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Database: PDB
Entry: 3N7S
LinkDB: 3N7S
Original site: 3N7S 
HEADER    MEMBRANE PROTEIN                        27-MAY-10   3N7S              
TITLE     CRYSTAL STRUCTURE OF THE ECTODOMAIN COMPLEX OF THE CGRP RECEPTOR, A   
TITLE    2 CLASS-B GPCR, REVEALS THE SITE OF DRUG ANTAGONISM                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCITONIN GENE-RELATED PEPTIDE TYPE 1 RECEPTOR;           
COMPND   3 CHAIN: A, B;                                                         
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: C, D;                                                         
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 3N7S    1       REMARK                                   
REVDAT   2   22-SEP-10 3N7S    1       JRNL                                     
REVDAT   1   15-SEP-10 3N7S    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.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 30514                          
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)  : 0.209                          
REMARK   3   R VALUE            (WORKING SET)  : 0.208                          
REMARK   3   FREE R VALUE                      : 0.226                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.950                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1509                           
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               : 15                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.10                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.17                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1615                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2460                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1537                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2450                   
REMARK   3   BIN FREE R VALUE                        : 0.2600                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.83                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 78                       
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            : 2900                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 85                                      
REMARK   3   SOLVENT ATOMS            : 131                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.95200                                             
REMARK   3    B22 (A**2) : 2.73200                                              
REMARK   3    B33 (A**2) : 6.22000                                              
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) : 0.323               
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      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3088   ; 2.000  ; NULL                
REMARK   3    BOND ANGLES               : 4204   ; 2.000  ; NULL                
REMARK   3    TORSION ANGLES            : 986    ; 2.000  ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : 102    ; 2.000  ; NULL                
REMARK   3    GENERAL PLANES            : 461    ; 5.000  ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : 3088   ; 20.000 ; NULL                
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 372    ; 5.000  ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3703   ; 4.000  ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.02                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.91                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 20.95                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|32 - A|57 A|61 - A|128 }                           
REMARK   3    ORIGIN FOR THE GROUP (A):   21.1672   31.6801   68.2154           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0691 T22:   -0.1078                                    
REMARK   3     T33:   -0.0805 T12:    0.0989                                    
REMARK   3     T13:   -0.0698 T23:   -0.0573                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.8727 L22:    2.0028                                    
REMARK   3     L33:    3.6114 L12:   -0.2941                                    
REMARK   3     L13:    1.8963 L23:   -0.6240                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1564 S12:   -0.1538 S13:    0.4001                     
REMARK   3     S21:    0.3073 S22:   -0.0172 S23:   -0.0324                     
REMARK   3     S31:   -0.5358 S32:   -0.0848 S33:    0.1736                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|32 - B|55 B|60 - B|129 }                           
REMARK   3    ORIGIN FOR THE GROUP (A):   35.3148    0.2362   89.5793           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0309 T22:   -0.0688                                    
REMARK   3     T33:   -0.0961 T12:   -0.0372                                    
REMARK   3     T13:   -0.0080 T23:   -0.0104                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2647 L22:    3.6935                                    
REMARK   3     L33:    2.6231 L12:    1.0967                                    
REMARK   3     L13:    0.4932 L23:    0.5183                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0384 S12:   -0.0151 S13:    0.0255                     
REMARK   3     S21:    0.0432 S22:    0.0118 S23:   -0.0335                     
