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Entry: 2WG3
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HEADER    SIGNALING PROTEIN                       15-APR-09   2WG3              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN HUMAN HEDGEHOG-              
TITLE    2 INTERACTING PROTEIN HIP AND DESERT HEDGEHOG WITHOUT CALCIUM          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DESERT HEDGEHOG PROTEIN N-PRODUCT;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: N-TERMINAL SIGNALLING DOMAIN OF DHH, RESIDUES 40-194;      
COMPND   5 SYNONYM: DESERT HEDGEHOG PROTEIN, DHH, HHG-3;                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HEDGEHOG-INTERACTING PROTEIN;                              
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 FRAGMENT: C-TERMINAL DOMAIN OF HIP, RESIDUES 214-670;                
COMPND  11 SYNONYM: HHIP, HIP, HEDGEHOG-INTERACTING PROTEIN HIP;                
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET22B;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: HUMAN EMBRYONIC KIDNEY (HEK) 293T       
SOURCE  17  CELLS;                                                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    LIPOPROTEIN, DEVELOPMENT, MEMBRANE, SECRETED, PROTEASE, PALMITATE,    
KEYWDS   2 HYDROLASE, DEVELOPMENTAL PROTEIN, AUTOCATALYTIC CLEAVAGE, SIGNAL     
KEYWDS   3 TRANSDUCTION, EGF-LIKE DOMAIN, DISEASE MUTATION, HEDGEHOG            
KEYWDS   4 SIGNALING, GLYCOPROTEIN, CELL MEMBRANE, DISULFIDE BOND, SIGNALING    
KEYWDS   5 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.BISHOP,A.R.ARICESCU,K.HARLOS,C.A.O'CALLAGHAN,E.Y.JONES, C.SIEBOLD   
REVDAT   3   13-JUL-11 2WG3    1       VERSN                                    
REVDAT   2   21-JUL-09 2WG3    1       JRNL                                     
REVDAT   1   30-JUN-09 2WG3    0                                                
JRNL        AUTH   B.BISHOP,A.R.ARICESCU,K.HARLOS,C.A.O'CALLAGHAN,E.Y.JONES,    
JRNL        AUTH 2 C.SIEBOLD                                                    
JRNL        TITL   STRUCTURAL INSIGHTS INTO HEDGEHOG LIGAND SEQUESTRATION BY    
JRNL        TITL 2 THE HUMAN HEDGEHOG-INTERACTING PROTEIN HIP                   
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  16   698 2009              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   19561611                                                     
JRNL        DOI    10.1038/NSMB.1607                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0047                                      
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 48634                          
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2592                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3477                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 184                          
REMARK   3   BIN FREE R VALUE                    : 0.4020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8811                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 123                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.65000                                              
REMARK   3    B22 (A**2) : -3.41000                                             
REMARK   3    B33 (A**2) : -5.23000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.499         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.319         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.236         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.589        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.879                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9063 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  6298 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12269 ; 1.329 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15204 ; 0.864 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1108 ; 7.019 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   433 ;30.242 ;23.372       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1509 ;17.458 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    75 ;20.174 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1316 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10093 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1873 ; 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):  5545 ; 0.381 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2279 ; 0.073 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8922 ; 0.738 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3518 ; 1.185 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3347 ; 1.995 ; 4.500       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 5                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C    215       C     252      5                      
REMARK   3           1     D    215       D     252      5                      
REMARK   3           2     C    262       C     305      5                      
REMARK   3           2     D    262       D     305      5                      
REMARK   3           3     C    317       C     435      5                      
REMARK   3           3     D    317       D     435      5                      
REMARK   3           4     C    490       C     523      5                      
REMARK   3           4     D    490       D     523      5                      
REMARK   3           5     C    530       C     630      5                      
REMARK   3           5     D    530       D     630      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1959 ;  0.21 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   2557 ;  0.43 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1959 ;  0.30 ;  2.00           
REMARK   3   LOOSE THERMAL      1    D (A**2):   2557 ;  0.37 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     39       A      88      5                      
REMARK   3           1     B     39       B      88      5                      
REMARK   3           2     A     95       A     191      5                      
REMARK   3           2     B     95       B     191      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    863 ;  0.15 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2    B    (A):   1145 ;  0.40 ;  5.00           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    863 ;  0.25 ;  2.00           
REMARK   3   LOOSE THERMAL      2    B (A**2):   1145 ;  0.38 ; 10.00           
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    39        A   198                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.7970  -8.0270  20.8270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0297 T22:   0.1580                                     
