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Database: PDB
Entry: 3N7R
LinkDB: 3N7R
Original site: 3N7R 
HEADER    MEMBRANE PROTEIN                        27-MAY-10   3N7R              
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 3N7R    1       REMARK                                   
REVDAT   2   22-SEP-10 3N7R    1       JRNL                                     
REVDAT   1   15-SEP-10 3N7R    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.    2.90 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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 10386                          
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)  : 0.234                          
REMARK   3   R VALUE            (WORKING SET)  : 0.232                          
REMARK   3   FREE R VALUE                      : 0.267                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.730                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 491                            
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               : 5                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.90                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.24                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1310                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2704                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1255                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2708                   
REMARK   3   BIN FREE R VALUE                        : 0.2627                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.20                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 55                       
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            : 2692                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 94                                      
REMARK   3   SOLVENT ATOMS            : 38                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 91.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -38.24910                                            
REMARK   3    B22 (A**2) : 15.36280                                             
REMARK   3    B33 (A**2) : 22.88630                                             
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) : 0.542               
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      : 0.881                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.841                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2891   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3943   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 877    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 96     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 451    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2891   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 360    ; 5.000  ; SEMIHARMONIC        
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   : 3362   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.03                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.69                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.10                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A32-A56 A63-A128 }                                   
REMARK   3    ORIGIN FOR THE GROUP (A):   22.4092   31.3066   67.4817           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2466 T22:   -0.1281                                    
REMARK   3     T33:   -0.1734 T12:    0.1497                                    
REMARK   3     T13:   -0.0210 T23:    0.0172                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.6966 L22:    0.6063                                    
REMARK   3     L33:    2.0397 L12:   -0.1063                                    
REMARK   3     L13:    2.9104 L23:    2.2039                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0531 S12:   -0.1184 S13:    0.2959                     
REMARK   3     S21:    0.1401 S22:    0.0898 S23:    0.0269                     
REMARK   3     S31:   -0.3962 S32:    0.0080 S33:   -0.0367                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B33-B55 B60-B129 }                                   
REMARK   3    ORIGIN FOR THE GROUP (A):   36.9980   -0.4719   86.7207           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1144 T22:   -0.0859                                    
REMARK   3     T33:   -0.0464 T12:   -0.0058                                    
REMARK   3     T13:   -0.0700 T23:   -0.0260                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.5465 L22:    5.5889                                    
REMARK   3     L33:    3.7900 L12:    2.8890                                    
REMARK   3     L13:    1.3426 L23:    1.0621                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0155 S12:    0.0400 S13:   -0.3020                     
REMARK   3     S21:   -0.0709 S22:    0.1796 S23:   -0.1865                     
REMARK   3     S31:    0.1639 S32:    0.0536 S33:   -0.1952                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C26-C107 }                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   38.0556   18.4806   84.5808           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0841 T22:   -0.0129                                    
REMARK   3     T33:   -0.0669 T12:   -0.0057                                    
REMARK   3     T13:    0.0119 T23:    0.0010                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3491 L22:    3.4903                                    
REMARK   3     L33:    3.5299 L12:    0.1584                                    
REMARK   3     L13:    0.4730 L23:   -1.2421                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0595 S12:    0.0918 S13:    0.1080                     
REMARK   3     S21:   -0.1306 S22:   -0.1817 S23:    0.1263                     
REMARK   3     S31:   -0.0784 S32:    0.1714 S33:    0.1222                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D27-D106 }                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   19.7425   18.6416   54.1447           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0166 T22:   -0.0733                                    
REMARK   3     T33:   -0.0378 T12:    0.0365                                    
REMARK   3     T13:   -0.0405 T23:    0.0422                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2901 L22:    2.2374                                    
REMARK   3     L33:    1.9442 L12:   -0.4843                                    
REMARK   3     L13:   -1.1219 L23:    0.6304                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0083 S12:    0.0598 S13:   -0.1937                     
