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Database: PDB
Entry: 3HO4
LinkDB: 3HO4
Original site: 3HO4 
HEADER    SIGNALING PROTEIN                       01-JUN-09   3HO4              
TITLE     CRYSTAL STRUCTURE OF HEDGEHOG-INTERACTING PROTEIN (HHIP)              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEDGEHOG-INTERACTING PROTEIN;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 193-667;                                      
COMPND   5 SYNONYM: HHIP, HIP;                                                  
COMPND   6 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: HHIP, HHIP ORFNAMES: UNQ5825/PRO19644, HIP, UNQ5825/PRO19644;  
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: INSECT CELLS;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: GATEWAY VECTOR PENTR/D-TOPO           
SOURCE  10 (INVITROGEN);                                                        
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PENTR/D-TOPO WITH HONEYBEE MELITTIN       
SOURCE  12 SECRETION SIGNAL                                                     
KEYWDS    RECEPTOR ECTODOMAIN, SIX-BLADED-PROPELLER DOMAIN, EGF DOMAIN,         
KEYWDS   2 DISULFIDE BOND, CELL MEMBRANE, EGF-LIKE DOMAIN, GLYCOPROTEIN,        
KEYWDS   3 MEMBRANE, SECRETED, SIGNALING PROTEIN                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.G.HYMOWITZ,I.BOSANAC                                                
REVDAT   3   13-JUL-11 3HO4    1       VERSN                                    
REVDAT   2   28-APR-10 3HO4    1       JRNL                                     
REVDAT   1   23-JUN-09 3HO4    0                                                
JRNL        AUTH   I.BOSANAC,H.R.MAUN,S.J.SCALES,X.WEN,A.LINGEL,J.F.BAZAN,      
JRNL        AUTH 2 F.J.DE SAUVAGE,S.G.HYMOWITZ,R.A.LAZARUS                      
JRNL        TITL   THE STRUCTURE OF SHH IN COMPLEX WITH HHIP REVEALS A          
JRNL        TITL 2 RECOGNITION ROLE FOR THE SHH PSEUDO ACTIVE SITE IN           
JRNL        TITL 3 SIGNALING.                                                   
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  16   691 2009              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   19561609                                                     
JRNL        DOI    10.1038/NSMB.1632                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 31970                          
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) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1709                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 25                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1858                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 105                          
REMARK   3   BIN FREE R VALUE                    : 0.3820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6868                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
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) : 72.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.03000                                              
REMARK   3    B22 (A**2) : 2.03000                                              
REMARK   3    B33 (A**2) : -3.04000                                             
REMARK   3    B12 (A**2) : 1.01000                                              
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): 0.842         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.369         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.290         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.622        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.893                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7036 ; 0.008 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9511 ; 1.203 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   872 ; 6.906 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   324 ;33.315 ;23.488       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1191 ;20.045 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    50 ;20.521 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1003 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5384 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2882 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4552 ; 0.309 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   220 ; 0.123 ; 0.200       
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):    42 ; 0.169 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.136 ; 0.200       
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):  4441 ; 2.331 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6989 ; 3.913 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2860 ; 2.178 ; 2.500       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2522 ; 3.531 ; 5.000       
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  : 6                                          
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   215        A   603                          
