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Database: PDB
Entry: 4I7C
LinkDB: 4I7C
Original site: 4I7C 
HEADER    LIGASE/LIGASE INHIBITOR                 30-NOV-12   4I7C              
TITLE     SIAH1 MUTANT BOUND TO SYNTHETIC PEPTIDE (ACE)KLRPV(23P)MVRPWVR        
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 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PROTEIN PHYLLOPOD;                                         
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: SIAH-BINDING PEPTIDE (UNP RESIDUES 113-125);               
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 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: SIAH1, HUMSIAH;                                                
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 4I7C    1       JRNL                                     
REVDAT   1   14-AUG-13 4I7C    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.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 17329                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 938                             
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1205                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 62                           
REMARK   3   BIN FREE R VALUE                    : 0.4280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3198                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 7                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 86.47                          
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): 0.444         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.271         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.222         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.588        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3334 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2266 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4519 ; 1.163 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5517 ; 0.802 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   408 ; 5.841 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;34.124 ;23.800       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   559 ;14.706 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;16.299 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   494 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3689 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   687 ; 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): -56.1560  61.3780 -14.0860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0412 T22:   0.1578                                     
REMARK   3      T33:   0.0827 T12:   0.0310                                     
REMARK   3      T13:  -0.0243 T23:  -0.1129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1907 L22:   2.5528                                     
REMARK   3      L33:   1.9424 L12:   0.7811                                     
REMARK   3      L13:  -0.0235 L23:  -0.2342                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1023 S12:  -0.0517 S13:   0.0710                       
REMARK   3      S21:  -0.1025 S22:  -0.0967 S23:   0.1374                       
REMARK   3      S31:  -0.1955 S32:   0.0095 S33:  -0.0057                       
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   113        B   125                          
REMARK   3    ORIGIN FOR THE GROUP (A): -63.1430  68.2590 -16.5500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1704 T22:   0.1603                                     
REMARK   3      T33:   0.2159 T12:   0.1165                                     
REMARK   3      T13:  -0.0830 T23:  -0.1503                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.2885 L22:   4.6180                                     
REMARK   3      L33:   9.6167 L12:   6.8389                                     
REMARK   3      L13: -10.9198 L23:  -4.4708                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7787 S12:  -0.3206 S13:   0.4635                       
REMARK   3      S21:  -0.0150 S22:  -0.4260 S23:   0.4006                       
REMARK   3      S31:  -0.7968 S32:   0.0771 S33:  -0.3527                       
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): -54.8570  38.7970 -19.8970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0423 T22:   0.0960                                     
REMARK   3      T33:   0.1509 T12:  -0.0041                                     
REMARK   3      T13:   0.0349 T23:  -0.0852                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3689 L22:   2.7639                                     
REMARK   3      L33:   2.4896 L12:   0.5790                                     
REMARK   3      L13:   0.2094 L23:   0.3909                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0871 S12:  -0.1062 S13:  -0.1588                       
REMARK   3      S21:  -0.1525 S22:   0.0581 S23:  -0.4213                       
REMARK   3      S31:   0.2487 S32:  -0.0781 S33:   0.0290                       
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   113        D   125                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.6630  31.0970 -16.4410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4268 T22:   0.3026                                     
REMARK   3      T33:   1.1048 T12:  -0.0426                                     
REMARK   3      T13:  -0.0908 T23:  -0.1375                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5101 L22:   7.0835                                     
REMARK   3      L33:  27.8387 L12:   4.1481                                     
REMARK   3      L13:  -8.2949 L23: -10.8687                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1416 S12:   0.0334 S13:   0.4169                       
REMARK   3      S21:  -0.4306 S22:   0.3839 S23:  -1.3465                       
REMARK   3      S31:   2.4221 S32:  -0.8330 S33:  -0.2423                       
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): -49.4050  79.1570  -9.1170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2803 T22:   0.2199                                     
