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Database: PDB
Entry: 3N7P
LinkDB: 3N7P
Original site: 3N7P 
HEADER    MEMBRANE PROTEIN                        27-MAY-10   3N7P              
TITLE     CRYSTAL STRUCTURE OF THE ECTODOMAIN COMPLEX OF THE CGRP RECEPTOR, A   
TITLE    2 CLASS-B GPCR, REVEALS THE SITE OF DRUG ANTAGONISM                    
CAVEAT     3N7P    THE BACKBONE ON SEVERAL RESIDUES HAVE HIGH BOND ANGLE        
CAVEAT   2 3N7P    DEVIATION                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCITONIN GENE-RELATED PEPTIDE TYPE 1 RECEPTOR;           
COMPND   3 CHAIN: A, B, C, J;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 23-133;                                       
COMPND   5 SYNONYM: CGRP TYPE 1 RECEPTOR, CALCITONIN RECEPTOR-LIKE RECEPTOR;    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RECEPTOR ACTIVITY-MODIFYING PROTEIN 1;                     
COMPND   9 CHAIN: D, E, F, R;                                                   
COMPND  10 FRAGMENT: EXTRA-CELLULAR DOMAIN RESIDUES 26-117;                     
COMPND  11 SYNONYM: CALCITONIN-RECEPTOR-LIKE RECEPTOR ACTIVITY-MODIFYING PROTEIN
COMPND  12 1, CRLR ACTIVITY-MODIFYING PROTEIN 1;                                
COMPND  13 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: CALCRL, CALRL_HUMAN, CGRPR;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: RAMP1, RAMP1_HUMAN;                                            
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;                               
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    GPCR, CLASS B GPCR, ANTAGONIST, OLCEGEPANT, TELCAGEPANT, MIGRAINE,    
KEYWDS   2 MEMBRANE PROTEIN                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.TER HAAR                                                            
REVDAT   3   08-NOV-17 3N7P    1       REMARK                                   
REVDAT   2   22-SEP-10 3N7P    1       JRNL                                     
REVDAT   1   15-SEP-10 3N7P    0                                                
JRNL        AUTH   E.TER HAAR,C.M.KOTH,N.ABDUL-MANAN,L.SWENSON,J.T.COLL,        
JRNL        AUTH 2 J.A.LIPPKE,C.A.LEPRE,M.GARCIA-GUZMAN,J.M.MOORE               
JRNL        TITL   CRYSTAL STRUCTURE OF THE ECTODOMAIN COMPLEX OF THE CGRP      
JRNL        TITL 2 RECEPTOR, A CLASS-B GPCR, REVEALS THE SITE OF DRUG           
JRNL        TITL 3 ANTAGONISM.                                                  
JRNL        REF    STRUCTURE                     V.  18  1083 2010              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   20826335                                                     
JRNL        DOI    10.1016/J.STR.2010.05.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT BUSTER 2.9.2                              
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 37201                          
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)  : 0.215                          
REMARK   3   R VALUE            (WORKING SET)  : 0.214                          
REMARK   3   FREE R VALUE                      : 0.241                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.960                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1845                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 19                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.87                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1010                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2864                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 962                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2832                   
REMARK   3   BIN FREE R VALUE                        : 0.3524                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.75                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 48                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5324                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 80                                      
REMARK   3   SOLVENT ATOMS            : 53                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 97.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -15.56920                                            
REMARK   3    B22 (A**2) : -15.56920                                            
REMARK   3    B33 (A**2) : 31.13850                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.532               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.896                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.872                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5654   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7758   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1772   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 132    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 871    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5654   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 724    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : 6      ; 1.000  ; HARMONIC            
REMARK   3    UTILITY DISTANCES         : 20     ; 1.000  ; HARMONIC            
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 6195   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.06                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.44                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.29                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A29-A128 }                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   62.1708   45.9357   36.8736           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2245 T22:    0.1687                                    
REMARK   3     T33:   -0.1986 T12:   -0.0422                                    
REMARK   3     T13:   -0.1209 T23:    0.0039                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.6612 L22:    0.5600                                    
REMARK   3     L33:    5.6756 L12:   -1.6642                                    
REMARK   3     L13:    2.0276 L23:   -2.1814                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0010 S12:   -0.5805 S13:   -0.0558                     
REMARK   3     S21:    0.2539 S22:    0.0899 S23:   -0.2256                     
REMARK   3     S31:   -0.2206 S32:    0.1078 S33:   -0.0909                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B31-B129 }                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   37.8551   56.9652   36.0082           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3007 T22:    0.1283                                    
REMARK   3     T33:   -0.2726 T12:   -0.0676                                    
REMARK   3     T13:    0.0067 T23:   -0.0157                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.2767 L22:    3.2685                                    
REMARK   3     L33:    6.2873 L12:   -0.9099                                    
REMARK   3     L13:   -2.0910 L23:    2.1534                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0320 S12:   -0.6011 S13:    0.2810                     
REMARK   3     S21:    0.2819 S22:    0.0827 S23:    0.1838                     
REMARK   3     S31:    0.0056 S32:   -0.1084 S33:   -0.1147                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C35-C57 C66-C75 C|81-C91 C101-C124 }                 
