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Database: PDB
Entry: 4I7D
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HEADER    LIGASE/LIGASE INHIBITOR                 30-NOV-12   4I7D              
TITLE     SIAH1 BOUND TO SYNTHETIC PEPTIDE (ACE)KLRPVAMVRP(PRK)VR               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE SIAH1;                         
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUES 90-282);                   
COMPND   5 SYNONYM: SEVEN IN ABSENTIA HOMOLOG 1, SIAH-1, SIAH-1A;               
COMPND   6 EC: 6.3.2.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROTEIN PHYLLOPOD;                                         
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: SIAH-BINDING PEPTIDE (UNP RESIDUES 113-125);               
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HUMSIAH, SIAH1;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  14 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  15 ORGANISM_TAXID: 7227                                                 
KEYWDS    SINA, BETA SANDWICH, ZINC FINGER, UBIQUITIN LIGASE, COVALENT          
KEYWDS   2 INHIBITOR, LIGASE-LIGASE INHIBITOR COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.SANTELLI,J.L.STEBBINS,Y.FENG,S.K.DE,A.PURVES,K.MOTAMEDCHABOKI,B.WU, 
AUTHOR   2 Z.A.RONAI,R.C.LIDDINGTON,M.PELLECCHIA                                
REVDAT   2   11-SEP-13 4I7D    1       JRNL                                     
REVDAT   1   14-AUG-13 4I7D    0                                                
JRNL        AUTH   J.L.STEBBINS,E.SANTELLI,Y.FENG,S.K.DE,A.PURVES,              
JRNL        AUTH 2 K.MOTAMEDCHABOKI,B.WU,Z.A.RONAI,R.C.LIDDINGTON,M.PELLECCHIA  
JRNL        TITL   STRUCTURE-BASED DESIGN OF COVALENT SIAH INHIBITORS.          
JRNL        REF    CHEM.BIOL.                    V.  20   973 2013              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   23891150                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2013.06.008                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 27176                          
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) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1390                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1770                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 98                           
REMARK   3   BIN FREE R VALUE                    : 0.3310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3180                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 144                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.217         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.177         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.165        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3267 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2224 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4419 ; 1.030 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5418 ; 0.780 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   398 ; 5.224 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   148 ;34.498 ;23.851       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   551 ;12.046 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;18.941 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   488 ; 0.065 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3603 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   667 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   156        A   282                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.6450  20.9010  65.7670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0906 T22:   0.0916                                     
REMARK   3      T33:   0.0215 T12:  -0.0102                                     
REMARK   3      T13:   0.0006 T23:   0.0294                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0339 L22:   4.0761                                     
REMARK   3      L33:   2.3073 L12:   0.3427                                     
REMARK   3      L13:  -0.0939 L23:  -0.6826                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1128 S12:   0.2351 S13:   0.0163                       
REMARK   3      S21:  -0.0362 S22:  -0.0901 S23:  -0.0561                       
REMARK   3      S31:   0.2670 S32:   0.0665 S33:  -0.0227                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   112        B   125                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.5930  14.7070  63.7750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1860 T22:   0.2028                                     
