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Database: PDB
Entry: 4I7B
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HEADER    LIGASE/LIGASE INHIBITOR                 30-NOV-12   4I7B              
TITLE     SIAH1 BOUND TO SYNTHETIC PEPTIDE (ACE)KLRPV(ABA)MVRPTVR               
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                                                      
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, LIGASE-LIGASE     
KEYWDS   2 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 4I7B    1       JRNL                                     
REVDAT   1   14-AUG-13 4I7B    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.    3.00 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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 8126                           
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 375                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 528                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.85                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 26                           
REMARK   3   BIN FREE R VALUE                    : 0.4370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3123                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 14                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 101.82                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.76000                                             
REMARK   3    B22 (A**2) : 1.99000                                              
REMARK   3    B33 (A**2) : -1.00000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.11000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.506         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.457         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 56.542        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3195 ; 0.005 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  2140 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4327 ; 0.907 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5217 ; 0.891 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   392 ; 5.019 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   146 ;30.550 ;23.973       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   535 ;12.575 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;10.243 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   482 ; 0.056 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3536 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   650 ; 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 : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    92        A   125                          
REMARK   3    RESIDUE RANGE :   A   602        A   602                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.5580  21.4620   8.9020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9104 T22:   0.5575                                     
REMARK   3      T33:   0.8199 T12:   0.1262                                     
REMARK   3      T13:   0.1251 T23:   0.0238                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  26.2133 L22:   7.6307                                     
REMARK   3      L33:  13.4758 L12:   8.8796                                     
REMARK   3      L13:   8.1854 L23:  -2.4407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5399 S12:  -0.8224 S13:  -1.5320                       
REMARK   3      S21:   0.5611 S22:   0.2823 S23:  -0.9057                       
REMARK   3      S31:   0.2683 S32:   0.3214 S33:   0.2576                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    94        C   125                          
REMARK   3    RESIDUE RANGE :   C   602        C   602                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5610 -49.4020  13.9160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4546 T22:   0.7599                                     
REMARK   3      T33:   1.1354 T12:  -0.0431                                     
REMARK   3      T13:  -0.0516 T23:  -0.0532                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  20.1159 L22:   7.2596                                     
REMARK   3      L33:  10.3948 L12:   9.2959                                     
REMARK   3      L13:  11.9519 L23:   8.5899                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1480 S12:  -0.3519 S13:  -0.2635                       
REMARK   3      S21:  -0.8537 S22:   0.0774 S23:  -0.0657                       
REMARK   3      S31:  -1.1474 S32:  -0.2412 S33:   0.0706                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   126        A   154                          
REMARK   3    RESIDUE RANGE :   A   601        A   601                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7890  12.1780   0.6290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5553 T22:   0.2990                                     
REMARK   3      T33:   0.2887 T12:   0.1160                                     
REMARK   3      T13:   0.1778 T23:   0.1947                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.7375 L22:  15.0533                                     
REMARK   3      L33:  11.6014 L12:   3.2825                                     
REMARK   3      L13:   3.5897 L23:   0.1873                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1402 S12:   0.7701 S13:   0.2207                       
REMARK   3      S21:  -0.3397 S22:   1.2278 S23:   0.2200                       
REMARK   3      S31:  -0.3295 S32:  -0.7930 S33:  -0.0876                       
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 :   A   155        A   282                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.2170  -3.9630  10.5670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2090 T22:   0.2240                                     
