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Entry: 2VNS
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HEADER    OXIDOREDUCTASE                          07-FEB-08   2VNS              
TITLE     CRYSTAL STRUCTURE OF THE MEMBRANE PROXIMAL OXIDOREDUCTASE             
TITLE    2 DOMAIN OF HUMAN STEAP3, THE DOMINANT FERRIC REDUCTASE OF             
TITLE    3 THE ERYTHROID TRANSFERRIN CYCLE                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METALLOREDUCTASE STEAP3;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: NADPH/FLAVIN DEPENDENT OXIDOREDUCTASE, RESIDUES            
COMPND   5  1-215;                                                              
COMPND   6 SYNONYM: SIX-TRANSMEMBRANE EPITHELIAL ANTIGEN OF PROSTATE            
COMPND   7  3, TUMOR SUPPRESSOR-ACTIVATED PATHWAY PROTEIN 6, HTSAP6,            
COMPND   8  PHYDE, HPHYDE, DUDULIN-2, STEAP3 DIMER;                             
COMPND   9 EC: 1.16.1.2;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 OTHER_DETAILS: RESIDUES 1-215 CLONED                                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: KIDNEY, RENAL CELL ADENOCARCINOMA;                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: RIL;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PDEST14                                   
KEYWDS    METAL-BINDING, TRANSMEMBRANE, ROSSMANN FOLD, TRANSPORT,               
KEYWDS   2 CELL CYCLE, TRANSFERRIN, FLAVOPROTEIN, ALTERNATIVE                   
KEYWDS   3 SPLICING, TRANSFERRIN RECEPTOR, FERRIREDUCTASE, FERRIC-              
KEYWDS   4 REDUCTASE, IRON TRANSPORT, PHOSPHOPROTEIN, OXIDOREDUCTASE,           
KEYWDS   5 STEAP3, COPPER, MEMBRANE, ENDOSOME, APOPTOSIS, TF, NAD,              
KEYWDS   6 TFR, FAD, FNO, NADP, TFR1, IRON, STEAP, POLYMORPHISM,                
KEYWDS   7 GLYCOPROTEIN, ION TRANSPORT, DINUCLEOTIDE-BINDING DOMAIN             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.K.SENDAMARAI,R.S.OHGAMI,M.D.FLEMING,C.M.LAWRENCE                    
REVDAT   3   24-FEB-09 2VNS    1       VERSN                                    
REVDAT   2   03-JUN-08 2VNS    1       JRNL                                     
REVDAT   1   06-MAY-08 2VNS    0                                                
JRNL        AUTH   A.K.SENDAMARAI,R.S.OHGAMI,M.D.FLEMING,C.M.LAWRENCE           
JRNL        TITL   STRUCTURE OF THE MEMBRANE PROXIMAL OXIDOREDUCTASE            
JRNL        TITL 2 DOMAIN OF HUMAN STEAP3, THE DOMINANT                         
JRNL        TITL 3 FERRIREDUCTASE OF THE ERYTHROID TRANSFERRIN CYCLE            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105  7410 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18495927                                                     
JRNL        DOI    10.1073/PNAS.0801318105                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.S.OHGAMI,D.R.CAMPAGNA,E.L.GREER,B.ANTIOCHOS,               
REMARK   1  AUTH 2 A.MCDONALD,J.CHEN,J.J.SHARP,Y.FUJIWARA,J.E.BARKER,           
REMARK   1  AUTH 3 M.D.FLEMING                                                  
REMARK   1  TITL   IDENTIFICATION OF A FERRIREDUCTASE REQUIRED FOR              
REMARK   1  TITL 2 EFFICIENT TRANSFERRIN-DEPENDENT IRON UPTAKE IN               
REMARK   1  TITL 3 ERYTHROID CELLS                                              
REMARK   1  REF    NAT.GENET.                    V.  37  1264 2005              
REMARK   1  REFN                   ISSN 1061-4036                               
REMARK   1  PMID   16227996                                                     
REMARK   1  DOI    10.1038/NG1658                                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   R.S.OHGAMI,D.R.CAMPAGNA,B.ANTIOCHOS,E.B.WOOD,                
REMARK   1  AUTH 2 J.J.SHARP,J.E.BARKER,M.D.FLEMING                             
REMARK   1  TITL   NM1054, A SPONTANEOUS, RECESSIVE, HYPOCHROMIC,               
REMARK   1  TITL 2 MICROCYTIC ANEMIA MUTATION IN THE MOUSE                      
REMARK   1  REF    BLOOD                         V. 106  3625 2005              
REMARK   1  REFN                   ISSN 0006-4971                               
REMARK   1  PMID   15994289                                                     
REMARK   1  DOI    10.1182/BLOOD-2005-01-0379                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.0  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 23241                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1268                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1686                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 101                          
REMARK   3   BIN FREE R VALUE                    : 0.2930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2770                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 13                                      
REMARK   3   SOLVENT ATOMS            : 136                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 1.84000                                              