REMARK   3      T33:   0.2232 T12:   0.1325                                     
REMARK   3      T13:   0.0537 T23:   0.1120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.1132 L22:  15.2510                                     
REMARK   3      L33:  14.3001 L12:   6.3454                                     
REMARK   3      L13:   5.9282 L23:   8.2795                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1278 S12:   0.4661 S13:  -0.1154                       
REMARK   3      S21:  -0.3270 S22:   0.2126 S23:  -0.4180                       
REMARK   3      S31:   0.0645 S32:   0.5346 S33:  -0.3404                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   156        C   282                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.1040  42.8610  58.5280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0582 T22:   0.1005                                     
REMARK   3      T33:   0.0711 T12:  -0.0531                                     
REMARK   3      T13:  -0.0303 T23:   0.0726                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3213 L22:   3.0671                                     
REMARK   3      L33:   2.7247 L12:  -0.1985                                     
REMARK   3      L13:  -0.6664 L23:  -0.8521                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0272 S12:  -0.0009 S13:   0.0111                       
REMARK   3      S21:  -0.1845 S22:   0.1016 S23:   0.1939                       
REMARK   3      S31:  -0.1107 S32:  -0.0204 S33:  -0.0744                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   112        D   125                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.7630  50.0200  61.6850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1713 T22:   0.1220                                     
REMARK   3      T33:   0.2959 T12:   0.0918                                     
REMARK   3      T13:   0.0014 T23:   0.0906                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1515 L22:   3.5197                                     
REMARK   3      L33:  15.5949 L12:   2.7944                                     
REMARK   3      L13:   1.6288 L23:   0.7974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1204 S12:  -0.3507 S13:   0.0901                       
REMARK   3      S21:  -0.0215 S22:   0.0315 S23:   0.4959                       
REMARK   3      S31:  -0.2415 S32:  -0.6431 S33:  -0.1519                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   125        A   155                          
REMARK   3    RESIDUE RANGE :   A   601        A   601                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.4060   2.6540  71.2240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4001 T22:   0.0453                                     
REMARK   3      T33:   0.3744 T12:  -0.0219                                     
REMARK   3      T13:  -0.0487 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.3026 L22:   9.7804                                     
REMARK   3      L33:   9.0476 L12:  -0.7974                                     
REMARK   3      L13:  -5.6661 L23:   2.0071                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1428 S12:   0.1523 S13:  -1.7071                       
REMARK   3      S21:   0.0970 S22:  -0.3742 S23:   0.5945                       
REMARK   3      S31:   0.6558 S32:   0.0460 S33:   0.5170                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   125        C   155                          
REMARK   3    RESIDUE RANGE :   C   601        C   601                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.8420  57.5780  45.8790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2048 T22:   0.1625                                     
REMARK   3      T33:   0.1806 T12:   0.0228                                     
REMARK   3      T13:   0.0110 T23:   0.1448                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8825 L22:   7.4790                                     
REMARK   3      L33:   5.8393 L12:   3.2008                                     
REMARK   3      L13:  -0.4030 L23:   0.0738                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3770 S12:   0.5452 S13:   0.5777                       
REMARK   3      S21:   0.0023 S22:  -0.1814 S23:   0.3430                       
REMARK   3      S31:  -0.6449 S32:  -0.0944 S33:  -0.1957                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    91        A   124                          
REMARK   3    RESIDUE RANGE :   A   602        A   602                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.7480   9.2580  79.4680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3530 T22:   0.2375                                     