REMARK   3      T33:   0.3140 T12:  -0.1483                                     
REMARK   3      T13:  -0.1109 T23:  -0.0584                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2440 L22:   2.7127                                     
REMARK   3      L33:  10.3911 L12:  -0.0669                                     
REMARK   3      L13:  -0.8102 L23:  -1.4839                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4304 S12:   0.5025 S13:   0.8644                       
REMARK   3      S21:   0.4554 S22:  -0.1104 S23:   0.1138                       
REMARK   3      S31:  -1.5344 S32:   0.7533 S33:   0.5408                       
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): -57.9580  22.8260 -30.7440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2807 T22:   0.1031                                     
REMARK   3      T33:   0.1873 T12:  -0.0418                                     
REMARK   3      T13:   0.0743 T23:  -0.1275                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3289 L22:   3.0688                                     
REMARK   3      L33:   6.6896 L12:   0.0279                                     
REMARK   3      L13:   2.8466 L23:  -1.2297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2208 S12:   0.2923 S13:  -0.5277                       
REMARK   3      S21:  -0.5114 S22:  -0.0220 S23:   0.0092                       
REMARK   3      S31:   0.9310 S32:   0.3383 S33:  -0.1989                       
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): -28.0890  71.4420   2.4920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2554 T22:   0.5018                                     
REMARK   3      T33:   0.1115 T12:  -0.1969                                     
REMARK   3      T13:   0.0324 T23:  -0.1385                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.6457 L22:   1.5785                                     
REMARK   3      L33:   9.9293 L12:  -4.3584                                     
REMARK   3      L13:   8.8230 L23:  -3.8247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3502 S12:   0.9074 S13:   0.7766                       
REMARK   3      S21:  -0.2275 S22:  -0.1245 S23:  -0.2176                       
REMARK   3      S31:   0.9279 S32:   0.0015 S33:   0.4747                       
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    91        C   124                          
REMARK   3    RESIDUE RANGE :   C   602        C   602                          
REMARK   3    ORIGIN FOR THE GROUP (A): -77.7300  31.5330 -43.7770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2552 T22:   0.1332                                     
REMARK   3      T33:   0.1592 T12:  -0.1522                                     
REMARK   3      T13:   0.0737 T23:  -0.0804                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.1193 L22:   1.8342                                     
REMARK   3      L33:   5.1533 L12:  -1.3411                                     
REMARK   3      L13:   3.0466 L23:  -1.1260                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3134 S12:   0.2149 S13:   0.4628                       
REMARK   3      S21:   0.0452 S22:   0.0073 S23:   0.0610                       
REMARK   3      S31:  -0.3742 S32:   0.4864 S33:  -0.3207                       
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 4I7C 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 RCSB076395.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAY-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                       : BL9-2                              
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                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18317                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.400                             
REMARK 200  R MERGE                    (I) : 0.12300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.63700                            
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: PDB ENTRY 4I7D                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90                     
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       82.11500            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       82.11500            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       82.11500            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       82.11500            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       82.11500            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       82.11500            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       82.11500            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       82.11500            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       82.11500            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       82.11500            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       82.11500            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       82.11500            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       82.11500            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       82.11500            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       82.11500            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       82.11500            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       82.11500            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       82.11500            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       82.11500            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       82.11500            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       82.11500            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       82.11500            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       82.11500            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       82.11500            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       82.11500            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       82.11500            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       82.11500            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       82.11500            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       82.11500            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       82.11500            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       82.11500            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       82.11500            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       82.11500            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       82.11500            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       82.11500            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       82.11500            