REMARK   3     S31:    0.2921 S32:   -0.0431 S33:   -0.0502                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|26 - C|115 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   37.1353   18.0055   89.1422           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0072 T22:   -0.0517                                    
REMARK   3     T33:   -0.0696 T12:   -0.0052                                    
REMARK   3     T13:    0.0328 T23:    0.0044                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6539 L22:    2.4670                                    
REMARK   3     L33:    2.1897 L12:   -0.0004                                    
REMARK   3     L13:    0.2192 L23:   -0.2683                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0511 S12:    0.0805 S13:    0.0784                     
REMARK   3     S21:   -0.0674 S22:   -0.0481 S23:    0.0942                     
REMARK   3     S31:   -0.1397 S32:    0.1596 S33:   -0.0030                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|27 - D|111 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   18.6699   18.5450   55.5648           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0797 T22:   -0.0908                                    
REMARK   3     T33:   -0.0847 T12:    0.0669                                    
REMARK   3     T13:   -0.0106 T23:   -0.0144                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.4125 L22:    2.8741                                    
REMARK   3     L33:    2.1473 L12:   -1.6237                                    
REMARK   3     L13:    1.0547 L23:   -0.2414                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0630 S12:    0.1305 S13:   -0.2221                     
REMARK   3     S21:   -0.2506 S22:   -0.0154 S23:    0.2370                     
REMARK   3     S31:    0.2373 S32:   -0.0294 S33:   -0.0476                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3N7S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059487.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JAN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30529                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.9                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 51.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CLR/RAMP1 COMPLEX WAS MIXED WITH         
REMARK 280  OLCEGEPANT PRIOR TO CRYSTALLIZATION IN A 1:4 (PROTEIN:COMPOUND)     
REMARK 280  MOLAR RATIO. CRYSTALS WERE OBTAINED BY MIXING 0.6UL PROTEIN WITH    
REMARK 280  0.3UL RESERVOIR SOLUTION CONTAINING 1-1.3M AMMONIUM SULFATE, 6-8%   
REMARK 280  DIOXANE, 60-80MM MES PH 6.5, 0.4 M POTASSIUM THIOCYANATE. THE       
REMARK 280  CRYSTALS WERE TRANSFERRED TO 2.1M NAMALONATE (PH 7.0) PRIOR TO      
REMARK 280  FREEZING IN LIQUID NITROGEN, HANGING DROP, TEMPERATURE 298K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.57900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.57900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       36.65250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       59.56550            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       36.65250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       59.56550            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       68.57900            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       36.65250            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       59.56550            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       68.57900            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       36.65250            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       59.56550            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9830 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 2080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 218  LIES ON A SPECIAL POSITION.                          
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     GLU A    29                                                      
REMARK 465     ASP A    30                                                      
REMARK 465     SER A    31                                                      
REMARK 465     GLN A    58                                                      
REMARK 465     GLN A    59                                                      
REMARK 465     ALA A    60                                                      
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     SER B    31                                                      
REMARK 465     PRO B    56                                                      
REMARK 465     ILE B    57                                                      
REMARK 465     GLN B    58                                                      
REMARK 465     GLN B    59                                                      
REMARK 465     THR B   131                                                      
REMARK 465     HIS B   132                                                      
REMARK 465     GLU B   133                                                      
REMARK 465     GLY C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     HIS C    24                                                      
REMARK 465     MET C    25                                                      
REMARK 465     SER C   117                                                      
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     VAL D   111                                                      
REMARK 465     ARG D   112                                                      
