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Database: PDB
Entry: 3L95
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HEADER    IMMUNE SYSTEM                           04-JAN-10   3L95              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN NOTCH1 NEGATIVE REGULATORY REGION (NRR)
TITLE    2 BOUND TO THE FAB FRAGMENT OF AN ANTAGONIST ANTIBODY                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANTI-NRR1 FAB FRAGMENT LIGHT CHAIN;                        
COMPND   3 CHAIN: A, L;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: ANTI-NRR1 FAB FRAGMENT HEAVY CHAIN;                        
COMPND   7 CHAIN: B, H;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND  11 CHAIN: X, Y;                                                         
COMPND  12 FRAGMENT: NEGATIVE REGULATORY REGION (NRR1);                         
COMPND  13 SYNONYM: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1, 
COMPND  14 NOTCH 1 EXTRACELLULAR TRUNCATION, NOTCH 1 INTRACELLULAR DOMAIN;      
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606;                                                
SOURCE   6 OTHER_DETAILS: SYNTHETIC ANTIBODY GENERATED WITH PHAGE DISPLAY;      
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 OTHER_DETAILS: SYNTHETIC ANTIBODY GENERATED WITH PHAGE DISPLAY;      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 GENE: HUMAN NOTCH 1, NOTCH1, TAN1;                                   
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 OTHER_DETAILS: PROTEIN SELECTED BY PHAGE DISPLAY                     
KEYWDS    NRR, FAB FRAGMENT, ANTIBODY, ALPHA-BETA-SANDWICH, SEA DOMAIN, LNR,    
KEYWDS   2 LIN12 NOTCH CYSTEINE-RICH, HD DOMAIN, CELL CYCLE, SIGNALING PROTEIN, 
KEYWDS   3 ACTIVATOR, ANK REPEAT, CELL MEMBRANE, DEVELOPMENTAL PROTEIN,         
KEYWDS   4 DIFFERENTIATION, EGF-LIKE DOMAIN, GLYCOPROTEIN, MEMBRANE, METAL-     
KEYWDS   5 BINDING, NOTCH SIGNALING PATHWAY, IMMUNE SYSTEM                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.G.HYMOWITZ,G.P.DE LEON                                              
REVDAT   6   02-AUG-17 3L95    1       SOURCE REMARK                            
REVDAT   5   25-SEP-13 3L95    1       SOURCE                                   
REVDAT   4   13-JUL-11 3L95    1       VERSN                                    
REVDAT   3   28-APR-10 3L95    1       JRNL                                     
REVDAT   2   14-APR-10 3L95    1       JRNL                                     
REVDAT   1   09-MAR-10 3L95    0                                                
JRNL        AUTH   Y.WU,C.CAIN-HOM,L.CHOY,T.J.HAGENBEEK,G.P.DE LEON,Y.CHEN,     
JRNL        AUTH 2 D.FINKLE,R.VENOOK,X.WU,J.RIDGWAY,D.SCHAHIN-REED,G.J.DOW,     
JRNL        AUTH 3 A.SHELTON,S.STAWICKI,R.J.WATTS,J.ZHANG,R.CHOY,P.HOWARD,      
JRNL        AUTH 4 L.KADYK,M.YAN,J.ZHA,C.A.CALLAHAN,S.G.HYMOWITZ,C.W.SIEBEL     
JRNL        TITL   THERAPEUTIC ANTIBODY TARGETING OF INDIVIDUAL NOTCH           
JRNL        TITL 2 RECEPTORS.                                                   
JRNL        REF    NATURE                        V. 464  1052 2010              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   20393564                                                     
JRNL        DOI    10.1038/NATURE08878                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 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) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 62930                          
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 6979                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 25                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.19                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.24                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3061                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2950                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 322                          
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9986                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 81                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.92000                                             
REMARK   3    B22 (A**2) : 0.40000                                              
REMARK   3    B33 (A**2) : 1.51000                                              
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): 0.341         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.248         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.209         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.318        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10292 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  6840 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14012 ; 1.139 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16619 ; 0.821 ; 3.006       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1302 ; 5.872 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   451 ;35.236 ;24.568       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1590 ;15.618 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    43 ;17.149 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1534 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11599 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2072 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2043 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  6794 ; 0.185 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4950 ; 0.174 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5539 ; 0.082 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   247 ; 0.140 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    19 ; 0.119 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    67 ; 0.190 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   140 ; 0.197 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.159 ; 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):  6708 ; 2.397 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2654 ; 0.570 ; 2.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10463 ; 3.579 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4187 ; 2.202 ; 2.500       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3548 ; 3.199 ; 5.000       
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 L                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     107      4                      
REMARK   3           1     L      1       L     107      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1373 ;  0.42 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1373 ;  0.56 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B H                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      1       B     111      4                      
