARK 465     SER C   350                                                      
REMARK 465     ARG C   351                                                      
REMARK 465     LEU C   352                                                      
REMARK 465     SER C   353                                                      
REMARK 465     LYS C   354                                                      
REMARK 465     ARG C   355                                                      
REMARK 465     ASN C   356                                                      
REMARK 465     SER C   357                                                      
REMARK 465     THR C   358                                                      
REMARK 465     ASP C   359                                                      
REMARK 465     SER C   360                                                      
REMARK 465     ARG C   361                                                      
REMARK 465     PRO C   362                                                      
REMARK 465     SER C   395                                                      
REMARK 465     ARG C   396                                                      
REMARK 465     ALA C   397                                                      
REMARK 465     ARG C   398                                                      
REMARK 465     THR C   399                                                      
REMARK 465     HIS C   400                                                      
REMARK 465     THR C   401                                                      
REMARK 465     ASN C   402                                                      
REMARK 465     VAL C   403                                                      
REMARK 465     MET C   404                                                      
REMARK 465     ASN C   405                                                      
REMARK 465     ALA C   406                                                      
REMARK 465     THR C   407                                                      
REMARK 465     SER C   408                                                      
REMARK 465     PRO C   409                                                      
REMARK 465     PRO C   410                                                      
REMARK 465     ALA C   411                                                      
REMARK 465     GLY C   412                                                      
REMARK 465     SER C   413                                                      
REMARK 465     ASN C   414                                                      
REMARK 465     GLY C   415                                                      
REMARK 465     ASN C   416                                                      
REMARK 465     SER C   417                                                      
REMARK 465     VAL C   418                                                      
REMARK 465     THR C   419                                                      
REMARK 465     THR C   420                                                      
REMARK 465     PRO C   421                                                      
REMARK 465     GLY C   422                                                      
REMARK 465     ASN C   423                                                      
REMARK 465     SER C   424                                                      
REMARK 465     VAL C   425                                                      
REMARK 465     PRO C   426                                                      
REMARK 465     PRO C   427                                                      
REMARK 465     PRO C   428                                                      
REMARK 465     LEU C   429                                                      
REMARK 465     PRO C   430                                                      
REMARK 465     ARG C   431                                                      
REMARK 465     SER C   432                                                      
REMARK 465     ASN C   433                                                      
REMARK 465     SER C   434                                                      
REMARK 465     LEU C   435                                                      
REMARK 465     PRO C   436                                                      
REMARK 465     HIS C   437                                                      
REMARK 465     SER C   438                                                      
REMARK 465     ALA C   439                                                      
REMARK 465     VAL C   440                                                      
REMARK 465     SER C   441                                                      
REMARK 465     ASN C   442                                                      
REMARK 465     ALA C   443                                                      
REMARK 465     GLY C   444                                                      
REMARK 465     SER C   445                                                      