REMARK 465     ASP D   113                                                      
REMARK 465     PRO D   114                                                      
REMARK 465     PRO D   115                                                      
REMARK 465     GLY D   116                                                      
REMARK 465     SER D   117                                                      
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     ILE A  32    CB   CG1  CG2  CD1                                  
REMARK 470     LEU A  34    CG   CD1  CD2                                       
REMARK 470     LYS A  40    CG   CD   CE   NZ                                   
REMARK 470     GLU A  61    CB   CG   CD   OE1  OE2                             
REMARK 470     VAL A  63    CG1  CG2                                            
REMARK 470     VAL A  78    CG1  CG2                                            
REMARK 470     ASP A  96    CB   CG   OD1  OD2                                  
REMARK 470     LYS A 100    CG   CD   CE   NZ                                   
REMARK 470     GLN A 107    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 118    CG   OD1  ND2                                       
REMARK 470     ILE B  32    CG1  CG2  CD1                                       
REMARK 470     GLN B  33    CG   CD   OE1  NE2                                  
REMARK 470     ALA B  60    CB                                                  
REMARK 470     GLU B  61    CB   CG   CD   OE1  OE2                             
REMARK 470     VAL B 129    CB   CG1  CG2                                       
REMARK 470     ASN B 130    CB   CG   OD1  ND2                                  
REMARK 470     ILE C 106    CG1  CG2  CD1                                       
REMARK 470     ARG C 109    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ALA C 110    CB                                                  
REMARK 470     GLU D  29    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER D 107    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   NH2  ARG D    37     O    HOH D   205              1.90            
REMARK 500   NE1  TRP B    72     O    HOH B   238              2.16            
REMARK 500   NH2  ARG B    38     OD2  ASP C    71              2.16            
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    ALA C 110   N   -  CA  -  C   ANGL. DEV. =  16.2 DEGREES          
REMARK 500    PRO C 115   CB  -  CA  -  C   ANGL. DEV. =  15.0 DEGREES          
REMARK 500    GLY C 116   N   -  CA  -  C   ANGL. DEV. = -17.7 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    ARG A  67      139.17    -39.24                                   
REMARK 500    TRP A  72      -37.13   -133.57                                   
REMARK 500    TRP B  72      -41.59   -133.61                                   
REMARK 500    ASN B 128      -70.88   -101.88                                   
REMARK 500    VAL B 129       35.86     71.02                                   
REMARK 500    GLN C  28       87.20    -69.43                                   
REMARK 500    ALA C 110       56.32   -147.06                                   
REMARK 500    VAL C 111      -70.06   -120.07                                   
REMARK 500    PRO D  85     -163.08    -79.27                                   
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 ASN B  128     VAL B  129                  140.55                    
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 3N6 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3N7 B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3N7P   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N7R   RELATED DB: PDB                                   
DBREF  3N7S A   23   133  UNP    Q16602   CALRL_HUMAN     23    133             
DBREF  3N7S B   23   133  UNP    Q16602   CALRL_HUMAN     23    133             
DBREF  3N7S C   26   117  UNP    O60894   RAMP1_HUMAN     26    117             
DBREF  3N7S D   26   117  UNP    O60894   RAMP1_HUMAN     26    117             
SEQADV 3N7S GLY A   19  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7S SER A   20  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7S HIS A   21  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7S MET A   22  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7S GLY B   19  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7S SER B   20  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7S HIS B   21  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7S MET B   22  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7S GLY C   22  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7S SER C   23  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7S HIS C   24  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7S MET C   25  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7S GLY D   22  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7S SER D   23  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7S HIS D   24  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7S MET D   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 MET THR ALA          
SEQRES   3 A  115  GLN TYR GLU CYS TYR GLN LYS ILE MET 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 MET 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 MET THR ALA          
SEQRES   3 B  115  GLN TYR GLU CYS TYR GLN LYS ILE MET 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 MET 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   96  GLY SER HIS MET ALA CYS GLN GLU ALA ASN TYR GLY ALA          