REMARK   3    B33 (A**2) : -1.84000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.177         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.122         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.467         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2820 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1911 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3837 ; 1.500 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4667 ; 1.406 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   370 ;29.107 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   113 ;36.356 ;23.982       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   457 ;14.111 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;20.076 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   437 ; 0.196 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3184 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   558 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   561 ; 0.222 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1942 ; 0.213 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1393 ; 0.175 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1535 ; 0.082 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   134 ; 0.233 ; 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):    19 ; 0.381 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    63 ; 0.322 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.534 ; 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):  2308 ; 2.057 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2938 ; 2.417 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1132 ; 2.631 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   897 ; 3.860 ; 4.500       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 5                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     29       A     104      2                      
REMARK   3           1     B     29       B     104      2                      
REMARK   3           2     A    105       A     159      2                      
REMARK   3           2     B    105       B     159      2                      
REMARK   3           3     A    160       A     161      3                      
REMARK   3           3     B    160       B     161      3                      
REMARK   3           4     A    163       A     204      2                      
REMARK   3           4     B    163       B     204      2                      
REMARK   3           5     A    205       A     209      3                      
REMARK   3           5     B    205       B     209      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1053 ;  0.05 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1200 ;  0.38 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):     42 ;  0.64 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1053 ;  0.08 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1200 ;  0.41 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):     42 ;  1.75 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 22                                         
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    29        A    47                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.5824 -26.2961  57.9569              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0848 T22:   0.1104                                     
REMARK   3      T33:   0.1003 T12:  -0.0152                                     
REMARK   3      T13:  -0.0139 T23:  -0.0218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2199 L22:   2.7622                                     
REMARK   3      L33:   3.1887 L12:  -1.7860                                     
REMARK   3      L13:   1.0616 L23:  -0.9765                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0679 S12:  -0.0063 S13:  -0.0405                       
REMARK   3      S21:  -0.0108 S22:  -0.0165 S23:   0.1157                       
REMARK   3      S31:   0.0868 S32:  -0.1412 S33:  -0.0514                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    48        A    66                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.2473 -22.5638  64.0259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0687 T22:   0.1171                                     
REMARK   3      T33:   0.0295 T12:   0.0194                                     
REMARK   3      T13:   0.0110 T23:  -0.0270                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2052 L22:   2.8639                                     
REMARK   3      L33:   1.4102 L12:   0.5487                                     
REMARK   3      L13:   2.1559 L23:   0.9506                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1339 S12:  -0.0037 S13:  -0.0534                       
REMARK   3      S21:   0.2384 S22:   0.1381 S23:  -0.1225                       
REMARK   3      S31:   0.0892 S32:   0.0411 S33:  -0.0042                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    67        A    96                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.3547 -28.5376  61.4705              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0876 T22:   0.0955                                     
REMARK   3      T33:   0.0892 T12:   0.0047                                     
REMARK   3      T13:  -0.0028 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0113 L22:   1.1012                                     
REMARK   3      L33:   1.0915 L12:  -0.5435                                     
REMARK   3      L13:   0.1395 L23:   0.7355                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0364 S12:   0.0128 S13:   0.0455                       
REMARK   3      S21:   0.0642 S22:   0.0969 S23:  -0.0520                       
REMARK   3      S31:   0.0571 S32:  -0.0304 S33:  -0.0605                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    97        A   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.5555 -35.4023  63.3242              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1271 T22:   0.1321                                     
REMARK   3      T33:   0.0690 T12:   0.0571                                     
REMARK   3      T13:  -0.0497 T23:  -0.0437                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3583 L22:   0.8570                                     