REMARK 465     LYS C   446                                                      
REMARK 465     SER C   447                                                      
REMARK 465     SER C   448                                                      
REMARK 465     VAL C   449                                                      
REMARK 465     MET C   450                                                      
REMARK 465     ASP C   451                                                      
REMARK 465     GLY C   452                                                      
REMARK 465     ALA C   453                                                      
REMARK 465     ILE C   454                                                      
REMARK 465     ALA C   455                                                      
REMARK 465     SER C   456                                                      
REMARK 465     GLY C   457                                                      
REMARK 465     VAL C   458                                                      
REMARK 465     SER C   459                                                      
REMARK 465     LYS C   460                                                      
REMARK 465     PHE C   461                                                      
REMARK 465     ALA C   462                                                      
REMARK 465     THR C   463                                                      
REMARK 465     LEU C   464                                                      
REMARK 465     SER C   465                                                      
REMARK 465     LEU C   466                                                      
REMARK 465     HIS C   467                                                      
REMARK 465     ASP C   468                                                      
REMARK 465     ARG C   469                                                      
REMARK 465     LYS C   470                                                      
REMARK 465     GLU C   471                                                      
REMARK 465     ARG C   472                                                      
REMARK 465     HIS C   473                                                      
REMARK 465     HIS C   474                                                      
REMARK 465     GLU C   475                                                      
REMARK 465     LYS C   476                                                      
REMARK 465     ASP C   477                                                      
REMARK 465     HIS C   478                                                      
REMARK 465     LYS C   479                                                      
REMARK 465     ARG C   480                                                      
REMARK 465     ASN C   481                                                      
REMARK 465     HIS C   482                                                      
REMARK 465     SER C   483                                                      
REMARK 465     MET C   484                                                      
REMARK 465     GLY C   485                                                      
REMARK 465     HIS C   486                                                      
REMARK 465     ILE C   487                                                      
REMARK 465     SER C   488                                                      
REMARK 465     SER C   489                                                      
REMARK 465     LYS C   490                                                      
REMARK 465     SER C   491                                                      
REMARK 465     SER C   492                                                      
REMARK 465     ASP C   493                                                      
REMARK 465     LYS C   494                                                      
REMARK 465     LEU C   495                                                      
REMARK 465     ASN C   496                                                      
REMARK 465     LEU C   497                                                      
REMARK 465     VAL C   498                                                      
REMARK 465     THR C   499                                                      
REMARK 465     LYS C   500                                                      
REMARK 465     THR C   501                                                      
REMARK 465     LYS C   502                                                      
REMARK 465     THR C   503                                                      
REMARK 465     ASP C   504                                                      
REMARK 465     PRO C   505                                                      
REMARK 465     ALA C   506                                                      
REMARK 465     LYS C   507                                                      
REMARK 465     THR C   508                                                      
REMARK 465     PRO C   569                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A  37    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  65    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  66    CG   CD   CE   NZ                                   