REMARK   3    ORIGIN FOR THE GROUP (A):   21.6673   78.0336   65.4585           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1034 T22:    0.1397                                    
REMARK   3     T33:   -0.1565 T12:   -0.2417                                    
REMARK   3     T13:    0.0937 T23:   -0.1214                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -2.1760 L22:    2.6687                                    
REMARK   3     L33:    1.1743 L12:    1.6252                                    
REMARK   3     L13:   -1.6568 L23:    2.1399                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0763 S12:   -0.2160 S13:    0.1010                     
REMARK   3     S21:    0.0873 S22:   -0.0185 S23:   -0.0970                     
REMARK   3     S31:   -0.1785 S32:   -0.0796 S33:   -0.0578                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D27-D116 }                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   63.0695   46.9200   19.4082           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2767 T22:    0.1183                                    
REMARK   3     T33:   -0.1948 T12:   -0.0485                                    
REMARK   3     T13:   -0.0664 T23:   -0.0253                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.3164 L22:    2.0217                                    
REMARK   3     L33:    3.4957 L12:   -1.1990                                    
REMARK   3     L13:   -0.2973 L23:    0.2375                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1822 S12:   -0.0641 S13:   -0.0738                     
REMARK   3     S21:   -0.2127 S22:    0.0716 S23:   -0.1937                     
REMARK   3     S31:    0.2080 S32:    0.5965 S33:   -0.2538                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { E27-E105 }                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   62.5751   44.7246  -19.9140           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0648 T22:    0.0164                                    
REMARK   3     T33:   -0.2963 T12:    0.2336                                    
REMARK   3     T13:    0.0824 T23:   -0.1108                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.8769 L22:    3.9242                                    
REMARK   3     L33:    5.3816 L12:   -0.0624                                    
REMARK   3     L13:    0.3342 L23:    0.4331                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1698 S12:    0.1744 S13:   -0.2170                     
REMARK   3     S21:   -0.5185 S22:   -0.0844 S23:   -0.2045                     
REMARK   3     S31:   -0.0412 S32:    0.5619 S33:   -0.0854                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { F27-F105 }                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   32.5675   79.2559   51.4906           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1769 T22:    0.1716                                    
REMARK   3     T33:   -0.0212 T12:   -0.2456                                    
REMARK   3     T13:    0.1125 T23:   -0.1105                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1537 L22:    2.8985                                    
REMARK   3     L33:    3.1946 L12:    0.9955                                    
REMARK   3     L13:    0.0658 L23:    3.3734                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0101 S12:    0.0769 S13:    0.3221                     
REMARK   3     S21:   -0.0013 S22:   -0.0772 S23:   -0.0933                     
REMARK   3     S31:   -0.3593 S32:    0.0192 S33:    0.0671                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { J32-J128 }                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   55.2822   52.5889   -4.3181           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1306 T22:   -0.0781                                    
REMARK   3     T33:   -0.2262 T12:    0.0334                                    
REMARK   3     T13:   -0.0174 T23:   -0.0350                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.8759 L22:    2.1049                                    
REMARK   3     L33:    6.1248 L12:    0.9153                                    
REMARK   3     L13:   -1.0364 L23:   -0.1892                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1450 S12:    0.3438 S13:   -0.1027                     
REMARK   3     S21:   -0.2331 S22:   -0.1185 S23:   -0.2343                     
REMARK   3     S31:   -0.3006 S32:    0.3627 S33:   -0.0265                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { R27-R117 }                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   37.1227   53.8072   18.8850           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2135 T22:    0.0441                                    
REMARK   3     T33:   -0.1397 T12:   -0.0535                                    
REMARK   3     T13:   -0.0376 T23:    0.0117                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.5010 L22:    0.3731                                    
REMARK   3     L33:    2.3128 L12:   -1.3576                                    
REMARK   3     L13:   -0.2251 L23:   -0.0605                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.3630 S12:   -0.1304 S13:    0.0870                     
REMARK   3     S21:   -0.2296 S22:   -0.0139 S23:   -0.0091                     
REMARK   3     S31:   -0.1533 S32:   -0.4593 S33:   -0.3491                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3N7P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059484.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-SEP-06; 29-SEP-06               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ALS; ALS                           
REMARK 200  BEAMLINE                       : 5.0.2; 5.0.2                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9804; 1.0                        
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC QUANTUM     
REMARK 200                                   315                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39158                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.9                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 36.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SAD; SINGLE WAVELENGTH                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
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   (%): 73.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1-1.3M AMMONIUM SULFATE, 6-8% DIOXANE,   
REMARK 280  60-80MM MES PH 6.5, 10MM TRIS PH8.5 AND 200MM SODIUM NITRATE.       
REMARK 280  THE CRYSTALS WERE TRANSFERED TO 2.1M NAMALONATE (PH 7.0) PRIOR      
REMARK 280  TO FREEZING IN LIQUID NITROGEN., VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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      150.26667            
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       75.13333            
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       75.13333            
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      150.26667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: 2630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, R                                  
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: 2470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 1060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9390 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
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: 4                                                       