REMARK   3    ORIGIN FOR THE GROUP (A): -89.2077  30.7648  48.6769              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3548 T22:  -0.0409                                     
REMARK   3      T33:  -0.1698 T12:  -0.1444                                     
REMARK   3      T13:  -0.0226 T23:  -0.0466                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8249 L22:   1.8336                                     
REMARK   3      L33:   4.1633 L12:  -0.3983                                     
REMARK   3      L13:  -0.3707 L23:   0.0167                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0007 S12:   0.8755 S13:   0.1177                       
REMARK   3      S21:  -0.2625 S22:   0.0562 S23:   0.0034                       
REMARK   3      S31:   0.0116 S32:   0.2507 S33:  -0.0569                       
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 :   A   604        A   637                          
REMARK   3    ORIGIN FOR THE GROUP (A): -61.8737  20.2803  38.3951              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2491 T22:   0.7166                                     
REMARK   3      T33:  -0.0718 T12:   0.2007                                     
REMARK   3      T13:   0.1452 T23:  -0.1690                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  18.6726 L22:   2.4116                                     
REMARK   3      L33:   2.6537 L12:   3.7166                                     
REMARK   3      L13:  -7.0220 L23:  -1.2501                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1487 S12:   0.9052 S13:  -0.4648                       
REMARK   3      S21:  -0.4848 S22:  -0.7128 S23:  -0.2696                       
REMARK   3      S31:   0.6866 S32:  -0.0480 S33:   0.8616                       
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 :   A   638        A   669                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.2129  25.9043  30.3958              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2764 T22:  -0.1982                                     
REMARK   3      T33:  -0.0381 T12:   0.0379                                     
REMARK   3      T13:   0.1047 T23:   0.0823                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  22.4648 L22:   9.0509                                     
REMARK   3      L33:  13.7257 L12:  -2.6355                                     
REMARK   3      L13:  -4.6578 L23:   0.8083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3551 S12:   0.9748 S13:   2.1283                       
REMARK   3      S21:  -0.3953 S22:  -0.1893 S23:  -0.2305                       
REMARK   3      S31:  -1.3561 S32:  -0.8369 S33:  -0.1658                       
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 :   B   215        B   603                          
REMARK   3    ORIGIN FOR THE GROUP (A): -93.8268  25.7248  98.4159              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0456 T22:  -0.2718                                     
REMARK   3      T33:  -0.2398 T12:   0.0666                                     
REMARK   3      T13:   0.0588 T23:   0.1195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0675 L22:   3.2934                                     
REMARK   3      L33:   6.9591 L12:  -0.6101                                     
REMARK   3      L13:  -0.5175 L23:   1.6921                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2244 S12:  -0.6820 S13:  -0.2314                       
REMARK   3      S21:   0.9187 S22:   0.1942 S23:   0.0580                       
REMARK   3      S31:   1.3268 S32:   0.2802 S33:   0.0302                       
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 :   B   604        B   637                          
REMARK   3    ORIGIN FOR THE GROUP (A):-115.6982  44.2967 110.5126              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2655 T22:   0.3347                                     
REMARK   3      T33:  -0.0139 T12:   0.0112                                     
REMARK   3      T13:   0.2622 T23:  -0.2546                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6190 L22:  11.7823                                     
REMARK   3      L33:   5.6020 L12:  -6.5176                                     
REMARK   3      L13:  -4.1588 L23:   8.0994                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2671 S12:  -0.7537 S13:   0.0329                       
REMARK   3      S21:   0.8364 S22:  -0.7344 S23:   0.6956                       
REMARK   3      S31:   0.5133 S32:  -1.7316 S33:   1.0016                       
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 :   B   638        B   669                          
REMARK   3    ORIGIN FOR THE GROUP (A):-121.1590  63.5520 125.1252              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2171 T22:   0.2653                                     
REMARK   3      T33:   0.0980 T12:  -0.2963                                     
REMARK   3      T13:   0.1124 T23:  -0.2625                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.3274 L22:  17.8894                                     
REMARK   3      L33:  14.4959 L12: -12.4133                                     