REMARK   3      T33:   0.1133 T12:   0.0055                                     
REMARK   3      T13:   0.0503 T23:   0.0544                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9895 L22:   2.3056                                     
REMARK   3      L33:   2.1954 L12:   0.2573                                     
REMARK   3      L13:   0.3139 L23:   0.3121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0526 S12:  -0.0916 S13:   0.0055                       
REMARK   3      S21:   0.0284 S22:  -0.0622 S23:   0.1256                       
REMARK   3      S31:   0.0907 S32:  -0.0469 S33:   0.0095                       
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    39        B   192                          
REMARK   3    ORIGIN FOR THE GROUP (A): -66.1450   6.3650   3.9320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1265 T22:   0.1079                                     
REMARK   3      T33:   0.1138 T12:  -0.0345                                     
REMARK   3      T13:  -0.0722 T23:  -0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3516 L22:   2.2268                                     
REMARK   3      L33:   3.4781 L12:   0.4055                                     
REMARK   3      L13:  -0.0012 L23:  -0.8321                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0328 S12:  -0.0418 S13:  -0.1034                       
REMARK   3      S21:  -0.0880 S22:  -0.1081 S23:  -0.2272                       
REMARK   3      S31:  -0.2264 S32:   0.1859 S33:   0.0754                       
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   215        C   318                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.1810   9.7370 -15.7780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0999 T22:   0.1650                                     
REMARK   3      T33:   0.1855 T12:   0.0781                                     
REMARK   3      T13:   0.0336 T23:   0.0829                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6868 L22:   3.3223                                     
REMARK   3      L33:   3.4297 L12:   0.4437                                     
REMARK   3      L13:  -0.0832 L23:   0.1309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0877 S12:   0.2020 S13:   0.0514                       
REMARK   3      S21:   0.3116 S22:   0.0804 S23:   0.4214                       
REMARK   3      S31:  -0.4499 S32:  -0.5652 S33:  -0.1680                       
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 :   C   319        C   479                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6050   3.2480  -1.5470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0670 T22:   0.1411                                     
REMARK   3      T33:   0.2108 T12:   0.0471                                     
REMARK   3      T13:   0.0449 T23:   0.0617                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0007 L22:   1.0716                                     
REMARK   3      L33:   4.0971 L12:  -0.2443                                     
REMARK   3      L13:  -0.4784 L23:  -0.2619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0641 S12:  -0.1367 S13:   0.0466                       
REMARK   3      S21:   0.1671 S22:   0.0907 S23:  -0.1946                       
REMARK   3      S31:  -0.0467 S32:   0.2168 S33:  -0.1549                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   480        C   639                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.3230  13.6750 -15.4830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1052 T22:   0.2216                                     
REMARK   3      T33:   0.0646 T12:   0.0504                                     
REMARK   3      T13:  -0.0053 T23:   0.0470                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0458 L22:   4.6203                                     
REMARK   3      L33:   2.0026 L12:   0.7187                                     
REMARK   3      L13:  -0.2664 L23:  -0.0551                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0576 S12:   0.0248 S13:   0.0424                       
REMARK   3      S21:   0.2724 S22:   0.0290 S23:   0.0365                       
REMARK   3      S31:  -0.3605 S32:  -0.0534 S33:  -0.0866                       
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 :   D   215        D   318                          
REMARK   3    ORIGIN FOR THE GROUP (A): -80.9180  -9.5920 -35.1550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0075 T22:   0.1504                                     
REMARK   3      T33:   0.0876 T12:  -0.0079                                     
REMARK   3      T13:   0.0117 T23:  -0.0575                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3236 L22:   2.9591                                     
REMARK   3      L33:   2.8274 L12:   0.3006                                     
REMARK   3      L13:  -0.0982 L23:  -0.1483                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0718 S12:   0.2252 S13:  -0.0757                       
REMARK   3      S21:  -0.1290 S22:   0.1416 S23:  -0.3172                       
REMARK   3      S31:   0.0371 S32:   0.2623 S33:  -0.0699                       
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 :   D   319        D   479                          
REMARK   3    ORIGIN FOR THE GROUP (A): -86.3120  -2.9160 -18.5660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0384 T22:   0.1052                                     
REMARK   3      T33:   0.1324 T12:   0.0339                                     
REMARK   3      T13:  -0.0229 T23:  -0.0523                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3062 L22:   0.8441                                     
REMARK   3      L33:   2.5515 L12:   0.6118                                     
REMARK   3      L13:   0.5134 L23:   0.2853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0132 S12:  -0.0971 S13:   0.0501                       
REMARK   3      S21:   0.0708 S22:   0.0498 S23:   0.0497                       
REMARK   3      S31:  -0.2130 S32:  -0.1299 S33:  -0.0631                       
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   480        D   638                          
REMARK   3    ORIGIN FOR THE GROUP (A): -91.4610 -13.7580 -31.6320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0220 T22:   0.1971                                     
REMARK   3      T33:   0.0923 T12:   0.0252                                     
REMARK   3      T13:  -0.0069 T23:  -0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8783 L22:   3.0918                                     