REMARK   3      T33:   0.0856 T12:   0.1379                                     
REMARK   3      T13:   0.1048 T23:   0.0444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9936 L22:   9.1466                                     
REMARK   3      L33:   4.6248 L12:   0.9742                                     
REMARK   3      L13:   0.2923 L23:  -1.3278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1020 S12:   0.2899 S13:  -0.0587                       
REMARK   3      S21:  -0.3571 S22:   0.3388 S23:   0.0724                       
REMARK   3      S31:  -0.2065 S32:  -0.1541 S33:  -0.2368                       
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 :   C   126        C   154                          
REMARK   3    RESIDUE RANGE :   C   601        C   601                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.0090 -40.5960  24.4830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6732 T22:   0.5694                                     
REMARK   3      T33:   0.9933 T12:   0.1874                                     
REMARK   3      T13:   0.1102 T23:   0.2511                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  26.4133 L22:   7.5621                                     
REMARK   3      L33:   2.0992 L12:  -2.5189                                     
REMARK   3      L13:  -0.0240 L23:   3.6323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6132 S12:  -0.4970 S13:  -2.0215                       
REMARK   3      S21:   0.5758 S22:  -0.1124 S23:  -1.2516                       
REMARK   3      S31:   0.9773 S32:   0.0979 S33:  -0.5009                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   155        C   282                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.9330 -21.8530  22.7460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1474 T22:   0.1306                                     
REMARK   3      T33:   0.1862 T12:   0.0653                                     
REMARK   3      T13:   0.0953 T23:   0.1208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9593 L22:   9.0151                                     
REMARK   3      L33:   8.5376 L12:   0.4936                                     
REMARK   3      L13:   1.8731 L23:  -3.3728                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0321 S12:   0.0808 S13:   0.0711                       
REMARK   3      S21:   0.3171 S22:  -0.2767 S23:  -0.6955                       
REMARK   3      S31:   0.2635 S32:   0.0216 S33:   0.3088                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   114        B   124                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0124  -3.9238   7.0284              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1298 T22:   0.4925                                     
REMARK   3      T33:   0.1018 T12:  -0.0642                                     
REMARK   3      T13:  -0.0492 T23:   0.0222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.2153 L22:   8.4220                                     
REMARK   3      L33:   5.7070 L12:   2.0992                                     
REMARK   3      L13:  -9.5339 L23:   1.7701                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4892 S12:   1.5730 S13:   0.5928                       
REMARK   3      S21:  -0.2127 S22:   0.4200 S23:   0.7225                       
REMARK   3      S31:   0.2735 S32:  -0.8008 S33:   0.0692                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   114        D   124                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.0845 -20.2568  28.7835              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1468 T22:   0.1045                                     
REMARK   3      T33:   0.8200 T12:   0.0049                                     
REMARK   3      T13:  -0.1518 T23:   0.1007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2486 L22:   4.2273                                     
REMARK   3      L33:  15.7363 L12:   4.6830                                     
REMARK   3      L13:   1.2997 L23:   1.3357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7766 S12:  -0.1527 S13:  -0.2342                       
REMARK   3      S21:   0.7066 S22:  -0.1349 S23:  -0.4076                       
REMARK   3      S31:   0.7278 S32:   0.5944 S33:  -0.6417                       
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 4I7B 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 RCSB076394.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8152                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
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     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
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 2A25 CHAIN A                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG6000, 5% MPD, 100 MM HEPES, PH    
REMARK 280  6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       43.95650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: 1290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11320 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: 1310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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-117E1 IS OLIGOPEPTIDE, A   
REMARK 400 MEMBER OF INHIBITOR CLASS.                                           
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: MODIFIED PROTEIN PHYLLOPOD PEPTIDE BI-117E1                  
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     ACE B   112                                                      
REMARK 465     LYS B   113                                                      
REMARK 465     ARG B   125                                                      
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     ASN C    92                                                      
REMARK 465     SER C    93                                                      
REMARK 465     LYS C   198                                                      