REMARK   3      L13:  -3.0830 L23:   5.9628                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5721 S12:  -0.6673 S13:   1.4019                       
REMARK   3      S21:  -0.0751 S22:   0.9530 S23:  -1.5982                       
REMARK   3      S31:  -0.4095 S32:   1.9245 S33:  -0.3809                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3HO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053373.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
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) : 0.97940, 0.97955, 0.91176          
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200                                   SI(111). A SECOND SET OF SI(220)   
REMARK 200                                   CRYSTALS IS ALSO AVAILABLE.        
REMARK 200  OPTICS                         : FLAT COLLIMATING MIRROR, DOUBLE    
REMARK 200                                   CRYSTAL MONOCHROMATOR, TOROID      
REMARK 200                                   FOCUSING MIRROR                    
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   : 33657                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.56800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SAMPLES (0.3-2 UL) WERE          
REMARK 280  DEHYDRATED OVER 500 UL OF RESERVOIR SOLUTION OF 20 MM HEPES PH      
REMARK 280  7.2 AND 3 M NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      101.64100            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      203.28200            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      203.28200            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      101.64100            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     SER A   193                                                      
REMARK 465     ASN A   194                                                      
REMARK 465     TYR A   195                                                      
REMARK 465     LEU A   196                                                      
REMARK 465     ASP A   197                                                      
REMARK 465     GLN A   198                                                      
REMARK 465     MSE A   199                                                      
REMARK 465     GLU A   200                                                      
REMARK 465     GLU A   201                                                      
REMARK 465     TYR A   202                                                      
REMARK 465     ASP A   203                                                      
REMARK 465     LYS A   204                                                      
REMARK 465     VAL A   205                                                      
REMARK 465     GLU A   206                                                      
REMARK 465     GLU A   207                                                      
REMARK 465     ILE A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     ARG A   210                                                      
REMARK 465     LYS A   211                                                      
REMARK 465     HIS A   212                                                      
REMARK 465     LYS A   213                                                      
REMARK 465     ASN A   306                                                      
REMARK 465     GLN A   307                                                      
REMARK 465     GLU A   308                                                      
REMARK 465     ARG A   309                                                      
REMARK 465     TRP A   310                                                      
REMARK 465     ALA A   311                                                      
REMARK 465     ILE A   312                                                      
REMARK 465     GLY A   313                                                      
REMARK 465     PRO A   314                                                      
REMARK 465     PRO A   441                                                      
REMARK 465     THR A   442                                                      
REMARK 465     ASP A   443                                                      
REMARK 465     ILE A   444                                                      
REMARK 465     ASN A   445                                                      
REMARK 465     ILE A   446                                                      
REMARK 465     SER A   570                                                      
REMARK 465     MSE A   571                                                      
REMARK 465     THR A   572                                                      
REMARK 465     GLN A   573                                                      
REMARK 465     HIS A   670                                                      
REMARK 465     HIS A   671                                                      
REMARK 465     HIS A   672                                                      
REMARK 465     HIS A   673                                                      