REMARK   3      L33:   2.5381 L12:  -0.8716                                     
REMARK   3      L13:   2.8566 L23:  -1.0027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0191 S12:  -0.6135 S13:  -0.0633                       
REMARK   3      S21:   0.1448 S22:  -0.0705 S23:  -0.4082                       
REMARK   3      S31:   0.0924 S32:   0.5556 S33:   0.0896                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   107        A   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.8787 -34.0080  49.8479              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1057 T22:   0.0976                                     
REMARK   3      T33:   0.0980 T12:  -0.0105                                     
REMARK   3      T13:  -0.0057 T23:  -0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4123 L22:   2.6006                                     
REMARK   3      L33:   9.0737 L12:   0.7720                                     
REMARK   3      L13:  -3.2437 L23:  -3.6539                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0352 S12:  -0.0809 S13:   0.0172                       
REMARK   3      S21:  -0.1115 S22:   0.0584 S23:  -0.0089                       
REMARK   3      S31:   0.1165 S32:   0.0543 S33:  -0.0231                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   121        A   130                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.1036 -35.8794  41.7025              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1126 T22:   0.1136                                     
REMARK   3      T33:   0.0941 T12:   0.0241                                     
REMARK   3      T13:   0.0037 T23:  -0.0144                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4724 L22:   1.1690                                     
REMARK   3      L33:   7.4224 L12:   2.0147                                     
REMARK   3      L13:  -5.0768 L23:  -2.9456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0597 S12:  -0.4189 S13:   0.1343                       
REMARK   3      S21:  -0.0856 S22:  -0.1465 S23:   0.0116                       
REMARK   3      S31:   0.5120 S32:   0.5613 S33:   0.0868                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   131        A   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.6807 -37.9010  51.7852              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1166 T22:   0.0859                                     
REMARK   3      T33:   0.1004 T12:  -0.0050                                     
REMARK   3      T13:  -0.0018 T23:  -0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3570 L22:   1.2929                                     
REMARK   3      L33:   1.5363 L12:  -1.5749                                     
REMARK   3      L13:   1.3569 L23:  -0.6951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0052 S12:   0.0219 S13:  -0.0452                       
REMARK   3      S21:   0.0383 S22:  -0.0235 S23:   0.0531                       
REMARK   3      S31:   0.0562 S32:   0.0473 S33:   0.0182                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   151        A   155                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6882 -21.5247  49.3888              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0932 T22:   0.0887                                     
REMARK   3      T33:   0.0917 T12:  -0.0205                                     
REMARK   3      T13:  -0.0110 T23:   0.0201                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.9494 L22:   5.5061                                     
REMARK   3      L33:   1.2912 L12:  -1.7724                                     
REMARK   3      L13:   1.2651 L23:   2.2757                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1695 S12:   0.0955 S13:   0.0640                       
REMARK   3      S21:  -0.4019 S22:  -0.0976 S23:   0.4109                       
REMARK   3      S31:  -0.1814 S32:   0.1416 S33:  -0.0718                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   156        A   172                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.1936 -36.5157  47.8376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1283 T22:   0.1530                                     
REMARK   3      T33:   0.1436 T12:  -0.0018                                     
REMARK   3      T13:  -0.0094 T23:  -0.0463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5179 L22:   7.4878                                     
REMARK   3      L33:   1.8169 L12:  -0.4662                                     
REMARK   3      L13:   0.6094 L23:  -1.4868                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0368 S12:  -0.0265 S13:  -0.2212                       
REMARK   3      S21:   0.0766 S22:  -0.0908 S23:   0.7781                       
REMARK   3      S31:  -0.0929 S32:  -0.3966 S33:   0.0540                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   173        A   195                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.4653 -39.9595  50.8278              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0757 T22:   0.0727                                     
REMARK   3      T33:   0.1423 T12:  -0.0715                                     
REMARK   3      T13:   0.0025 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8713 L22:   3.1807                                     
REMARK   3      L33:   0.8583 L12:  -3.4983                                     
REMARK   3      L13:   0.5267 L23:  -0.5993                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0167 S12:   0.0263 S13:  -0.2300                       
REMARK   3      S21:   0.0365 S22:   0.0237 S23:   0.1811                       
