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Database: PDB
Entry: 2X57
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Original site: 2X57 
HEADER    IMMUNE SYSTEM                           05-FEB-10   2X57              
TITLE     CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN VASOACTIVE     
TITLE    2 INTESTINAL POLYPEPTIDE RECEPTOR 2                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 2;              
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 26-118;                     
COMPND   5 SYNONYM: PITUITARY ADENYLATE CYCLASE-ACTIVATING POLYPEPTIDE TYPE III 
COMPND   6 RECEPTOR, PACAP TYPE III RECEPTOR, HELODERMIN-PREFERRING VIP         
COMPND   7 RECEPTOR, PACAP-R-3;                                                 
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    G-PROTEIN COUPLED RECEPTOR, CIRCADIAN RHYTHM, MALE REPRODUCTION,      
KEYWDS   2 HORMONE BINDING, GROWTH, RECEPTOR, TRANSDUCER, CLASS B GPCR, IMMUNE  
KEYWDS   3 SYSTEM                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.W.PIKE,A.J.BARR,A.QUIGLEY,N.BURGESS BROWN,A.DE RISO,A.BULLOCK,    
AUTHOR   2 G.BERRIDGE,J.R.C.MUNIZ,A.CHAIKAUD,M.VOLLMAR,T.KROJER,E.UGOCHUKWU,    
AUTHOR   3 F.VON DELFT,A.EDWARDS,C.H.ARROWSMITH,J.WEIGELT,C.BOUNTRA,            
AUTHOR   4 E.P.CARPENTER                                                        
REVDAT   3   24-JAN-18 2X57    1       JRNL                                     
REVDAT   2   13-JUL-11 2X57    1       VERSN                                    
REVDAT   1   09-MAR-10 2X57    0                                                
JRNL        AUTH   A.C.W.PIKE,A.J.BARR,A.QUIGLEY,N.BURGESS BROWN,A.DE RISO,     
JRNL        AUTH 2 A.BULLOCK,G.BERRIDGE,J.R.C.MUNIZ,A.CHAIKAUD,M.VOLLMAR,       
JRNL        AUTH 3 T.KROJER,E.UGOCHUKWU,F.VON DELFT,A.EDWARDS,C.H.ARROWSMITH,   
JRNL        AUTH 4 J.WEIGELT,C.BOUNTRA,E.P.CARPENTER                            
JRNL        TITL   CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN       
JRNL        TITL 2 VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 2                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 29739                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1577                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2144                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 117                          
REMARK   3   BIN FREE R VALUE                    : 0.4370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2430                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 137                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 37.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.30000                                              
REMARK   3    B22 (A**2) : 0.30000                                              
REMARK   3    B33 (A**2) : -0.61000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.161         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.148         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.093         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.793         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2514 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1679 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3421 ; 1.347 ; 1.924       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4073 ; 1.337 ; 3.009       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   308 ; 5.943 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   124 ;45.854 ;25.161       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   394 ;14.418 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;19.382 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   361 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2832 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   512 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   545 ; 0.229 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1586 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1263 ; 0.197 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1294 ; 0.094 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   115 ; 0.186 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    10 ; 0.117 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    49 ; 0.152 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.053 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1548 ; 3.679 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   625 ; 1.211 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2507 ; 5.979 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   966 ; 8.544 ; 8.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   914 ;12.093 ;12.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 5                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     16       A      20      5                      
REMARK   3           1     B     16       B      20      5                      
REMARK   3           1     C     16       C      20      5                      
REMARK   3           2     A     22       A      24      5                      
REMARK   3           2     B     22       B      24      5                      