REMARK   3           1     H      1       H     111      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   1542 ;  0.39 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    B (A**2):   1542 ;  0.60 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A L                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    108       A     212      4                      
REMARK   3           1     L    108       L     212      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):   1366 ;  0.41 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    A (A**2):   1366 ;  0.30 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : B H                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    112       B     214      4                      
REMARK   3           1     H    112       H     214      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  4    B    (A):   1224 ;  0.42 ;  0.50           
REMARK   3   MEDIUM THERMAL     4    B (A**2):   1224 ;  0.39 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : X Y                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     X   1461       X    1721      6                      
REMARK   3           1     Y   1461       Y    1721      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   5    X    (A):   2697 ;  0.59 ;  5.00           
REMARK   3   LOOSE THERMAL      5    X (A**2):   2697 ;  3.22 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
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 :   X  1447        X  1727                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.1002 -25.4332   1.3977              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1362 T22:  -0.1808                                     
REMARK   3      T33:  -0.0868 T12:  -0.0023                                     
REMARK   3      T13:   0.0086 T23:  -0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4419 L22:   1.1034                                     
REMARK   3      L33:   0.7321 L12:  -0.2074                                     
REMARK   3      L13:   0.2254 L23:   0.3498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0340 S12:   0.0943 S13:   0.1010                       
REMARK   3      S21:  -0.0582 S22:  -0.0498 S23:   0.0322                       
REMARK   3      S31:  -0.0816 S32:   0.0048 S33:   0.0158                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   106                          
REMARK   3    RESIDUE RANGE :   B     1        B   111                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.0428 -30.9795  28.4490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1511 T22:  -0.1338                                     
REMARK   3      T33:  -0.2433 T12:  -0.0029                                     
REMARK   3      T13:   0.0028 T23:  -0.0159                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7199 L22:   0.6112                                     
REMARK   3      L33:   1.1723 L12:   0.3945                                     
REMARK   3      L13:   0.3381 L23:   0.0323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0168 S12:  -0.4188 S13:  -0.0273                       
REMARK   3      S21:   0.0456 S22:  -0.0514 S23:  -0.0075                       
REMARK   3      S31:  -0.0447 S32:  -0.0127 S33:   0.0347                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   107        A   212                          
REMARK   3    RESIDUE RANGE :   B   112        B   214                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5366 -30.8855  63.3461              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0121 T22:  -0.0027                                     
REMARK   3      T33:  -0.1758 T12:   0.0959                                     
REMARK   3      T13:   0.0371 T23:  -0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4399 L22:   1.6613                                     
REMARK   3      L33:   5.4864 L12:   1.7021                                     
REMARK   3      L13:  -1.5726 L23:  -1.8068                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0091 S12:  -0.0024 S13:   0.1996                       
REMARK   3      S21:   0.2154 S22:   0.2959 S23:  -0.0378                       
REMARK   3      S31:  -0.5495 S32:  -0.6572 S33:  -0.2868                       
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 :   Y  1461        Y  1726                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4883  20.1126  16.4180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0593 T22:  -0.1216                                     
REMARK   3      T33:   0.0171 T12:  -0.0017                                     
REMARK   3      T13:  -0.0276 T23:  -0.0808                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7346 L22:   1.2211                                     
REMARK   3      L33:   1.3379 L12:  -0.3479                                     
REMARK   3      L13:  -0.2312 L23:   0.2572                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0369 S12:  -0.2490 S13:   0.0204                       
REMARK   3      S21:  -0.0798 S22:  -0.0147 S23:   0.0208                       
REMARK   3      S31:  -0.0384 S32:  -0.0030 S33:   0.0516                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L   106                          
REMARK   3    RESIDUE RANGE :   H     1        H   111                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.1848   9.2761  43.0114              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0690 T22:   0.2230                                     
REMARK   3      T33:   0.0234 T12:   0.1143                                     
REMARK   3      T13:   0.0622 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7095 L22:   3.2052                                     
REMARK   3      L33:   5.2128 L12:   0.6681                                     
REMARK   3      L13:   1.0891 L23:  -0.5049                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1650 S12:  -0.5337 S13:  -0.3404                       
REMARK   3      S21:   0.0524 S22:   0.0125 S23:  -0.2646                       
REMARK   3      S31:   0.6946 S32:  -0.1282 S33:   0.1525                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   107        L   212                          
REMARK   3    RESIDUE RANGE :   H   112        H   213                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.6178  -2.0566  74.9825              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6264 T22:   0.2958                                     