REMARK   3      T33:   0.1407 T12:  -0.1216                                     
REMARK   3      T13:   0.0658 T23:   0.0650                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.7993 L22:   4.7580                                     
REMARK   3      L33:   6.6625 L12:  -2.6691                                     
REMARK   3      L13:  -3.7340 L23:   1.6732                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3735 S12:   0.6374 S13:   0.9769                       
REMARK   3      S21:  -0.8026 S22:  -0.0858 S23:  -0.4723                       
REMARK   3      S31:  -0.8750 S32:   0.2005 S33:  -0.2877                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    92        C   124                          
REMARK   3    RESIDUE RANGE :   C   602        C   602                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5220  49.8280  35.8990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3788 T22:   0.3710                                     
REMARK   3      T33:   0.3906 T12:  -0.0820                                     
REMARK   3      T13:   0.1089 T23:   0.0416                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  25.2191 L22:   5.4093                                     
REMARK   3      L33:  12.8046 L12: -10.9747                                     
REMARK   3      L13: -11.9098 L23:   7.1313                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0689 S12:   0.7801 S13:  -1.1574                       
REMARK   3      S21:   0.2111 S22:  -0.3973 S23:   0.4095                       
REMARK   3      S31:   0.5724 S32:  -1.0730 S33:   0.3284                       
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 4I7D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB076396.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27179                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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: PDB ENTRY 2A25 CHAIN A                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 65% MPD, 100 MM BICINE, PH 9.0, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      24555   -Y+1/2,-Z+1/2,X+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
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        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       80.48850            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       80.48850            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       80.48850            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       80.48850            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       80.48850            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       80.48850            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       80.48850            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       80.48850            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       80.48850            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       80.48850            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       80.48850            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       80.48850            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       80.48850            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       80.48850            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       80.48850            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       80.48850            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       80.48850            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       80.48850            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       80.48850            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       80.48850            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       80.48850            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       80.48850            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       80.48850            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       80.48850            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       80.48850            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       80.48850            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       80.48850            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       80.48850            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       80.48850            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       80.48850            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       80.48850            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       80.48850            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       80.48850            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       80.48850            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       80.48850            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       80.48850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 701  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE MODIFIED PROTEIN PHYLLOPOD PEPTIDE BI-117F7 IS OLIGOPEPTIDE, A   