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: 2520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9890 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, J                                  
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     GLY A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     MET A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     GLU A    25                                                      
REMARK 465     GLU A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     VAL A   129                                                      
REMARK 465     ASN A   130                                                      
REMARK 465     THR A   131                                                      
REMARK 465     HIS A   132                                                      
REMARK 465     GLU A   133                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     HIS B    21                                                      
REMARK 465     MET B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     LEU B    24                                                      
REMARK 465     GLU B    25                                                      
REMARK 465     GLU B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     GLU B    29                                                      
REMARK 465     ASP B    30                                                      
REMARK 465     ASN B   130                                                      
REMARK 465     THR B   131                                                      
REMARK 465     HIS B   132                                                      
REMARK 465     GLU B   133                                                      
REMARK 465     GLY C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     HIS C    21                                                      
REMARK 465     MET C    22                                                      
REMARK 465     GLU C    23                                                      
REMARK 465     LEU C    24                                                      
REMARK 465     GLU C    25                                                      
REMARK 465     GLU C    26                                                      
REMARK 465     SER C    27                                                      
REMARK 465     PRO C    28                                                      
REMARK 465     GLU C    29                                                      
REMARK 465     ASP C    30                                                      
REMARK 465     SER C    31                                                      
REMARK 465     ILE C    32                                                      
REMARK 465     GLN C    33                                                      
REMARK 465     LEU C    34                                                      
REMARK 465     GLN C    58                                                      
REMARK 465     GLN C    59                                                      
REMARK 465     ALA C    60                                                      
REMARK 465     GLU C    61                                                      
REMARK 465     GLY C    62                                                      
REMARK 465     VAL C    63                                                      
REMARK 465     TYR C    64                                                      
REMARK 465     CYS C    65                                                      
REMARK 465     ASN C    76                                                      
REMARK 465     ASP C    77                                                      
REMARK 465     VAL C    78                                                      
REMARK 465     ALA C    79                                                      
REMARK 465     ALA C    80                                                      
REMARK 465     PHE C    92                                                      
REMARK 465     GLN C    93                                                      
REMARK 465     ASP C    94                                                      
REMARK 465     PHE C    95                                                      
REMARK 465     ASP C    96                                                      
REMARK 465     PRO C    97                                                      
REMARK 465     SER C    98                                                      
REMARK 465     GLU C    99                                                      
REMARK 465     LYS C   100                                                      
REMARK 465     THR C   125                                                      
REMARK 465     GLN C   126                                                      
REMARK 465     CYS C   127                                                      
REMARK 465     ASN C   128                                                      
REMARK 465     VAL C   129                                                      
REMARK 465     ASN C   130                                                      
REMARK 465     THR C   131                                                      
REMARK 465     HIS C   132                                                      
REMARK 465     GLU C   133                                                      
REMARK 465     GLY D    22                                                      
REMARK 465     SER D    23                                                      
REMARK 465     HIS D    24                                                      
REMARK 465     MET D    25                                                      
REMARK 465     ALA D    26                                                      
REMARK 465     SER D   117                                                      
REMARK 465     GLY E    22                                                      
REMARK 465     SER E    23                                                      
REMARK 465     HIS E    24                                                      
REMARK 465     MET E    25                                                      
REMARK 465     ALA E    26                                                      
REMARK 465     ILE E   106                                                      
REMARK 465     SER E   107                                                      
REMARK 465     GLY E   108                                                      
REMARK 465     ARG E   109                                                      
REMARK 465     ALA E   110                                                      
REMARK 465     VAL E   111                                                      
REMARK 465     ARG E   112                                                      
REMARK 465     ASP E   113                                                      
REMARK 465     PRO E   114                                                      
REMARK 465     PRO E   115                                                      
REMARK 465     GLY E   116                                                      
REMARK 465     SER E   117                                                      
REMARK 465     GLY F    22                                                      
REMARK 465     SER F    23                                                      
REMARK 465     HIS F    24                                                      
REMARK 465     MET F    25                                                      