REMARK 465     SER B   193                                                      
REMARK 465     ASN B   194                                                      
REMARK 465     TYR B   195                                                      
REMARK 465     LEU B   196                                                      
REMARK 465     ASP B   197                                                      
REMARK 465     GLN B   198                                                      
REMARK 465     MSE B   199                                                      
REMARK 465     GLU B   200                                                      
REMARK 465     GLU B   201                                                      
REMARK 465     TYR B   202                                                      
REMARK 465     ASP B   203                                                      
REMARK 465     LYS B   204                                                      
REMARK 465     VAL B   205                                                      
REMARK 465     GLU B   206                                                      
REMARK 465     GLU B   207                                                      
REMARK 465     ILE B   208                                                      
REMARK 465     SER B   209                                                      
REMARK 465     ARG B   210                                                      
REMARK 465     LYS B   211                                                      
REMARK 465     HIS B   212                                                      
REMARK 465     LYS B   213                                                      
REMARK 465     ASN B   306                                                      
REMARK 465     GLN B   307                                                      
REMARK 465     GLU B   308                                                      
REMARK 465     ARG B   309                                                      
REMARK 465     TRP B   310                                                      
REMARK 465     ALA B   311                                                      
REMARK 465     ILE B   312                                                      
REMARK 465     GLY B   313                                                      
REMARK 465     PRO B   314                                                      
REMARK 465     PRO B   441                                                      
REMARK 465     THR B   442                                                      
REMARK 465     ASP B   443                                                      
REMARK 465     ILE B   444                                                      
REMARK 465     ASN B   445                                                      
REMARK 465     ILE B   446                                                      
REMARK 465     HIS B   671                                                      
REMARK 465     HIS B   672                                                      
REMARK 465     HIS B   673                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  381   CB   CG   CD   OE1  OE2                             
REMARK 480     LYS B  277   CB   CG   CD   CE   NZ                              
REMARK 480     ASP B  383   CB   CG   OD1  OD2                                  
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    LYS B 277   CB  -  CA  -  C   ANGL. DEV. = -12.1 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    VAL A 222      -62.08    -95.37                                   
REMARK 500    GLN A 228       79.78     51.52                                   
REMARK 500    LYS A 277     -155.28   -141.46                                   
REMARK 500    ASP A 362       -8.25     72.72                                   
REMARK 500    ASP A 383      -75.54   -106.09                                   
REMARK 500    ASN A 403      -72.76    -94.56                                   
REMARK 500    ARG A 410      -79.73     14.03                                   
REMARK 500    SER A 417      153.27     64.56                                   
REMARK 500    THR A 418      -36.18   -159.76                                   
REMARK 500    GLN A 420      139.30     75.42                                   
REMARK 500    HIS A 430      -75.53   -111.07                                   
REMARK 500    ILE A 469     -169.17   -105.17                                   
REMARK 500    LYS A 470       98.29    -68.56                                   
REMARK 500    LYS A 528       -0.53     62.17                                   
REMARK 500    HIS A 575       42.32    129.58                                   
REMARK 500    CYS A 612       86.84    -57.77                                   
REMARK 500    ARG A 613      -76.28    -45.90                                   
REMARK 500    PRO A 627      118.53    -35.36                                   
REMARK 500    GLU A 640      -70.83    -48.21                                   
REMARK 500    SER B 224     -164.82   -122.74                                   