REMARK   3      T33:   0.1061 T12:   0.3322                                     
REMARK   3      T13:   0.0379 T23:  -0.0646                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5629 L22:   2.5132                                     
REMARK   3      L33:   9.0204 L12:   2.8562                                     
REMARK   3      L13:  -1.8259 L23:  -2.3299                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1107 S12:   0.1923 S13:  -0.1970                       
REMARK   3      S21:  -0.2396 S22:  -0.2474 S23:  -0.2052                       
REMARK   3      S31:   1.4866 S32:  -0.3169 S33:   0.3581                       
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                                                           
REMARK   4                                                                      
REMARK   4 3L95 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000056989.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69923                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB 2OO4, FAB FRAGMENT                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: EQUAL VOLUMES OF PROTEIN AND WELL        
REMARK 280  SOLUTIONS. PROTEIN: 6 MG/ML IN 150 MM NACL, 20 MM BIS-TRIS PH       
REMARK 280  6.5. WELL SOLUTION: 300 MM DI-AMMONIUM SULFATE, 20% PEG 5000 MME,   
REMARK 280  100 MM TRIS PH 7.5, VAPOR DIFFUSION, TEMPERATURE 292K               
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       23.12700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       89.81000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       81.96700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       89.81000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.12700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.96700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, X, H, Y                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, L, H, Y                            
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     GLU A   213                                                      
REMARK 465     CYS A   214                                                      
REMARK 465     SER B   215                                                      
REMARK 465     CYS B   216                                                      
REMARK 465     ASP B   217                                                      
REMARK 465     LYS B   218                                                      
REMARK 465     THR B   219                                                      
REMARK 465     HIS B   220                                                      
REMARK 465     THR B   221                                                      
REMARK 465     GLN X  1688                                                      
REMARK 465     ALA X  1689                                                      
REMARK 465     SER X  1690                                                      
REMARK 465     GLU X  1728                                                      
REMARK 465     PRO X  1729                                                      
REMARK 465     ALA X  1730                                                      
REMARK 465     ASN X  1731                                                      
REMARK 465     SER X  1732                                                      
REMARK 465     HIS X  1733                                                      
REMARK 465     HIS X  1734                                                      
REMARK 465     HIS X  1735                                                      
REMARK 465     HIS X  1736                                                      
REMARK 465     HIS X  1737                                                      
REMARK 465     HIS X  1738                                                      
REMARK 465     GLU L   213                                                      
REMARK 465     CYS L   214                                                      
REMARK 465     LYS H   214                                                      
REMARK 465     SER H   215                                                      
REMARK 465     CYS H   216                                                      
REMARK 465     ASP H   217                                                      
REMARK 465     LYS H   218                                                      
REMARK 465     THR H   219                                                      
REMARK 465     HIS H   220                                                      
REMARK 465     THR H   221                                                      
REMARK 465     GLY Y  1447                                                      
REMARK 465     SER Y  1448                                                      
REMARK 465     ALA Y  1449                                                      
REMARK 465     CYS Y  1450                                                      
REMARK 465     GLU Y  1451                                                      
REMARK 465     LEU Y  1452                                                      
REMARK 465     PRO Y  1453                                                      
REMARK 465     GLU Y  1454                                                      
REMARK 465     CYS Y  1455                                                      
REMARK 465     GLN Y  1456                                                      
REMARK 465     GLU Y  1457                                                      
REMARK 465     ASP Y  1458                                                      
REMARK 465     ALA Y  1459                                                      
REMARK 465     GLY Y  1460                                                      
REMARK 465     ARG Y  1524                                                      
REMARK 465     ALA Y  1525                                                      
REMARK 465     GLU Y  1526                                                      
REMARK 465     VAL Y  1727                                                      
REMARK 465     GLU Y  1728                                                      
REMARK 465     PRO Y  1729                                                      
REMARK 465     ALA Y  1730                                                      
REMARK 465     ASN Y  1731                                                      
REMARK 465     SER Y  1732                                                      
REMARK 465     HIS Y  1733                                                      
REMARK 465     HIS Y  1734                                                      
REMARK 465     HIS Y  1735                                                      