REMARK 465     TYR C   199                                                      
REMARK 465     ACE D   112                                                      
REMARK 465     LYS D   113                                                      
REMARK 465     ARG D   125                                                      
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    ASN A  92       31.68   -155.37                                   
REMARK 500    ASP A 255       58.17    -96.77                                   
REMARK 500    CYS A 256     -171.63   -174.20                                   
REMARK 500    PHE C 123       58.29    -91.49                                   
REMARK 500    HIS C 152       71.10   -118.79                                   
REMARK 500    ASP C 255       59.57    -93.07                                   
REMARK 500    CYS C 256     -173.94   -170.78                                   
REMARK 500    ASN C 270       62.03     37.75                                   
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 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 147   NE2                                                    
REMARK 620 2 HIS C 152   NE2 102.7                                              
REMARK 620 3 CYS C 135   SG  120.3 122.5                                        
REMARK 620 4 CYS C 128   SG  106.2  97.7 104.0                                  
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 CYS A 105   SG                                                     
REMARK 620 2 HIS A 117   NE2 105.6                                              
REMARK 620 3 CYS A  98   SG  111.8 114.5                                        
REMARK 620 4 CYS A 121   SG  106.4 100.6 116.8                                  
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 HIS A 147   NE2 112.0                                              
REMARK 620 3 CYS A 135   SG  115.0 105.8                                        
REMARK 620 4 CYS A 128   SG  115.6 102.8 104.4                                  
REMARK 620 N                    1     2     3                                   
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 CYS C 105   SG                                                     
REMARK 620 2 HIS C 117   NE2  83.9                                              
REMARK 620 3 CYS C 121   SG  114.6 119.6                                        
REMARK 620 4 CYS C  98   SG  115.2 114.4 107.8                                  
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 ZN C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF PROTEIN PHYLLOPOD      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
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: 4I7C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4I7D   RELATED DB: PDB                                   
DBREF  4I7B A   90   282  UNP    Q8IUQ4   SIAH1_HUMAN     90    282             
DBREF  4I7B B  113   125  UNP    Q27934   PHYL_DROME     113    125             
DBREF  4I7B C   90   282  UNP    Q8IUQ4   SIAH1_HUMAN     90    282             
DBREF  4I7B D  113   125  UNP    Q27934   PHYL_DROME     113    125             
SEQADV 4I7B GLY A   87  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7B SER A   88  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7B HIS A   89  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7B ACE B  112  UNP  Q27934              ACETYLATION                    
SEQADV 4I7B GLY C   87  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7B SER C   88  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7B HIS C   89  UNP  Q8IUQ4              EXPRESSION TAG                 
SEQADV 4I7B ACE D  112  UNP  Q27934              ACETYLATION                    
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 ABA MET VAL ARG PRO THR 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 ABA MET VAL ARG PRO THR VAL          
SEQRES   2 D   14  ARG                                                          
MODRES 4I7B ABA B  118  ALA  ALPHA-AMINOBUTYRIC ACID                            
MODRES 4I7B ABA D  118  ALA  ALPHA-AMINOBUTYRIC ACID                            
HET    ABA  B 118       6                                                       
HET    ABA  D 118       6                                                       
HET     ZN  A 601       1                                                       
HET     ZN  A 602       1                                                       
HET     ZN  C 601       1                                                       
HET     ZN  C 602       1                                                       
HETNAM     ABA ALPHA-AMINOBUTYRIC ACID                                          
HETNAM      ZN ZINC ION                                                         
FORMUL   2  ABA    2(C4 H9 N O2)                                                
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   9  HOH   *14(H2 O)                                                     
HELIX    1   1 TYR A  100  GLY A  104  5                                   5    
HELIX    2   2 PRO A  110  GLU A  113  5                                   4    
HELIX    3   3 LYS A  114  GLU A  119  1                                   6    
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  GLU C  118  1                                   9    
HELIX   10  10 SER C  140  HIS C  152  1                                  13    
HELIX   11  11 THR C  214  GLU C  219  1                                   6    
HELIX   12  12 ILE C  247  ASN C  253  1                                   7    
HELIX   13  13 THR C  261  PHE C  267  1                                   7    
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  ILE A 212 -1  O  PHE A 206   N  GLU A 194           
SHEET    5   C 5 ARG A 241  SER A 242  1  O  ARG A 241   N  LEU A 211           
SHEET    1   D 5 THR A 157  GLN A 159  0                                        