REMARK   3      L33:   1.5607 L12:   0.4033                                     
REMARK   3      L13:  -0.2529 L23:  -0.1376                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0104 S12:   0.0198 S13:  -0.0170                       
REMARK   3      S21:   0.1496 S22:   0.0166 S23:  -0.0382                       
REMARK   3      S31:  -0.1286 S32:   0.0311 S33:  -0.0061                       
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          
REMARK   3  RIDING POSITIONS. U VALUES RESIDUAL ONLY                            
REMARK   4                                                                      
REMARK   4 2WG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-APR-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-39481.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49775                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.60                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10                                 
REMARK 200  R MERGE                    (I) : 0.18                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.1                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.81                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.70                               
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 ENTRIES 2WFQ AND 2WFT                            
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 62.07                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M SODIUM/POTASSIUM                   
REMARK 280  PHOSPHATE, PH 5.0                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       51.41050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.19050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.35050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.19050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.41050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.35050            
REMARK 290   SMTRY3   4  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: 2860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.47 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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: 2500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.75 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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     ASP A    89                                                      
REMARK 465     GLU A    90                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     ASN A    92                                                      
REMARK 465     SER A    93                                                      
REMARK 465     HIS A   199                                                      
REMARK 465     HIS A   200                                                      
REMARK 465     HIS A   201                                                      
REMARK 465     HIS A   202                                                      
REMARK 465     ASP B    89                                                      
REMARK 465     GLU B    90                                                      
REMARK 465     GLU B    91                                                      
REMARK 465     ASN B    92                                                      
REMARK 465     ALA B   193                                                      
REMARK 465     VAL B   194                                                      
REMARK 465     LEU B   195                                                      
REMARK 465     GLU B   196                                                      
REMARK 465     HIS B   197                                                      
REMARK 465     HIS B   198                                                      
REMARK 465     HIS B   199                                                      
REMARK 465     HIS B   200                                                      
REMARK 465     HIS B   201                                                      
REMARK 465     HIS B   202                                                      
REMARK 465     HIS C   214                                                      
REMARK 465     ASN C   456                                                      
REMARK 465     GLY C   457                                                      
REMARK 465     LYS C   458                                                      
REMARK 465     ASN C   459                                                      
REMARK 465     ARG C   460                                                      
REMARK 465     SER C   461                                                      
REMARK 465     LYS C   470                                                      
REMARK 465     GLY C   471                                                      
REMARK 465     LYS C   472                                                      
REMARK 465     ASP C   473                                                      
REMARK 465     PHE C   486                                                      
REMARK 465     SER C   487                                                      
REMARK 465     ASN C   488                                                      
REMARK 465     GLY C   489                                                      
REMARK 465     SER C   524                                                      
REMARK 465     PRO C   525                                                      
REMARK 465     VAL C   526                                                      
REMARK 465     THR C   527                                                      
REMARK 465     LYS C   528                                                      
REMARK 465     GLU C   640                                                      
REMARK 465     PRO C   641                                                      
REMARK 465     ALA C   642                                                      
REMARK 465     CYS C   643                                                      
REMARK 465     ARG C   644                                                      
REMARK 465     HIS C   645                                                      
REMARK 465     GLY C   646                                                      
REMARK 465     GLY C   647                                                      
REMARK 465     VAL C   648                                                      
REMARK 465     CYS C   649                                                      
REMARK 465     VAL C   650                                                      
REMARK 465     ARG C   651                                                      
REMARK 465     PRO C   652                                                      