REMARK 465     HIS Y  1736                                                      
REMARK 465     HIS Y  1737                                                      
REMARK 465     HIS Y  1738                                                      
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 214    CG   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   ND2  ASN X  1588     O    HOH X    19              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS X1529   CA  -  CB  -  SG  ANGL. DEV. =   6.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  30     -107.86     30.14                                   
REMARK 500    ALA A  51      -52.26     78.30                                   
REMARK 500    GLU A  81        0.22    -67.06                                   
REMARK 500    ALA A  84      173.23    172.50                                   
REMARK 500    ASN A 152      -22.12     75.58                                   
REMARK 500    SER B  96     -166.52   -101.29                                   
REMARK 500    SER B 132       71.71   -119.27                                   
REMARK 500    SER X1481       51.83   -113.69                                   
REMARK 500    ASP X1486      107.39    -33.35                                   
REMARK 500    ALA X1563       46.54   -174.44                                   
REMARK 500    PRO X1716       15.17    -69.46                                   
REMARK 500    SER L  30     -117.16     47.46                                   
REMARK 500    ALA L  51      -50.08     72.41                                   
REMARK 500    ALA L  84      154.21    173.00                                   
REMARK 500    PRO L  95       94.66    -63.08                                   
REMARK 500    VAL L 110       97.64    -62.21                                   
REMARK 500    ASN L 138       73.57     54.10                                   
REMARK 500    ASN L 152       -2.40     68.36                                   
REMARK 500    SER H   7      177.05    172.69                                   
REMARK 500    SER H  96     -165.94    -78.51                                   
REMARK 500    PHE H  98       97.98    -69.83                                   
REMARK 500    SER H 112     -153.06   -142.03                                   
REMARK 500    ASP H 144       85.18     59.80                                   
REMARK 500    THR H 191      -61.25    -93.59                                   
REMARK 500    LYS Y1462      -28.31     72.15                                   
REMARK 500    ASP Y1486       94.59     28.52                                   
REMARK 500    CYS Y1522       59.70   -100.11                                   
REMARK 500    ALA Y1563       42.27   -154.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA X2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL X1463   O                                                      
REMARK 620 2 ASN X1461   OD1  91.8                                              
REMARK 620 3 ASP X1476   OD2  81.3 148.7                                        
REMARK 620 4 ASP X1479   OD2  82.4  75.0  73.8                                  
REMARK 620 5 ASP X1458   O   161.0  72.7 106.2  83.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA X2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS X1545   O                                                      
REMARK 620 2 ASP X1547   OD2  83.4                                              
REMARK 620 3 ASP X1561   OD2  85.0 168.0                                        
REMARK 620 4 HIS X1540   O   157.3  96.0  95.9                                  
REMARK 620 5 ASP X1543   OD1  84.5 113.2  68.7  74.9                            
REMARK 620 6 ASP X1558   OD1 125.1  91.0  93.0  77.6 144.8                      
REMARK 620 7 ASP X1558   OD2  77.9  85.3  89.1 124.8 152.8  47.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA Y2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP Y1507   OD2                                                    
REMARK 620 2 ASP Y1503   OD1 100.1                                              
REMARK 620 3 HIS Y1505   O    82.4  88.0                                        
REMARK 620 4 TYR Y1500   O    98.6  72.2 160.1                                  
REMARK 620 5 ASP Y1518   OD1  91.0 150.7 120.5  79.4                            
REMARK 620 6 ASP Y1521   OD2 159.1  69.4  79.2  95.3 107.0                      
REMARK 620 7 ASP Y1518   OD2  90.8 154.3  70.3 129.4  50.6  92.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA X2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS X1505   O                                                      
REMARK 620 2 ASP X1507   OD2  78.2                                              
REMARK 620 3 TYR X1500   O   159.3  99.7                                        
REMARK 620 4 ASP X1521   OD2  90.8 168.2  89.2                                  
REMARK 620 5 ASP X1503   OD1  83.6  94.4  76.0  80.2                            
REMARK 620 6 ASP X1518   OD2  77.2  93.0 123.5  88.5 157.6                      
REMARK 620 7 ASP X1518   OD1 126.3  94.0  74.2  95.8 150.0  49.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA Y2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL Y1463   O                                                      
REMARK 620 2 SER Y1465   OG  103.6                                              
REMARK 620 3 ASP Y1476   OD2  69.6  74.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA Y2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS Y1545   O                                                      
REMARK 620 2 HIS Y1540   O   155.5                                              
REMARK 620 3 ASP Y1547   OD2  88.7  93.3                                        
REMARK 620 4 ASP Y1558   OD2  76.8 127.3  94.0                                  
REMARK 620 5 ASP Y1561   OD2  87.1  91.4 175.3  82.9                            
REMARK 620 6 ASP Y1543   OD1  79.5  76.3 104.7 149.3  76.6                      
REMARK 620 7 ASP Y1558   OD1 127.2  77.1  92.6  50.4  88.3 149.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 222                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA X 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA X 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA X 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X 2005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Y 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Y 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Y 2003                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ETO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE S1-CLEAVED NOTCH1 NEGATIVE REGULATORY       