REMARK   3      S31:   0.0363 S32:  -0.2280 S33:  -0.0404                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   196        A   208                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.7922 -35.0187  40.0813              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1141 T22:   0.0968                                     
REMARK   3      T33:   0.0707 T12:   0.0084                                     
REMARK   3      T13:  -0.0124 T23:  -0.0203                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2280 L22:   4.0580                                     
REMARK   3      L33:   1.1939 L12:  -3.1454                                     
REMARK   3      L13:   1.3729 L23:  -0.5594                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0639 S12:   0.0939 S13:  -0.1413                       
REMARK   3      S21:  -0.2528 S22:  -0.0727 S23:  -0.1285                       
REMARK   3      S31:   0.0232 S32:  -0.0147 S33:   0.0088                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    29        B    47                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.9959  -7.8886  57.3296              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0785 T22:   0.0964                                     
REMARK   3      T33:   0.0802 T12:   0.0104                                     
REMARK   3      T13:   0.0022 T23:   0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0056 L22:   3.2976                                     
REMARK   3      L33:   2.9055 L12:  -0.8931                                     
REMARK   3      L13:  -1.2855 L23:  -0.0994                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0519 S12:  -0.1101 S13:  -0.0938                       
REMARK   3      S21:   0.0536 S22:  -0.0011 S23:  -0.1772                       
REMARK   3      S31:  -0.0067 S32:   0.0604 S33:  -0.0508                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    48        B    67                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4853 -11.5030  63.6145              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0713 T22:   0.1094                                     
REMARK   3      T33:   0.0529 T12:   0.0083                                     
REMARK   3      T13:  -0.0038 T23:   0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8096 L22:   4.1185                                     
REMARK   3      L33:   1.1891 L12:   1.5679                                     
REMARK   3      L13:  -1.6739 L23:  -0.9274                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0206 S12:   0.1055 S13:  -0.1088                       
REMARK   3      S21:   0.3494 S22:   0.0751 S23:   0.1286                       
REMARK   3      S31:  -0.0621 S32:  -0.0054 S33:  -0.0545                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    68        B    96                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2036  -4.8530  60.7166              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0823 T22:   0.1503                                     
REMARK   3      T33:   0.0887 T12:   0.0249                                     
REMARK   3      T13:   0.0061 T23:  -0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1593 L22:   1.6157                                     
REMARK   3      L33:   0.6625 L12:  -0.5074                                     
REMARK   3      L13:   0.3249 L23:  -1.0346                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1094 S12:  -0.0648 S13:  -0.0646                       
REMARK   3      S21:   0.1488 S22:   0.1463 S23:   0.0421                       
REMARK   3      S31:  -0.0865 S32:  -0.0257 S33:  -0.0369                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    97        B   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0618   1.8448  62.5367              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0914 T22:   0.1505                                     
REMARK   3      T33:   0.0441 T12:   0.0958                                     
REMARK   3      T13:   0.0459 T23:   0.0709                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0978 L22:   1.5271                                     
REMARK   3      L33:  11.1678 L12:   1.9423                                     
REMARK   3      L13:   5.8147 L23:   4.1205                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4614 S12:  -0.6369 S13:  -0.2376                       
REMARK   3      S21:   0.1388 S22:   0.0769 S23:   0.3484                       
REMARK   3      S31:  -0.0786 S32:  -0.2782 S33:   0.3845                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   107        B   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7303  -0.5047  48.6364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0909 T22:   0.0928                                     
REMARK   3      T33:   0.0902 T12:  -0.0141                                     
REMARK   3      T13:   0.0003 T23:   0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1338 L22:   1.7075                                     
REMARK   3      L33:   5.3053 L12:   1.0960                                     
REMARK   3      L13:   2.2099 L23:   1.3320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0698 S12:   0.0262 S13:  -0.0378                       
REMARK   3      S21:   0.1580 S22:   0.0441 S23:  -0.0574                       
REMARK   3      S31:   0.2303 S32:   0.0115 S33:  -0.1139                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   121        B   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5912   0.5143  39.4864              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0768 T22:   0.1054                                     