REMARK 465     ALA F    26                                                      
REMARK 465     ILE F   106                                                      
REMARK 465     SER F   107                                                      
REMARK 465     GLY F   108                                                      
REMARK 465     ARG F   109                                                      
REMARK 465     ALA F   110                                                      
REMARK 465     VAL F   111                                                      
REMARK 465     ARG F   112                                                      
REMARK 465     ASP F   113                                                      
REMARK 465     PRO F   114                                                      
REMARK 465     PRO F   115                                                      
REMARK 465     GLY F   116                                                      
REMARK 465     SER F   117                                                      
REMARK 465     GLY J    19                                                      
REMARK 465     SER J    20                                                      
REMARK 465     HIS J    21                                                      
REMARK 465     MET J    22                                                      
REMARK 465     GLU J    23                                                      
REMARK 465     LEU J    24                                                      
REMARK 465     GLU J    25                                                      
REMARK 465     GLU J    26                                                      
REMARK 465     SER J    27                                                      
REMARK 465     PRO J    28                                                      
REMARK 465     GLU J    29                                                      
REMARK 465     ASP J    30                                                      
REMARK 465     SER J    31                                                      
REMARK 465     VAL J   129                                                      
REMARK 465     ASN J   130                                                      
REMARK 465     THR J   131                                                      
REMARK 465     HIS J   132                                                      
REMARK 465     GLU J   133                                                      
REMARK 465     GLY R    22                                                      
REMARK 465     SER R    23                                                      
REMARK 465     HIS R    24                                                      
REMARK 465     MET R    25                                                      
REMARK 465     ALA R    26                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  29    CB   CG   CD   OE1  OE2                             
REMARK 470     ASP A  30    CG   OD1  OD2                                       
REMARK 470     SER A  31    OG                                                  
REMARK 470     VAL A  36    CG1  CG2                                            
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     ILE A  57    CG1  CG2  CD1                                       
REMARK 470     GLN A  58    CB   CG   CD   OE1  NE2                             
REMARK 470     GLN A  59    CB   CG   CD   OE1  NE2                             
REMARK 470     ALA A  60    CB                                                  
REMARK 470     GLU A  61    CB   CG   CD   OE1  OE2                             
REMARK 470     LEU A  87    CG   CD1  CD2                                       
REMARK 470     GLN A  93    CG   CD   OE1  NE2                                  
REMARK 470     SER A  98    OG                                                  
REMARK 470     ILE A 104    CG1  CG2  CD1                                       
REMARK 470     ARG A 119    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B  31    OG                                                  
REMARK 470     ILE B  32    CB   CG1  CG2  CD1                                  
REMARK 470     VAL B  36    CG1  CG2                                            
REMARK 470     ILE B  57    CG1  CG2  CD1                                       
REMARK 470     GLN B  58    CB   CG   CD   OE1  NE2                             
REMARK 470     GLN B  59    CB   CG   CD   OE1  NE2                             
REMARK 470     ALA B  60    CB                                                  
REMARK 470     GLU B  61    CB   CG   CD   OE1  OE2                             
REMARK 470     SER B  84    OG                                                  
REMARK 470     ASP B  96    CG   OD1  OD2                                       
REMARK 470     SER B  98    OG                                                  
REMARK 470     ILE B 104    CG1  CG2  CD1                                       
REMARK 470     ASN B 128    CG   OD1  ND2                                       
REMARK 470     VAL B 129    CG1  CG2                                            
REMARK 470     VAL C  36    CG1  CG2                                            
REMARK 470     ARG C  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN C  39    CG   OD1  ND2                                       
REMARK 470     LYS C  40    CG   CD   CE   NZ                                   
REMARK 470     ILE C  41    CG1  CG2  CD1                                       
REMARK 470     THR C  43    OG1  CG2                                            
REMARK 470     GLN C  45    CG   CD   OE1  NE2                                  
REMARK 470     TYR C  46    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU C  47    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  50    CG   CD   OE1  NE2                                  
REMARK 470     LYS C  51    CG   CD   CE   NZ                                   
REMARK 470     ILE C  52    CG1  CG2  CD1                                       
REMARK 470     GLN C  54    CG   CD   OE1  NE2                                  
REMARK 470     ASP C  55    CG   OD1  OD2                                       
REMARK 470     PRO C  56    CG   CD                                             
REMARK 470     ILE C  57    CG1  CG2  CD1                                       
REMARK 470     ASN C  66    CG   OD1  ND2                                       
REMARK 470     ARG C  67    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR C  68    OG1  CG2                                            
REMARK 470     LEU C  73    CG   CD1  CD2                                       
REMARK 470     TRP C  75    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C  75    CZ3  CH2                                            
REMARK 470     THR C  82    OG1  CG2                                            
REMARK 470     GLU C  83    CG   CD   OE1  OE2                                  
REMARK 470     SER C  84    OG                                                  
REMARK 470     MSE C  85    CG  SE    CE                                        
REMARK 470     GLN C  86    CG   CD   OE1  NE2                                  
REMARK 470     LEU C  87    CG   CD1  CD2                                       
REMARK 470     CYS C  88    SG                                                  
REMARK 470     PRO C  89    CG   CD                                             
REMARK 470     ASP C  90    CG   OD1  OD2                                       