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: 1890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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: 1820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE MODIFIED PROTEIN PHYLLOPOD PEPTIDE BI-117C3 IS OLIGOPEPTIDE, A   
REMARK 400 MEMBER OF INHIBITOR CLASS.                                           
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: MODIFIED PROTEIN PHYLLOPOD PEPTIDE BI-117C3                  
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     TYR A   199                                                      
REMARK 465     ASP A   200                                                      
REMARK 465     GLY A   201                                                      
REMARK 465     HIS A   202                                                      
REMARK 465     ACE B   112                                                      
REMARK 465     GLY C    87                                                      
REMARK 465     SER C    88                                                      
REMARK 465     HIS C    89                                                      
REMARK 465     VAL C    90                                                      
REMARK 465     TYR C   199                                                      
REMARK 465     ASP C   200                                                      
REMARK 465     ACE D   112                                                      
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    HIS A 111      -38.39    -37.89                                   
REMARK 500    PHE A 185       29.98     49.49                                   
REMARK 500    HIS A 230      106.90    -56.27                                   
REMARK 500    CYS A 256     -178.41    177.31                                   
REMARK 500    ASN C  92      -78.09    -66.32                                   
REMARK 500    CYS C 256     -166.27   -168.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 602  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 117   NE2                                                    
REMARK 620 2 CYS C 105   SG  105.2                                              
REMARK 620 3 CYS C  98   SG  106.6 114.4                                        
REMARK 620 4 CYS C 121   SG  110.7 103.5 116.0                                  
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 152   NE2                                                    
REMARK 620 2 CYS A 135   SG  135.7                                              
REMARK 620 3 HIS A 147   NE2 107.1  99.8                                        
REMARK 620 4 CYS A 128   SG  104.8 102.7 102.7                                  
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 147   NE2                                                    
REMARK 620 2 HIS C 152   NE2 105.8                                              
REMARK 620 3 CYS C 128   SG  108.1 115.9                                        
REMARK 620 4 CYS C 135   SG  103.8 111.9 110.5                                  
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  104.7                                              
REMARK 620 3 CYS A  98   SG   98.4 118.3                                        
REMARK 620 4 CYS A 121   SG  105.2 113.7 113.9                                  
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 ZN A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 603                 
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: 4I7D   RELATED DB: PDB                                   
DBREF  4I7C A   90   282  UNP    Q8IUQ4   SIAH1_HUMAN     90    282             
DBREF  4I7C B  113   125  UNP    Q27934   PHYL_DROME     113    125             
DBREF  4I7C C   90   282  UNP    Q8IUQ4   SIAH1_HUMAN     90    282             
DBREF  4I7C D  113   125  UNP    Q27934   PHYL_DROME     113    125             
SEQADV 4I7C GLY A   87  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7C SER A   88  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7C HIS A   89  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7C CYS A  156  UNP  Q8IUQ4    THR   156 ENGINEERED MUTATION            
SEQADV 4I7C ACE B  112  UNP  Q27934              ACETYLATION                    
SEQADV 4I7C TRP B  123  UNP  Q27934    THR   123 ENGINEERED MUTATION            
SEQADV 4I7C GLY C   87  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7C SER C   88  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7C HIS C   89  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7C CYS C  156  UNP  Q8IUQ4    THR   156 ENGINEERED MUTATION            
SEQADV 4I7C ACE D  112  UNP  Q27934              ACETYLATION                    
SEQADV 4I7C TRP 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 CYS 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 23P MET VAL ARG PRO TRP 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 CYS 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 23P MET VAL ARG PRO TRP VAL          
SEQRES   2 D   14  ARG                                                          
MODRES 4I7C 23P B  118  ALA  3-(PROPANOYLAMINO)-L-ALANINE                       
MODRES 4I7C 23P D  118  ALA  3-(PROPANOYLAMINO)-L-ALANINE                       
HET    23P  B 118      20                                                       
HET    23P  D 118      20                                                       