SHEET    2   D 5 VAL A 176  CYS A 184  1  O  SER A 183   N  LEU A 158           
SHEET    3   D 5 PHE A 187  GLN A 196 -1  O  LEU A 191   N  MET A 180           
SHEET    4   D 5 GLN A 204  ILE A 212 -1  O  PHE A 206   N  GLU A 194           
SHEET    5   D 5 LEU A 257  ASP A 260 -1  O  PHE A 259   N  PHE A 205           
SHEET    1   E 9 VAL B 117  VAL B 120  0                                        
SHEET    2   E 9 ASP A 162  THR A 168  1  N  VAL A 164   O  ABA B 118           
SHEET    3   E 9 ASN A 272  MET A 281 -1  O  LEU A 273   N  ALA A 167           
SHEET    4   E 9 PHE A 221  GLY A 229 -1  N  ALA A 222   O  SER A 280           
SHEET    5   E 9 ARG A 232  ALA A 238 -1  O  TRP A 236   N  LEU A 225           
SHEET    6   E 9 ARG C 232  ALA C 238 -1  O  THR C 235   N  THR A 235           
SHEET    7   E 9 PHE C 221  GLY C 229 -1  N  GLY C 229   O  ARG C 232           
SHEET    8   E 9 ASN C 272  MET C 281 -1  O  ASN C 276   N  GLU C 226           
SHEET    9   E 9 ALA C 268  GLU C 269 -1  N  GLU C 269   O  ASN C 272           
SHEET    1   F10 VAL B 117  VAL B 120  0                                        
SHEET    2   F10 ASP A 162  THR A 168  1  N  VAL A 164   O  ABA B 118           
SHEET    3   F10 ASN A 272  MET A 281 -1  O  LEU A 273   N  ALA A 167           
SHEET    4   F10 PHE A 221  GLY A 229 -1  N  ALA A 222   O  SER A 280           
SHEET    5   F10 ARG A 232  ALA A 238 -1  O  TRP A 236   N  LEU A 225           
SHEET    6   F10 ARG C 232  ALA C 238 -1  O  THR C 235   N  THR A 235           
SHEET    7   F10 PHE C 221  GLY C 229 -1  N  GLY C 229   O  ARG C 232           
SHEET    8   F10 ASN C 272  MET C 281 -1  O  ASN C 276   N  GLU C 226           
SHEET    9   F10 ASP C 162  THR C 168 -1  N  PHE C 165   O  ILE C 275           
SHEET   10   F10 VAL D 117  VAL D 120  1  O  ABA D 118   N  LEU C 166           
SHEET    1   G 2 PHE C  96  PRO C  97  0                                        
SHEET    2   G 2 THR C 108  LEU C 109 -1  O  LEU C 109   N  PHE C  96           
SHEET    1   H 2 TYR C 126  SER C 127  0                                        
SHEET    2   H 2 GLN C 138  GLY C 139 -1  O  GLY C 139   N  TYR C 126           
SHEET    1   I 5 THR C 157  GLN C 159  0                                        
SHEET    2   I 5 VAL C 176  CYS C 184  1  O  SER C 183   N  LEU C 158           
SHEET    3   I 5 PHE C 187  GLN C 196 -1  O  LEU C 193   N  TRP C 178           
SHEET    4   I 5 GLN C 204  LEU C 211 -1  O  GLN C 210   N  MET C 190           
SHEET    5   I 5 ARG C 241  SER C 242  1  O  ARG C 241   N  LEU C 211           
SHEET    1   J 5 THR C 157  GLN C 159  0                                        
SHEET    2   J 5 VAL C 176  CYS C 184  1  O  SER C 183   N  LEU C 158           
SHEET    3   J 5 PHE C 187  GLN C 196 -1  O  LEU C 193   N  TRP C 178           
SHEET    4   J 5 GLN C 204  LEU C 211 -1  O  GLN C 210   N  MET C 190           
SHEET    5   J 5 LEU C 257  ASP C 260 -1  O  PHE C 259   N  PHE C 205           
LINK         C   VAL B 117                 N   ABA B 118     1555   1555  1.33  
LINK         C   ABA B 118                 N   MET B 119     1555   1555  1.33  
LINK         C   VAL D 117                 N   ABA D 118     1555   1555  1.33  
LINK         C   ABA D 118                 N   MET D 119     1555   1555  1.33  
LINK         NE2 HIS C 147                ZN    ZN C 601     1555   1555  2.00  
LINK         SG  CYS A 105                ZN    ZN A 602     1555   1555  2.01  
LINK         NE2 HIS A 152                ZN    ZN A 601     1555   1555  2.09  
LINK         NE2 HIS A 147                ZN    ZN A 601     1555   1555  2.09  
LINK         SG  CYS C 105                ZN    ZN C 602     1555   1555  2.13  
LINK         NE2 HIS C 152                ZN    ZN C 601     1555   1555  2.16  
LINK         NE2 HIS C 117                ZN    ZN C 602     1555   1555  2.17  
LINK         SG  CYS A 135                ZN    ZN A 601     1555   1555  2.21  
LINK         SG  CYS C 121                ZN    ZN C 602     1555   1555  2.24  
LINK         SG  CYS C 135                ZN    ZN C 601     1555   1555  2.27  
LINK         SG  CYS A 128                ZN    ZN A 601     1555   1555  2.31  
LINK         NE2 HIS A 117                ZN    ZN A 602     1555   1555  2.42  
LINK         SG  CYS C 128                ZN    ZN C 601     1555   1555  2.46  
LINK         SG  CYS A  98                ZN    ZN A 602     1555   1555  2.47  
LINK         SG  CYS A 121                ZN    ZN A 602     1555   1555  2.56  
LINK         SG  CYS C  98                ZN    ZN C 602     1555   1555  2.64  
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  4 CYS C 128  CYS C 135  HIS C 147  HIS C 152                    
SITE     1 AC4  4 CYS C  98  CYS C 105  HIS C 117  CYS C 121                    
SITE     1 AC5 19 THR A 156  LEU A 158  ASP A 162  ILE A 163                    
SITE     2 AC5 19 VAL A 164  PHE A 165  LEU A 166  THR A 168                    
SITE     3 AC5 19 ALA A 175  VAL A 176  ASP A 177  TRP A 178                    
SITE     4 AC5 19 VAL A 179  MET A 180  ASN A 276  THR A 278                    
SITE     5 AC5 19 HOH B 201  ALA C 268  GLU C 269                               
SITE     1 AC6 17 HIS A 230  THR C 156  LEU C 158  ASP C 162                    
SITE     2 AC6 17 ILE C 163  VAL C 164  PHE C 165  LEU C 166                    
SITE     3 AC6 17 THR C 168  VAL C 176  ASP C 177  TRP C 178                    
SITE     4 AC6 17 VAL C 179  MET C 180  ASN C 276  CYS C 282                    
SITE     5 AC6 17 HOH D 201                                                     
CRYST1   39.745   87.913   59.884  90.00 100.59  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.025160  0.000000  0.004704        0.00000                         
SCALE2      0.000000  0.011375  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016988        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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