REMARK 400 MEMBER OF INHIBITOR CLASS.                                           
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: MODIFIED PROTEIN PHYLLOPOD PEPTIDE BI-117F7                  
REMARK 400   CHAIN: B, D                                                        
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   DESCRIPTION: NULL                                                  
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     GLY A    87                                                      
REMARK 465     SER A    88                                                      
REMARK 465     HIS A    89                                                      
REMARK 465     VAL A    90                                                      
REMARK 465     LYS A   198                                                      
REMARK 465     TYR A   199                                                      
REMARK 465     ASP A   200                                                      
REMARK 465     GLY A   201                                                      
REMARK 465     HIS A   202                                                      
REMARK 465     GLY C    87                                                      
REMARK 465     SER C    88                                                      
REMARK 465     HIS C    89                                                      
REMARK 465     VAL C    90                                                      
REMARK 465     ALA C    91                                                      
REMARK 465     TYR C   199                                                      
REMARK 465     ASP C   200                                                      
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    CYS A 256     -175.46   -173.41                                   
REMARK 500    SER C 154      113.83    -24.20                                   
REMARK 500    CYS C 256     -176.00   -176.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 730        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH C 753        DISTANCE =  6.74 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 602  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 117   NE2                                                    
REMARK 620 2 CYS C  98   SG  104.9                                              
REMARK 620 3 CYS C 105   SG  102.8 112.5                                        
REMARK 620 4 CYS C 121   SG  115.1 109.4 111.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 152   NE2                                                    
REMARK 620 2 HIS C 147   NE2 106.3                                              
REMARK 620 3 CYS C 128   SG  105.9  91.5                                        
REMARK 620 4 CYS C 135   SG  118.6 114.4 116.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 147   NE2                                                    
REMARK 620 2 CYS A 135   SG   98.2                                              
REMARK 620 3 HIS A 152   NE2 108.6 118.9                                        
REMARK 620 4 CYS A 128   SG  109.4 114.8 106.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 602  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 117   NE2                                                    
REMARK 620 2 CYS A 105   SG  105.0                                              
REMARK 620 3 CYS A  98   SG  102.4 112.1                                        
REMARK 620 4 CYS A 121   SG  113.2 110.2 113.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE B 112                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE D 112                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF PROTEIN PHYLLOPOD      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF PROTEIN PHYLLOPOD      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1K2F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2A25   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2AN6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4I7B   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4I7C   RELATED DB: PDB                                   