HET     ZN  A 601       1                                                       
HET     ZN  A 602       1                                                       
HET     ZN  C 601       1                                                       
HET    MPD  A 603       8                                                       
HET     ZN  C 602       1                                                       
HET    MPD  C 603       8                                                       
HETNAM     23P 3-(PROPANOYLAMINO)-L-ALANINE                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
FORMUL   2  23P    2(C6 H12 N2 O3)                                              
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   8  MPD    2(C6 H14 O2)                                                 
FORMUL  11  HOH   *7(H2 O)                                                      
HELIX    1   1 LYS A   99  SER A  102  5                                   4    
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  HIS A  152  1                                  13    
HELIX    5   5 THR A  214  GLU A  219  1                                   6    
HELIX    6   6 ILE A  247  ASN A  253  1                                   7    
HELIX    7   7 THR A  261  ALA A  268  1                                   8    
HELIX    8   8 TYR C  100  GLY C  104  5                                   5    
HELIX    9   9 PRO C  110  CYS C  121  1                                  12    
HELIX   10  10 SER C  140  ASP C  142  5                                   3    
HELIX   11  11 ALA C  143  HIS C  152  1                                  10    
HELIX   12  12 THR C  214  GLU C  219  1                                   6    
HELIX   13  13 ILE C  247  SER C  254  1                                   8    
HELIX   14  14 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 157  GLN A 159  0                                        
SHEET    2   C 5 VAL A 176  CYS A 184  1  O  SER A 183   N  LEU A 158           
SHEET    3   C 5 PHE A 187  GLN A 196 -1  O  LEU A 191   N  MET A 180           
SHEET    4   C 5 GLN A 204  LEU A 211 -1  O  GLN A 210   N  MET A 190           
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  MET A 190   O  GLN A 210           
SHEET    4   D 5 VAL A 176  CYS A 184 -1  N  MET A 180   O  LEU A 191           
SHEET    5   D 5 TRP B 123  VAL B 124 -1  O  TRP 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  ARG A 224   O  THR A 278           
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  LEU C 225   O  TRP C 236           
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  VAL D 120   N  LEU C 166           
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  PHE C 189   N  GLN C 182           
SHEET    4   H 5 GLN C 203  LEU C 211 -1  O  GLN C 204   N  GLN C 196           
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  GLN C 196   O  GLN C 204           
SHEET    4   I 5 VAL C 176  CYS C 184 -1  N  GLN C 182   O  PHE C 189           
SHEET    5   I 5 TRP D 123  VAL D 124 -1  O  TRP D 123   N  ASP C 177           
LINK         SG ACYS A 156                 CZ A23P B 118     1555   1555  1.76  
LINK         SG BCYS A 156                 CZ B23P B 118     1555   1555  1.76  
LINK         SG ACYS C 156                 CZ A23P D 118     1555   1555  1.75  
LINK         SG BCYS C 156                 CZ B23P D 118     1555   1555  1.75  
LINK         C  A23P B 118                 N   MET B 119     1555   1555  1.33  
LINK         C  B23P B 118                 N   MET B 119     1555   1555  1.33  
LINK         C  A23P D 118                 N   MET D 119     1555   1555  1.33  
LINK         C  B23P D 118                 N   MET D 119     1555   1555  1.33  
LINK         C   VAL B 117                 N  A23P B 118     1555   1555  1.33  
LINK         C   VAL B 117                 N  B23P B 118     1555   1555  1.33  
LINK         C   VAL D 117                 N  A23P D 118     1555   1555  1.33  
LINK         C   VAL D 117                 N  B23P D 118     1555   1555  1.33  
LINK         NE2 HIS C 117                ZN    ZN C 602     1555   1555  1.95  
LINK         NE2 HIS A 152                ZN    ZN A 601     1555   1555  2.02  
LINK         NE2 HIS C 147                ZN    ZN C 601     1555   1555  2.02  
LINK         SG  CYS A 135                ZN    ZN A 601     1555   1555  2.03  
LINK         NE2 HIS C 152                ZN    ZN C 601     1555   1555  2.05  
LINK         NE2 HIS A 117                ZN    ZN A 602     1555   1555  2.07  
LINK         NE2 HIS A 147                ZN    ZN A 601     1555   1555  2.12  
LINK         SG  CYS C 128                ZN    ZN C 601     1555   1555  2.14  
LINK         SG  CYS A 128                ZN    ZN A 601     1555   1555  2.15  
LINK         SG  CYS C 135                ZN    ZN C 601     1555   1555  2.16  
LINK         SG  CYS A 105                ZN    ZN A 602     1555   1555  2.18  
LINK         SG  CYS C 105                ZN    ZN C 602     1555   1555  2.20  
LINK         SG  CYS A  98                ZN    ZN A 602     1555   1555  2.23  
LINK         SG  CYS A 121                ZN    ZN A 602     1555   1555  2.23  
LINK         SG  CYS C  98                ZN    ZN C 602     1555   1555  2.31  
LINK         SG  CYS C 121                ZN    ZN C 602     1555   1555  2.33  
SITE     1 AC1  4 CYS A 128  CYS A 135  HIS A 147  HIS A 152                    
SITE     1 AC2  4 CYS A  98  CYS A 105  HIS A 117  CYS A 121                    
SITE     1 AC3  6 CYS A 130  PRO A 131  HIS A 152  SER A 154                    
SITE     2 AC3  6 ASP A 177  TRP B 123                                          
SITE     1 AC4  4 CYS C 128  CYS C 135  HIS C 147  HIS C 152                    
SITE     1 AC5  4 CYS C  98  CYS C 105  HIS C 117  CYS C 121                    
SITE     1 AC6  4 PRO C 131  HIS C 152  SER C 154  TRP D 123                    
CRYST1  164.230  164.230  164.230  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      0.006089  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006089  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006089        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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