REMARK 900 REGION (NRR)                                                         
REMARK 900 RELATED ID: 2OO4   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LNR-HD (NEGATIVE REGULATORY REGION) FROM HUMAN NOTCH2   
DBREF  3L95 X 1449  1622  UNP    P46531   NOTC1_HUMAN   1448   1621             
DBREF  3L95 X 1671  1729  UNP    P46531   NOTC1_HUMAN   1670   1728             
DBREF  3L95 Y 1449  1622  UNP    P46531   NOTC1_HUMAN   1448   1621             
DBREF  3L95 Y 1671  1729  UNP    P46531   NOTC1_HUMAN   1670   1728             
DBREF  3L95 A    1   214  PDB    3L95     3L95             1    214             
DBREF  3L95 B    1   221  PDB    3L95     3L95             1    227             
DBREF  3L95 L    1   214  PDB    3L95     3L95             1    214             
DBREF  3L95 H    1   221  PDB    3L95     3L95             1    227             
SEQADV 3L95 ALA X 1730  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 ASN X 1731  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 SER X 1732  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 HIS X 1733  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 HIS X 1734  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 HIS X 1735  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 HIS X 1736  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 HIS X 1737  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 HIS X 1738  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 ALA Y 1730  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 ASN Y 1731  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 SER Y 1732  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 HIS Y 1733  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 HIS Y 1734  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 HIS Y 1735  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 HIS Y 1736  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 HIS Y 1737  UNP  P46531              EXPRESSION TAG                 
SEQADV 3L95 HIS Y 1738  UNP  P46531              EXPRESSION TAG                 
SEQRES   1 A  214  ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 A  214  SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER          
SEQRES   3 A  214  GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS          
SEQRES   4 A  214  PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER          
SEQRES   5 A  214  PHE LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 A  214  GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 A  214  GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN PHE          
SEQRES   8 A  214  TYR THR THR PRO SER THR PHE GLY GLN GLY THR LYS VAL          
SEQRES   9 A  214  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 A  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 A  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 A  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 A  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 A  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 A  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 A  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 A  214  PHE ASN ARG GLY GLU CYS                                      
SEQRES   1 B  227  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 B  227  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 B  227  PHE THR PHE SER SER TYR TRP ILE HIS TRP VAL ARG GLN          
SEQRES   4 B  227  ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ASN          
SEQRES   5 B  227  PRO PRO ASN ARG SER ASN GLN TYR ALA ASP SER VAL LYS          
SEQRES   6 B  227  GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR          
SEQRES   7 B  227  ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 B  227  ALA VAL TYR TYR CYS ALA ARG GLY SER GLY PHE ARG TRP          
SEQRES   9 B  227  VAL MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL          
SEQRES  10 B  227  SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU          
SEQRES  11 B  227  ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA          
SEQRES  12 B  227  LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL          
SEQRES  13 B  227  THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL          
SEQRES  14 B  227  HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR          
SEQRES  15 B  227  SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU          
SEQRES  16 B  227  GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO          
SEQRES  17 B  227  SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER          
SEQRES  18 B  227  CYS ASP LYS THR HIS THR                                      
SEQRES   1 X  244  GLY SER ALA CYS GLU LEU PRO GLU CYS GLN GLU ASP ALA          
SEQRES   2 X  244  GLY ASN LYS VAL CYS SER LEU GLN CYS ASN ASN HIS ALA          
SEQRES   3 X  244  CYS GLY TRP ASP GLY GLY ASP CYS SER LEU ASN PHE ASN          
SEQRES   4 X  244  ASP PRO TRP LYS ASN CYS THR GLN SER LEU GLN CYS TRP          
SEQRES   5 X  244  LYS TYR PHE SER ASP GLY HIS CYS ASP SER GLN CYS ASN          
SEQRES   6 X  244  SER ALA GLY CYS LEU PHE ASP GLY PHE ASP CYS GLN ARG          
SEQRES   7 X  244  ALA GLU GLY GLN CYS ASN PRO LEU TYR ASP GLN TYR CYS          
SEQRES   8 X  244  LYS ASP HIS PHE SER ASP GLY HIS CYS ASP GLN GLY CYS          
SEQRES   9 X  244  ASN SER ALA GLU CYS GLU TRP ASP GLY LEU ASP CYS ALA          
SEQRES  10 X  244  GLU HIS VAL PRO GLU ARG LEU ALA ALA GLY THR LEU VAL          
SEQRES  11 X  244  VAL VAL VAL LEU MET PRO PRO GLU GLN LEU ARG ASN SER          
SEQRES  12 X  244  SER PHE HIS PHE LEU ARG GLU LEU SER ARG VAL LEU HIS          
SEQRES  13 X  244  THR ASN VAL VAL PHE LYS ARG ASP ALA HIS GLY GLN GLN          
SEQRES  14 X  244  MET ILE PHE PRO TYR TYR GLY ASP VAL ARG GLY SER ILE          
SEQRES  15 X  244  VAL TYR LEU GLU ILE ASP ASN ARG GLN CYS VAL GLN ALA          
SEQRES  16 X  244  SER SER GLN CYS PHE GLN SER ALA THR ASP VAL ALA ALA          
SEQRES  17 X  244  PHE LEU GLY ALA LEU ALA SER LEU GLY SER LEU ASN ILE          
SEQRES  18 X  244  PRO TYR LYS ILE GLU ALA VAL GLN SER GLU THR VAL GLU          
SEQRES  19 X  244  PRO ALA ASN SER HIS HIS HIS HIS HIS HIS                      
SEQRES   1 L  214  ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 L  214  SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER          
SEQRES   3 L  214  GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER          
SEQRES   5 L  214  PHE LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 L  214  GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN PHE          
SEQRES   8 L  214  TYR THR THR PRO SER THR PHE GLY GLN GLY THR LYS VAL          