DBREF  4I7D A   90   282  UNP    Q8IUQ4   SIAH1_HUMAN     90    282             
DBREF  4I7D B  113   125  UNP    Q27934   PHYL_DROME     113    125             
DBREF  4I7D C   90   282  UNP    Q8IUQ4   SIAH1_HUMAN     90    282             
DBREF  4I7D D  113   125  UNP    Q27934   PHYL_DROME     113    125             
SEQADV 4I7D GLY A   87  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7D SER A   88  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7D HIS A   89  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7D ACE B  112  UNP  Q27934              ACETYLATION                    
SEQADV 4I7D PRK B  123  UNP  Q27934    THR   123 ENGINEERED MUTATION            
SEQADV 4I7D GLY C   87  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7D SER C   88  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7D HIS C   89  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7D ACE D  112  UNP  Q27934              ACETYLATION                    
SEQADV 4I7D PRK D  123  UNP  Q27934    THR   123 ENGINEERED MUTATION            
SEQRES   1 A  196  GLY SER HIS VAL ALA ASN SER VAL LEU PHE PRO CYS LYS          
SEQRES   2 A  196  TYR ALA SER SER GLY CYS GLU ILE THR LEU PRO HIS THR          
SEQRES   3 A  196  GLU LYS ALA ASP HIS GLU GLU LEU CYS GLU PHE ARG PRO          
SEQRES   4 A  196  TYR SER CYS PRO CYS PRO GLY ALA SER CYS LYS TRP GLN          
SEQRES   5 A  196  GLY SER LEU ASP ALA VAL MET PRO HIS LEU MET HIS GLN          
SEQRES   6 A  196  HIS LYS SER ILE THR THR LEU GLN GLY GLU ASP ILE VAL          
SEQRES   7 A  196  PHE LEU ALA THR ASP ILE ASN LEU PRO GLY ALA VAL ASP          
SEQRES   8 A  196  TRP VAL MET MET GLN SER CYS PHE GLY PHE HIS PHE MET          
SEQRES   9 A  196  LEU VAL LEU GLU LYS GLN GLU LYS TYR ASP GLY HIS GLN          
SEQRES  10 A  196  GLN PHE PHE ALA ILE VAL GLN LEU ILE GLY THR ARG LYS          
SEQRES  11 A  196  GLN ALA GLU ASN PHE ALA TYR ARG LEU GLU LEU ASN GLY          
SEQRES  12 A  196  HIS ARG ARG ARG LEU THR TRP GLU ALA THR PRO ARG SER          
SEQRES  13 A  196  ILE HIS GLU GLY ILE ALA THR ALA ILE MET ASN SER ASP          
SEQRES  14 A  196  CYS LEU VAL PHE ASP THR SER ILE ALA GLN LEU PHE ALA          
SEQRES  15 A  196  GLU ASN GLY ASN LEU GLY ILE ASN VAL THR ILE SER MET          
SEQRES  16 A  196  CYS                                                          
SEQRES   1 B   14  ACE LYS LEU ARG PRO VAL ALA MET VAL ARG PRO PRK VAL          
SEQRES   2 B   14  ARG                                                          
SEQRES   1 C  196  GLY SER HIS VAL ALA ASN SER VAL LEU PHE PRO CYS LYS          
SEQRES   2 C  196  TYR ALA SER SER GLY CYS GLU ILE THR LEU PRO HIS THR          
SEQRES   3 C  196  GLU LYS ALA ASP HIS GLU GLU LEU CYS GLU PHE ARG PRO          
SEQRES   4 C  196  TYR SER CYS PRO CYS PRO GLY ALA SER CYS LYS TRP GLN          
SEQRES   5 C  196  GLY SER LEU ASP ALA VAL MET PRO HIS LEU MET HIS GLN          
SEQRES   6 C  196  HIS LYS SER ILE THR THR LEU GLN GLY GLU ASP ILE VAL          
SEQRES   7 C  196  PHE LEU ALA THR ASP ILE ASN LEU PRO GLY ALA VAL ASP          
SEQRES   8 C  196  TRP VAL MET MET GLN SER CYS PHE GLY PHE HIS PHE MET          
SEQRES   9 C  196  LEU VAL LEU GLU LYS GLN GLU LYS TYR ASP GLY HIS GLN          
SEQRES  10 C  196  GLN PHE PHE ALA ILE VAL GLN LEU ILE GLY THR ARG LYS          
SEQRES  11 C  196  GLN ALA GLU ASN PHE ALA TYR ARG LEU GLU LEU ASN GLY          
SEQRES  12 C  196  HIS ARG ARG ARG LEU THR TRP GLU ALA THR PRO ARG SER          
SEQRES  13 C  196  ILE HIS GLU GLY ILE ALA THR ALA ILE MET ASN SER ASP          
SEQRES  14 C  196  CYS LEU VAL PHE ASP THR SER ILE ALA GLN LEU PHE ALA          
SEQRES  15 C  196  GLU ASN GLY ASN LEU GLY ILE ASN VAL THR ILE SER MET          
SEQRES  16 C  196  CYS                                                          
SEQRES   1 D   14  ACE LYS LEU ARG PRO VAL ALA MET VAL ARG PRO PRK VAL          
SEQRES   2 D   14  ARG                                                          
MODRES 4I7D PRK B  123  LYS  N~6~-PROPANOYL-L-LYSINE                            
MODRES 4I7D PRK D  123  LYS  N~6~-PROPANOYL-L-LYSINE                            
HET    ACE  B 112       3                                                       
HET    PRK  B 123      13                                                       
HET    ACE  D 112       3                                                       
HET    PRK  D 123      13                                                       
HET     ZN  A 601       1                                                       
HET     ZN  A 602       1                                                       
HET    MPD  A 603       8                                                       