REMARK 470     VAL C 101    CG1  CG2                                            
REMARK 470     THR C 102    OG1  CG2                                            
REMARK 470     LYS C 103    CG   CD   CE   NZ                                   
REMARK 470     ILE C 104    CG1  CG2  CD1                                       
REMARK 470     CYS C 105    SG                                                  
REMARK 470     ASP C 106    CG   OD1  OD2                                       
REMARK 470     GLN C 107    CG   CD   OE1  NE2                                  
REMARK 470     ASP C 108    CG   OD1  OD2                                       
REMARK 470     TYR C 124    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN D  28    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  29    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  79    CG   CD   CE   NZ                                   
REMARK 470     ARG D 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER D 107    OG                                                  
REMARK 470     ARG D 109    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN E  28    CG   CD   OE1  NE2                                  
REMARK 470     GLU E  29    CG   CD   OE1  OE2                                  
REMARK 470     ASP E  47    CG   OD1  OD2                                       
REMARK 470     GLU E  49    CG   CD   OE1  OE2                                  
REMARK 470     VAL E  51    CB   CG1  CG2                                       
REMARK 470     LEU E  55    CG   CD1  CD2                                       
REMARK 470     ARG E  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E  63    CG1  CG2  CD1                                       
REMARK 470     ARG E  67    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER E 103    OG                                                  
REMARK 470     GLN F  28    CG   CD   OE1  NE2                                  
REMARK 470     GLU F  29    CG   CD   OE1  OE2                                  
REMARK 470     LEU F  35    CG   CD1  CD2                                       
REMARK 470     ARG F  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE F  44    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP F  47    CG   OD1  OD2                                       
REMARK 470     VAL F  51    CG1  CG2                                            
REMARK 470     THR F  54    OG1  CG2                                            
REMARK 470     LEU F  55    CG   CD1  CD2                                       
REMARK 470     TRP F  59    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP F  59    CZ3  CH2                                            
REMARK 470     ARG F  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR F  62    OG1  CG2                                            
REMARK 470     ILE F  63    CG1  CG2  CD1                                       
REMARK 470     ARG F  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER F  65    OG                                                  
REMARK 470     ARG F  67    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP F  71    CG   OD1  OD2                                       
REMARK 470     GLU F  88    CG   CD   OE1  OE2                                  
REMARK 470     VAL F  89    CG1  CG2                                            
REMARK 470     LEU F  94    CG   CD1  CD2                                       
REMARK 470     ARG F  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE F 101    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE J  32    CB   CG1  CG2  CD1                                  
REMARK 470     GLN J  33    CB   CG   CD   OE1  NE2                             
REMARK 470     LEU J  34    CG   CD1  CD2                                       
REMARK 470     VAL J  36    CG1  CG2                                            
REMARK 470     ILE J  57    CG1  CG2  CD1                                       
REMARK 470     GLN J  58    CB   CG   CD   OE1  NE2                             
REMARK 470     GLN J  59    CB   CG   CD   OE1  NE2                             
REMARK 470     GLU J  61    CG   CD   OE1  OE2                                  
REMARK 470     SER J  98    OG                                                  
REMARK 470     LYS J 100    CG   CD   CE   NZ                                   
REMARK 470     GLU R  29    CG   CD   OE1  OE2                                  
REMARK 470     GLN R  43    CG   CD   OE1  NE2                                  
REMARK 470     GLN R  45    CG   CD   OE1  NE2                                  
REMARK 470     LYS R  79    CG   CD   CE   NZ                                   
REMARK 470     ARG R 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER R 103    OG                                                  
REMARK 470     ARG R 109    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER R 117    OG                                                  
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   O    PRO B    56     NH2  ARG B    67              2.11            
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    PRO A  56   C     ILE A  57   N       0.211                       
REMARK 500    PRO B  56   C     ILE B  57   N       0.211                       
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    PRO A  56   CA  -  C   -  N   ANGL. DEV. = -31.3 DEGREES          
REMARK 500    PRO A  56   O   -  C   -  N   ANGL. DEV. =  25.6 DEGREES          
REMARK 500    GLN A  59   CA  -  C   -  N   ANGL. DEV. =  16.2 DEGREES          
REMARK 500    GLN A  59   O   -  C   -  N   ANGL. DEV. = -23.2 DEGREES          
REMARK 500    ALA A  60   C   -  N   -  CA  ANGL. DEV. =  50.4 DEGREES          
REMARK 500    PRO B  56   CA  -  C   -  N   ANGL. DEV. = -31.3 DEGREES          
REMARK 500    PRO B  56   O   -  C   -  N   ANGL. DEV. =  25.6 DEGREES          
REMARK 500    GLN B  59   CA  -  C   -  N   ANGL. DEV. =  16.2 DEGREES          
REMARK 500    GLN B  59   O   -  C   -  N   ANGL. DEV. = -23.2 DEGREES          
REMARK 500    ALA B  60   C   -  N   -  CA  ANGL. DEV. =  50.3 DEGREES          
REMARK 500    PRO B  89   N   -  CA  -  C   ANGL. DEV. =  18.2 DEGREES          
REMARK 500    ALA E  30   CB  -  CA  -  C   ANGL. DEV. = -12.4 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    SER A  31       36.45    -90.08                                   
REMARK 500    GLN A  33       30.19    -82.37                                   
REMARK 500    GLN A  59       76.30    -64.53                                   
REMARK 500    ALA A  60       75.05     50.67                                   
REMARK 500    ASP A  90       33.38    -84.52                                   
REMARK 500    ILE B  32       -8.07     65.60                                   
REMARK 500    GLN B  59       76.28    -64.55                                   
REMARK 500    ALA B  60       75.06     50.70                                   
REMARK 500    THR C  37       36.84    -93.09                                   
REMARK 500    LYS C 103      118.07   -160.30                                   
REMARK 500    THR D  54      -15.01    -46.43                                   
REMARK 500    ALA E  30       -7.01     77.39                                   
REMARK 500    THR E  54      -16.73    -45.76                                   
REMARK 500    GLN J  58       64.51     65.68                                   
REMARK 500    GLN J  59       90.63    -68.88                                   