REMARK 500    GLN B 228       72.08     44.03                                   
REMARK 500    GLN B 240       34.60    -79.19                                   
REMARK 500    LYS B 277     -153.88   -111.85                                   
REMARK 500    PRO B 291      -17.59    -49.33                                   
REMARK 500    ASP B 316     -104.88     64.54                                   
REMARK 500    ASP B 362       -5.12     68.37                                   
REMARK 500    ASP B 398       54.56    -92.03                                   
REMARK 500    ASN B 416       38.71    -84.08                                   
REMARK 500    SER B 417     -101.83     41.67                                   
REMARK 500    THR B 418      -75.34     42.13                                   
REMARK 500    ASN B 419       99.67    -63.33                                   
REMARK 500    HIS B 430      -81.14   -102.71                                   
REMARK 500    LEU B 480       54.61   -108.52                                   
REMARK 500    ASN B 488       32.12   -156.01                                   
REMARK 500    SER B 524      115.21    -37.73                                   
REMARK 500    VAL B 526      -71.39   -114.15                                   
REMARK 500    LYS B 528       85.35     61.03                                   
REMARK 500    SER B 542      -26.71    -38.39                                   
REMARK 500    HIS B 575       71.36     40.98                                   
REMARK 500    ASN B 576       50.95   -141.19                                   
REMARK 500    ASN B 614       42.46     87.48                                   
REMARK 500    TYR B 616     -179.49    -68.50                                   
REMARK 500    ALA B 642      177.71    159.54                                   
REMARK 500    HIS B 669      -72.85    -71.43                                   
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 GLU A  281     ARG A  282                 -149.85                    
REMARK 500 PRO A  409     ARG A  410                  146.55                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLN B 420        23.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3HO3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HO5   RELATED DB: PDB                                   
DBREF  3HO4 A  193   667  UNP    Q96QV1   HHIP_HUMAN     193    667             
DBREF  3HO4 B  193   667  UNP    Q96QV1   HHIP_HUMAN     193    667             
SEQADV 3HO4 HIS A  668  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO4 HIS A  669  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO4 HIS A  670  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO4 HIS A  671  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO4 HIS A  672  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO4 HIS A  673  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO4 HIS B  668  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO4 HIS B  669  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO4 HIS B  670  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO4 HIS B  671  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO4 HIS B  672  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO4 HIS B  673  UNP  Q96QV1              EXPRESSION TAG                 
SEQRES   1 A  481  SER ASN TYR LEU ASP GLN MSE GLU GLU TYR ASP LYS VAL          
SEQRES   2 A  481  GLU GLU ILE SER ARG LYS HIS LYS HIS ASN CYS PHE CYS          
SEQRES   3 A  481  ILE GLN GLU VAL VAL SER GLY LEU ARG GLN PRO VAL GLY          
SEQRES   4 A  481  ALA LEU HIS SER GLY ASP GLY SER GLN ARG LEU PHE ILE          
SEQRES   5 A  481  LEU GLU LYS GLU GLY TYR VAL LYS ILE LEU THR PRO GLU          
SEQRES   6 A  481  GLY GLU ILE PHE LYS GLU PRO TYR LEU ASP ILE HIS LYS          
SEQRES   7 A  481  LEU VAL GLN SER GLY ILE LYS GLY GLY ASP GLU ARG GLY          
SEQRES   8 A  481  LEU LEU SER LEU ALA PHE HIS PRO ASN TYR LYS LYS ASN          
SEQRES   9 A  481  GLY LYS LEU TYR VAL SER TYR THR THR ASN GLN GLU ARG          
SEQRES  10 A  481  TRP ALA ILE GLY PRO HIS ASP HIS ILE LEU ARG VAL VAL          
SEQRES  11 A  481  GLU TYR THR VAL SER ARG LYS ASN PRO HIS GLN VAL ASP          
SEQRES  12 A  481  LEU ARG THR ALA ARG VAL PHE LEU GLU VAL ALA GLU LEU          
SEQRES  13 A  481  HIS ARG LYS HIS LEU GLY GLY GLN LEU LEU PHE GLY PRO          
SEQRES  14 A  481  ASP GLY PHE LEU TYR ILE ILE LEU GLY ASP GLY MSE ILE          
SEQRES  15 A  481  THR LEU ASP ASP MSE GLU GLU MSE ASP GLY LEU SER ASP          
SEQRES  16 A  481  PHE THR GLY SER VAL LEU ARG LEU ASP VAL ASP THR ASP          
SEQRES  17 A  481  MSE CYS ASN VAL PRO TYR SER ILE PRO ARG SER ASN PRO          
SEQRES  18 A  481  HIS PHE ASN SER THR ASN GLN PRO PRO GLU VAL PHE ALA          
SEQRES  19 A  481  HIS GLY LEU HIS ASP PRO GLY ARG CYS ALA VAL ASP ARG          
SEQRES  20 A  481  HIS PRO THR ASP ILE ASN ILE ASN LEU THR ILE LEU CYS          
SEQRES  21 A  481  SER ASP SER ASN GLY LYS ASN ARG SER SER ALA ARG ILE          
SEQRES  22 A  481  LEU GLN ILE ILE LYS GLY LYS ASP TYR GLU SER GLU PRO          