REMARK   3      T33:   0.0731 T12:  -0.0094                                     
REMARK   3      T13:  -0.0093 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3802 L22:   1.3929                                     
REMARK   3      L33:   8.0456 L12:   2.1436                                     
REMARK   3      L13:   3.1110 L23:  -0.5952                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1023 S12:  -0.3511 S13:   0.2648                       
REMARK   3      S21:  -0.2642 S22:  -0.1629 S23:   0.1471                       
REMARK   3      S31:  -0.2487 S32:  -0.4613 S33:   0.2652                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   129        B   151                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.8605   2.7266  50.0646              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0998 T22:   0.0872                                     
REMARK   3      T33:   0.1001 T12:  -0.0066                                     
REMARK   3      T13:   0.0038 T23:  -0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1358 L22:   1.0852                                     
REMARK   3      L33:   1.0484 L12:  -0.9433                                     
REMARK   3      L13:   0.3378 L23:  -0.1273                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0538 S12:   0.0349 S13:  -0.0356                       
REMARK   3      S21:  -0.0825 S22:   0.0306 S23:   0.0526                       
REMARK   3      S31:  -0.0936 S32:   0.0071 S33:   0.0232                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   152        B   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.1892 -13.0933  48.9475              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0898 T22:   0.1294                                     
REMARK   3      T33:   0.0786 T12:   0.0387                                     
REMARK   3      T13:   0.0308 T23:   0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.2379 L22:  20.4095                                     
REMARK   3      L33:   5.3977 L12:  -3.3254                                     
REMARK   3      L13:   6.8650 L23:  -8.5807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0079 S12:   0.2822 S13:  -0.0470                       
REMARK   3      S21:  -0.2782 S22:  -0.1963 S23:  -0.2012                       
REMARK   3      S31:   0.5129 S32:   0.1285 S33:   0.2041                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   158        B   176                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.1947   5.4804  48.1584              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0996 T22:   0.1127                                     
REMARK   3      T33:   0.1226 T12:  -0.0591                                     
REMARK   3      T13:  -0.0102 T23:   0.0551                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8624 L22:   7.1559                                     
REMARK   3      L33:   5.6134 L12:   0.9294                                     
REMARK   3      L13:  -2.4931 L23:   3.2904                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0231 S12:  -0.2529 S13:  -0.0761                       
REMARK   3      S21:   0.0574 S22:   0.0830 S23:  -0.6516                       
REMARK   3      S31:   0.0570 S32:   0.5790 S33:  -0.0600                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   177        B   196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0440   4.1911  48.0417              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0899 T22:   0.0521                                     
REMARK   3      T33:   0.0913 T12:  -0.0536                                     
REMARK   3      T13:  -0.0057 T23:  -0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4374 L22:   2.1529                                     
REMARK   3      L33:   2.0640 L12:  -3.0861                                     
REMARK   3      L13:   0.9153 L23:  -1.0667                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0064 S12:  -0.0058 S13:   0.1307                       
REMARK   3      S21:   0.0136 S22:  -0.0487 S23:  -0.1091                       
REMARK   3      S31:  -0.1073 S32:   0.1935 S33:   0.0550                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   197        B   208                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.9314  -0.8653  38.7053              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1025 T22:   0.1110                                     
REMARK   3      T33:   0.0877 T12:  -0.0108                                     
REMARK   3      T13:  -0.0062 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0899 L22:   3.5197                                     
REMARK   3      L33:   2.8385 L12:  -3.7941                                     
REMARK   3      L13:  -3.4072 L23:   3.1608                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0162 S12:   0.0471 S13:   0.0025                       
REMARK   3      S21:  -0.1249 S22:  -0.1934 S23:   0.1277                       
REMARK   3      S31:  -0.0509 S32:  -0.0001 S33:   0.2095                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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          
REMARK   3  RIDING POSITIONS. DISORDERED REGION BETWEEN RESIDUES 159 TO         
REMARK   3  164 HAS POOR DENSITY FOR SIDE CHAINS.                               
REMARK   4                                                                      
REMARK   4 2VNS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  07-FEB-08.                 