REMARK 470     LEU A  81    CG   CD1  CD2                                       
REMARK 470     THR A  82    OG1  CG2                                            
REMARK 470     LEU A  84    CG   CD1  CD2                                       
REMARK 470     ASP A  86    CG   OD1  OD2                                       
REMARK 470     PHE A  88    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A  94    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 104    CG   CD   CE   NZ                                   
REMARK 470     LYS A 105    CG   CD   CE   NZ                                   
REMARK 470     ARG A 109    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 112    CD   CE   NZ                                        
REMARK 470     TYR A 120    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET A 121    CG   SD   CE                                        
REMARK 470     ASN A 130    CG   OD1  ND2                                       
REMARK 470     LEU A 140    CG   CD1  CD2                                       
REMARK 470     LYS A 145    CG   CD   CE   NZ                                   
REMARK 470     GLU A 147    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 195    CG   CD   CE   NZ                                   
REMARK 470     LYS A 250    CG   CD   CE   NZ                                   
REMARK 470     TYR A 264    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET A 265    SD   CE                                             
REMARK 470     SER A 290    OG                                                  
REMARK 470     SER A 324    OG                                                  
REMARK 470     LYS A 338    CG   CD   CE   NZ                                   
REMARK 470     ILE A 354    CG1  CG2  CD1                                       
REMARK 470     LYS A 356    CG   CD   CE   NZ                                   
REMARK 470     ASN A 357    CG   OD1  ND2                                       
REMARK 470     SER A 358    OG                                                  
REMARK 470     LYS B  14    CG   CD   CE   NZ                                   
REMARK 470     LYS B 127    CG   CD   CE   NZ                                   
REMARK 470     ASN B 156    CG   OD1  ND2                                       
REMARK 470     LYS B 294    CG   CD   CE   NZ                                   
REMARK 470     LYS B 327    CG   CD   CE   NZ                                   
REMARK 470     LYS B 400    CG   CD   CE   NZ                                   
REMARK 470     LYS B 409    CG   CD   CE   NZ                                   
REMARK 470     LYS B 412    CG   CD   CE   NZ                                   
REMARK 470     LYS B 446    CG   CD   CE   NZ                                   
REMARK 470     GLN B 501    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 502    CG   CD   CE   NZ                                   
REMARK 470     LYS B 557    CG   CD   CE   NZ                                   
REMARK 470     MET B 559    CG   SD   CE                                        
REMARK 470     MET C   1    CG   SD   CE                                        
REMARK 470     GLN C  58    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 139    CG   CD   CE   NZ                                   
REMARK 470     LEU C 140    CG   CD1  CD2                                       
REMARK 470     GLU C 197    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 207    CG   CD   CE   NZ                                   
REMARK 470     LYS C 233    CG   CD   CE   NZ                                   
REMARK 470     LEU C 394    CG   CD1  CD2                                       
REMARK 470     LEU C 509    CG   CD1  CD2                                       
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   SG   CYS A   189    ZN     ZN A   401              1.31            
REMARK 500   SG   CYS A   186    ZN     ZN A   401              1.33            
REMARK 500   CG2  THR A   351     OE1  GLU C   534              1.57            
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    LYS A 105   C     LYS A 105   O       0.132                       
REMARK 500    PHE A 106   C     ILE A 107   N       0.167                       
REMARK 500    MET B  71   C     GLU B  72   N       0.152                       
REMARK 500    THR B  75   C     ASP B  76   N       0.164                       
REMARK 500    ASP B  76   C     ASP B  76   O      -0.123                       
REMARK 500    ASP B 307   C     ASP B 307   O       0.139                       
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 102   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    LYS A 104   O   -  C   -  N   ANGL. DEV. =  13.5 DEGREES          
REMARK 500    CYS A 186   CA  -  CB  -  SG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    CYS A 233   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500    CYS A 236   CA  -  CB  -  SG  ANGL. DEV. =   8.1 DEGREES          
REMARK 500    GLN A 342   CB  -  CA  -  C   ANGL. DEV. =  14.3 DEGREES          