SEQRES  23 A  481  SER LEU LEU GLU PHE LYS PRO PHE SER ASN GLY PRO LEU          
SEQRES  24 A  481  VAL GLY GLY PHE VAL TYR ARG GLY CYS GLN SER GLU ARG          
SEQRES  25 A  481  LEU TYR GLY SER TYR VAL PHE GLY ASP ARG ASN GLY ASN          
SEQRES  26 A  481  PHE LEU THR LEU GLN GLN SER PRO VAL THR LYS GLN TRP          
SEQRES  27 A  481  GLN GLU LYS PRO LEU CYS LEU GLY THR SER GLY SER CYS          
SEQRES  28 A  481  ARG GLY TYR PHE SER GLY HIS ILE LEU GLY PHE GLY GLU          
SEQRES  29 A  481  ASP GLU LEU GLY GLU VAL TYR ILE LEU SER SER SER LYS          
SEQRES  30 A  481  SER MSE THR GLN THR HIS ASN GLY LYS LEU TYR LYS ILE          
SEQRES  31 A  481  VAL ASP PRO LYS ARG PRO LEU MSE PRO GLU GLU CYS ARG          
SEQRES  32 A  481  ALA THR VAL GLN PRO ALA GLN THR LEU THR SER GLU CYS          
SEQRES  33 A  481  SER ARG LEU CYS ARG ASN GLY TYR CYS THR PRO THR GLY          
SEQRES  34 A  481  LYS CYS CYS CYS SER PRO GLY TRP GLU GLY ASP PHE CYS          
SEQRES  35 A  481  ARG THR ALA LYS CYS GLU PRO ALA CYS ARG HIS GLY GLY          
SEQRES  36 A  481  VAL CYS VAL ARG PRO ASN LYS CYS LEU CYS LYS LYS GLY          
SEQRES  37 A  481  TYR LEU GLY PRO GLN CYS GLU HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  481  SER ASN TYR LEU ASP GLN MSE GLU GLU TYR ASP LYS VAL          
SEQRES   2 B  481  GLU GLU ILE SER ARG LYS HIS LYS HIS ASN CYS PHE CYS          
SEQRES   3 B  481  ILE GLN GLU VAL VAL SER GLY LEU ARG GLN PRO VAL GLY          
SEQRES   4 B  481  ALA LEU HIS SER GLY ASP GLY SER GLN ARG LEU PHE ILE          
SEQRES   5 B  481  LEU GLU LYS GLU GLY TYR VAL LYS ILE LEU THR PRO GLU          
SEQRES   6 B  481  GLY GLU ILE PHE LYS GLU PRO TYR LEU ASP ILE HIS LYS          
SEQRES   7 B  481  LEU VAL GLN SER GLY ILE LYS GLY GLY ASP GLU ARG GLY          
SEQRES   8 B  481  LEU LEU SER LEU ALA PHE HIS PRO ASN TYR LYS LYS ASN          
SEQRES   9 B  481  GLY LYS LEU TYR VAL SER TYR THR THR ASN GLN GLU ARG          
SEQRES  10 B  481  TRP ALA ILE GLY PRO HIS ASP HIS ILE LEU ARG VAL VAL          
SEQRES  11 B  481  GLU TYR THR VAL SER ARG LYS ASN PRO HIS GLN VAL ASP          
SEQRES  12 B  481  LEU ARG THR ALA ARG VAL PHE LEU GLU VAL ALA GLU LEU          
SEQRES  13 B  481  HIS ARG LYS HIS LEU GLY GLY GLN LEU LEU PHE GLY PRO          
SEQRES  14 B  481  ASP GLY PHE LEU TYR ILE ILE LEU GLY ASP GLY MSE ILE          
SEQRES  15 B  481  THR LEU ASP ASP MSE GLU GLU MSE ASP GLY LEU SER ASP          
SEQRES  16 B  481  PHE THR GLY SER VAL LEU ARG LEU ASP VAL ASP THR ASP          
SEQRES  17 B  481  MSE CYS ASN VAL PRO TYR SER ILE PRO ARG SER ASN PRO          
SEQRES  18 B  481  HIS PHE ASN SER THR ASN GLN PRO PRO GLU VAL PHE ALA          
SEQRES  19 B  481  HIS GLY LEU HIS ASP PRO GLY ARG CYS ALA VAL ASP ARG          
SEQRES  20 B  481  HIS PRO THR ASP ILE ASN ILE ASN LEU THR ILE LEU CYS          
SEQRES  21 B  481  SER ASP SER ASN GLY LYS ASN ARG SER SER ALA ARG ILE          
SEQRES  22 B  481  LEU GLN ILE ILE LYS GLY LYS ASP TYR GLU SER GLU PRO          
SEQRES  23 B  481  SER LEU LEU GLU PHE LYS PRO PHE SER ASN GLY PRO LEU          
SEQRES  24 B  481  VAL GLY GLY PHE VAL TYR ARG GLY CYS GLN SER GLU ARG          
SEQRES  25 B  481  LEU TYR GLY SER TYR VAL PHE GLY ASP ARG ASN GLY ASN          
SEQRES  26 B  481  PHE LEU THR LEU GLN GLN SER PRO VAL THR LYS GLN TRP          
SEQRES  27 B  481  GLN GLU LYS PRO LEU CYS LEU GLY THR SER GLY SER CYS          
SEQRES  28 B  481  ARG GLY TYR PHE SER GLY HIS ILE LEU GLY PHE GLY GLU          
SEQRES  29 B  481  ASP GLU LEU GLY GLU VAL TYR ILE LEU SER SER SER LYS          
SEQRES  30 B  481  SER MSE THR GLN THR HIS ASN GLY LYS LEU TYR LYS ILE          
SEQRES  31 B  481  VAL ASP PRO LYS ARG PRO LEU MSE PRO GLU GLU CYS ARG          
SEQRES  32 B  481  ALA THR VAL GLN PRO ALA GLN THR LEU THR SER GLU CYS          
SEQRES  33 B  481  SER ARG LEU CYS ARG ASN GLY TYR CYS THR PRO THR GLY          
SEQRES  34 B  481  LYS CYS CYS CYS SER PRO GLY TRP GLU GLY ASP PHE CYS          
SEQRES  35 B  481  ARG THR ALA LYS CYS GLU PRO ALA CYS ARG HIS GLY GLY          
SEQRES  36 B  481  VAL CYS VAL ARG PRO ASN LYS CYS LEU CYS LYS LYS GLY          
SEQRES  37 B  481  TYR LEU GLY PRO GLN CYS GLU HIS HIS HIS HIS HIS HIS          
MODRES 3HO4 MSE A  373  MET  SELENOMETHIONINE                                   
MODRES 3HO4 MSE A  379  MET  SELENOMETHIONINE                                   
MODRES 3HO4 MSE A  382  MET  SELENOMETHIONINE                                   
MODRES 3HO4 MSE A  401  MET  SELENOMETHIONINE                                   
MODRES 3HO4 MSE A  590  MET  SELENOMETHIONINE                                   
MODRES 3HO4 MSE B  373  MET  SELENOMETHIONINE                                   
MODRES 3HO4 MSE B  379  MET  SELENOMETHIONINE                                   
MODRES 3HO4 MSE B  382  MET  SELENOMETHIONINE                                   
MODRES 3HO4 MSE B  401  MET  SELENOMETHIONINE                                   
MODRES 3HO4 MSE B  571  MET  SELENOMETHIONINE                                   
MODRES 3HO4 MSE B  590  MET  SELENOMETHIONINE                                   
HET    MSE  A 373       8                                                       