REMARK 100 THE PDBE ID CODE IS EBI-35237.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07149, 0.82654, 1.07199,         
REMARK 200                                    1.00545, 1.1271                   
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : FLAT COLLIMATING MIRROR,           
REMARK 200                                   DOUBLE CRYSTAL                     
REMARK 200                                   MONOCHROMATOR, TOROID              
REMARK 200                                   FOCUSING MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25300                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.98                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 3.8                                
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.24                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS                        
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: MIRAS TECHNIQUE INCLUDED MAD FROM INCORPORATED PT            
REMARK 200  AND MIR USING PT AND HG DERIVATIVES                                 
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M FECL3, 40-100MM                    
REMARK 280  NA3.CITRATE AND 4% V/V JEFFAMINE M600 PH5.6                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       18.84300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.68300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.40600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.68300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.84300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.40600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.3 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     MET A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     ILE A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     ASP A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     LYS A    23                                                      
REMARK 465     VAL A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     ASP A    26                                                      
REMARK 465     GLU A    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     LEU A   209                                                      
REMARK 465     PRO A   210                                                      
REMARK 465     ALA A   211                                                      
REMARK 465     TRP A   212                                                      
REMARK 465     LYS A   213                                                      
REMARK 465     VAL A   214                                                      
REMARK 465     PRO A   215                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     MET B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     ILE B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     LEU B    12                                                      
REMARK 465     HIS B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     ASP B    16                                                      
REMARK 465     SER B    17                                                      
REMARK 465     ASP B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     LEU B    21                                                      
REMARK 465     ALA B    22                                                      
REMARK 465     LYS B    23                                                      
REMARK 465     VAL B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     ASP B    26                                                      
REMARK 465     GLU B    27                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     LEU B   209                                                      
REMARK 465     PRO B   210                                                      
REMARK 465     ALA B   211                                                      
REMARK 465     TRP B   212                                                      
REMARK 465     LYS B   213                                                      
REMARK 465     VAL B   214                                                      
REMARK 465     PRO B   215                                                      
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     ASP A 104    CG   OD1  OD2                                       
REMARK 470     LEU B 208    CG   CD1  CD2                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     ARG A  63    CG   CD   NE   CZ  NH1  NH2                         
REMARK 480     ARG A 163    CG   CD   NE   CZ  NH1  NH2                         
REMARK 480     ARG B  63    CG   CD   NE   CZ  NH1  NH2                         
REMARK 480     ARG B 163    CG   CD   NE   CZ  NH1  NH2                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    CYS A   100  -  OG   SER A   103              2.05            
REMARK 500   SG   CYS A   100  -  O    HOH A  2033              2.10            
REMARK 500   SG   CYS B   100  -  O    HOH B  2051              2.19            
REMARK 500   CZ   ARG B   207  -  O    HOH B  2072              2.16            