REMARK 465     ASN C   653                                                      
REMARK 465     LYS C   654                                                      
REMARK 465     CYS C   655                                                      
REMARK 465     LEU C   656                                                      
REMARK 465     CYS C   657                                                      
REMARK 465     LYS C   658                                                      
REMARK 465     LYS C   659                                                      
REMARK 465     GLY C   660                                                      
REMARK 465     TYR C   661                                                      
REMARK 465     LEU C   662                                                      
REMARK 465     GLY C   663                                                      
REMARK 465     PRO C   664                                                      
REMARK 465     GLN C   665                                                      
REMARK 465     CYS C   666                                                      
REMARK 465     GLU C   667                                                      
REMARK 465     GLN C   668                                                      
REMARK 465     VAL C   669                                                      
REMARK 465     ASP C   670                                                      
REMARK 465     HIS C   671                                                      
REMARK 465     HIS C   672                                                      
REMARK 465     HIS C   673                                                      
REMARK 465     HIS C   674                                                      
REMARK 465     HIS C   675                                                      
REMARK 465     HIS C   676                                                      
REMARK 465     HIS D   214                                                      
REMARK 465     GLN D   307                                                      
REMARK 465     GLU D   308                                                      
REMARK 465     ARG D   309                                                      
REMARK 465     TRP D   310                                                      
REMARK 465     ALA D   311                                                      
REMARK 465     ILE D   312                                                      
REMARK 465     GLY D   313                                                      
REMARK 465     PRO D   314                                                      
REMARK 465     HIS D   315                                                      
REMARK 465     ASN D   456                                                      
REMARK 465     GLY D   457                                                      
REMARK 465     LYS D   458                                                      
REMARK 465     ASN D   459                                                      
REMARK 465     ARG D   460                                                      
REMARK 465     SER D   461                                                      
REMARK 465     CYS D   639                                                      
REMARK 465     GLU D   640                                                      
REMARK 465     PRO D   641                                                      
REMARK 465     ALA D   642                                                      
REMARK 465     CYS D   643                                                      
REMARK 465     ARG D   644                                                      
REMARK 465     HIS D   645                                                      
REMARK 465     GLY D   646                                                      
REMARK 465     GLY D   647                                                      
REMARK 465     VAL D   648                                                      
REMARK 465     CYS D   649                                                      
REMARK 465     VAL D   650                                                      
REMARK 465     ARG D   651                                                      
REMARK 465     PRO D   652                                                      
REMARK 465     ASN D   653                                                      
REMARK 465     LYS D   654                                                      
REMARK 465     CYS D   655                                                      
REMARK 465     LEU D   656                                                      
REMARK 465     CYS D   657                                                      
REMARK 465     LYS D   658                                                      
REMARK 465     LYS D   659                                                      
REMARK 465     GLY D   660                                                      
REMARK 465     TYR D   661                                                      
REMARK 465     LEU D   662                                                      
REMARK 465     GLY D   663                                                      
REMARK 465     PRO D   664                                                      
REMARK 465     GLN D   665                                                      
REMARK 465     CYS D   666                                                      
REMARK 465     GLU D   667                                                      
REMARK 465     GLN D   668                                                      
REMARK 465     VAL D   669                                                      
REMARK 465     ASP D   670                                                      
REMARK 465     HIS D   671                                                      
REMARK 465     HIS D   672                                                      
REMARK 465     HIS D   673                                                      
REMARK 465     HIS D   674                                                      
REMARK 465     HIS D   675                                                      
REMARK 465     HIS D   676                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG D   434     O1   PO4 D  1639              2.07            
REMARK 500   O    THR D   539     O    SER D   542              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS D 536   CB    CYS D 536   SG     -0.105                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS C 536   CA  -  CB  -  SG  ANGL. DEV. =  -7.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  59     -116.24    -94.74                                   