REMARK 500    ALA J  60      117.40   -160.65                                   
REMARK 500    ASP J  90       32.30    -85.29                                   
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 GLN A   59     ALA A   60                   42.68                    
REMARK 500 GLN B   59     ALA B   60                   42.66                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLN A  59         20.48                                           
REMARK 500    GLN B  59         20.50                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 16                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 17                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 12                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 15                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 11                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 19                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 20                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 14                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 R 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 R 13                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 R 18                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3N7S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N7R   RELATED DB: PDB                                   
DBREF  3N7P A   23   133  UNP    Q16602   CALRL_HUMAN     23    133             
DBREF  3N7P B   23   133  UNP    Q16602   CALRL_HUMAN     23    133             
DBREF  3N7P C   23   133  UNP    Q16602   CALRL_HUMAN     23    133             
DBREF  3N7P D   26   117  UNP    O60894   RAMP1_HUMAN     26    117             
DBREF  3N7P E   26   117  UNP    O60894   RAMP1_HUMAN     26    117             
DBREF  3N7P F   26   117  UNP    O60894   RAMP1_HUMAN     26    117             
DBREF  3N7P J   23   133  UNP    Q16602   CALRL_HUMAN     23    133             
DBREF  3N7P R   26   117  UNP    O60894   RAMP1_HUMAN     26    117             
SEQADV 3N7P GLY A   19  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P SER A   20  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P HIS A   21  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P MET A   22  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P GLY B   19  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P SER B   20  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P HIS B   21  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P MET B   22  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P GLY C   19  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P SER C   20  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P HIS C   21  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P MET C   22  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P GLY D   22  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P SER D   23  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P HIS D   24  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P MET D   25  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P GLY E   22  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P SER E   23  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P HIS E   24  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P MET E   25  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P GLY F   22  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P SER F   23  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P HIS F   24  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P MET F   25  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P GLY J   19  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P SER J   20  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P HIS J   21  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P MET J   22  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7P GLY R   22  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P SER R   23  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P HIS R   24  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7P MET R   25  UNP  O60894              EXPRESSION TAG                 
SEQRES   1 A  115  GLY SER HIS MET GLU LEU GLU GLU SER PRO GLU ASP SER          
SEQRES   2 A  115  ILE GLN LEU GLY VAL THR ARG ASN LYS ILE MSE THR ALA          
SEQRES   3 A  115  GLN TYR GLU CYS TYR GLN LYS ILE MSE GLN ASP PRO ILE          
SEQRES   4 A  115  GLN GLN ALA GLU GLY VAL TYR CYS ASN ARG THR TRP ASP          
SEQRES   5 A  115  GLY TRP LEU CYS TRP ASN ASP VAL ALA ALA GLY THR GLU          
SEQRES   6 A  115  SER MSE GLN LEU CYS PRO ASP TYR PHE GLN ASP PHE ASP          
SEQRES   7 A  115  PRO SER GLU LYS VAL THR LYS ILE CYS ASP GLN ASP GLY          
SEQRES   8 A  115  ASN TRP PHE ARG HIS PRO ALA SER ASN ARG THR TRP THR          
SEQRES   9 A  115  ASN TYR THR GLN CYS ASN VAL ASN THR HIS GLU                  
SEQRES   1 B  115  GLY SER HIS MET GLU LEU GLU GLU SER PRO GLU ASP SER          
SEQRES   2 B  115  ILE GLN LEU GLY VAL THR ARG ASN LYS ILE MSE THR ALA          
SEQRES   3 B  115  GLN TYR GLU CYS TYR GLN LYS ILE MSE GLN ASP PRO ILE          
SEQRES   4 B  115  GLN GLN ALA GLU GLY VAL TYR CYS ASN ARG THR TRP ASP          
SEQRES   5 B  115  GLY TRP LEU CYS TRP ASN ASP VAL ALA ALA GLY THR GLU          
SEQRES   6 B  115  SER MSE GLN LEU CYS PRO ASP TYR PHE GLN ASP PHE ASP          
SEQRES   7 B  115  PRO SER GLU LYS VAL THR LYS ILE CYS ASP GLN ASP GLY          
SEQRES   8 B  115  ASN TRP PHE ARG HIS PRO ALA SER ASN ARG THR TRP THR          
SEQRES   9 B  115  ASN TYR THR GLN CYS ASN VAL ASN THR HIS GLU                  
SEQRES   1 C  115  GLY SER HIS MET GLU LEU GLU GLU SER PRO GLU ASP SER          
SEQRES   2 C  115  ILE GLN LEU GLY VAL THR ARG ASN LYS ILE MSE THR ALA          
SEQRES   3 C  115  GLN TYR GLU CYS TYR GLN LYS ILE MSE GLN ASP PRO ILE          
SEQRES   4 C  115  GLN GLN ALA GLU GLY VAL TYR CYS ASN ARG THR TRP ASP          
SEQRES   5 C  115  GLY TRP LEU CYS TRP ASN ASP VAL ALA ALA GLY THR GLU          
SEQRES   6 C  115  SER MSE GLN LEU CYS PRO ASP TYR PHE GLN ASP PHE ASP          
SEQRES   7 C  115  PRO SER GLU LYS VAL THR LYS ILE CYS ASP GLN ASP GLY          
SEQRES   8 C  115  ASN TRP PHE ARG HIS PRO ALA SER ASN ARG THR TRP THR          
SEQRES   9 C  115  ASN TYR THR GLN CYS ASN VAL ASN THR HIS GLU                  
SEQRES   1 D   96  GLY SER HIS MET ALA CYS GLN GLU ALA ASN TYR GLY ALA          
SEQRES   2 D   96  LEU LEU ARG GLU LEU CYS LEU THR GLN PHE GLN VAL ASP          
SEQRES   3 D   96  MET GLU ALA VAL GLY GLU THR LEU TRP CYS ASP TRP GLY          
SEQRES   4 D   96  ARG THR ILE ARG SER TYR ARG GLU LEU ALA ASP CYS THR          
SEQRES   5 D   96  TRP HIS MET ALA GLU LYS LEU GLY CYS PHE TRP PRO ASN          
SEQRES   6 D   96  ALA GLU VAL ASP ARG PHE PHE LEU ALA VAL HIS GLY ARG          
SEQRES   7 D   96  TYR PHE ARG SER CYS PRO ILE SER GLY ARG ALA VAL ARG          
SEQRES   8 D   96  ASP PRO PRO GLY SER                                          
SEQRES   1 E   96  GLY SER HIS MET ALA CYS GLN GLU ALA ASN TYR GLY ALA          
SEQRES   2 E   96  LEU LEU ARG GLU LEU CYS LEU THR GLN PHE GLN VAL ASP          
SEQRES   3 E   96  MET GLU ALA VAL GLY GLU THR LEU TRP CYS ASP TRP GLY          
SEQRES   4 E   96  ARG THR ILE ARG SER TYR ARG GLU LEU ALA ASP CYS THR          
SEQRES   5 E   96  TRP HIS MET ALA GLU LYS LEU GLY CYS PHE TRP PRO ASN          
SEQRES   6 E   96  ALA GLU VAL ASP ARG PHE PHE LEU ALA VAL HIS GLY ARG          
SEQRES   7 E   96  TYR PHE ARG SER CYS PRO ILE SER GLY ARG ALA VAL ARG          