HET    MSE  A 379       8                                                       
HET    MSE  A 382       8                                                       
HET    MSE  A 401       8                                                       
HET    MSE  A 590       8                                                       
HET    MSE  B 373       8                                                       
HET    MSE  B 379       8                                                       
HET    MSE  B 382       8                                                       
HET    MSE  B 401       8                                                       
HET    MSE  B 571       8                                                       
HET    MSE  B 590       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    11(C5 H11 N O2 SE)                                           
HELIX    1   1 ASN A  292  GLY A  297  1                                   6    
HELIX    2   2 PRO A  361  GLY A  363  5                                   3    
HELIX    3   3 LEU A  376  MSE A  382  1                                   7    
HELIX    4   4 PRO A  591  ARG A  595  5                                   5    
HELIX    5   5 SER A  606  CYS A  612  1                                   7    
HELIX    6   6 ASN B  292  GLY B  297  1                                   6    
HELIX    7   7 PRO B  361  GLY B  363  5                                   3    
HELIX    8   8 LEU B  376  MSE B  382  1                                   7    
HELIX    9   9 SER B  568  THR B  574  1                                   7    
HELIX   10  10 PRO B  591  ARG B  595  5                                   5    
HELIX   11  11 SER B  606  CYS B  612  1                                   7    
SHEET    1   A 4 CYS A 218  LEU A 226  0                                        
SHEET    2   A 4 GLY A 577  VAL A 583 -1  O  VAL A 583   N  CYS A 218           
SHEET    3   A 4 VAL A 562  SER A 567 -1  N  SER A 566   O  LYS A 578           
SHEET    4   A 4 HIS A 550  GLU A 556 -1  N  LEU A 552   O  LEU A 565           
SHEET    1   B 4 PRO A 229  LEU A 233  0                                        
SHEET    2   B 4 LEU A 242  GLU A 246 -1  O  PHE A 243   N  LEU A 233           
SHEET    3   B 4 TYR A 250  LEU A 254 -1  O  LYS A 252   N  ILE A 244           
SHEET    4   B 4 LEU A 266  ASP A 267 -1  O  LEU A 266   N  VAL A 251           
SHEET    1   C 4 LEU A 284  PHE A 289  0                                        
SHEET    2   C 4 LYS A 298  THR A 304 -1  O  TYR A 300   N  ALA A 288           
SHEET    3   C 4 HIS A 317  VAL A 326 -1  O  VAL A 322   N  VAL A 301           
SHEET    4   C 4 VAL A 334  GLU A 347 -1  O  VAL A 345   N  LEU A 319           
SHEET    1   D 4 GLY A 354  PHE A 359  0                                        
SHEET    2   D 4 LEU A 365  LEU A 369 -1  O  TYR A 366   N  LEU A 358           
SHEET    3   D 4 SER A 391  LEU A 395 -1  O  LEU A 393   N  ILE A 367           
SHEET    4   D 4 VAL A 424  HIS A 427 -1  O  ALA A 426   N  VAL A 392           
SHEET    1   E 4 ALA A 436  ASP A 438  0                                        
SHEET    2   E 4 LEU A 448  ASP A 454 -1  O  THR A 449   N  ASP A 438           
SHEET    3   E 4 SER A 462  ILE A 468 -1  O  ARG A 464   N  CYS A 452           
SHEET    4   E 4 LEU A 481  PHE A 483 -1  O  PHE A 483   N  ALA A 463           
SHEET    1   F 4 GLY A 493  VAL A 496  0                                        
SHEET    2   F 4 TYR A 509  GLY A 512 -1  O  VAL A 510   N  PHE A 495           
SHEET    3   F 4 PHE A 518  GLN A 523 -1  O  LEU A 519   N  PHE A 511           
SHEET    4   F 4 TRP A 530  LEU A 535 -1  O  GLN A 531   N  GLN A 522           
SHEET    1   G 2 GLY A 615  CYS A 617  0                                        
SHEET    2   G 2 CYS A 623  CYS A 625 -1  O  CYS A 624   N  TYR A 616           
SHEET    1   H 2 TRP A 629  GLU A 630  0                                        
SHEET    2   H 2 THR A 636  ALA A 637 -1  O  THR A 636   N  GLU A 630           
SHEET    1   I 2 VAL A 648  ARG A 651  0                                        
SHEET    2   I 2 LYS A 654  LEU A 656 -1  O  LEU A 656   N  VAL A 648           
SHEET    1   J 4 CYS B 218  LEU B 226  0                                        
SHEET    2   J 4 GLY B 577  VAL B 583 -1  O  VAL B 583   N  CYS B 218           
SHEET    3   J 4 VAL B 562  SER B 567 -1  N  ILE B 564   O  TYR B 580           
SHEET    4   J 4 HIS B 550  GLU B 556 -1  N  LEU B 552   O  LEU B 565           
SHEET    1   K 4 PRO B 229  LEU B 233  0                                        
SHEET    2   K 4 LEU B 242  GLU B 246 -1  O  PHE B 243   N  LEU B 233           
SHEET    3   K 4 TYR B 250  LEU B 254 -1  O  TYR B 250   N  GLU B 246           
SHEET    4   K 4 LEU B 266  ASP B 267 -1  O  LEU B 266   N  VAL B 251           
SHEET    1   L 4 LEU B 284  PHE B 289  0                                        
SHEET    2   L 4 LYS B 298  THR B 304 -1  O  TYR B 300   N  ALA B 288           
SHEET    3   L 4 HIS B 317  VAL B 326 -1  O  TYR B 324   N  LEU B 299           
SHEET    4   L 4 VAL B 334  GLU B 347 -1  O  VAL B 345   N  LEU B 319           