SEQRES   9 L  214  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 L  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 L  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 L  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 L  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 L  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 L  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 L  214  PHE ASN ARG GLY GLU CYS                                      
SEQRES   1 H  227  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  227  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 H  227  PHE THR PHE SER SER TYR TRP ILE HIS TRP VAL ARG GLN          
SEQRES   4 H  227  ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ASN          
SEQRES   5 H  227  PRO PRO ASN ARG SER ASN GLN TYR ALA ASP SER VAL LYS          
SEQRES   6 H  227  GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR          
SEQRES   7 H  227  ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 H  227  ALA VAL TYR TYR CYS ALA ARG GLY SER GLY PHE ARG TRP          
SEQRES   9 H  227  VAL MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL          
SEQRES  10 H  227  SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU          
SEQRES  11 H  227  ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA          
SEQRES  12 H  227  LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  227  THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL          
SEQRES  14 H  227  HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR          
SEQRES  15 H  227  SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU          
SEQRES  16 H  227  GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO          
SEQRES  17 H  227  SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER          
SEQRES  18 H  227  CYS ASP LYS THR HIS THR                                      
SEQRES   1 Y  244  GLY SER ALA CYS GLU LEU PRO GLU CYS GLN GLU ASP ALA          
SEQRES   2 Y  244  GLY ASN LYS VAL CYS SER LEU GLN CYS ASN ASN HIS ALA          
SEQRES   3 Y  244  CYS GLY TRP ASP GLY GLY ASP CYS SER LEU ASN PHE ASN          
SEQRES   4 Y  244  ASP PRO TRP LYS ASN CYS THR GLN SER LEU GLN CYS TRP          
SEQRES   5 Y  244  LYS TYR PHE SER ASP GLY HIS CYS ASP SER GLN CYS ASN          
SEQRES   6 Y  244  SER ALA GLY CYS LEU PHE ASP GLY PHE ASP CYS GLN ARG          
SEQRES   7 Y  244  ALA GLU GLY GLN CYS ASN PRO LEU TYR ASP GLN TYR CYS          
SEQRES   8 Y  244  LYS ASP HIS PHE SER ASP GLY HIS CYS ASP GLN GLY CYS          
SEQRES   9 Y  244  ASN SER ALA GLU CYS GLU TRP ASP GLY LEU ASP CYS ALA          
SEQRES  10 Y  244  GLU HIS VAL PRO GLU ARG LEU ALA ALA GLY THR LEU VAL          
SEQRES  11 Y  244  VAL VAL VAL LEU MET PRO PRO GLU GLN LEU ARG ASN SER          
SEQRES  12 Y  244  SER PHE HIS PHE LEU ARG GLU LEU SER ARG VAL LEU HIS          
SEQRES  13 Y  244  THR ASN VAL VAL PHE LYS ARG ASP ALA HIS GLY GLN GLN          
SEQRES  14 Y  244  MET ILE PHE PRO TYR TYR GLY ASP VAL ARG GLY SER ILE          
SEQRES  15 Y  244  VAL TYR LEU GLU ILE ASP ASN ARG GLN CYS VAL GLN ALA          
SEQRES  16 Y  244  SER SER GLN CYS PHE GLN SER ALA THR ASP VAL ALA ALA          
SEQRES  17 Y  244  PHE LEU GLY ALA LEU ALA SER LEU GLY SER LEU ASN ILE          
SEQRES  18 Y  244  PRO TYR LYS ILE GLU ALA VAL GLN SER GLU THR VAL GLU          
SEQRES  19 Y  244  PRO ALA ASN SER HIS HIS HIS HIS HIS HIS                      
MODRES 3L95 ASN X 1490  ASN  GLYCOSYLATION SITE                                 
HET    SO4  B 222       5                                                       
HET     CA  X2001       1                                                       
HET     CA  X2002       1                                                       
HET     CA  X2003       1                                                       
HET    NAG  X2004      14                                                       
HET    NAG  X2005      14                                                       
HET     CA  Y2001       1                                                       
HET     CA  Y2002       1                                                       
HET     CA  Y2003       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   7  SO4    O4 S 2-                                                      
FORMUL   8   CA    6(CA 2+)                                                     
FORMUL  11  NAG    2(C8 H15 N O6)                                               
FORMUL  15  HOH   *81(H2 O)                                                     
HELIX    1   1 GLN A   79  PHE A   83  5                                   5    
HELIX    2   2 SER A  121  GLY A  128  1                                   8    
HELIX    3   3 LYS A  183  HIS A  189  1                                   7    
HELIX    4   4 THR B   28  TYR B   32  5                                   5    
HELIX    5   5 ARG B   83  THR B   87  5                                   5    
HELIX    6   6 SER B  127  THR B  131  5                                   5    
HELIX    7   7 SER B  187  GLN B  192  1                                   6    
HELIX    8   8 LYS B  201  ASN B  204  5                                   4    
HELIX    9   9 GLY X 1447  GLU X 1451  5                                   5    
HELIX   10  10 LEU X 1452  ALA X 1459  1                                   8    
HELIX   11  11 ASN X 1470  ALA X 1472  5                                   3    
HELIX   12  12 CYS X 1473  GLY X 1478  1                                   6    
HELIX   13  13 THR X 1492  TYR X 1500  5                                   9    
HELIX   14  14 ASP X 1507  ASN X 1511  5                                   5    
HELIX   15  15 CYS X 1515  ASP X 1521  5                                   7    
HELIX   16  16 ASN X 1530  LEU X 1532  5                                   3    
HELIX   17  17 TYR X 1533  HIS X 1540  1                                   8    
HELIX   18  18 ASP X 1547  ASN X 1551  5                                   5    
HELIX   19  19 CYS X 1555  ASP X 1561  5                                   7    
HELIX   20  20 PRO X 1582  SER X 1589  1                                   8    
HELIX   21  21 SER X 1589  HIS X 1602  1                                  14    
HELIX   22  22 SER X 1696  LEU X 1710  1                                  15    
HELIX   23  23 SER L  121  GLY L  128  1                                   8    
HELIX   24  24 LYS L  183  GLU L  187  1                                   5    
HELIX   25  25 THR H   28  TYR H   32  5                                   5    
HELIX   26  26 ASP H   61  LYS H   64  5                                   4    
HELIX   27  27 ARG H   83  THR H   87  5                                   5    
HELIX   28  28 ASN Y 1470  ALA Y 1472  5                                   3    