SEQRES   8 E   96  ASP PRO PRO GLY SER                                          
SEQRES   1 F   96  GLY SER HIS MET ALA CYS GLN GLU ALA ASN TYR GLY ALA          
SEQRES   2 F   96  LEU LEU ARG GLU LEU CYS LEU THR GLN PHE GLN VAL ASP          
SEQRES   3 F   96  MET GLU ALA VAL GLY GLU THR LEU TRP CYS ASP TRP GLY          
SEQRES   4 F   96  ARG THR ILE ARG SER TYR ARG GLU LEU ALA ASP CYS THR          
SEQRES   5 F   96  TRP HIS MET ALA GLU LYS LEU GLY CYS PHE TRP PRO ASN          
SEQRES   6 F   96  ALA GLU VAL ASP ARG PHE PHE LEU ALA VAL HIS GLY ARG          
SEQRES   7 F   96  TYR PHE ARG SER CYS PRO ILE SER GLY ARG ALA VAL ARG          
SEQRES   8 F   96  ASP PRO PRO GLY SER                                          
SEQRES   1 J  115  GLY SER HIS MET GLU LEU GLU GLU SER PRO GLU ASP SER          
SEQRES   2 J  115  ILE GLN LEU GLY VAL THR ARG ASN LYS ILE MSE THR ALA          
SEQRES   3 J  115  GLN TYR GLU CYS TYR GLN LYS ILE MSE GLN ASP PRO ILE          
SEQRES   4 J  115  GLN GLN ALA GLU GLY VAL TYR CYS ASN ARG THR TRP ASP          
SEQRES   5 J  115  GLY TRP LEU CYS TRP ASN ASP VAL ALA ALA GLY THR GLU          
SEQRES   6 J  115  SER MSE GLN LEU CYS PRO ASP TYR PHE GLN ASP PHE ASP          
SEQRES   7 J  115  PRO SER GLU LYS VAL THR LYS ILE CYS ASP GLN ASP GLY          
SEQRES   8 J  115  ASN TRP PHE ARG HIS PRO ALA SER ASN ARG THR TRP THR          
SEQRES   9 J  115  ASN TYR THR GLN CYS ASN VAL ASN THR HIS GLU                  
SEQRES   1 R   96  GLY SER HIS MET ALA CYS GLN GLU ALA ASN TYR GLY ALA          
SEQRES   2 R   96  LEU LEU ARG GLU LEU CYS LEU THR GLN PHE GLN VAL ASP          
SEQRES   3 R   96  MET GLU ALA VAL GLY GLU THR LEU TRP CYS ASP TRP GLY          
SEQRES   4 R   96  ARG THR ILE ARG SER TYR ARG GLU LEU ALA ASP CYS THR          
SEQRES   5 R   96  TRP HIS MET ALA GLU LYS LEU GLY CYS PHE TRP PRO ASN          
SEQRES   6 R   96  ALA GLU VAL ASP ARG PHE PHE LEU ALA VAL HIS GLY ARG          
SEQRES   7 R   96  TYR PHE ARG SER CYS PRO ILE SER GLY ARG ALA VAL ARG          
SEQRES   8 R   96  ASP PRO PRO GLY SER                                          
MODRES 3N7P MSE A   42  MET  SELENOMETHIONINE                                   
MODRES 3N7P MSE A   53  MET  SELENOMETHIONINE                                   
MODRES 3N7P MSE A   85  MET  SELENOMETHIONINE                                   
MODRES 3N7P MSE B   42  MET  SELENOMETHIONINE                                   
MODRES 3N7P MSE B   53  MET  SELENOMETHIONINE                                   
MODRES 3N7P MSE B   85  MET  SELENOMETHIONINE                                   
MODRES 3N7P MSE C   42  MET  SELENOMETHIONINE                                   
MODRES 3N7P MSE C   53  MET  SELENOMETHIONINE                                   
MODRES 3N7P MSE C   85  MET  SELENOMETHIONINE                                   
MODRES 3N7P MSE J   42  MET  SELENOMETHIONINE                                   
MODRES 3N7P MSE J   53  MET  SELENOMETHIONINE                                   
MODRES 3N7P MSE J   85  MET  SELENOMETHIONINE                                   
HET    MSE  A  42       8                                                       
HET    MSE  A  53       8                                                       
HET    MSE  A  85       8                                                       
HET    MSE  B  42       8                                                       
HET    MSE  B  53       8                                                       
HET    MSE  B  85       8                                                       
HET    MSE  C  42       8                                                       
HET    MSE  C  53       8                                                       
HET    MSE  C  85       5                                                       
HET    MSE  J  42       8                                                       
HET    MSE  J  53       8                                                       
HET    MSE  J  85       8                                                       
HET    SO4  A   5       5                                                       
HET    SO4  A  16       5                                                       
HET    SO4  A  17       5                                                       
HET    SO4  B   3       5                                                       
HET    SO4  B  12       5                                                       
HET    SO4  B  15       5                                                       
HET    SO4  D   2       5                                                       
HET    SO4  D  11       5                                                       
HET    SO4  D  19       5                                                       
HET    SO4  E   4       5                                                       
HET    SO4  E  20       5                                                       
HET    SO4  J   1       5                                                       
HET    SO4  J  14       5                                                       
HET    SO4  R   1       5                                                       
HET    SO4  R  13       5                                                       
HET    SO4  R  18       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   9  SO4    16(O4 S 2-)                                                  
FORMUL  25  HOH   *53(H2 O)                                                     
HELIX    1   1 GLY A   35  MSE A   53  1                                  19    
HELIX    2   2 GLY B   35  ASP B   55  1                                  21    
HELIX    3   3 THR C   37  GLN C   54  1                                  18    
HELIX    4   4 GLN D   28  GLY D   52  1                                  25    
HELIX    5   5 GLU D   53  TRP D   56  5                                   4    
HELIX    6   6 ASP D   58  GLY D   81  1                                  24    
HELIX    7   7 ASN D   86  PHE D  101  1                                  16    
HELIX    8   8 ASN E   31  CYS E   40  1                                  10    
HELIX    9   9 CYS E   40  GLY E   52  1                                  13    
HELIX   10  10 GLU E   53  TRP E   56  5                                   4    
HELIX   11  11 ASP E   58  GLY E   81  1                                  24    
HELIX   12  12 ASN E   86  PHE E  101  1                                  16    
HELIX   13  13 GLN F   28  CYS F   40  1                                  13    
HELIX   14  14 CYS F   40  GLY F   52  1                                  13    
HELIX   15  15 GLU F   53  TRP F   56  5                                   4    
HELIX   16  16 ASP F   58  GLY F   81  1                                  24    
HELIX   17  17 ASN F   86  PHE F  101  1                                  16    
HELIX   18  18 GLN J   33  ASP J   55  1                                  23    
HELIX   19  19 TYR J  124  ASN J  128  5                                   5    
HELIX   20  20 GLN R   28  CYS R   40  1                                  13    
HELIX   21  21 CYS R   40  GLY R   52  1                                  13    
HELIX   22  22 GLU R   53  TRP R   56  5                                   4    
HELIX   23  23 ASP R   58  GLY R   81  1                                  24    
HELIX   24  24 ASN R   86  PHE R  101  1                                  16    
SHEET    1   A 2 TYR A  64  CYS A  65  0                                        
SHEET    2   A 2 VAL A  78  ALA A  79 -1  O  VAL A  78   N  CYS A  65           