REMARK 500   NH1  ARG B   207  -  O    HOH B  2070              2.19            
REMARK 500   NH2  ARG B   207  -  O    HOH B  2072              1.59            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG B  63   CB A  ARG B  63   CG A   -0.165                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLN A 164   N   -  CA  -  C   ANGL. DEV. = -16.6 DEGREES          
REMARK 500    ILE A 167   CG1 -  CB  -  CG2 ANGL. DEV. =  17.8 DEGREES          
REMARK 500    ASN B 162   N   -  CA  -  C   ANGL. DEV. =  16.3 DEGREES          
REMARK 500    GLN B 164   N   -  CA  -  C   ANGL. DEV. = -18.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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    ALA A  90       55.38   -101.27                                   
REMARK 500    PHE A 146       -3.20     85.41                                   
REMARK 500    ARG A 159      -11.39   -151.85                                   
REMARK 500    ALA B  90       56.91    -98.97                                   
REMARK 500    PHE B 146        1.83     84.77                                   
REMARK 500    ARG B 159       11.59   -146.84                                   
REMARK 500    ASN B 162        6.82     97.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO A   29     LYS A   30                  -45.91                    
REMARK 500 GLY A   35     SER A   36                 -144.85                    
REMARK 500 GLY A  157     PRO A  158                  -39.53                    
REMARK 500 PRO A  158     ARG A  159                  105.92                    
REMARK 500 ARG A  159     ASP A  160                 -127.76                    
REMARK 500 ASN A  162     ARG A  163                  115.32                    
REMARK 500 ARG A  163     GLN A  164                 -132.47                    
REMARK 500 GLY A  169     ASP A  170                 -144.87                    
REMARK 500 PRO B   29     LYS B   30                  -46.22                    
REMARK 500 GLY B  157     PRO B  158                  -39.36                    
REMARK 500 PRO B  158     ARG B  159                   69.65                    
REMARK 500 ARG B  159     ASP B  160                 -139.89                    
REMARK 500 ASP B  160     GLY B  161                  139.03                    
REMARK 500 GLY B  161     ASN B  162                  147.31                    
REMARK 500 ARG B  163     GLN B  164                 -134.85                    
REMARK 500 GLY B  169     ASP B  170                 -145.43                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A1209                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VQ3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MEMBRANE PROXIMAL                          
REMARK 900  OXIDOREDUCTASE DOMAIN OF HUMAN STEAP3, THE                          
REMARK 900  DOMINANT FERRIC REDUCTASE OF THE ERYTHROID                          
REMARK 900  TRANSFERRIN CYCLE                                                   
DBREF  2VNS A    1   215  UNP    Q658P3   STEA3_HUMAN      1    215             
DBREF  2VNS B    1   215  UNP    Q658P3   STEA3_HUMAN      1    215             
SEQRES   1 A  215  MET PRO GLU GLU MET ASP LYS PRO LEU ILE SER LEU HIS          
SEQRES   2 A  215  LEU VAL ASP SER ASP SER SER LEU ALA LYS VAL PRO ASP          
SEQRES   3 A  215  GLU ALA PRO LYS VAL GLY ILE LEU GLY SER GLY ASP PHE          
SEQRES   4 A  215  ALA ARG SER LEU ALA THR ARG LEU VAL GLY SER GLY PHE          
SEQRES   5 A  215  LYS VAL VAL VAL GLY SER ARG ASN PRO LYS ARG THR ALA          
SEQRES   6 A  215  ARG LEU PHE PRO SER ALA ALA GLN VAL THR PHE GLN GLU          
SEQRES   7 A  215  GLU ALA VAL SER SER PRO GLU VAL ILE PHE VAL ALA VAL          
SEQRES   8 A  215  PHE ARG GLU HIS TYR SER SER LEU CYS SER LEU SER ASP          
SEQRES   9 A  215  GLN LEU ALA GLY LYS ILE LEU VAL ASP VAL SER ASN PRO          
SEQRES  10 A  215  THR GLU GLN GLU HIS LEU GLN HIS ARG GLU SER ASN ALA          
SEQRES  11 A  215  GLU TYR LEU ALA SER LEU PHE PRO THR CYS THR VAL VAL          
SEQRES  12 A  215  LYS ALA PHE ASN VAL ILE SER ALA TRP THR LEU GLN ALA          
SEQRES  13 A  215  GLY PRO ARG ASP GLY ASN ARG GLN VAL PRO ILE CYS GLY          
SEQRES  14 A  215  ASP GLN PRO GLU ALA LYS ARG ALA VAL SER GLU MET ALA          
SEQRES  15 A  215  LEU ALA MET GLY PHE MET PRO VAL ASP MET GLY SER LEU          
SEQRES  16 A  215  ALA SER ALA TRP GLU VAL GLU ALA MET PRO LEU ARG LEU          
SEQRES  17 A  215  LEU PRO ALA TRP LYS VAL PRO                                  
SEQRES   1 B  215  MET PRO GLU GLU MET ASP LYS PRO LEU ILE SER LEU HIS          
SEQRES   2 B  215  LEU VAL ASP SER ASP SER SER LEU ALA LYS VAL PRO ASP          
SEQRES   3 B  215  GLU ALA PRO LYS VAL GLY ILE LEU GLY SER GLY ASP PHE          
SEQRES   4 B  215  ALA ARG SER LEU ALA THR ARG LEU VAL GLY SER GLY PHE          
SEQRES   5 B  215  LYS VAL VAL VAL GLY SER ARG ASN PRO LYS ARG THR ALA          
SEQRES   6 B  215  ARG LEU PHE PRO SER ALA ALA GLN VAL THR PHE GLN GLU          
SEQRES   7 B  215  GLU ALA VAL SER SER PRO GLU VAL ILE PHE VAL ALA VAL          