REMARK 500    GLU A 359   CB  -  CA  -  C   ANGL. DEV. =  14.7 DEGREES          
REMARK 500    GLU A 359   N   -  CA  -  C   ANGL. DEV. = -21.4 DEGREES          
REMARK 500    GLY B  32   N   -  CA  -  C   ANGL. DEV. =  16.1 DEGREES          
REMARK 500    GLU B  72   O   -  C   -  N   ANGL. DEV. = -12.0 DEGREES          
REMARK 500    HIS B  74   CB  -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ASP B 307   C   -  N   -  CA  ANGL. DEV. = -19.6 DEGREES          
REMARK 500    PRO B 308   C   -  N   -  CD  ANGL. DEV. = -29.2 DEGREES          
REMARK 500    PRO B 309   C   -  N   -  CD  ANGL. DEV. = -20.3 DEGREES          
REMARK 500    GLU C 162   CB  -  CA  -  C   ANGL. DEV. =  15.4 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    PHE A  39     -139.52   -103.12                                   
REMARK 500    ASN A  46       55.08   -140.85                                   
REMARK 500    LYS A 112      -73.02    -86.05                                   
REMARK 500    ASP A 118       -0.60    -57.79                                   
REMARK 500    TYR A 120      -22.52     82.27                                   
REMARK 500    THR A 188      -68.66   -102.05                                   
REMARK 500    ASN A 209       62.48     61.14                                   
REMARK 500    SER A 227     -132.87     55.85                                   
REMARK 500    LYS A 260       74.01    -68.13                                   
REMARK 500    TYR A 264       76.51    -69.62                                   
REMARK 500    HIS A 269       48.22     71.88                                   
REMARK 500    SER A 275       38.23    -93.38                                   
REMARK 500    ASN A 288        1.37    -66.40                                   
REMARK 500    ARG A 298      111.97    -39.22                                   
REMARK 500    SER A 311       16.84   -140.79                                   
REMARK 500    HIS A 325     -126.83     57.17                                   
REMARK 500    ASP A 332      -70.40    -72.31                                   
REMARK 500    ASP A 333      -72.11   -125.79                                   
REMARK 500    PHE A 347       30.35    -99.23                                   
REMARK 500    THR A 351      -69.59   -101.60                                   
REMARK 500    ILE A 354        8.05    -65.44                                   
REMARK 500    LYS A 356      -95.10    -87.34                                   
REMARK 500    SER A 358       38.66     39.05                                   
REMARK 500    TYR A 362      -51.03   -154.70                                   
REMARK 500    GLU B  26       70.99     50.96                                   
REMARK 500    LEU B  38      -23.88   -153.24                                   
REMARK 500    ASP B  39       82.25     38.98                                   
REMARK 500    ASP B  51       35.56    -77.13                                   
REMARK 500    SER B  52       -9.33     68.80                                   
REMARK 500    ILE B  68      -53.23   -132.88                                   
REMARK 500    HIS B  73      -56.87   -138.87                                   
REMARK 500    ASP B  76     -109.03   -132.69                                   
REMARK 500    THR B 153     -159.78   -107.08                                   
REMARK 500    ASN B 156       59.78   -105.09                                   
REMARK 500    LEU B 174      118.37   -165.45                                   
REMARK 500    LYS B 190      -25.83     73.88                                   
REMARK 500    CYS B 200       10.15     83.00                                   
REMARK 500    GLN B 242       57.92     25.72                                   
REMARK 500    ARG B 249       68.83   -113.49                                   
REMARK 500    ASP B 273      -37.03    -36.75                                   
REMARK 500    ARG B 274      -23.34     87.95                                   
REMARK 500    ILE B 286       77.94   -104.15                                   
REMARK 500    ARG B 304       63.20   -118.86                                   
REMARK 500    PRO B 309      124.66     -6.01                                   
REMARK 500    ASP B 354      -87.00    -82.37                                   
REMARK 500    ARG B 373      -46.00   -149.56                                   
REMARK 500    ALA B 392       54.43     74.36                                   
REMARK 500    VAL B 395      -56.97   -129.70                                   
REMARK 500    MET B 413      103.85    -54.83                                   
REMARK 500    ALA B 441       88.00   -169.50                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      68 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 ASP A  205     VAL A  206                 -148.91                    
REMARK 500 ASN A  295     PRO A  296                 -148.93                    
REMARK 500 ASP A  334     ILE A  335                 -148.72                    
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    PRO A 103        -13.74                                           