REMARK   3     S21:   -0.1222 S22:    0.2375 S23:    0.0861                     
REMARK   3     S31:    0.0664 S32:   -0.0886 S33:   -0.2292                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3N7R 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_1000059486.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-AUG-07                          
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                       : 5.0.3                              
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   : 10420                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
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     (%) : 73.6                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 12.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43800                            
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: NULL                         
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   (%): 60.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14                     
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         
REMARK 280  WITH 0.3UL RESERVOIR SOLUTION CONTAINING 1-1.3M AMMONIUM SULFATE,   
REMARK 280  6-8% DIOXANE, 60-80MM MES PH 6.5, PLUS 0.4 M POTASSIUM              
REMARK 280  THIOCYANATE. TELCAGEPANT WAS SOAKED INTO THE LIGAND BINDING         
REMARK 280  SITE. THE CRYSTAL WAS TRANSFERRED TO 2.1M NAMALONATE (PH 7.0)       
REMARK 280  PRIOR TO FREEZING IN LIQUID NITROGEN., VAPOR DIFFUSION, HANGING     
REMARK 280  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       66.63000            
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       66.63000            
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       38.97000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       59.10000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       38.97000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       59.10000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       66.63000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       38.97000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       59.10000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       66.63000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       38.97000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       59.10000            
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 300 REMARK: CHAINS A & D OR CHAINS B & C                                 
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: 1920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9210 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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: 1910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9330 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 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     ILE A    57                                                      
REMARK 465     GLN A    58                                                      
REMARK 465     GLN A    59                                                      
REMARK 465     ALA A    60                                                      
REMARK 465     GLU A    61                                                      
REMARK 465     GLY A    62                                                      
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     ILE B    32                                                      
REMARK 465     GLN B    33                                                      
REMARK 465     PRO B    56                                                      
REMARK 465     ILE B    57                                                      
REMARK 465     GLN B    58                                                      
REMARK 465     GLN B    59                                                      
REMARK 465     ASN B   130                                                      
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     GLY C   108                                                      
REMARK 465     ARG C   109                                                      
REMARK 465     ALA C   110                                                      
REMARK 465     VAL C   111                                                      
REMARK 465     ARG C   112                                                      
REMARK 465     ASP C   113                                                      
REMARK 465     PRO C   114                                                      
REMARK 465     PRO C   115                                                      
REMARK 465     GLY C   116                                                      
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     SER D   107                                                      
REMARK 465     GLY D   108                                                      
REMARK 465     ARG D   109                                                      
REMARK 465     ALA D   110                                                      
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     ARG A  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A  39    CG   OD1  ND2                                       
REMARK 470     LYS A  40    CG   CD   CE   NZ                                   
REMARK 470     GLU A  47    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     VAL A  63    CB   CG1  CG2                                       
REMARK 470     TYR A  64    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A  67    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A  85    CG   SD   CE                                        
REMARK 470     LEU A  87    CG   CD1  CD2                                       
REMARK 470     ASP A  90    CG   OD1  OD2                                       
REMARK 470     ASP A  96    CB   CG   OD1  OD2                                  
REMARK 470     LYS A 100    CG   CD   CE   NZ                                   
REMARK 470     ILE A 104    CG1  CG2  CD1                                       
REMARK 470     GLN A 107    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  34    CB   CG   CD1  CD2                                  
REMARK 470     ARG B  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  51    CG   CD   CE   NZ                                   
REMARK 470     ALA B  60    CB                                                  
REMARK 470     GLU B  61    CB   CG   CD   OE1  OE2                             
REMARK 470     VAL B  63    CG1  CG2                                            
REMARK 470     ASN B  66    CG   OD1  ND2                                       