SHEET    1   M 4 GLY B 354  PHE B 359  0                                        
SHEET    2   M 4 LEU B 365  LEU B 369 -1  O  TYR B 366   N  LEU B 358           
SHEET    3   M 4 SER B 391  LEU B 395 -1  O  LEU B 393   N  ILE B 367           
SHEET    4   M 4 VAL B 424  HIS B 427 -1  O  ALA B 426   N  VAL B 392           
SHEET    1   N 4 ALA B 436  ASP B 438  0                                        
SHEET    2   N 4 LEU B 448  ASP B 454 -1  O  THR B 449   N  ASP B 438           
SHEET    3   N 4 SER B 462  ILE B 468 -1  O  ARG B 464   N  CYS B 452           
SHEET    4   N 4 GLU B 482  PHE B 483 -1  O  PHE B 483   N  ALA B 463           
SHEET    1   O 4 GLY B 493  VAL B 496  0                                        
SHEET    2   O 4 TYR B 509  GLY B 512 -1  O  VAL B 510   N  PHE B 495           
SHEET    3   O 4 PHE B 518  LEU B 521 -1  O  LEU B 519   N  PHE B 511           
SHEET    4   O 4 GLU B 532  LEU B 535 -1  O  LEU B 535   N  PHE B 518           
SHEET    1   P 2 TRP B 629  GLU B 630  0                                        
SHEET    2   P 2 THR B 636  ALA B 637 -1  O  THR B 636   N  GLU B 630           
SHEET    1   Q 2 VAL B 648  ARG B 651  0                                        
SHEET    2   Q 2 LYS B 654  LEU B 656 -1  O  LEU B 656   N  VAL B 648           
SSBOND   1 CYS A  216    CYS A  536                          1555   1555  2.03  
SSBOND   2 CYS A  218    CYS A  543                          1555   1555  2.02  
SSBOND   3 CYS A  402    CYS A  624                          1555   1555  2.04  
SSBOND   4 CYS A  435    CYS A  452                          1555   1555  2.02  
SSBOND   5 CYS A  500    CYS A  594                          1555   1555  2.04  
SSBOND   6 CYS A  608    CYS A  617                          1555   1555  2.03  
SSBOND   7 CYS A  612    CYS A  623                          1555   1555  2.04  
SSBOND   8 CYS A  625    CYS A  634                          1555   1555  2.03  
SSBOND   9 CYS A  639    CYS A  649                          1555   1555  2.04  
SSBOND  10 CYS A  643    CYS A  655                          1555   1555  2.04  
SSBOND  11 CYS A  657    CYS A  666                          1555   1555  2.04  
SSBOND  12 CYS B  216    CYS B  536                          1555   1555  2.04  
SSBOND  13 CYS B  218    CYS B  543                          1555   1555  2.03  
SSBOND  14 CYS B  402    CYS B  624                          1555   1555  2.03  
SSBOND  15 CYS B  435    CYS B  452                          1555   1555  2.04  
SSBOND  16 CYS B  500    CYS B  594                          1555   1555  2.04  
SSBOND  17 CYS B  608    CYS B  617                          1555   1555  2.03  
SSBOND  18 CYS B  612    CYS B  623                          1555   1555  2.03  
SSBOND  19 CYS B  625    CYS B  634                          1555   1555  2.03  
SSBOND  20 CYS B  639    CYS B  649                          1555   1555  2.03  
SSBOND  21 CYS B  643    CYS B  655                          1555   1555  2.03  
SSBOND  22 CYS B  657    CYS B  666                          1555   1555  2.03  
LINK         C   GLY A 372                 N   MSE A 373     1555   1555  1.34  
LINK         C   MSE A 373                 N   ILE A 374     1555   1555  1.33  
LINK         C   ASP A 378                 N   MSE A 379     1555   1555  1.33  
LINK         C   MSE A 379                 N   GLU A 380     1555   1555  1.33  
LINK         C   GLU A 381                 N   MSE A 382     1555   1555  1.33  
LINK         C   MSE A 382                 N   ASP A 383     1555   1555  1.33  
LINK         C   ASP A 400                 N   MSE A 401     1555   1555  1.33  
LINK         C   MSE A 401                 N   CYS A 402     1555   1555  1.33  
LINK         C   LEU A 589                 N   MSE A 590     1555   1555  1.33  
LINK         C   MSE A 590                 N   PRO A 591     1555   1555  1.35  
LINK         C   GLY B 372                 N   MSE B 373     1555   1555  1.33  
LINK         C   MSE B 373                 N   ILE B 374     1555   1555  1.33  
LINK         C   ASP B 378                 N   MSE B 379     1555   1555  1.33  
LINK         C   MSE B 379                 N   GLU B 380     1555   1555  1.33  
LINK         C   GLU B 381                 N   MSE B 382     1555   1555  1.33  
LINK         C   MSE B 382                 N   ASP B 383     1555   1555  1.33  
LINK         C   ASP B 400                 N   MSE B 401     1555   1555  1.33  
LINK         C   MSE B 401                 N   CYS B 402     1555   1555  1.33  
LINK         C   SER B 570                 N   MSE B 571     1555   1555  1.33  
LINK         C   MSE B 571                 N   THR B 572     1555   1555  1.34  
LINK         C   LEU B 589                 N   MSE B 590     1555   1555  1.33  
LINK         C   MSE B 590                 N   PRO B 591     1555   1555  1.35  
CRYST1  101.042  101.042  304.923  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009897  0.005714  0.000000        0.00000                         
SCALE2      0.000000  0.011428  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003280        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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