HELIX   29  29 CYS Y 1473  GLY Y 1478  1                                   6    
HELIX   30  30 THR Y 1492  TYR Y 1500  5                                   9    
HELIX   31  31 ASP Y 1507  ASN Y 1511  5                                   5    
HELIX   32  32 CYS Y 1515  ASP Y 1521  5                                   7    
HELIX   33  33 TYR Y 1533  HIS Y 1540  1                                   8    
HELIX   34  34 ASP Y 1547  ASN Y 1551  5                                   5    
HELIX   35  35 SER Y 1552  ASP Y 1561  5                                  10    
HELIX   36  36 PRO Y 1582  SER Y 1589  1                                   8    
HELIX   37  37 SER Y 1589  HIS Y 1602  1                                  14    
HELIX   38  38 GLN Y 1685  SER Y 1690  1                                   6    
HELIX   39  39 SER Y 1696  LEU Y 1710  1                                  15    
SHEET    1   A 4 MET A   4  SER A   7  0                                        
SHEET    2   A 4 VAL A  19  ALA A  25 -1  O  THR A  22   N  SER A   7           
SHEET    3   A 4 ASP A  70  ILE A  75 -1  O  PHE A  71   N  CYS A  23           
SHEET    4   A 4 PHE A  62  SER A  65 -1  N  SER A  63   O  THR A  74           
SHEET    1   B 6 SER A  10  ALA A  13  0                                        
SHEET    2   B 6 THR A 102  ILE A 106  1  O  GLU A 105   N  LEU A  11           
SHEET    3   B 6 ALA A  84  GLN A  90 -1  N  ALA A  84   O  VAL A 104           
SHEET    4   B 6 VAL A  33  GLN A  38 -1  N  GLN A  38   O  THR A  85           
SHEET    5   B 6 LYS A  45  TYR A  49 -1  O  LEU A  47   N  TRP A  35           
SHEET    6   B 6 PHE A  53  LEU A  54 -1  O  PHE A  53   N  TYR A  49           
SHEET    1   C 4 SER A  10  ALA A  13  0                                        
SHEET    2   C 4 THR A 102  ILE A 106  1  O  GLU A 105   N  LEU A  11           
SHEET    3   C 4 ALA A  84  GLN A  90 -1  N  ALA A  84   O  VAL A 104           
SHEET    4   C 4 THR A  97  PHE A  98 -1  O  THR A  97   N  GLN A  90           
SHEET    1   D 4 SER A 114  PHE A 118  0                                        
SHEET    2   D 4 THR A 129  PHE A 139 -1  O  ASN A 137   N  SER A 114           
SHEET    3   D 4 TYR A 173  SER A 182 -1  O  LEU A 181   N  ALA A 130           
SHEET    4   D 4 SER A 159  VAL A 163 -1  N  SER A 162   O  SER A 176           
SHEET    1   E 4 ALA A 153  LEU A 154  0                                        
SHEET    2   E 4 ALA A 144  VAL A 150 -1  N  VAL A 150   O  ALA A 153           
SHEET    3   E 4 VAL A 191  HIS A 198 -1  O  GLU A 195   N  GLN A 147           
SHEET    4   E 4 VAL A 205  ASN A 210 -1  O  VAL A 205   N  VAL A 196           
SHEET    1   F 4 GLN B   3  SER B   7  0                                        
SHEET    2   F 4 LEU B  18  SER B  25 -1  O  SER B  25   N  GLN B   3           
SHEET    3   F 4 THR B  77  MET B  82 -1  O  MET B  82   N  LEU B  18           
SHEET    4   F 4 PHE B  67  ASP B  72 -1  N  THR B  68   O  GLN B  81           
SHEET    1   G 6 GLY B  10  VAL B  12  0                                        
SHEET    2   G 6 THR B 107  VAL B 111  1  O  THR B 110   N  VAL B  12           
SHEET    3   G 6 ALA B  88  GLY B  95 -1  N  TYR B  90   O  THR B 107           
SHEET    4   G 6 ILE B  34  GLN B  39 -1  N  HIS B  35   O  ALA B  93           
SHEET    5   G 6 LEU B  45  ASN B  52 -1  O  GLU B  46   N  ARG B  38           
SHEET    6   G 6 SER B  56  TYR B  59 -1  O  SER B  56   N  ASN B  52           
SHEET    1   H 4 GLY B  10  VAL B  12  0                                        
SHEET    2   H 4 THR B 107  VAL B 111  1  O  THR B 110   N  VAL B  12           
SHEET    3   H 4 ALA B  88  GLY B  95 -1  N  TYR B  90   O  THR B 107           
SHEET    4   H 4 MET B 100K TRP B 103 -1  O  TYR B 102   N  ARG B  94           
SHEET    1   I 4 SER B 120  LEU B 124  0                                        
SHEET    2   I 4 THR B 135  TYR B 145 -1  O  LEU B 141   N  PHE B 122           
SHEET    3   I 4 TYR B 176  PRO B 185 -1  O  LEU B 178   N  VAL B 142           
SHEET    4   I 4 VAL B 163  THR B 165 -1  N  HIS B 164   O  VAL B 181           
SHEET    1   J 4 SER B 120  LEU B 124  0                                        
SHEET    2   J 4 THR B 135  TYR B 145 -1  O  LEU B 141   N  PHE B 122           
SHEET    3   J 4 TYR B 176  PRO B 185 -1  O  LEU B 178   N  VAL B 142           
SHEET    4   J 4 VAL B 169  LEU B 170 -1  N  VAL B 169   O  SER B 177           
SHEET    1   K 3 THR B 151  TRP B 154  0                                        
SHEET    2   K 3 TYR B 194  HIS B 200 -1  O  ASN B 197   N  SER B 153           
SHEET    3   K 3 THR B 205  VAL B 211 -1  O  VAL B 207   N  VAL B 198           
SHEET    1   L 3 ASN X1604  PHE X1607  0                                        
SHEET    2   L 3 SER X1675  ASP X1682 -1  O  GLU X1680   N  VAL X1606           
SHEET    3   L 3 ILE X1617  PRO X1619 -1  N  PHE X1618   O  ILE X1676           
SHEET    1   M 4 ASN X1604  PHE X1607  0                                        
SHEET    2   M 4 SER X1675  ASP X1682 -1  O  GLU X1680   N  VAL X1606           
SHEET    3   M 4 THR X1574  VAL X1579 -1  N  LEU X1575   O  LEU X1679           
SHEET    4   M 4 ILE X1719  GLU X1725 -1  O  ALA X1721   N  VAL X1578           
SHEET    1   N 4 MET L   4  SER L   7  0                                        
SHEET    2   N 4 VAL L  19  ALA L  25 -1  O  ARG L  24   N  THR L   5           
SHEET    3   N 4 ASP L  70  ILE L  75 -1  O  LEU L  73   N  ILE L  21           
SHEET    4   N 4 PHE L  62  SER L  65 -1  N  SER L  65   O  THR L  72           
SHEET    1   O 6 SER L  10  SER L  14  0                                        
SHEET    2   O 6 THR L 102  LYS L 107  1  O  LYS L 107   N  ALA L  13           
SHEET    3   O 6 ALA L  84  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4   O 6 VAL L  33  GLN L  38 -1  N  ALA L  34   O  GLN L  89           
SHEET    5   O 6 LYS L  45  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6   O 6 PHE L  53  LEU L  54 -1  O  PHE L  53   N  TYR L  49           
SHEET    1   P 4 SER L  10  SER L  14  0                                        
SHEET    2   P 4 THR L 102  LYS L 107  1  O  LYS L 107   N  ALA L  13           
SHEET    3   P 4 ALA L  84  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4   P 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1   Q 4 SER L 114  PHE L 118  0                                        
SHEET    2   Q 4 THR L 129  PHE L 139 -1  O  LEU L 135   N  PHE L 116           
SHEET    3   Q 4 TYR L 173  SER L 182 -1  O  TYR L 173   N  PHE L 139           
SHEET    4   Q 4 SER L 159  VAL L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1   R 4 ALA L 153  LEU L 154  0                                        
SHEET    2   R 4 LYS L 145  VAL L 150 -1  N  VAL L 150   O  ALA L 153           