REMARK 500    ARG A  69      123.68    -39.70                                   
REMARK 500    LEU A 192     -110.99   -155.83                                   
REMARK 500    VAL A 194     -158.01   -113.18                                   
REMARK 500    ALA B  59     -122.62    -94.01                                   
REMARK 500    LYS C 277     -168.76   -112.86                                   
REMARK 500    ARG C 309      -96.62   -120.28                                   
REMARK 500    HIS C 315       48.94     39.59                                   
REMARK 500    ASP C 387       -1.47     77.48                                   
REMARK 500    ASP C 398       48.93    -89.54                                   
REMARK 500    HIS C 430      -72.51   -103.43                                   
REMARK 500    PRO C 441      151.55    -37.94                                   
REMARK 500    CYS C 500      -38.78   -132.68                                   
REMARK 500    SER C 542      127.62    136.37                                   
REMARK 500    CYS C 543       39.59    -68.74                                   
REMARK 500    MET C 571      -58.42    -26.91                                   
REMARK 500    CYS C 612       73.23    -63.48                                   
REMARK 500    ASN C 614       56.81    -99.06                                   
REMARK 500    SER D 224     -164.07   -127.02                                   
REMARK 500    ASP D 387       -5.22     79.77                                   
REMARK 500    ASN D 488      -92.41    -85.17                                   
REMARK 500    CYS D 543       48.48    -89.25                                   
REMARK 500    MET D 571      -59.64    -29.78                                   
REMARK 500    SER D 606      128.32    -35.93                                   
REMARK 500    ASN D 614       54.82    -94.03                                   
REMARK 500    ALA D 637     -124.29    -89.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS D  528     GLN D  529                 -147.95                    
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 A1199  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 141   NE2                                                    
REMARK 620 2 HIS A 183   ND1 106.7                                              
REMARK 620 3 ASP C 383   OD2  91.9 102.4                                        
REMARK 620 4 ASP A 148   OD1 124.2 107.9 120.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 383   OD2                                                    
REMARK 620 2 HIS B 141   NE2  99.3                                              
REMARK 620 3 ASP B 148   OD1 123.1 117.6                                        
REMARK 620 4 HIS B 183   ND1 103.7 110.5 101.8                                  
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 A1199                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C1640                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D1639                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1640                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1641                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1642                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL D1641                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL D1642                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL D1643                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WFX   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN                            
REMARK 900  HUMAN HEDGEHOG-INTERACTING PROTEIN HIP AND                          
REMARK 900  SONIC HEDGEHOG IN THE PRESENCE OF CALCIUM                           
REMARK 900 RELATED ID: 2WFQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE N-TERMINAL                                 
REMARK 900  SIGNALLING DOMAIN OF HUMAN DHH WITHOUT                              
REMARK 900  CALCIUM                                                             
REMARK 900 RELATED ID: 2WFR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE N-TERMINAL                                 
REMARK 900  SIGNALLING DOMAIN OF HUMAN DHH WITH CALCIUM                         
REMARK 900 RELATED ID: 2WFT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN HIP                                  
REMARK 900  ECTODOMAIN                                                          
REMARK 900 RELATED ID: 2WG4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN                            
REMARK 900  HUMAN HEDGEHOG-INTERACTING PROTEIN HIP AND                          
REMARK 900  SONIC HEDGEHOG WITHOUT CALCIUM                                      
DBREF  2WG3 A   39    39  PDB    2WG3     2WG3            39     39             
DBREF  2WG3 A   40   194  UNP    O43323   DHH_HUMAN       40    194             
DBREF  2WG3 A  195   202  PDB    2WG3     2WG3           195    202             
DBREF  2WG3 B   39    39  PDB    2WG3     2WG3            39     39             
DBREF  2WG3 B   40   194  UNP    O43323   DHH_HUMAN       40    194             
DBREF  2WG3 B  195   202  PDB    2WG3     2WG3           195    202             
DBREF  2WG3 C  214   670  UNP    Q96QV1   HHIP_HUMAN     214    670             
DBREF  2WG3 C  671   676  PDB    2WG3     2WG3           671    676             
DBREF  2WG3 D  214   670  UNP    Q96QV1   HHIP_HUMAN     214    670             
DBREF  2WG3 D  671   676  PDB    2WG3     2WG3           671    676             
SEQRES   1 A  164  ALA LEU VAL PRO LEU LEU TYR LYS GLN PHE VAL PRO GLY          
SEQRES   2 A  164  VAL PRO GLU ARG THR LEU GLY ALA SER GLY PRO ALA GLU          
SEQRES   3 A  164  GLY ARG VAL ALA ARG GLY SER GLU ARG PHE ARG ASP LEU          
SEQRES   4 A  164  VAL PRO ASN TYR ASN PRO ASP ILE ILE PHE LYS ASP GLU          
SEQRES   5 A  164  GLU ASN SER GLY ALA ASP ARG LEU MET THR GLU ARG CYS          
SEQRES   6 A  164  LYS GLU ARG VAL ASN ALA LEU ALA ILE ALA VAL MET ASN          
SEQRES   7 A  164  MET TRP PRO GLY VAL ARG LEU ARG VAL THR GLU GLY TRP          
SEQRES   8 A  164  ASP GLU ASP GLY HIS HIS ALA GLN ASP SER LEU HIS TYR          
SEQRES   9 A  164  GLU GLY ARG ALA LEU ASP ILE THR THR SER ASP ARG ASP          
SEQRES  10 A  164  ARG ASN LYS TYR GLY LEU LEU ALA ARG LEU ALA VAL GLU          
SEQRES  11 A  164  ALA GLY PHE ASP TRP VAL TYR TYR GLU SER ARG ASN HIS          
SEQRES  12 A  164  VAL HIS VAL SER VAL LYS ALA ASP ASN SER LEU ALA VAL          
SEQRES  13 A  164  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  164  ALA LEU VAL PRO LEU LEU TYR LYS GLN PHE VAL PRO GLY          