REMARK 500    LYS A 105        -10.22                                           
REMARK 500    ALA B 306        -10.08                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TAM C 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5K1A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5K1B   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5K19   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5K16   RELATED DB: PDB                                   
DBREF  5K1C A   16   370  UNP    O75317   UBP12_HUMAN     16    370             
DBREF  5K1C B    1   563  UNP    Q8TAF3   WDR48_HUMAN      1    563             
DBREF  5K1C C    1   569  UNP    Q8TBZ3   WDR20_HUMAN      1    569             
SEQRES   1 A  355  MET GLY ALA ASN ALA SER ALA LEU GLU LYS GLU ILE GLY          
SEQRES   2 A  355  PRO GLU GLN PHE PRO VAL ASN GLU HIS TYR PHE GLY LEU          
SEQRES   3 A  355  VAL ASN PHE GLY ASN THR CYS TYR CYS ASN SER VAL LEU          
SEQRES   4 A  355  GLN ALA LEU TYR PHE CYS ARG PRO PHE ARG GLU LYS VAL          
SEQRES   5 A  355  LEU ALA TYR LYS SER GLN PRO ARG LYS LYS GLU SER LEU          
SEQRES   6 A  355  LEU THR CYS LEU ALA ASP LEU PHE HIS SER ILE ALA THR          
SEQRES   7 A  355  GLN LYS LYS LYS VAL GLY VAL ILE PRO PRO LYS LYS PHE          
SEQRES   8 A  355  ILE THR ARG LEU ARG LYS GLU ASN GLU LEU PHE ASP ASN          
SEQRES   9 A  355  TYR MET GLN GLN ASP ALA HIS GLU PHE LEU ASN TYR LEU          
SEQRES  10 A  355  LEU ASN THR ILE ALA ASP ILE LEU GLN GLU GLU ARG LYS          
SEQRES  11 A  355  GLN GLU LYS GLN ASN GLY ARG LEU PRO ASN GLY ASN ILE          
SEQRES  12 A  355  ASP ASN GLU ASN ASN ASN SER THR PRO ASP PRO THR TRP          
SEQRES  13 A  355  VAL HIS GLU ILE PHE GLN GLY THR LEU THR ASN GLU THR          
SEQRES  14 A  355  ARG CYS LEU THR CYS GLU THR ILE SER SER LYS ASP GLU          
SEQRES  15 A  355  ASP PHE LEU ASP LEU SER VAL ASP VAL GLU GLN ASN THR          
SEQRES  16 A  355  SER ILE THR HIS CYS LEU ARG GLY PHE SER ASN THR GLU          
SEQRES  17 A  355  THR LEU CYS SER GLU TYR LYS TYR TYR CYS GLU GLU CYS          
SEQRES  18 A  355  ARG SER LYS GLN GLU ALA HIS LYS ARG MET LYS VAL LYS          
SEQRES  19 A  355  LYS LEU PRO MET ILE LEU ALA LEU HIS LEU LYS ARG PHE          
SEQRES  20 A  355  LYS TYR MET ASP GLN LEU HIS ARG TYR THR LYS LEU SER          
SEQRES  21 A  355  TYR ARG VAL VAL PHE PRO LEU GLU LEU ARG LEU PHE ASN          
SEQRES  22 A  355  THR SER GLY ASP ALA THR ASN PRO ASP ARG MET TYR ASP          
SEQRES  23 A  355  LEU VAL ALA VAL VAL VAL HIS CYS GLY SER GLY PRO ASN          
SEQRES  24 A  355  ARG GLY HIS TYR ILE ALA ILE VAL LYS SER HIS ASP PHE          
SEQRES  25 A  355  TRP LEU LEU PHE ASP ASP ASP ILE VAL GLU LYS ILE ASP          
SEQRES  26 A  355  ALA GLN ALA ILE GLU GLU PHE TYR GLY LEU THR SER ASP          
SEQRES  27 A  355  ILE SER LYS ASN SER GLU SER GLY TYR ILE LEU PHE TYR          
SEQRES  28 A  355  GLN SER ARG ASP                                              
SEQRES   1 B  563  MET ALA ALA HIS HIS ARG GLN ASN THR ALA GLY ARG ARG          
SEQRES   2 B  563  LYS VAL GLN VAL SER TYR VAL ILE ARG ASP GLU VAL GLU          
SEQRES   3 B  563  LYS TYR ASN ARG ASN GLY VAL ASN ALA LEU GLN LEU ASP          
SEQRES   4 B  563  PRO ALA LEU ASN ARG LEU PHE THR ALA GLY ARG ASP SER          
SEQRES   5 B  563  ILE ILE ARG ILE TRP SER VAL ASN GLN HIS LYS GLN ASP          
SEQRES   6 B  563  PRO TYR ILE ALA SER MET GLU HIS HIS THR ASP TRP VAL          
SEQRES   7 B  563  ASN ASP ILE VAL LEU CYS CYS ASN GLY LYS THR LEU ILE          
SEQRES   8 B  563  SER ALA SER SER ASP THR THR VAL LYS VAL TRP ASN ALA          
SEQRES   9 B  563  HIS LYS GLY PHE CYS MET SER THR LEU ARG THR HIS LYS          
SEQRES  10 B  563  ASP TYR VAL LYS ALA LEU ALA TYR ALA LYS ASP LYS GLU          
SEQRES  11 B  563  LEU VAL ALA SER ALA GLY LEU ASP ARG GLN ILE PHE LEU          
SEQRES  12 B  563  TRP ASP VAL ASN THR LEU THR ALA LEU THR ALA SER ASN          
SEQRES  13 B  563  ASN THR VAL THR THR SER SER LEU SER GLY ASN LYS ASP          
SEQRES  14 B  563  SER ILE TYR SER LEU ALA MET ASN GLN LEU GLY THR ILE          
SEQRES  15 B  563  ILE VAL SER GLY SER THR GLU LYS VAL LEU ARG VAL TRP          
SEQRES  16 B  563  ASP PRO ARG THR CYS ALA LYS LEU MET LYS LEU LYS GLY          
SEQRES  17 B  563  HIS THR ASP ASN VAL LYS ALA LEU LEU LEU ASN ARG ASP          
SEQRES  18 B  563  GLY THR GLN CYS LEU SER GLY SER SER ASP GLY THR ILE          
SEQRES  19 B  563  ARG LEU TRP SER LEU GLY GLN GLN ARG CYS ILE ALA THR          
SEQRES  20 B  563  TYR ARG VAL HIS ASP GLU GLY VAL TRP ALA LEU GLN VAL          
SEQRES  21 B  563  ASN ASP ALA PHE THR HIS VAL TYR SER GLY GLY ARG ASP          
SEQRES  22 B  563  ARG LYS ILE TYR CYS THR ASP LEU ARG ASN PRO ASP ILE          
SEQRES  23 B  563  ARG VAL LEU ILE CYS GLU GLU LYS ALA PRO VAL LEU LYS          
SEQRES  24 B  563  MET GLU LEU ASP ARG SER ALA ASP PRO PRO PRO ALA ILE          
SEQRES  25 B  563  TRP VAL ALA THR THR LYS SER THR VAL ASN LYS TRP THR          
SEQRES  26 B  563  LEU LYS GLY ILE HIS ASN PHE ARG ALA SER GLY ASP TYR          
SEQRES  27 B  563  ASP ASN ASP CYS THR ASN PRO ILE THR PRO LEU CYS THR          