REMARK   3           2     C     22       C      24      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):     47 ;  0.09 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):     47 ;  0.10 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):     47 ;  0.11 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):     51 ;  0.16 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):     51 ;  0.13 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):     51 ;  0.17 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):     47 ;  1.49 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):     47 ;  1.90 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):     47 ;  1.21 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):     51 ;  1.66 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):     51 ;  1.62 ; 10.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):     51 ;  1.35 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 7                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     25       A      28      5                      
REMARK   3           1     B     25       B      28      5                      
REMARK   3           1     C     25       C      28      5                      
REMARK   3           2     A     29       A      32      1                      
REMARK   3           2     B     29       B      32      1                      
REMARK   3           2     C     29       C      32      1                      
REMARK   3           3     A     34       A      44      1                      
REMARK   3           3     B     34       B      44      1                      
REMARK   3           3     C     34       C      44      1                      
REMARK   3           4     A     45       A      50      6                      
REMARK   3           4     B     45       B      50      6                      
REMARK   3           4     C     45       C      50      6                      
REMARK   3           5     A     51       A      56      1                      
REMARK   3           5     B     51       B      56      1                      
REMARK   3           5     C     51       C      56      1                      
REMARK   3           6     A     58       A      59      6                      
REMARK   3           6     B     58       B      59      6                      
REMARK   3           6     C     58       C      59      6                      
REMARK   3           7     A     60       A      65      4                      
REMARK   3           7     B     60       B      65      4                      
REMARK   3           7     C     60       C      65      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    277 ;  0.23 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    B    (A):    277 ;  0.23 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    C    (A):    277 ;  0.26 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    114 ;  0.34 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    114 ;  0.29 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):    114 ;  0.29 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2    A    (A):    152 ;  0.53 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    B    (A):    152 ;  0.57 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    C    (A):    152 ;  0.61 ;  5.00           
REMARK   3   TIGHT THERMAL      2    A (A**2):    277 ;  1.36 ;  0.50           
REMARK   3   TIGHT THERMAL      2    B (A**2):    277 ;  1.21 ;  0.50           
REMARK   3   TIGHT THERMAL      2    C (A**2):    277 ;  1.23 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    114 ;  1.19 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    114 ;  1.41 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    C (A**2):    114 ;  1.21 ;  2.00           
REMARK   3   LOOSE THERMAL      2    A (A**2):    152 ;  1.09 ; 10.00           
REMARK   3   LOOSE THERMAL      2    B (A**2):    152 ;  1.19 ; 10.00           
REMARK   3   LOOSE THERMAL      2    C (A**2):    152 ;  1.22 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     68       A      76      1                      
REMARK   3           1     B     68       B      76      1                      
REMARK   3           1     C     68       C      76      1                      
REMARK   3           2     A     89       A      90      1                      
REMARK   3           2     B     89       B      90      1                      
REMARK   3           2     C     89       C      90      1                      
REMARK   3           3     A     92       A      93      1                      
REMARK   3           3     B     92       B      93      1                      
REMARK   3           3     C     92       C      93      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):    147 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    B    (A):    147 ;  0.07 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    C    (A):    147 ;  0.05 ;  0.05           
REMARK   3   TIGHT THERMAL      3    A (A**2):    147 ;  0.21 ;  0.50           
REMARK   3   TIGHT THERMAL      3    B (A**2):    147 ;  0.27 ;  0.50           
REMARK   3   TIGHT THERMAL      3    C (A**2):    147 ;  0.24 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     94       A      95      2                      
REMARK   3           1     B     94       B      95      2                      
REMARK   3           1     C     94       C      95      2                      
REMARK   3           2     A     97       A      97      4                      