SEQRES   2 B  164  VAL PRO GLU ARG THR LEU GLY ALA SER GLY PRO ALA GLU          
SEQRES   3 B  164  GLY ARG VAL ALA ARG GLY SER GLU ARG PHE ARG ASP LEU          
SEQRES   4 B  164  VAL PRO ASN TYR ASN PRO ASP ILE ILE PHE LYS ASP GLU          
SEQRES   5 B  164  GLU ASN SER GLY ALA ASP ARG LEU MET THR GLU ARG CYS          
SEQRES   6 B  164  LYS GLU ARG VAL ASN ALA LEU ALA ILE ALA VAL MET ASN          
SEQRES   7 B  164  MET TRP PRO GLY VAL ARG LEU ARG VAL THR GLU GLY TRP          
SEQRES   8 B  164  ASP GLU ASP GLY HIS HIS ALA GLN ASP SER LEU HIS TYR          
SEQRES   9 B  164  GLU GLY ARG ALA LEU ASP ILE THR THR SER ASP ARG ASP          
SEQRES  10 B  164  ARG ASN LYS TYR GLY LEU LEU ALA ARG LEU ALA VAL GLU          
SEQRES  11 B  164  ALA GLY PHE ASP TRP VAL TYR TYR GLU SER ARG ASN HIS          
SEQRES  12 B  164  VAL HIS VAL SER VAL LYS ALA ASP ASN SER LEU ALA VAL          
SEQRES  13 B  164  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  463  HIS ASN CYS PHE CYS ILE GLN GLU VAL VAL SER GLY LEU          
SEQRES   2 C  463  ARG GLN PRO VAL GLY ALA LEU HIS SER GLY ASP GLY SER          
SEQRES   3 C  463  GLN ARG LEU PHE ILE LEU GLU LYS GLU GLY TYR VAL LYS          
SEQRES   4 C  463  ILE LEU THR PRO GLU GLY GLU ILE PHE LYS GLU PRO TYR          
SEQRES   5 C  463  LEU ASP ILE HIS LYS LEU VAL GLN SER GLY ILE LYS GLY          
SEQRES   6 C  463  GLY ASP GLU ARG GLY LEU LEU SER LEU ALA PHE HIS PRO          
SEQRES   7 C  463  ASN TYR LYS LYS ASN GLY LYS LEU TYR VAL SER TYR THR          
SEQRES   8 C  463  THR ASN GLN GLU ARG TRP ALA ILE GLY PRO HIS ASP HIS          
SEQRES   9 C  463  ILE LEU ARG VAL VAL GLU TYR THR VAL SER ARG LYS ASN          
SEQRES  10 C  463  PRO HIS GLN VAL ASP LEU ARG THR ALA ARG VAL PHE LEU          
SEQRES  11 C  463  GLU VAL ALA GLU LEU HIS ARG LYS HIS LEU GLY GLY GLN          
SEQRES  12 C  463  LEU LEU PHE GLY PRO ASP GLY PHE LEU TYR ILE ILE LEU          
SEQRES  13 C  463  GLY ASP GLY MET ILE THR LEU ASP ASP MET GLU GLU MET          
SEQRES  14 C  463  ASP GLY LEU SER ASP PHE THR GLY SER VAL LEU ARG LEU          
SEQRES  15 C  463  ASP VAL ASP THR ASP MET CYS ASN VAL PRO TYR SER ILE          
SEQRES  16 C  463  PRO ARG SER ASN PRO HIS PHE ASN SER THR ASN GLN PRO          
SEQRES  17 C  463  PRO GLU VAL PHE ALA HIS GLY LEU HIS ASP PRO GLY ARG          
SEQRES  18 C  463  CYS ALA VAL ASP ARG HIS PRO THR ASP ILE ASN ILE ASN          
SEQRES  19 C  463  LEU THR ILE LEU CYS SER ASP SER ASN GLY LYS ASN ARG          
SEQRES  20 C  463  SER SER ALA ARG ILE LEU GLN ILE ILE LYS GLY LYS ASP          
SEQRES  21 C  463  TYR GLU SER GLU PRO SER LEU LEU GLU PHE LYS PRO PHE          
SEQRES  22 C  463  SER ASN GLY PRO LEU VAL GLY GLY PHE VAL TYR ARG GLY          
SEQRES  23 C  463  CYS GLN SER GLU ARG LEU TYR GLY SER TYR VAL PHE GLY          
SEQRES  24 C  463  ASP ARG ASN GLY ASN PHE LEU THR LEU GLN GLN SER PRO          
SEQRES  25 C  463  VAL THR LYS GLN TRP GLN GLU LYS PRO LEU CYS LEU GLY          
SEQRES  26 C  463  THR SER GLY SER CYS ARG GLY TYR PHE SER GLY HIS ILE          
SEQRES  27 C  463  LEU GLY PHE GLY GLU ASP GLU LEU GLY GLU VAL TYR ILE          
SEQRES  28 C  463  LEU SER SER SER LYS SER MET THR GLN THR HIS ASN GLY          
SEQRES  29 C  463  LYS LEU TYR LYS ILE VAL ASP PRO LYS ARG PRO LEU MET          
SEQRES  30 C  463  PRO GLU GLU CYS ARG ALA THR VAL GLN PRO ALA GLN THR          
SEQRES  31 C  463  LEU THR SER GLU CYS SER ARG LEU CYS ARG ASN GLY TYR          
SEQRES  32 C  463  CYS THR PRO THR GLY LYS CYS CYS CYS SER PRO GLY TRP          
SEQRES  33 C  463  GLU GLY ASP PHE CYS ARG THR ALA LYS CYS GLU PRO ALA          
SEQRES  34 C  463  CYS ARG HIS GLY GLY VAL CYS VAL ARG PRO ASN LYS CYS          
SEQRES  35 C  463  LEU CYS LYS LYS GLY TYR LEU GLY PRO GLN CYS GLU GLN          
SEQRES  36 C  463  VAL ASP HIS HIS HIS HIS HIS HIS                              
SEQRES   1 D  463  HIS ASN CYS PHE CYS ILE GLN GLU VAL VAL SER GLY LEU          
SEQRES   2 D  463  ARG GLN PRO VAL GLY ALA LEU HIS SER GLY ASP GLY SER          
SEQRES   3 D  463  GLN ARG LEU PHE ILE LEU GLU LYS GLU GLY TYR VAL LYS          
SEQRES   4 D  463  ILE LEU THR PRO GLU GLY GLU ILE PHE LYS GLU PRO TYR          
SEQRES   5 D  463  LEU ASP ILE HIS LYS LEU VAL GLN SER GLY ILE LYS GLY          
SEQRES   6 D  463  GLY ASP GLU ARG GLY LEU LEU SER LEU ALA PHE HIS PRO          
SEQRES   7 D  463  ASN TYR LYS LYS ASN GLY LYS LEU TYR VAL SER TYR THR          
SEQRES   8 D  463  THR ASN GLN GLU ARG TRP ALA ILE GLY PRO HIS ASP HIS          
SEQRES   9 D  463  ILE LEU ARG VAL VAL GLU TYR THR VAL SER ARG LYS ASN          
SEQRES  10 D  463  PRO HIS GLN VAL ASP LEU ARG THR ALA ARG VAL PHE LEU          
SEQRES  11 D  463  GLU VAL ALA GLU LEU HIS ARG LYS HIS LEU GLY GLY GLN          
SEQRES  12 D  463  LEU LEU PHE GLY PRO ASP GLY PHE LEU TYR ILE ILE LEU          
SEQRES  13 D  463  GLY ASP GLY MET ILE THR LEU ASP ASP MET GLU GLU MET          
SEQRES  14 D  463  ASP GLY LEU SER ASP PHE THR GLY SER VAL LEU ARG LEU          
SEQRES  15 D  463  ASP VAL ASP THR ASP MET CYS ASN VAL PRO TYR SER ILE          
SEQRES  16 D  463  PRO ARG SER ASN PRO HIS PHE ASN SER THR ASN GLN PRO          
SEQRES  17 D  463  PRO GLU VAL PHE ALA HIS GLY LEU HIS ASP PRO GLY ARG          
SEQRES  18 D  463  CYS ALA VAL ASP ARG HIS PRO THR ASP ILE ASN ILE ASN          
SEQRES  19 D  463  LEU THR ILE LEU CYS SER ASP SER ASN GLY LYS ASN ARG          
SEQRES  20 D  463  SER SER ALA ARG ILE LEU GLN ILE ILE LYS GLY LYS ASP          
SEQRES  21 D  463  TYR GLU SER GLU PRO SER LEU LEU GLU PHE LYS PRO PHE          
SEQRES  22 D  463  SER ASN GLY PRO LEU VAL GLY GLY PHE VAL TYR ARG GLY          
SEQRES  23 D  463  CYS GLN SER GLU ARG LEU TYR GLY SER TYR VAL PHE GLY          
SEQRES  24 D  463  ASP ARG ASN GLY ASN PHE LEU THR LEU GLN GLN SER PRO          
SEQRES  25 D  463  VAL THR LYS GLN TRP GLN GLU LYS PRO LEU CYS LEU GLY          
SEQRES  26 D  463  THR SER GLY SER CYS ARG GLY TYR PHE SER GLY HIS ILE          
SEQRES  27 D  463  LEU GLY PHE GLY GLU ASP GLU LEU GLY GLU VAL TYR ILE          
SEQRES  28 D  463  LEU SER SER SER LYS SER MET THR GLN THR HIS ASN GLY          
SEQRES  29 D  463  LYS LEU TYR LYS ILE VAL ASP PRO LYS ARG PRO LEU MET          
SEQRES  30 D  463  PRO GLU GLU CYS ARG ALA THR VAL GLN PRO ALA GLN THR          
SEQRES  31 D  463  LEU THR SER GLU CYS SER ARG LEU CYS ARG ASN GLY TYR          
SEQRES  32 D  463  CYS THR PRO THR GLY LYS CYS CYS CYS SER PRO GLY TRP          
SEQRES  33 D  463  GLU GLY ASP PHE CYS ARG THR ALA LYS CYS GLU PRO ALA          
SEQRES  34 D  463  CYS ARG HIS GLY GLY VAL CYS VAL ARG PRO ASN LYS CYS          
SEQRES  35 D  463  LEU CYS LYS LYS GLY TYR LEU GLY PRO GLN CYS GLU GLN          
SEQRES  36 D  463  VAL ASP HIS HIS HIS HIS HIS HIS                              