SEQRES   8 B  215  PHE ARG GLU HIS TYR SER SER LEU CYS SER LEU SER ASP          
SEQRES   9 B  215  GLN LEU ALA GLY LYS ILE LEU VAL ASP VAL SER ASN PRO          
SEQRES  10 B  215  THR GLU GLN GLU HIS LEU GLN HIS ARG GLU SER ASN ALA          
SEQRES  11 B  215  GLU TYR LEU ALA SER LEU PHE PRO THR CYS THR VAL VAL          
SEQRES  12 B  215  LYS ALA PHE ASN VAL ILE SER ALA TRP THR LEU GLN ALA          
SEQRES  13 B  215  GLY PRO ARG ASP GLY ASN ARG GLN VAL PRO ILE CYS GLY          
SEQRES  14 B  215  ASP GLN PRO GLU ALA LYS ARG ALA VAL SER GLU MET ALA          
SEQRES  15 B  215  LEU ALA MET GLY PHE MET PRO VAL ASP MET GLY SER LEU          
SEQRES  16 B  215  ALA SER ALA TRP GLU VAL GLU ALA MET PRO LEU ARG LEU          
SEQRES  17 B  215  LEU PRO ALA TRP LYS VAL PRO                                  
HET    CIT  A1209      13                                                       
HETNAM     CIT CITRIC ACID                                                      
FORMUL   3  CIT    C6 H8 O7                                                     
FORMUL   4  HOH   *136(H2 O1)                                                   
HELIX    1   1 GLY A   37  SER A   50  1                                  14    
HELIX    2   2 ASN A   60  PHE A   68  1                                   9    
HELIX    3   3 GLN A   77  VAL A   81  1                                   5    
HELIX    4   4 PHE A   92  TYR A   96  5                                   5    
HELIX    5   5 TYR A   96  SER A  101  5                                   6    
HELIX    6   6 LEU A  102  ALA A  107  1                                   6    
HELIX    7   7 THR A  118  HIS A  125  1                                   8    
HELIX    8   8 SER A  128  PHE A  137  1                                  10    
HELIX    9   9 SER A  150  ALA A  156  1                                   7    
HELIX   10  10 GLN A  171  MET A  185  1                                  15    
HELIX   11  11 SER A  194  ALA A  196  5                                   3    
HELIX   12  12 SER A  197  MET A  204  1                                   8    
HELIX   13  13 GLY B   37  SER B   50  1                                  14    
HELIX   14  14 ASN B   60  ARG B   66  1                                   7    
HELIX   15  15 GLN B   77  VAL B   81  1                                   5    
HELIX   16  16 PHE B   92  TYR B   96  5                                   5    
HELIX   17  17 TYR B   96  SER B  101  5                                   6    
HELIX   18  18 LEU B  102  ALA B  107  1                                   6    
HELIX   19  19 THR B  118  HIS B  125  1                                   8    
HELIX   20  20 SER B  128  PHE B  137  1                                  10    
HELIX   21  21 SER B  150  ALA B  156  1                                   7    
HELIX   22  22 GLN B  171  MET B  185  1                                  15    
HELIX   23  23 SER B  194  ALA B  196  5                                   3    
HELIX   24  24 SER B  197  MET B  204  1                                   8    
SHEET    1  AA 8 GLN A  73  PHE A  76  0                                        
SHEET    2  AA 8 VAL A  54  SER A  58  1  O  VAL A  54   N  GLN A  73           
SHEET    3  AA 8 VAL A  31  LEU A  34  1  O  VAL A  31   N  VAL A  55           
SHEET    4  AA 8 VAL A  86  VAL A  89  1  O  VAL A  86   N  GLY A  32           
SHEET    5  AA 8 ILE A 110  ASP A 113  1  O  ILE A 110   N  ILE A  87           
SHEET    6  AA 8 THR A 141  ALA A 145  1  O  THR A 141   N  LEU A 111           
SHEET    7  AA 8 GLN A 164  GLY A 169 -1  O  CYS A 168   N  LYS A 144           
SHEET    8  AA 8 MET A 188  ASP A 191  1  O  MET A 188   N  VAL A 165           
SHEET    1  BA 8 GLN B  73  PHE B  76  0                                        
SHEET    2  BA 8 VAL B  54  SER B  58  1  O  VAL B  54   N  GLN B  73           
SHEET    3  BA 8 VAL B  31  LEU B  34  1  O  VAL B  31   N  VAL B  55           
SHEET    4  BA 8 VAL B  86  VAL B  89  1  O  VAL B  86   N  GLY B  32           
SHEET    5  BA 8 ILE B 110  ASP B 113  1  O  ILE B 110   N  ILE B  87           
SHEET    6  BA 8 THR B 141  ALA B 145  1  O  THR B 141   N  LEU B 111           
SHEET    7  BA 8 ARG B 163  GLY B 169 -1  O  CYS B 168   N  LYS B 144           
SHEET    8  BA 8 PHE B 187  ASP B 191  1  O  MET B 188   N  VAL B 165           
CISPEP   1 ARG B  207    LEU B  208          0       -13.35                     
SITE     1 AC1  1 LYS A  62                                                     
CRYST1   37.686   66.812  143.366  90.00  90.00  90.00 P 21 21 21    8          
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      0.026535  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014967  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006975        0.00000                         
MTRIX1   1 -1.000000  0.002000  0.013000       55.92755    1                    
MTRIX2   1 -0.002000 -0.998000  0.067000      -37.84579    1                    
MTRIX3   1  0.013000  0.067000  0.998000        0.74035    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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