SHEET    1   B 2 THR A  68  TRP A  69  0                                        
SHEET    2   B 2 CYS A  74  TRP A  75 -1  O  TRP A  75   N  THR A  68           
SHEET    1   C 2 THR A  82  LEU A  87  0                                        
SHEET    2   C 2 LYS A 100  CYS A 105 -1  O  VAL A 101   N  GLN A  86           
SHEET    1   D 2 TYR B  64  CYS B  65  0                                        
SHEET    2   D 2 VAL B  78  ALA B  79 -1  O  VAL B  78   N  CYS B  65           
SHEET    1   E 2 THR B  68  TRP B  69  0                                        
SHEET    2   E 2 CYS B  74  TRP B  75 -1  O  TRP B  75   N  THR B  68           
SHEET    1   F 2 THR B  82  LEU B  87  0                                        
SHEET    2   F 2 LYS B 100  CYS B 105 -1  O  LYS B 103   N  SER B  84           
SHEET    1   G 2 SER C  84  MSE C  85  0                                        
SHEET    2   G 2 THR C 102  LYS C 103 -1  O  LYS C 103   N  SER C  84           
SHEET    1   H 2 TYR J  64  CYS J  65  0                                        
SHEET    2   H 2 VAL J  78  ALA J  79 -1  O  VAL J  78   N  CYS J  65           
SHEET    1   I 2 THR J  68  TRP J  69  0                                        
SHEET    2   I 2 CYS J  74  TRP J  75 -1  O  TRP J  75   N  THR J  68           
SHEET    1   J 2 THR J  82  LEU J  87  0                                        
SHEET    2   J 2 LYS J 100  CYS J 105 -1  O  VAL J 101   N  GLN J  86           
SSBOND   1 CYS A   48    CYS A   74                          1555   1555  2.03  
SSBOND   2 CYS A   65    CYS A  105                          1555   1555  2.03  
SSBOND   3 CYS A   88    CYS A  127                          1555   1555  2.03  
SSBOND   4 CYS B   48    CYS B   74                          1555   1555  2.03  
SSBOND   5 CYS B   65    CYS B  105                          1555   1555  2.03  
SSBOND   6 CYS B   88    CYS B  127                          1555   1555  2.04  
SSBOND   7 CYS C   48    CYS C   74                          1555   1555  2.03  
SSBOND   8 CYS D   27    CYS D   82                          1555   1555  2.03  
SSBOND   9 CYS D   40    CYS D   72                          1555   1555  2.03  
SSBOND  10 CYS D   57    CYS D  104                          1555   1555  2.03  
SSBOND  11 CYS E   27    CYS E   82                          1555   1555  2.02  
SSBOND  12 CYS E   40    CYS E   72                          1555   1555  2.03  
SSBOND  13 CYS E   57    CYS E  104                          1555   1555  2.03  
SSBOND  14 CYS F   27    CYS F   82                          1555   1555  2.03  
SSBOND  15 CYS F   40    CYS F   72                          1555   1555  2.04  
SSBOND  16 CYS F   57    CYS F  104                          1555   1555  2.04  
SSBOND  17 CYS J   48    CYS J   74                          1555   1555  2.05  
SSBOND  18 CYS J   65    CYS J  105                          1555   1555  2.03  
SSBOND  19 CYS J   88    CYS J  127                          1555   1555  2.04  
SSBOND  20 CYS R   27    CYS R   82                          1555   1555  2.03  
SSBOND  21 CYS R   40    CYS R   72                          1555   1555  2.03  
SSBOND  22 CYS R   57    CYS R  104                          1555   1555  2.03  
LINK         C   ILE A  41                 N   MSE A  42     1555   1555  1.35  
LINK         C   MSE A  42                 N   THR A  43     1555   1555  1.37  
LINK         C   ILE A  52                 N   MSE A  53     1555   1555  1.31  
LINK         C   MSE A  53                 N   GLN A  54     1555   1555  1.32  
LINK         C   SER A  84                 N   MSE A  85     1555   1555  1.33  
LINK         C   MSE A  85                 N   GLN A  86     1555   1555  1.33  
LINK         C   ILE B  41                 N   MSE B  42     1555   1555  1.35  
LINK         C   MSE B  42                 N   THR B  43     1555   1555  1.35  
LINK         C   ILE B  52                 N   MSE B  53     1555   1555  1.33  
LINK         C   MSE B  53                 N   GLN B  54     1555   1555  1.35  
LINK         C   SER B  84                 N   MSE B  85     1555   1555  1.34  
LINK         C   MSE B  85                 N   GLN B  86     1555   1555  1.33  
LINK         C   ILE C  41                 N   MSE C  42     1555   1555  1.35  
LINK         C   MSE C  42                 N   THR C  43     1555   1555  1.36  
LINK         C   ILE C  52                 N   MSE C  53     1555   1555  1.35  
LINK         C   MSE C  53                 N   GLN C  54     1555   1555  1.36  
LINK         C   SER C  84                 N   MSE C  85     1555   1555  1.34  
LINK         C   MSE C  85                 N   GLN C  86     1555   1555  1.35  
LINK         C   ILE J  41                 N   MSE J  42     1555   1555  1.36  
LINK         C   MSE J  42                 N   THR J  43     1555   1555  1.35  
LINK         C   ILE J  52                 N   MSE J  53     1555   1555  1.33  
LINK         C   MSE J  53                 N   GLN J  54     1555   1555  1.34  
LINK         C   SER J  84                 N   MSE J  85     1555   1555  1.32  
LINK         C   MSE J  85                 N   GLN J  86     1555   1555  1.34  
CISPEP   1 TRP D   84    PRO D   85          0        -3.85                     
CISPEP   2 TRP E   84    PRO E   85          0        -3.17                     
CISPEP   3 TRP F   84    PRO F   85          0        -4.48                     
CISPEP   4 TRP R   84    PRO R   85          0        -3.98                     
SITE     1 AC1  6 ASP A  70  TRP A  72  THR A 120  TRP A 121                    
SITE     2 AC1  6 THR A 122  TYR A 124                                          
SITE     1 AC2  3 ARG A 113  ASN D  86  ALA D  87                               
SITE     1 AC3  4 CYS A  74  TRP A  75  ASN A  76  GLN A  86                    
SITE     1 AC4  3 ARG B 119  TRP B 121  GLY D 116                               
SITE     1 AC5  4 ARG B 119  THR B 120  THR B 122  TYR B 124                    
SITE     1 AC6  3 ARG B 113  ASN R  86  ALA R  87                               
SITE     1 AC7  4 PRO D 105  ILE D 106  SER D 107  GLY D 108                    
SITE     1 AC8  7 ALA D  70  ASP D  71  TRP D  74  TRP D  84                    
SITE     2 AC8  7 HOH D 124  VAL R 111  ARG R 112                               
SITE     1 AC9  3 ARG D  64  GLU D  68  ARG R  61                               
SITE     1 BC1  5 TRP E  84  PRO E  85  ASP J  70  GLY J  71                    
SITE     2 BC1  5 TRP J  72                                                     
SITE     1 BC2  4 ALA E  70  ASP E  71  TRP E  74  MSE J  42                    
SITE     1 BC3  5 ARG J 119  THR J 120  TRP J 121  THR J 122                    
SITE     2 BC3  5 TYR J 124                                                     
SITE     1 BC4  2 HIS J 114  TRP J 121                                          
SITE     1 BC5  4 PRO R 105  ILE R 106  SER R 107  GLY R 108                    
SITE     1 BC6  7 VAL D 111  ARG D 112  ALA R  70  ASP R  71                    
SITE     2 BC6  7 TRP R  74  TRP R  84  HOH R 124                               
SITE     1 BC7  4 TRP A 121  PRO R 115  GLY R 116  SER R 117                    
CRYST1  118.000  118.000  225.400  90.00  90.00 120.00 P 32 2 1     24          
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      0.008475  0.004893  0.000000        0.00000                         
SCALE2      0.000000  0.009786  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004437        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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