HET     ZN  A1199       1                                                       
HET     ZN  B1193       1                                                       
HET    PO4  C1640       5                                                       
HET    PO4  D1639       5                                                       
HET    NAG  D1640      14                                                       
HET    NAG  C1641      14                                                       
HET     CL  C1642       1                                                       
HET     CL  D1641       1                                                       
HET     CL  C1643       1                                                       
HET     CL  A1200       1                                                       
HET     CL  D1642       1                                                       
HET     CL  D1643       1                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   5  PO4    2(O4 P 3-)                                                   
FORMUL   6   CL    6(CL 1-)                                                     
FORMUL   7   ZN    2(ZN 2+)                                                     
FORMUL   8  NAG    2(C8 H15 N O6)                                               
FORMUL   9  HOH   *123(H2 O)                                                    
HELIX    1   1 ARG A   73  LEU A   77  5                                   5    
HELIX    2   2 GLY A   94  ASP A   96  5                                   3    
HELIX    3   3 THR A  100  TRP A  118  1                                  19    
HELIX    4   4 SER A  139  GLU A  143  5                                   5    
HELIX    5   5 ASP A  155  ASN A  157  5                                   3    
HELIX    6   6 LYS A  158  ALA A  169  1                                  12    
HELIX    7   7 GLY B   94  ASP B   96  5                                   3    
HELIX    8   8 THR B  100  TRP B  118  1                                  19    
HELIX    9   9 SER B  139  GLU B  143  5                                   5    
HELIX   10  10 ASP B  155  ASN B  157  5                                   3    
HELIX   11  11 LYS B  158  ALA B  169  1                                  12    
HELIX   12  12 ASN C  292  GLY C  297  1                                   6    
HELIX   13  13 ASP C  335  ALA C  339  5                                   5    
HELIX   14  14 THR C  375  MET C  382  1                                   8    
HELIX   15  15 SER C  570  THR C  574  5                                   5    
HELIX   16  16 PRO C  591  ARG C  595  5                                   5    
HELIX   17  17 SER C  606  CYS C  612  1                                   7    
HELIX   18  18 ASN D  292  GLY D  297  1                                   6    
HELIX   19  19 THR D  375  MET D  382  1                                   8    
HELIX   20  20 SER D  570  THR D  574  5                                   5    
HELIX   21  21 PRO D  591  ARG D  595  5                                   5    
HELIX   22  22 SER D  606  CYS D  612  1                                   7    
SHEET    1  AA 6 PHE A  48  VAL A  49  0                                        
SHEET    2  AA 6 TRP A 173  TYR A 175 -1  O  VAL A 174   N  VAL A  49           
SHEET    3  AA 6 VAL A 182  SER A 185 -1  O  HIS A 183   N  TYR A 175           
SHEET    4  AA 6 ALA A 146  THR A 151 -1  O  LEU A 147   N  VAL A 184           
SHEET    5  AA 6 LEU A 123  GLU A 127 -1  O  ARG A 124   N  THR A 150           
SHEET    6  AA 6 ILE A  86  PHE A  87  1  O  ILE A  86   N  VAL A 125           
SHEET    1  AB 2 VAL A  78  PRO A  79  0                                        
SHEET    2  AB 2 LEU A  98  MET A  99 -1  O  MET A  99   N  VAL A  78           
SHEET    1  BA 6 PHE B  48  VAL B  49  0                                        
SHEET    2  BA 6 TRP B 173  SER B 178 -1  O  VAL B 174   N  VAL B  49           
SHEET    3  BA 6 HIS B 181  SER B 185 -1  O  HIS B 181   N  SER B 178           
SHEET    4  BA 6 ALA B 146  THR B 151 -1  O  LEU B 147   N  VAL B 184           
SHEET    5  BA 6 LEU B 123  GLU B 127 -1  O  ARG B 124   N  THR B 150           
SHEET    6  BA 6 ILE B  85  PHE B  87  1  O  ILE B  86   N  VAL B 125           
SHEET    1  BB 2 VAL B  78  PRO B  79  0                                        
SHEET    2  BB 2 LEU B  98  MET B  99 -1  O  MET B  99   N  VAL B  78           
SHEET    1  CA 5 LEU C 537  THR C 539  0                                        
SHEET    2  CA 5 PHE C 217  LEU C 226  1  O  PHE C 217   N  GLY C 538           
SHEET    3  CA 5 GLY C 577  VAL C 583 -1  O  GLY C 577   N  LEU C 226           
SHEET    4  CA 5 VAL C 562  SER C 567 -1  O  VAL C 562   N  ILE C 582           
SHEET    5  CA 5 HIS C 550  GLU C 556 -1  O  HIS C 550   N  SER C 567           
SHEET    1  CB 4 PRO C 229  LEU C 233  0                                        
SHEET    2  CB 4 LEU C 242  GLU C 246 -1  O  PHE C 243   N  LEU C 233           
SHEET    3  CB 4 TYR C 250  LEU C 254 -1  O  TYR C 250   N  GLU C 246           
SHEET    4  CB 4 LEU C 266  ASP C 267 -1  O  LEU C 266   N  VAL C 251           
SHEET    1  CC 4 LEU C 284  PHE C 289  0                                        
SHEET    2  CC 4 LYS C 298  THR C 305 -1  O  TYR C 300   N  ALA C 288           
SHEET    3  CC 4 HIS C 317  THR C 325 -1  O  ILE C 318   N  THR C 305           
SHEET    4  CC 4 ARG C 340  GLU C 347 -1  O  ARG C 340   N  GLU C 323           
SHEET    1  CD 4 GLY C 354  PHE C 359  0                                        
SHEET    2  CD 4 LEU C 365  LEU C 369 -1  O  TYR C 366   N  LEU C 358           
SHEET    3  CD 4 SER C 391  LEU C 395 -1  O  SER C 391   N  LEU C 369           
SHEET    4  CD 4 VAL C 424  HIS C 427 -1  N  PHE C 425   O  VAL C 392           
SHEET    1  CE 4 CYS C 435  ASP C 438  0                                        
SHEET    2  CE 4 LEU C 448  SER C 453 -1  O  THR C 449   N  ASP C 438           
SHEET    3  CE 4 ALA C 463  ILE C 468 -1  O  ARG C 464   N  CYS C 452           
SHEET    4  CE 4 LEU C 481  GLU C 482 -1  O  LEU C 481   N  ILE C 465           
SHEET    1  CF 4 LEU C 491  VAL C 496  0                                        
SHEET    2  CF 4 TYR C 509  ASP C 513 -1  O  VAL C 510   N  PHE C 495           
SHEET    3  CF 4 PHE C 518  GLN C 522 -1  O  LEU C 519   N  PHE C 511           
SHEET    4  CF 4 GLN C 531  LEU C 535 -1  O  GLN C 531   N  GLN C 522           
SHEET    1  CG 2 GLY C 615  CYS C 617  0                                        
SHEET    2  CG 2 CYS C 623  CYS C 625 -1  O  CYS C 624   N  TYR C 616           
SHEET    1  CH 2 TRP C 629  GLU C 630  0                                        
SHEET    2  CH 2 THR C 636  ALA C 637 -1  O  THR C 636   N  GLU C 630           