SEQRES  28 B  563  GLN PRO ASP GLN VAL ILE LYS GLY GLY ALA SER ILE ILE          
SEQRES  29 B  563  GLN CYS HIS ILE LEU ASN ASP LYS ARG HIS ILE LEU THR          
SEQRES  30 B  563  LYS ASP THR ASN ASN ASN VAL ALA TYR TRP ASP VAL LEU          
SEQRES  31 B  563  LYS ALA CYS LYS VAL GLU ASP LEU GLY LYS VAL ASP PHE          
SEQRES  32 B  563  GLU ASP GLU ILE LYS LYS ARG PHE LYS MET VAL TYR VAL          
SEQRES  33 B  563  PRO ASN TRP PHE SER VAL ASP LEU LYS THR GLY MET LEU          
SEQRES  34 B  563  THR ILE THR LEU ASP GLU SER ASP CYS PHE ALA ALA TRP          
SEQRES  35 B  563  VAL SER ALA LYS ASP ALA GLY PHE SER SER PRO ASP GLY          
SEQRES  36 B  563  SER ASP PRO LYS LEU ASN LEU GLY GLY LEU LEU LEU GLN          
SEQRES  37 B  563  ALA LEU LEU GLU TYR TRP PRO ARG THR HIS VAL ASN PRO          
SEQRES  38 B  563  MET ASP GLU GLU GLU ASN GLU VAL ASN HIS VAL ASN GLY          
SEQRES  39 B  563  GLU GLN GLU ASN ARG VAL GLN LYS GLY ASN GLY TYR PHE          
SEQRES  40 B  563  GLN VAL PRO PRO HIS THR PRO VAL ILE PHE GLY GLU ALA          
SEQRES  41 B  563  GLY GLY ARG THR LEU PHE ARG LEU LEU CYS ARG ASP SER          
SEQRES  42 B  563  GLY GLY GLU THR GLU SER MET LEU LEU ASN GLU THR VAL          
SEQRES  43 B  563  PRO GLN TRP VAL ILE ASP ILE THR VAL ASP LYS ASN MET          
SEQRES  44 B  563  PRO LYS PHE ASN                                              
SEQRES   1 C  569  MET ALA THR GLU GLY GLY GLY LYS GLU MET ASN GLU ILE          
SEQRES   2 C  569  LYS THR GLN PHE THR THR ARG GLU GLY LEU TYR LYS LEU          
SEQRES   3 C  569  LEU PRO HIS SER GLU TYR SER ARG PRO ASN ARG VAL PRO          
SEQRES   4 C  569  PHE ASN SER GLN GLY SER ASN PRO VAL ARG VAL SER PHE          
SEQRES   5 C  569  VAL ASN LEU ASN ASP GLN SER GLY ASN GLY ASP ARG LEU          
SEQRES   6 C  569  CYS PHE ASN VAL GLY ARG GLU LEU TYR PHE TYR ILE TYR          
SEQRES   7 C  569  LYS GLY VAL ARG LYS ALA ALA ASP LEU SER LYS PRO ILE          
SEQRES   8 C  569  ASP LYS ARG ILE TYR LYS GLY THR GLN PRO THR CYS HIS          
SEQRES   9 C  569  ASP PHE ASN HIS LEU THR ALA THR ALA GLU SER VAL SER          
SEQRES  10 C  569  LEU LEU VAL GLY PHE SER ALA GLY GLN VAL GLN LEU ILE          
SEQRES  11 C  569  ASP PRO ILE LYS LYS GLU THR SER LYS LEU PHE ASN GLU          
SEQRES  12 C  569  GLU ARG LEU ILE ASP LYS SER ARG VAL THR CYS VAL LYS          
SEQRES  13 C  569  TRP VAL PRO GLY SER GLU SER LEU PHE LEU VAL ALA HIS          
SEQRES  14 C  569  SER SER GLY ASN MET TYR LEU TYR ASN VAL GLU HIS THR          
SEQRES  15 C  569  CYS GLY THR THR ALA PRO HIS TYR GLN LEU LEU LYS GLN          
SEQRES  16 C  569  GLY GLU SER PHE ALA VAL HIS THR CYS LYS SER LYS SER          
SEQRES  17 C  569  THR ARG ASN PRO LEU LEU LYS TRP THR VAL GLY GLU GLY          
SEQRES  18 C  569  ALA LEU ASN GLU PHE ALA PHE SER PRO ASP GLY LYS PHE          
SEQRES  19 C  569  LEU ALA CYS VAL SER GLN ASP GLY PHE LEU ARG VAL PHE          
SEQRES  20 C  569  ASN PHE ASP SER VAL GLU LEU HIS GLY THR MET LYS SER          
SEQRES  21 C  569  TYR PHE GLY GLY LEU LEU CYS VAL CYS TRP SER PRO ASP          
SEQRES  22 C  569  GLY LYS TYR ILE VAL THR GLY GLY GLU ASP ASP LEU VAL          
SEQRES  23 C  569  THR VAL TRP SER PHE VAL ASP CYS ARG VAL ILE ALA ARG          
SEQRES  24 C  569  GLY HIS GLY HIS LYS SER TRP VAL SER VAL VAL ALA PHE          
SEQRES  25 C  569  ASP PRO TYR THR THR SER VAL GLU GLU GLY ASP PRO MET          
SEQRES  26 C  569  GLU PHE SER GLY SER ASP GLU ASP PHE GLN ASP LEU LEU          
SEQRES  27 C  569  HIS PHE GLY ARG ASP ARG ALA ASN SER THR GLN SER ARG          
SEQRES  28 C  569  LEU SER LYS ARG ASN SER THR ASP SER ARG PRO VAL SER          
SEQRES  29 C  569  VAL THR TYR ARG PHE GLY SER VAL GLY GLN ASP THR GLN          
SEQRES  30 C  569  LEU CYS LEU TRP ASP LEU THR GLU ASP ILE LEU PHE PRO          
SEQRES  31 C  569  HIS GLN PRO LEU SER ARG ALA ARG THR HIS THR ASN VAL          
SEQRES  32 C  569  MET ASN ALA THR SER PRO PRO ALA GLY SER ASN GLY ASN          
SEQRES  33 C  569  SER VAL THR THR PRO GLY ASN SER VAL PRO PRO PRO LEU          
SEQRES  34 C  569  PRO ARG SER ASN SER LEU PRO HIS SER ALA VAL SER ASN          
SEQRES  35 C  569  ALA GLY SER LYS SER SER VAL MET ASP GLY ALA ILE ALA          
SEQRES  36 C  569  SER GLY VAL SER LYS PHE ALA THR LEU SER LEU HIS ASP          
SEQRES  37 C  569  ARG LYS GLU ARG HIS HIS GLU LYS ASP HIS LYS ARG ASN          
SEQRES  38 C  569  HIS SER MET GLY HIS ILE SER SER LYS SER SER ASP LYS          
SEQRES  39 C  569  LEU ASN LEU VAL THR LYS THR LYS THR ASP PRO ALA LYS          
SEQRES  40 C  569  THR LEU GLY THR PRO LEU CYS PRO ARG MET GLU ASP VAL          
SEQRES  41 C  569  PRO LEU LEU GLU PRO LEU ILE CYS LYS LYS ILE ALA HIS          
SEQRES  42 C  569  GLU ARG LEU THR VAL LEU ILE PHE LEU GLU ASP CYS ILE          
SEQRES  43 C  569  VAL THR ALA CYS GLN GLU GLY PHE ILE CYS THR TRP GLY          
SEQRES  44 C  569  ARG PRO GLY LYS VAL VAL SER PHE ASN PRO                      
HET     ZN  A 401       1                                                       
HET    PO4  B 601       5                                                       
HET    TAM  C 601      11                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     TAM TRIS(HYDROXYETHYL)AMINOMETHANE                                   