REMARK   3           2     B     97       B      97      4                      
REMARK   3           2     C     97       C      97      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    A    (A):     12 ;  0.07 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    B    (A):     12 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    C    (A):     12 ;  0.06 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  4    A    (A):     15 ;  0.24 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    B    (A):     15 ;  0.26 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    C    (A):     15 ;  0.15 ;  0.50           
REMARK   3   TIGHT THERMAL      4    A (A**2):     12 ;  1.40 ;  0.50           
REMARK   3   TIGHT THERMAL      4    B (A**2):     12 ;  1.22 ;  0.50           
REMARK   3   TIGHT THERMAL      4    C (A**2):     12 ;  1.41 ;  0.50           
REMARK   3   MEDIUM THERMAL     4    A (A**2):     15 ;  1.72 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    B (A**2):     15 ;  1.46 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    C (A**2):     15 ;  1.54 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     98       A     111      2                      
REMARK   3           1     C     98       C     111      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   5    A    (A):     82 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   5    C    (A):     82 ;  0.05 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  5    A    (A):    104 ;  0.05 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  5    C    (A):    104 ;  0.05 ;  0.50           
REMARK   3   TIGHT THERMAL      5    A (A**2):     82 ;  0.20 ;  0.50           
REMARK   3   TIGHT THERMAL      5    C (A**2):     82 ;  0.20 ;  0.50           
REMARK   3   MEDIUM THERMAL     5    A (A**2):    104 ;  0.22 ;  2.00           
REMARK   3   MEDIUM THERMAL     5    C (A**2):    104 ;  0.22 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    12        A   114                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5111   0.4955 -13.8984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1218 T22:   0.1133                                     
REMARK   3      T33:   0.0697 T12:  -0.0420                                     
REMARK   3      T13:   0.0469 T23:  -0.0484                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1528 L22:   2.1211                                     
REMARK   3      L33:   5.4756 L12:   0.2464                                     
REMARK   3      L13:   0.0520 L23:   0.1672                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1211 S12:  -0.4405 S13:   0.1771                       
REMARK   3      S21:   0.2694 S22:   0.0489 S23:  -0.0987                       
REMARK   3      S31:  -0.1748 S32:   0.0677 S33:  -0.1700                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    10        B   114                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.6107  -2.4020 -40.1620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1025 T22:   0.0434                                     
REMARK   3      T33:   0.0431 T12:  -0.0081                                     
REMARK   3      T13:   0.0168 T23:  -0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6525 L22:   3.9732                                     
REMARK   3      L33:   0.8400 L12:  -1.6959                                     
REMARK   3      L13:   0.7911 L23:  -1.6229                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0921 S12:   0.1935 S13:  -0.0137                       
REMARK   3      S21:  -0.3301 S22:  -0.0761 S23:  -0.1404                       
REMARK   3      S31:   0.1509 S32:   0.0728 S33:  -0.0161                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    12        C   114                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.5291 -16.9331 -22.5056              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0705 T22:   0.0285                                     
REMARK   3      T33:   0.1880 T12:  -0.0070                                     
REMARK   3      T13:  -0.0226 T23:   0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6213 L22:   2.8687                                     
REMARK   3      L33:   0.4438 L12:  -1.2925                                     
REMARK   3      L13:  -0.1114 L23:   0.8525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0272 S12:  -0.1659 S13:  -0.0023                       
REMARK   3      S21:   0.1155 S22:   0.0948 S23:  -0.4729                       
REMARK   3      S31:   0.0033 S32:   0.0339 S33:  -0.0676                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES RESIDUAL ONLY.                                  
REMARK   4                                                                      
REMARK   4 2X57 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-FEB-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290042800.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9809, 0.9799                     
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31377                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.410                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.600                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