SHEET    1  DA 9 LEU D 266  ASP D 267  0                                        
SHEET    2  DA 9 TYR D 250  LEU D 254 -1  N  VAL D 251   O  LEU D 266           
SHEET    3  DA 9 LEU D 242  GLU D 246 -1  O  LEU D 242   N  LEU D 254           
SHEET    4  DA 9 PRO D 229  LEU D 233 -1  N  VAL D 230   O  LEU D 245           
SHEET    5  DA 9 HIS D 550  GLU D 556  1  O  PHE D 554   N  ALA D 232           
SHEET    6  DA 9 VAL D 562  SER D 567 -1  O  TYR D 563   N  GLY D 555           
SHEET    7  DA 9 GLY D 577  VAL D 583 -1  O  LYS D 578   N  SER D 566           
SHEET    8  DA 9 PHE D 217  LEU D 226 -1  O  CYS D 218   N  VAL D 583           
SHEET    9  DA 9 LEU D 537  GLY D 538  1  O  GLY D 538   N  ILE D 219           
SHEET    1  DB 4 LEU D 284  PHE D 289  0                                        
SHEET    2  DB 4 LYS D 298  THR D 305 -1  O  TYR D 300   N  ALA D 288           
SHEET    3  DB 4 ILE D 318  SER D 327 -1  O  ILE D 318   N  THR D 305           
SHEET    4  DB 4 ASN D 330  ALA D 346 -1  N  ASN D 330   O  SER D 327           
SHEET    1  DC 4 GLY D 354  PHE D 359  0                                        
SHEET    2  DC 4 LEU D 365  LEU D 369 -1  O  TYR D 366   N  LEU D 358           
SHEET    3  DC 4 SER D 391  LEU D 395 -1  O  SER D 391   N  LEU D 369           
SHEET    4  DC 4 VAL D 424  HIS D 427 -1  N  PHE D 425   O  VAL D 392           
SHEET    1  DD 4 ALA D 436  ASP D 438  0                                        
SHEET    2  DD 4 ILE D 446  SER D 453 -1  O  THR D 449   N  ASP D 438           
SHEET    3  DD 4 ALA D 463  ILE D 469 -1  O  ARG D 464   N  CYS D 452           
SHEET    4  DD 4 LEU D 481  GLU D 482 -1  O  LEU D 481   N  ILE D 465           
SHEET    1  DE 4 LEU D 491  TYR D 497  0                                        
SHEET    2  DE 4 SER D 508  ASP D 513 -1  O  SER D 508   N  TYR D 497           
SHEET    3  DE 4 PHE D 518  GLN D 523 -1  O  LEU D 519   N  PHE D 511           
SHEET    4  DE 4 TRP D 530  LEU D 535 -1  O  GLN D 531   N  GLN D 522           
SHEET    1  DF 2 GLY D 615  CYS D 617  0                                        
SHEET    2  DF 2 CYS D 623  CYS D 625 -1  O  CYS D 624   N  TYR D 616           
SSBOND   1 CYS C  216    CYS C  536                          1555   1555  2.05  
SSBOND   2 CYS C  218    CYS C  543                          1555   1555  2.03  
SSBOND   3 CYS C  402    CYS C  624                          1555   1555  2.05  
SSBOND   4 CYS C  435    CYS C  452                          1555   1555  2.04  
SSBOND   5 CYS C  500    CYS C  594                          1555   1555  2.05  
SSBOND   6 CYS C  608    CYS C  617                          1555   1555  2.05  
SSBOND   7 CYS C  612    CYS C  623                          1555   1555  2.04  
SSBOND   8 CYS C  625    CYS C  634                          1555   1555  2.04  
SSBOND   9 CYS D  216    CYS D  536                          1555   1555  2.04  
SSBOND  10 CYS D  218    CYS D  543                          1555   1555  2.05  
SSBOND  11 CYS D  402    CYS D  624                          1555   1555  2.04  
SSBOND  12 CYS D  435    CYS D  452                          1555   1555  2.05  
SSBOND  13 CYS D  500    CYS D  594                          1555   1555  2.05  
SSBOND  14 CYS D  608    CYS D  617                          1555   1555  2.05  
SSBOND  15 CYS D  612    CYS D  623                          1555   1555  2.04  
SSBOND  16 CYS D  625    CYS D  634                          1555   1555  2.05  
LINK        ZN    ZN A1199                 NE2 HIS A 141     1555   1555  2.11  
LINK        ZN    ZN A1199                 ND1 HIS A 183     1555   1555  1.93  
LINK        ZN    ZN A1199                 OD2 ASP C 383     1555   1555  2.03  
LINK        ZN    ZN A1199                 OD1 ASP A 148     1555   1555  1.98  
LINK        ZN    ZN B1193                 OD1 ASP B 148     1555   1555  1.96  
LINK        ZN    ZN B1193                 NE2 HIS B 141     1555   1555  2.13  
LINK        ZN    ZN B1193                 ND1 HIS B 183     1555   1555  1.97  
LINK        ZN    ZN B1193                 OD2 ASP D 383     1555   1555  2.09  
LINK         ND2 ASN C 447                 C1  NAG C1641     1555   1555  1.44  
LINK         ND2 ASN D 447                 C1  NAG D1640     1555   1555  1.46  
CISPEP   1 VAL A   49    PRO A   50          0         0.80                     
CISPEP   2 VAL B   49    PRO B   50          0        -0.84                     
CISPEP   3 GLN C  307    GLU C  308          0        18.76                     
CISPEP   4 GLU C  308    ARG C  309          0        -3.02                     
CISPEP   5 LYS C  484    PRO C  485          0       -11.27                     
CISPEP   6 LYS D  484    PRO D  485          0        -6.05                     
SITE     1 AC1  4 HIS A 141  ASP A 148  HIS A 183  ASP C 383                    
SITE     1 AC2  4 HIS B 141  ASP B 148  HIS B 183  ASP D 383                    
SITE     1 AC3  4 HIS C 315  HIS C 349  ARG C 350  HOH C2038                    
SITE     1 AC4  5 ARG D 434  ALA D 436  VAL D 437  PHE D 495                    
SITE     2 AC4  5 VAL D 496                                                     
SITE     1 AC5  6 LYS C 294  LYS C 295  PRO D 361  ARG D 439                    
SITE     2 AC5  6 ASN D 447  LYS D 470                                          
SITE     1 AC6  7 SER C 411  ASN C 447  ILE C 468  ILE C 469                    
SITE     2 AC6  7 TYR C 474  GLU D 475  SER D 476                               
SITE     1 AC7  2 ARG C 434  VAL C 496                                          
SITE     1 AC8  3 VAL D 326  ARG D 328  ASP D 335                               
SITE     1 AC9  1 GLU A  72                                                     
SITE     1 BC1  3 GLU D 221  SER D 224  LYS D 578                               
SITE     1 BC2  1 GLU D 532                                                     
CRYST1  102.821  110.701  144.381  90.00  90.00  90.00 P 21 21 21    8          
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      0.009726  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009033  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006926        0.00000                         
MTRIX1   1 -0.998400 -0.003371  0.056010     -100.20000    1                    
MTRIX2   1  0.001286 -0.999300 -0.037210       -0.30930    1                    
MTRIX3   1  0.056100 -0.037080  0.997700       21.69000    1                    
MTRIX1   2 -0.999800 -0.000944  0.017810       -0.97870    1                    
MTRIX2   2  0.000479 -0.999700 -0.026090       -0.00380    1                    
MTRIX3   2  0.017830 -0.026080  0.999500        0.13010    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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