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5  PO4    O4 P 3-                                                      
FORMUL   6  TAM    C7 H17 N O3                                                  
FORMUL   7  HOH   *75(H2 O)                                                     
HELIX    1 AA1 THR A   47  PHE A   59  1                                  13    
HELIX    2 AA2 CYS A   60  TYR A   70  1                                  11    
HELIX    3 AA3 LEU A   80  GLN A   94  1                                  15    
HELIX    4 AA4 PRO A  103  ASN A  114  1                                  12    
HELIX    5 AA5 ASP A  124  GLN A  141  1                                  18    
HELIX    6 AA6 GLN A  141  GLU A  147  1                                   7    
HELIX    7 AA7 ILE A  212  SER A  220  1                                   9    
HELIX    8 AA8 CYS A  226  LYS A  230  5                                   5    
HELIX    9 AA9 ASP A  340  TYR A  348  5                                   9    
HELIX   10 AB1 LYS B  127  LYS B  129  5                                   3    
HELIX   11 AB2 VAL B  146  ALA B  151  1                                   6    
HELIX   12 AB3 ASP B  402  ARG B  410  1                                   9    
HELIX   13 AB4 ALA B  445  GLY B  449  1                                   5    
HELIX   14 AB5 LEU B  462  LEU B  471  1                                  10    
HELIX   15 AB6 TRP B  474  HIS B  478  5                                   5    
HELIX   16 AB7 ARG B  531  GLY B  534  5                                   4    
HELIX   17 AB8 GLY B  535  VAL B  546  1                                  12    
HELIX   18 AB9 PRO B  547  VAL B  555  1                                   9    
HELIX   19 AC1 PRO C   28  GLU C   31  5                                   4    
HELIX   20 AC2 PRO C  314  THR C  317  5                                   4    
HELIX   21 AC3 THR C  384  PHE C  389  1                                   6    
SHEET    1 AA1 4 ILE A 192  PHE A 199  0                                        
SHEET    2 AA1 4 GLY A 178  CYS A 186 -1  N  GLY A 178   O  PHE A 199           
SHEET    3 AA1 4 ALA A 242  LYS A 250 -1  O  LYS A 249   N  THR A 179           
SHEET    4 AA1 4 THR A 222  LEU A 225 -1  N  GLU A 223   O  LYS A 244           
SHEET    1 AA2 5 ASP A 201  VAL A 204  0                                        
SHEET    2 AA2 5 ILE A 254  LEU A 259  1  O  HIS A 258   N  VAL A 204           
SHEET    3 AA2 5 GLY A 361  SER A 368 -1  O  LEU A 364   N  LEU A 257           
SHEET    4 AA2 5 TYR A 300  CYS A 309 -1  N  ASP A 301   O  GLN A 367           
SHEET    5 AA2 5 GLU A 283  LEU A 284 -1  N  LEU A 284   O  TYR A 300           
SHEET    1 AA3 7 ASP A 201  VAL A 204  0                                        
SHEET    2 AA3 7 ILE A 254  LEU A 259  1  O  HIS A 258   N  VAL A 204           
SHEET    3 AA3 7 GLY A 361  SER A 368 -1  O  LEU A 364   N  LEU A 257           
SHEET    4 AA3 7 TYR A 300  CYS A 309 -1  N  ASP A 301   O  GLN A 367           
SHEET    5 AA3 7 HIS A 317  LYS A 323 -1  O  HIS A 317   N  CYS A 309           
SHEET    6 AA3 7 TRP A 328  PHE A 331 -1  O  LEU A 329   N  VAL A 322           
SHEET    7 AA3 7 VAL A 336  LYS A 338 -1  O  GLU A 337   N  LEU A 330           
SHEET    1 AA4 2 THR A 210  SER A 211  0                                        
SHEET    2 AA4 2 VAL A 278  VAL A 279  1  O  VAL A 279   N  THR A 210           
SHEET    1 AA5 2 TYR A 231  CYS A 233  0                                        
SHEET    2 AA5 2 SER A 238  GLN A 240 -1  O  GLN A 240   N  TYR A 231           
SHEET    1 AA6 2 PHE A 262  LYS A 263  0                                        
SHEET    2 AA6 2 THR A 272  LYS A 273 -1  O  THR A 272   N  LYS A 263           
SHEET    1 AA7 5 SER B 421  ASP B 423  0                                        
SHEET    2 AA7 5 LEU B 429  LEU B 433 -1  O  THR B 432   N  SER B 421           
SHEET    3 AA7 5 VAL B  17  ILE B  21 -1  N  VAL B  17   O  LEU B 433           
SHEET    4 AA7 5 PRO B 514  PHE B 517 -1  O  ILE B 516   N  SER B  18           
SHEET    5 AA7 5 PHE B 526  LEU B 529 -1  O  LEU B 528   N  VAL B 515           
SHEET    1 AA8 4 VAL B  33  GLN B  37  0                                        
SHEET    2 AA8 4 PHE B  46  GLY B  49 -1  O  ALA B  48   N  ASN B  34           
SHEET    3 AA8 4 ILE B  54  ILE B  56 -1  O  ARG B  55   N  THR B  47           
SHEET    4 AA8 4 ALA B  69  MET B  71 -1  O  MET B  71   N  ILE B  54           
SHEET    1 AA9 4 VAL B  78  CYS B  84  0                                        
SHEET    2 AA9 4 THR B  89  SER B  94 -1  O  ILE B  91   N  VAL B  82           
SHEET    3 AA9 4 VAL B  99  ASN B 103 -1  O  TRP B 102   N  LEU B  90           
SHEET    4 AA9 4 PHE B 108  LEU B 113 -1  O  LEU B 113   N  VAL B  99           
SHEET    1 AB1 3 VAL B 120  ALA B 126  0                                        
SHEET    2 AB1 3 LEU B 131  GLY B 136 -1  O  ALA B 133   N  ALA B 124           
SHEET    3 AB1 3 ILE B 141  ASP B 145 -1  O  TRP B 144   N  VAL B 132           
SHEET    1 AB2 4 ILE B 171  MET B 176  0                                        