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) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.87000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXDE                                               
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG300 0.1M CITRATE PHOSPHATE        
REMARK 280  PH4.2                                                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       52.17000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       49.85000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       49.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       26.08500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       49.85000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       49.85000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       78.25500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       49.85000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.85000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       26.08500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       49.85000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.85000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       78.25500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       52.17000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15470 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350   BIOMT1   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -52.17000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     MSE A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     GLU A   115                                                      
REMARK 465     ASP A   116                                                      
REMARK 465     GLU A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     MSE B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     GLU B   115                                                      
REMARK 465     ASP B   116                                                      
REMARK 465     GLU B   117                                                      
REMARK 465     SER B   118                                                      
REMARK 465     MSE C   -22                                                      
REMARK 465     HIS C   -21                                                      
REMARK 465     HIS C   -20                                                      
REMARK 465     HIS C   -19                                                      
REMARK 465     HIS C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     SER C   -15                                                      
REMARK 465     SER C   -14                                                      
REMARK 465     GLU C   115                                                      
REMARK 465     ASP C   116                                                      
REMARK 465     GLU C   117                                                      
REMARK 465     SER C   118                                                      
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     LYS B  77    CE   NZ                                             
REMARK 470     GLU C  47    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  48    CD   CE   NZ                                        
REMARK 470     LYS C  77    CD   CE   NZ                                        
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   OE1  GLU B    -7     O    HOH B  2006              2.19            
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    HIS B  49       79.31     47.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2X57 A  -22     0  PDB    2X57     2X57           -22      0             
DBREF  2X57 A   26   118  UNP    P41587   VIPR2_HUMAN     26    118             
DBREF  2X57 B  -22     0  PDB    2X57     2X57           -22      0             
DBREF  2X57 B   26   118  UNP    P41587   VIPR2_HUMAN     26    118             
DBREF  2X57 C  -22     0  PDB    2X57     2X57           -22      0             
DBREF  2X57 C   26   118  UNP    P41587   VIPR2_HUMAN     26    118             
SEQRES   1 A  116  MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  116  GLY THR GLU ASN LEU TYR PHE GLN SER MSE ARG PHE HIS          
SEQRES   3 A  116  LEU GLU ILE GLN GLU GLU GLU THR LYS CYS ALA GLU LEU          
SEQRES   4 A  116  LEU ARG SER GLN THR GLU LYS HIS LYS ALA CYS SER GLY          
SEQRES   5 A  116  VAL TRP ASP ASN ILE THR CYS TRP ARG PRO ALA ASN VAL          
SEQRES   6 A  116  GLY GLU THR VAL THR VAL PRO CYS PRO LYS VAL PHE SER          
SEQRES   7 A  116  ASN PHE TYR SER LYS ALA GLY ASN ILE SER LYS ASN CYS          
SEQRES   8 A  116  THR SER ASP GLY TRP SER GLU THR PHE PRO ASP PHE VAL          
SEQRES   9 A  116  ASP ALA CYS GLY TYR SER ASP PRO GLU ASP GLU SER              
SEQRES   1 B  116  MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  116  GLY THR GLU ASN LEU TYR PHE GLN SER MSE ARG PHE HIS          
SEQRES   3 B  116  LEU GLU ILE GLN GLU GLU GLU THR LYS CYS ALA GLU LEU          
SEQRES   4 B  116  LEU ARG SER GLN THR GLU LYS HIS LYS ALA CYS SER GLY          
SEQRES   5 B  116  VAL TRP ASP ASN ILE THR CYS TRP ARG PRO ALA ASN VAL          
SEQRES   6 B  116  GLY GLU THR VAL THR VAL PRO CYS PRO LYS VAL PHE SER          
SEQRES   7 B  116  ASN PHE TYR SER LYS ALA GLY ASN ILE SER LYS ASN CYS          
SEQRES   8 B  116  THR SER ASP GLY TRP SER GLU THR PHE PRO ASP PHE VAL          