HET     ZN  C 601       1                                                       
HET     ZN  C 602       1                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     PRK N~6~-PROPANOYL-L-LYSINE                                          
HETNAM      ZN ZINC ION                                                         
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETSYN     PRK N(6)-PROPIONYLLYSINE                                             
FORMUL   2  ACE    2(C2 H4 O)                                                   
FORMUL   2  PRK    2(C9 H18 N2 O3)                                              
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   7  MPD    C6 H14 O2                                                    
FORMUL  10  HOH   *144(H2 O)                                                    
HELIX    1   1 LYS A   99  GLY A  104  5                                   6    
HELIX    2   2 PRO A  110  THR A  112  5                                   3    
HELIX    3   3 GLU A  113  CYS A  121  1                                   9    
HELIX    4   4 SER A  140  ASP A  142  5                                   3    
HELIX    5   5 ALA A  143  HIS A  152  1                                  10    
HELIX    6   6 THR A  214  GLU A  219  1                                   6    
HELIX    7   7 ILE A  247  ASN A  253  1                                   7    
HELIX    8   8 THR A  261  ALA A  268  1                                   8    
HELIX    9   9 TYR C  100  GLY C  104  5                                   5    
HELIX   10  10 GLU C  113  CYS C  121  1                                   9    
HELIX   11  11 SER C  140  ASP C  142  5                                   3    
HELIX   12  12 ALA C  143  HIS C  152  1                                  10    
HELIX   13  13 THR C  214  GLU C  219  1                                   6    
HELIX   14  14 ILE C  247  ASN C  253  1                                   7    
HELIX   15  15 THR C  261  ALA C  268  1                                   8    
SHEET    1   A 2 PHE A  96  PRO A  97  0                                        
SHEET    2   A 2 THR A 108  LEU A 109 -1  O  LEU A 109   N  PHE A  96           
SHEET    1   B 2 TYR A 126  SER A 127  0                                        
SHEET    2   B 2 GLN A 138  GLY A 139 -1  O  GLY A 139   N  TYR A 126           
SHEET    1   C 5 THR A 156  GLN A 159  0                                        
SHEET    2   C 5 VAL A 176  CYS A 184  1  O  MET A 181   N  THR A 156           
SHEET    3   C 5 PHE A 187  GLN A 196 -1  O  LYS A 195   N  VAL A 176           
SHEET    4   C 5 GLN A 204  LEU A 211 -1  O  PHE A 206   N  GLU A 194           
SHEET    5   C 5 LEU A 257  ASP A 260 -1  O  PHE A 259   N  PHE A 205           
SHEET    1   D 5 ARG A 241  SER A 242  0                                        
SHEET    2   D 5 GLN A 204  LEU A 211  1  N  LEU A 211   O  ARG A 241           
SHEET    3   D 5 PHE A 187  GLN A 196 -1  N  GLU A 194   O  PHE A 206           
SHEET    4   D 5 VAL A 176  CYS A 184 -1  N  VAL A 176   O  LYS A 195           
SHEET    5   D 5 PRK B 123  VAL B 124 -1  O  PRK B 123   N  ASP A 177           
SHEET    1   E10 VAL B 117  VAL B 120  0                                        
SHEET    2   E10 ASP A 162  ALA A 167  1  N  LEU A 166   O  VAL B 120           
SHEET    3   E10 LEU A 273  MET A 281 -1  O  ILE A 275   N  PHE A 165           
SHEET    4   E10 PHE A 221  GLY A 229 -1  N  ALA A 222   O  SER A 280           
SHEET    5   E10 ARG A 232  ALA A 238 -1  O  TRP A 236   N  LEU A 225           
SHEET    6   E10 ARG C 232  ALA C 238 -1  O  THR C 235   N  THR A 235           
SHEET    7   E10 PHE C 221  GLY C 229 -1  N  TYR C 223   O  ALA C 238           
SHEET    8   E10 LEU C 273  MET C 281 -1  O  SER C 280   N  ALA C 222           
SHEET    9   E10 ASP C 162  ALA C 167 -1  N  PHE C 165   O  ILE C 275           
SHEET   10   E10 VAL D 117  VAL D 120  1  O  ALA D 118   N  VAL C 164           
SHEET    1   F 2 PHE C  96  PRO C  97  0                                        
SHEET    2   F 2 THR C 108  LEU C 109 -1  O  LEU C 109   N  PHE C  96           
SHEET    1   G 2 TYR C 126  SER C 127  0                                        
SHEET    2   G 2 GLN C 138  GLY C 139 -1  O  GLY C 139   N  TYR C 126           
SHEET    1   H 5 THR C 157  GLN C 159  0                                        
SHEET    2   H 5 VAL C 176  CYS C 184  1  O  SER C 183   N  LEU C 158           
SHEET    3   H 5 PHE C 187  GLU C 197 -1  O  LEU C 191   N  MET C 180           
SHEET    4   H 5 GLN C 203  LEU C 211 -1  O  PHE C 206   N  GLU C 194           
SHEET    5   H 5 LEU C 257  ASP C 260 -1  O  PHE C 259   N  PHE C 205           