SHEET    2 AB2 4 ILE B 183  SER B 187 -1  O  VAL B 184   N  ALA B 175           
SHEET    3 AB2 4 LEU B 192  TRP B 195 -1  O  ARG B 193   N  SER B 185           
SHEET    4 AB2 4 LYS B 202  LEU B 206 -1  O  LEU B 203   N  VAL B 194           
SHEET    1 AB3 4 ALA B 215  LEU B 218  0                                        
SHEET    2 AB3 4 GLN B 224  GLY B 228 -1  O  LEU B 226   N  LEU B 217           
SHEET    3 AB3 4 ILE B 234  SER B 238 -1  O  ARG B 235   N  SER B 227           
SHEET    4 AB3 4 ARG B 243  TYR B 248 -1  O  ARG B 243   N  SER B 238           
SHEET    1 AB4 4 VAL B 255  VAL B 260  0                                        
SHEET    2 AB4 4 HIS B 266  GLY B 271 -1  O  TYR B 268   N  GLN B 259           
SHEET    3 AB4 4 LYS B 275  ASP B 280 -1  O  THR B 279   N  VAL B 267           
SHEET    4 AB4 4 VAL B 288  GLU B 292 -1  O  CYS B 291   N  ILE B 276           
SHEET    1 AB5 4 VAL B 297  LEU B 302  0                                        
SHEET    2 AB5 4 ALA B 311  THR B 316 -1  O  ALA B 315   N  LEU B 298           
SHEET    3 AB5 4 VAL B 321  THR B 325 -1  O  TRP B 324   N  ILE B 312           
SHEET    4 AB5 4 VAL B 356  ILE B 357 -1  O  ILE B 357   N  VAL B 321           
SHEET    1 AB6 4 ILE B 363  ILE B 368  0                                        
SHEET    2 AB6 4 HIS B 374  ASP B 379 -1  O  LEU B 376   N  HIS B 367           
SHEET    3 AB6 4 ALA B 385  ASP B 388 -1  O  TRP B 387   N  ILE B 375           
SHEET    4 AB6 4 CYS B 393  ASP B 397 -1  O  CYS B 393   N  ASP B 388           
SHEET    1 AB7 2 TRP B 442  SER B 444  0                                        
SHEET    2 AB7 2 LYS B 459  ASN B 461 -1  O  LEU B 460   N  VAL B 443           
SHEET    1 AB8 5 GLN C  16  THR C  19  0                                        
SHEET    2 AB8 5 GLY C  22  LEU C  26 -1  O  TYR C  24   N  PHE C  17           
SHEET    3 AB8 5 ILE C 555  GLY C 559 -1  O  GLY C 559   N  LYS C  25           
SHEET    4 AB8 5 CYS C 545  CYS C 550 -1  N  THR C 548   O  CYS C 556           
SHEET    5 AB8 5 LEU C 536  LEU C 542 -1  N  THR C 537   O  ALA C 549           
SHEET    1 AB9 3 VAL C  50  ASN C  54  0                                        
SHEET    2 AB9 3 ASP C  63  VAL C  69 -1  O  ARG C  64   N  VAL C  53           
SHEET    3 AB9 3 GLU C  72  ILE C  77 -1  O  GLU C  72   N  VAL C  69           
SHEET    1 AC1 3 PRO C 101  ALA C 111  0                                        
SHEET    2 AC1 3 VAL C 116  PHE C 122 -1  O  SER C 117   N  ASN C 107           
SHEET    3 AC1 3 VAL C 127  ILE C 130 -1  O  GLN C 128   N  VAL C 120           
SHEET    1 AC2 6 VAL C 152  TRP C 157  0                                        
SHEET    2 AC2 6 LEU C 164  HIS C 169 -1  O  ALA C 168   N  THR C 153           
SHEET    3 AC2 6 ASN C 173  ASN C 178 -1  O  TYR C 177   N  PHE C 165           
SHEET    4 AC2 6 LEU C 214  VAL C 218 -1  O  TRP C 216   N  MET C 174           
SHEET    5 AC2 6 PHE C 199  CYS C 204 -1  N  ALA C 200   O  THR C 217           
SHEET    6 AC2 6 TYR C 190  GLY C 196 -1  N  LEU C 193   O  VAL C 201           
SHEET    1 AC3 4 LEU C 223  PHE C 228  0                                        
SHEET    2 AC3 4 PHE C 234  SER C 239 -1  O  ALA C 236   N  ALA C 227           
SHEET    3 AC3 4 PHE C 243  ASN C 248 -1  O  PHE C 247   N  LEU C 235           
SHEET    4 AC3 4 GLU C 253  LYS C 259 -1  O  GLU C 253   N  ASN C 248           
SHEET    1 AC4 5 CYS C 269  TRP C 270  0                                        
SHEET    2 AC4 5 TYR C 276  GLY C 280 -1  O  VAL C 278   N  CYS C 269           
SHEET    3 AC4 5 LEU C 285  SER C 290 -1  O  TRP C 289   N  ILE C 277           
SHEET    4 AC4 5 ARG C 295  HIS C 301 -1  O  ARG C 295   N  SER C 290           
SHEET    5 AC4 5 LEU C 522  LEU C 523  1  O  LEU C 523   N  ARG C 299           
SHEET    1 AC5 4 VAL C 307  PHE C 312  0                                        
SHEET    2 AC5 4 TYR C 367  GLY C 373 -1  O  GLY C 370   N  ALA C 311           
SHEET    3 AC5 4 GLN C 377  LEU C 383 -1  O  TRP C 381   N  PHE C 369           
SHEET    4 AC5 4 ILE C 527  LYS C 530 -1  O  LYS C 529   N  LEU C 378           
SSBOND   1 CYS A  186    CYS A  189                          1555   1555  2.25  
SSBOND   2 CYS A  186    CYS A  236                          1555   1555  2.38  
SSBOND   3 CYS A  186    CYS A  233                          1555   1555  2.88  
SSBOND   4 CYS A  189    CYS A  236                          1555   1555  2.30  
SSBOND   5 CYS A  189    CYS A  233                          1555   1555  1.85  
SITE     1 AC1  4 CYS A 186  CYS A 189  CYS A 233  CYS A 236                    
SITE     1 AC2  4 LYS B 168  ARG B 193  LYS B 202  LYS B 205                    
SITE     1 AC3  7 ASP C  63  TYR C  78  TYR C 315  LEU C 542                    
SITE     2 AC3  7 GLU C 543  ASP C 544  HOH C 715                               
CRYST1  217.903  217.903  223.819  90.00  90.00 120.00 P 61 2 2     12          
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      0.004589  0.002650  0.000000        0.00000                         
SCALE2      0.000000  0.005299  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004468        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system