SEQRES   9 B  116  ASP ALA CYS GLY TYR SER ASP PRO GLU ASP GLU SER              
SEQRES   1 C  116  MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 C  116  GLY THR GLU ASN LEU TYR PHE GLN SER MSE ARG PHE HIS          
SEQRES   3 C  116  LEU GLU ILE GLN GLU GLU GLU THR LYS CYS ALA GLU LEU          
SEQRES   4 C  116  LEU ARG SER GLN THR GLU LYS HIS LYS ALA CYS SER GLY          
SEQRES   5 C  116  VAL TRP ASP ASN ILE THR CYS TRP ARG PRO ALA ASN VAL          
SEQRES   6 C  116  GLY GLU THR VAL THR VAL PRO CYS PRO LYS VAL PHE SER          
SEQRES   7 C  116  ASN PHE TYR SER LYS ALA GLY ASN ILE SER LYS ASN CYS          
SEQRES   8 C  116  THR SER ASP GLY TRP SER GLU THR PHE PRO ASP PHE VAL          
SEQRES   9 C  116  ASP ALA CYS GLY TYR SER ASP PRO GLU ASP GLU SER              
MODRES 2X57 MSE A    0  MET  SELENOMETHIONINE                                   
MODRES 2X57 MSE B    0  MET  SELENOMETHIONINE                                   
MODRES 2X57 MSE C    0  MET  SELENOMETHIONINE                                   
HET    MSE  A   0       8                                                       
HET    MSE  B   0       8                                                       
HET    MSE  C   0       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    3(C5 H11 N O2 SE)                                            
FORMUL   4  HOH   *137(H2 O)                                                    
HELIX    1   1 GLY A   -9  GLN A   45  1                                  30    
HELIX    2   2 PRO A   76  PHE A   82  5                                   7    
HELIX    3   3 ASP A  104  GLY A  110  1                                   7    
HELIX    4   4 SER B  -14  GLY B   -9  1                                   6    
HELIX    5   5 GLY B   -9  SER B   -1  1                                   9    
HELIX    6   6 MSE B    0  GLN B   45  1                                  21    
HELIX    7   7 THR B   46  HIS B   49  5                                   4    
HELIX    8   8 PRO B   76  PHE B   82  5                                   7    
HELIX    9   9 ASP B  104  GLY B  110  1                                   7    
HELIX   10  10 GLY C   -9  GLN C   45  1                                  30    
HELIX   11  11 PRO C   76  PHE C   82  5                                   7    
HELIX   12  12 ASP C  104  GLY C  110  1                                   7    
SHEET    1  AA 2 VAL A  55  ASP A  57  0                                        
SHEET    2  AA 2 THR A  60  TRP A  62 -1  O  THR A  60   N  ASP A  57           
SHEET    1  AB 3 THR A  70  PRO A  74  0                                        
SHEET    2  AB 3 ASN A  88  THR A  94 -1  O  ILE A  89   N  VAL A  73           
SHEET    3  AB 3 GLY A  97  TRP A  98 -1  O  GLY A  97   N  THR A  94           
SHEET    1  BA 2 VAL B  55  ASP B  57  0                                        
SHEET    2  BA 2 THR B  60  TRP B  62 -1  O  THR B  60   N  ASP B  57           
SHEET    1  BB 3 THR B  70  PRO B  74  0                                        
SHEET    2  BB 3 ASN B  88  THR B  94 -1  O  ILE B  89   N  VAL B  73           
SHEET    3  BB 3 GLY B  97  TRP B  98 -1  O  GLY B  97   N  THR B  94           
SHEET    1  CA 2 VAL C  55  ASP C  57  0                                        
SHEET    2  CA 2 THR C  60  TRP C  62 -1  O  THR C  60   N  ASP C  57           
SHEET    1  CB 3 THR C  70  PRO C  74  0                                        
SHEET    2  CB 3 ASN C  88  THR C  94 -1  O  ILE C  89   N  VAL C  73           
SHEET    3  CB 3 GLY C  97  TRP C  98 -1  O  GLY C  97   N  THR C  94           
SSBOND   1 CYS A   38    CYS A   61                          1555   1555  2.13  
SSBOND   2 CYS A   52    CYS A   93                          1555   1555  2.05  
SSBOND   3 CYS A   75    CYS A  109                          1555   1555  2.02  
SSBOND   4 CYS B   38    CYS B   61                          1555   1555  2.14  
SSBOND   5 CYS B   52    CYS B   93                          1555   1555  2.01  
SSBOND   6 CYS B   75    CYS B  109                          1555   1555  1.96  
SSBOND   7 CYS C   38    CYS C   61                          1555   1555  2.13  
SSBOND   8 CYS C   52    CYS C   93                          1555   1555  2.02  
SSBOND   9 CYS C   75    CYS C  109                          1555   1555  2.02  
LINK         C   SER A  -1                 N   MSE A   0     1555   1555  1.32  
LINK         C   MSE A   0                 N   ARG A  26     1555   1555  1.31  
LINK         C   SER B  -1                 N   MSE B   0     1555   1555  1.32  
LINK         C   MSE B   0                 N   ARG B  26     1555   1555  1.33  
LINK         C   SER C  -1                 N   MSE C   0     1555   1555  1.32  
LINK         C   MSE C   0                 N   ARG C  26     1555   1555  1.32  
CISPEP   1 PHE A  102    PRO A  103          0       -13.54                     
CISPEP   2 PHE B  102    PRO B  103          0        -3.79                     
CISPEP   3 PHE C  102    PRO C  103          0        -8.68                     
CRYST1   99.700   99.700  104.340  90.00  90.00  90.00 P 41 21 2    24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010030  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010030  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009584        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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