REMARK 470     GLN B  93    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 104    CG1  CG2  CD1                                       
REMARK 470     ASN B 128    CG   OD1  ND2                                       
REMARK 470     GLU C  78    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  79    CG   CD   CE   NZ                                   
REMARK 470     ARG C 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE C 106    CG1  CG2  CD1                                       
REMARK 470     SER C 107    OG                                                  
REMARK 470     GLU D  29    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  38    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  49    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  91    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D  94    CG   CD1  CD2                                       
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    LEU B  34   N   -  CA  -  C   ANGL. DEV. =  19.9 DEGREES          
REMARK 500    GLY B  35   N   -  CA  -  C   ANGL. DEV. =  28.9 DEGREES          
REMARK 500    VAL B  36   N   -  CA  -  CB  ANGL. DEV. = -27.4 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    TRP A  72      -38.93   -132.04                                   
REMARK 500    TRP B  72      -39.80   -131.68                                   
REMARK 500    ASN B 118       21.70     80.45                                   
REMARK 500    ILE C 106      -69.68    -91.89                                   
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 N7R B 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3N7P   RELATED DB: PDB                                   
DBREF  3N7R A   23   133  UNP    Q16602   CALRL_HUMAN     23    133             
DBREF  3N7R B   23   133  UNP    Q16602   CALRL_HUMAN     23    133             
DBREF  3N7R C   26   117  UNP    O60894   RAMP1_HUMAN     26    117             
DBREF  3N7R D   26   117  UNP    O60894   RAMP1_HUMAN     26    117             
SEQADV 3N7R GLY A   19  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7R SER A   20  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7R HIS A   21  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7R MET A   22  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7R GLY B   19  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7R SER B   20  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7R HIS B   21  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7R MET B   22  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3N7R GLY C   22  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7R SER C   23  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7R HIS C   24  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7R MET C   25  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7R GLY D   22  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7R SER D   23  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7R HIS D   24  UNP  O60894              EXPRESSION TAG                 
SEQADV 3N7R 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    N7R  B   1      40                                                       
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     N7R N-[(3R,6S)-6-(2,3-DIFLUOROPHENYL)-2-OXO-1-(2,2,2-                
HETNAM   2 N7R  TRIFLUOROETHYL)AZEPAN-3-YL]-4-(2-OXO-2,3-DIHYDRO-1H-            
HETNAM   3 N7R  IMIDAZO[4,5-B]PYRIDIN-1-YL)PIPERIDINE-1-CARBOXAMIDE             
HETSYN     3N6 OLCEGEPANT                                                       
FORMUL   5  3N6    C38 H47 BR2 N9 O5                                            
FORMUL   6  N7R    C26 H27 F5 N6 O3                                             
FORMUL   7  HOH   *38(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 LEU B   34  GLN B   54  1                                  21    
HELIX    4   4 TYR B  124  ASN B  128  5                                   5    
HELIX    5   5 GLN C   28  LEU C   39  1                                  12    
HELIX    6   6 LEU C   39  GLY C   52  1                                  14    
HELIX    7   7 GLU C   53  TRP C   56  5                                   4    
HELIX    8   8 ASP C   58  GLY C   81  1                                  24    
HELIX    9   9 ASN C   86  PHE C  101  1                                  16    
HELIX   10  10 GLN D   28  LEU D   39  1                                  12    
HELIX   11  11 LEU D   39  GLY D   52  1                                  14    
HELIX   12  12 GLU D   53  TRP D   56  5                                   4    
HELIX   13  13 ASP D   58  GLY D   81  1                                  24    
HELIX   14  14 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  2.05  
SSBOND   2 CYS A   65    CYS A  105                          1555   1555  2.04  
SSBOND   3 CYS A   88    CYS A  127                          1555   1555  2.04  
SSBOND   4 CYS B   48    CYS B   74                          1555   1555  2.03  
SSBOND   5 CYS B   65    CYS B  105                          1555   1555  2.02  
SSBOND   6 CYS B   88    CYS B  127                          1555   1555  2.02  
SSBOND   7 CYS C   27    CYS C   82                          1555   1555  2.05  
SSBOND   8 CYS C   40    CYS C   72                          1555   1555  2.04  
SSBOND   9 CYS C   57    CYS C  104                          1555   1555  2.07  
SSBOND  10 CYS D   27    CYS D   82                          1555   1555  2.04  
SSBOND  11 CYS D   40    CYS D   72                          1555   1555  2.04  
SSBOND  12 CYS D   57    CYS D  104                          1555   1555  2.04  
CISPEP   1 TRP C   84    PRO C   85          0        -4.17                     
CISPEP   2 TRP D   84    PRO D   85          0        -3.46                     
SITE     1 AC1 18 ILE A  41  ASP A  70  GLY A  71  TRP A  72                    
SITE     2 AC1 18 PHE A  92  ASP A  94  ARG A 119  TRP A 121                    
SITE     3 AC1 18 THR A 122  TYR A 124  ASN C  31  LEU C  39                    
SITE     4 AC1 18 LYS C  79  LEU C  80  ALA D  70  ASP D  71                    
SITE     5 AC1 18 TRP D  74  TRP D  84                                          
SITE     1 AC2 13 ILE B  41  MET B  42  ASP B  70  GLY B  71                    
SITE     2 AC2 13 TRP B  72  TRP B 121  THR B 122  TYR B 124                    
SITE     3 AC2 13 ARG C  67  ALA C  70  ASP C  71  TRP C  74                    
SITE     4 AC2 13 TRP C  84                                                     
CRYST1   77.940  118.200  133.260  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      0.012830  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008460  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007504        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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