SHEET    1   I 5 ARG C 241  SER C 242  0                                        
SHEET    2   I 5 GLN C 203  LEU C 211  1  N  LEU C 211   O  ARG C 241           
SHEET    3   I 5 PHE C 187  GLU C 197 -1  N  GLU C 194   O  PHE C 206           
SHEET    4   I 5 VAL C 176  CYS C 184 -1  N  MET C 180   O  LEU C 191           
SHEET    5   I 5 PRK D 123  VAL D 124 -1  O  PRK D 123   N  ASP C 177           
LINK         SG  CYS A 130                 CAA PRK B 123     1555   1555  1.77  
LINK         SG  CYS C 130                 CAA PRK D 123     1555   1555  1.77  
LINK         C   ACE B 112                 N   LYS B 113     1555   1555  1.34  
LINK         C   PRO B 122                 N   PRK B 123     1555   1555  1.33  
LINK         C   PRK B 123                 N   VAL B 124     1555   1555  1.33  
LINK         C   ACE D 112                 N   LYS D 113     1555   1555  1.33  
LINK         C   PRO D 122                 N   PRK D 123     1555   1555  1.33  
LINK         C   PRK D 123                 N   VAL D 124     1555   1555  1.33  
LINK         NE2 HIS C 117                ZN    ZN C 602     1555   1555  2.00  
LINK         NE2 HIS C 152                ZN    ZN C 601     1555   1555  2.01  
LINK         NE2 HIS A 147                ZN    ZN A 601     1555   1555  2.02  
LINK         NE2 HIS A 117                ZN    ZN A 602     1555   1555  2.04  
LINK         NE2 HIS C 147                ZN    ZN C 601     1555   1555  2.11  
LINK         SG  CYS A 135                ZN    ZN A 601     1555   1555  2.14  
LINK         NE2 HIS A 152                ZN    ZN A 601     1555   1555  2.24  
LINK         SG  CYS A 105                ZN    ZN A 602     1555   1555  2.25  
LINK         SG  CYS A 128                ZN    ZN A 601     1555   1555  2.27  
LINK         SG  CYS C  98                ZN    ZN C 602     1555   1555  2.28  
LINK         SG  CYS C 128                ZN    ZN C 601     1555   1555  2.29  
LINK         SG  CYS C 105                ZN    ZN C 602     1555   1555  2.29  
LINK         SG  CYS C 135                ZN    ZN C 601     1555   1555  2.30  
LINK         SG  CYS A  98                ZN    ZN A 602     1555   1555  2.32  
LINK         SG  CYS C 121                ZN    ZN C 602     1555   1555  2.33  
LINK         SG  CYS A 121                ZN    ZN A 602     1555   1555  2.36  
SITE     1 AC1  2 PRO A  97  LYS B 113                                          
SITE     1 AC2  2 PRO C  97  LYS D 113                                          
SITE     1 AC3  4 CYS A 128  CYS A 135  HIS A 147  HIS A 152                    
SITE     1 AC4  4 CYS A  98  CYS A 105  HIS A 117  CYS A 121                    
SITE     1 AC5  5 ARG A 231  ARG A 233  ALA C 222  ALA C 238                    
SITE     2 AC5  5 HOH C 732                                                     
SITE     1 AC6  4 CYS C 128  CYS C 135  HIS C 147  HIS C 152                    
SITE     1 AC7  4 CYS C  98  CYS C 105  HIS C 117  CYS C 121                    
SITE     1 AC8 31 ALA A  91  ASN A  92  SER A  93  VAL A  94                    
SITE     2 AC8 31 LEU A  95  PHE A  96  PRO A  97  THR A 108                    
SITE     3 AC8 31 CYS A 130  LEU A 158  ASP A 162  ILE A 163                    
SITE     4 AC8 31 VAL A 164  PHE A 165  LEU A 166  THR A 168                    
SITE     5 AC8 31 LEU A 172  VAL A 176  ASP A 177  TRP A 178                    
SITE     6 AC8 31 VAL A 179  MET A 180  GLU A 194  ARG A 224                    
SITE     7 AC8 31 VAL A 277  THR A 278  ACE B 112  HOH B 201                    
SITE     8 AC8 31 HOH B 202  HOH B 203  HOH B 204                               
SITE     1 AC9 33 SER A 134  ASN C  92  SER C  93  VAL C  94                    
SITE     2 AC9 33 LEU C  95  PHE C  96  THR C 108  CYS C 130                    
SITE     3 AC9 33 PRO C 131  THR C 156  LEU C 158  GLN C 159                    
SITE     4 AC9 33 GLU C 161  ASP C 162  ILE C 163  VAL C 164                    
SITE     5 AC9 33 PHE C 165  LEU C 166  THR C 168  PRO C 173                    
SITE     6 AC9 33 ALA C 175  VAL C 176  ASP C 177  TRP C 178                    
SITE     7 AC9 33 VAL C 179  GLU C 194  GLU C 197  ACE D 112                    
SITE     8 AC9 33 HOH D 201  HOH D 202  HOH D 203  HOH D 204                    
SITE     9 AC9 33 HOH D 205                                                     
CRYST1  160.977  160.977  160.977  90.00  90.00  90.00 I 2 3        48          
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      0.006212  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006212  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006212        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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