SEQRES   2 C   96  LEU LEU ARG GLU LEU CYS LEU THR GLN PHE GLN VAL ASP          
SEQRES   3 C   96  MET GLU ALA VAL GLY GLU THR LEU TRP CYS ASP TRP GLY          
SEQRES   4 C   96  ARG THR ILE ARG SER TYR ARG GLU LEU ALA ASP CYS THR          
SEQRES   5 C   96  TRP HIS MET ALA GLU LYS LEU GLY CYS PHE TRP PRO ASN          
SEQRES   6 C   96  ALA GLU VAL ASP ARG PHE PHE LEU ALA VAL HIS GLY ARG          
SEQRES   7 C   96  TYR PHE ARG SER CYS PRO ILE SER GLY ARG ALA VAL ARG          
SEQRES   8 C   96  ASP PRO PRO GLY SER                                          
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                                          
HET    3N6  A   1      54                                                       
HET    3N7  B   1      26                                                       
HET    SO4  C   1       5                                                       
HETNAM     3N6 N-{(1S)-5-AMINO-1-[(4-PYRIDIN-4-YLPIPERAZIN-1-YL)                
HETNAM   2 3N6  CARBONYL]PENTYL}-3,5-DIBROMO-NALPHA-{[4-(2-OXO-1,4-             
HETNAM   3 3N6  DIHYDROQUINAZOLIN-3(2H)-YL)PIPERIDIN-1-YL]CARBONYL}-D-          
HETNAM   4 3N6  TYROSINAMIDE                                                    
HETNAM     3N7 N~4~-(5-CYCLOPROPYL-1H-PYRAZOL-3-YL)-N~2~-1H-INDAZOL-5-          
HETNAM   2 3N7  YL-6-METHYLPYRIMIDINE-2,4-DIAMINE                               
HETNAM     SO4 SULFATE ION                                                      
HETSYN     3N6 OLCEGEPANT                                                       
FORMUL   5  3N6    C38 H47 BR2 N9 O5                                            
FORMUL   6  3N7    C18 H18 N8                                                   
FORMUL   7  SO4    O4 S 2-                                                      
FORMUL   8  HOH   *131(H2 O)                                                    
HELIX    1   1 ILE A   32  MET A   53  1                                  22    
HELIX    2   2 TYR A  124  ASN A  128  5                                   5    
HELIX    3   3 GLY B   35  GLN B   54  1                                  20    
HELIX    4   4 GLN C   28  CYS C   40  1                                  13    
HELIX    5   5 CYS C   40  GLY C   52  1                                  13    
HELIX    6   6 GLU C   53  TRP C   56  5                                   4    
HELIX    7   7 ASP C   58  GLY C   81  1                                  24    
HELIX    8   8 ASN C   86  PHE C  101  1                                  16    
HELIX    9   9 GLN D   28  LEU D   39  1                                  12    
HELIX   10  10 LEU D   39  GLY D   52  1                                  14    
HELIX   11  11 GLU D   53  TRP D   56  5                                   4    
HELIX   12  12 ASP D   58  GLY D   81  1                                  24    
HELIX   13  13 ASN D   86  PHE D  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 GLU A  83  LEU A  87  0                                        
SHEET    2   C 2 LYS A 100  ILE A 104 -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 GLU B  83  LEU B  87  0                                        
SHEET    2   F 2 LYS B 100  ILE B 104 -1  O  VAL B 101   N  GLN B  86           
SSBOND   1 CYS A   48    CYS A   74                          1555   1555  2.04  
SSBOND   2 CYS A   65    CYS A  105                          1555   1555  2.03  
SSBOND   3 CYS A   88    CYS A  127                          1555   1555  2.04  
SSBOND   4 CYS B   48    CYS B   74                          1555   1555  2.05  
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   27    CYS C   82                          1555   1555  2.04  
SSBOND   8 CYS C   40    CYS C   72                          1555   1555  2.05  
SSBOND   9 CYS C   57    CYS C  104                          1555   1555  2.04  
SSBOND  10 CYS D   27    CYS D   82                          1555   1555  2.03  
SSBOND  11 CYS D   40    CYS D   72                          1555   1555  2.05  
SSBOND  12 CYS D   57    CYS D  104                          1555   1555  2.04  
CISPEP   1 TRP C   84    PRO C   85          0        -5.02                     
CISPEP   2 PRO C  115    GLY C  116          0        -1.94                     
CISPEP   3 TRP D   84    PRO D   85          0        -3.49                     
SITE     1 AC1 20 ASP A  70  GLY A  71  TRP A  72  PHE A  92                    
SITE     2 AC1 20 ASP A  94  ARG A 119  TRP A 121  THR A 122                    
SITE     3 AC1 20 TYR A 124  HOH A 201  HOH A 202  HOH A 204                    
SITE     4 AC1 20 ASN C  31  LEU C  39  LYS C  79  LEU C  80                    
SITE     5 AC1 20 ALA D  70  ASP D  71  TRP D  74  TRP D  84                    
SITE     1 AC2 15 LYS B  40  ALA B  44  GLU B  47  CYS B  48                    
SITE     2 AC2 15 LYS B  51  CYS B  74  TRP B  75  ASN B  76                    
SITE     3 AC2 15 SER B  84  MET B  85  GLN B  86  ASP B  90                    
SITE     4 AC2 15 HOH B 208  HOH B 216  HOH B 219                               
SITE     1 AC3  6 MET B  42  ALA C  70  ASP C  71  TRP C  74                    
SITE     2 AC3  6 TRP C  84  VAL C 111                                          
CRYST1   73.305  119.131  137.158  90.00  90.00  90.00 C 2 2 21     16          
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      0.013642  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008394  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007291        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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