SHEET    3   R 4 ALA L 193  THR L 197 -1  O  THR L 197   N  LYS L 145           
SHEET    4   R 4 VAL L 205  THR L 206 -1  O  VAL L 205   N  VAL L 196           
SHEET    1   S 4 GLN H   3  SER H   7  0                                        
SHEET    2   S 4 LEU H  18  SER H  25 -1  O  SER H  25   N  GLN H   3           
SHEET    3   S 4 THR H  77  MET H  82 -1  O  ALA H  78   N  CYS H  22           
SHEET    4   S 4 THR H  68  ASP H  72 -1  N  ASP H  72   O  THR H  77           
SHEET    1   T 6 GLY H  10  LEU H  11  0                                        
SHEET    2   T 6 THR H 107  THR H 110  1  O  THR H 110   N  GLY H  10           
SHEET    3   T 6 ALA H  88  ARG H  94 -1  N  TYR H  90   O  THR H 107           
SHEET    4   T 6 ILE H  34  GLN H  39 -1  N  VAL H  37   O  TYR H  91           
SHEET    5   T 6 LEU H  45  ILE H  51 -1  O  VAL H  48   N  TRP H  36           
SHEET    6   T 6 ASN H  57  TYR H  59 -1  O  GLN H  58   N  ARG H  50           
SHEET    1   U 4 GLY H  10  LEU H  11  0                                        
SHEET    2   U 4 THR H 107  THR H 110  1  O  THR H 110   N  GLY H  10           
SHEET    3   U 4 ALA H  88  ARG H  94 -1  N  TYR H  90   O  THR H 107           
SHEET    4   U 4 TYR H 102  TRP H 103 -1  O  TYR H 102   N  ARG H  94           
SHEET    1   V 4 SER H 120  LEU H 124  0                                        
SHEET    2   V 4 THR H 135  TYR H 145 -1  O  GLY H 139   N  LEU H 124           
SHEET    3   V 4 TYR H 176  PRO H 185 -1  O  VAL H 184   N  ALA H 136           
SHEET    4   V 4 VAL H 163  THR H 165 -1  N  HIS H 164   O  VAL H 181           
SHEET    1   W 4 SER H 120  LEU H 124  0                                        
SHEET    2   W 4 THR H 135  TYR H 145 -1  O  GLY H 139   N  LEU H 124           
SHEET    3   W 4 TYR H 176  PRO H 185 -1  O  VAL H 184   N  ALA H 136           
SHEET    4   W 4 VAL H 169  LEU H 170 -1  O  VAL H 169   N  SER H 177           
SHEET    1   X 3 THR H 151  TRP H 154  0                                        
SHEET    2   X 3 TYR H 194  HIS H 200 -1  O  ASN H 197   N  SER H 153           
SHEET    3   X 3 THR H 205  VAL H 211 -1  O  VAL H 207   N  VAL H 198           
SHEET    1   Y 3 ASN Y1604  PHE Y1607  0                                        
SHEET    2   Y 3 SER Y1675  ASP Y1682 -1  O  ASP Y1682   N  ASN Y1604           
SHEET    3   Y 3 ILE Y1617  PRO Y1619 -1  N  PHE Y1618   O  ILE Y1676           
SHEET    1   Z 4 ASN Y1604  PHE Y1607  0                                        
SHEET    2   Z 4 SER Y1675  ASP Y1682 -1  O  ASP Y1682   N  ASN Y1604           
SHEET    3   Z 4 THR Y1574  VAL Y1579 -1  N  VAL Y1577   O  VAL Y1677           
SHEET    4   Z 4 ILE Y1719  GLU Y1725 -1  O  GLN Y1723   N  VAL Y1576           
SSBOND   1 CYS A   23    CYS A   88                          1555   1555  2.06  
SSBOND   2 CYS A  134    CYS A  194                          1555   1555  2.03  
SSBOND   3 CYS B   22    CYS B   92                          1555   1555  2.06  
SSBOND   4 CYS B  140    CYS B  196                          1555   1555  2.05  
SSBOND   5 CYS X 1450    CYS X 1473                          1555   1555  2.07  
SSBOND   6 CYS X 1455    CYS X 1468                          1555   1555  2.06  
SSBOND   7 CYS X 1464    CYS X 1480                          1555   1555  2.06  
SSBOND   8 CYS X 1491    CYS X 1515                          1555   1555  2.05  
SSBOND   9 CYS X 1497    CYS X 1510                          1555   1555  2.04  
SSBOND  10 CYS X 1506    CYS X 1522                          1555   1555  2.06  
SSBOND  11 CYS X 1529    CYS X 1555                          1555   1555  2.05  
SSBOND  12 CYS X 1537    CYS X 1550                          1555   1555  2.04  
SSBOND  13 CYS X 1546    CYS X 1562                          1555   1555  2.04  
SSBOND  14 CYS X 1686    CYS X 1693                          1555   1555  2.04  
SSBOND  15 CYS L   23    CYS L   88                          1555   1555  2.05  
SSBOND  16 CYS L  134    CYS L  194                          1555   1555  2.03  
SSBOND  17 CYS H   22    CYS H   92                          1555   1555  2.05  
SSBOND  18 CYS H  140    CYS H  196                          1555   1555  2.02  
SSBOND  19 CYS Y 1464    CYS Y 1480                          1555   1555  2.03  
SSBOND  20 CYS Y 1491    CYS Y 1515                          1555   1555  2.06  
SSBOND  21 CYS Y 1497    CYS Y 1510                          1555   1555  2.05  
SSBOND  22 CYS Y 1506    CYS Y 1522                          1555   1555  2.05  
SSBOND  23 CYS Y 1529    CYS Y 1555                          1555   1555  2.05  
SSBOND  24 CYS Y 1537    CYS Y 1550                          1555   1555  2.06  
SSBOND  25 CYS Y 1546    CYS Y 1562                          1555   1555  2.04  
SSBOND  26 CYS Y 1686    CYS Y 1693                          1555   1555  2.04  
LINK         O4  NAG X2004                 C1  NAG X2005     1555   1555  1.44  
LINK         ND2 ASN X1490                 C1  NAG X2004     1555   1555  1.46  
LINK         O   VAL X1463                CA    CA X2001     1555   1555  2.15  
LINK         O   HIS X1545                CA    CA X2003     1555   1555  2.17  
LINK         OD2 ASP Y1507                CA    CA Y2002     1555   1555  2.25  
LINK         OD1 ASP Y1503                CA    CA Y2002     1555   1555  2.26  
LINK         O   HIS X1505                CA    CA X2002     1555   1555  2.29  
LINK         OD2 ASP X1547                CA    CA X2003     1555   1555  2.31  
LINK         OD2 ASP X1507                CA    CA X2002     1555   1555  2.31  
LINK         O   VAL Y1463                CA    CA Y2001     1555   1555  2.32  
LINK         O   TYR X1500                CA    CA X2002     1555   1555  2.32  
LINK         O   HIS Y1505                CA    CA Y2002     1555   1555  2.35  
LINK         OD2 ASP X1561                CA    CA X2003     1555   1555  2.35  
LINK         OD2 ASP X1521                CA    CA X2002     1555   1555  2.36  
LINK         O   HIS Y1545                CA    CA Y2003     1555   1555  2.39  
LINK         O   TYR Y1500                CA    CA Y2002     1555   1555  2.39  
LINK         O   HIS X1540                CA    CA X2003     1555   1555  2.39  
LINK         OD1 ASN X1461                CA    CA X2001     1555   1555  2.39  
LINK         OD1 ASP X1543                CA    CA X2003     1555   1555  2.40  
LINK         OD1 ASP Y1518                CA    CA Y2002     1555   1555  2.41  
LINK         O   HIS Y1540                CA    CA Y2003     1555   1555  2.42  
LINK         OG  SER Y1465                CA    CA Y2001     1555   1555  2.44  
LINK         OD2 ASP Y1547                CA    CA Y2003     1555   1555  2.45  
LINK         OD2 ASP Y1558                CA    CA Y2003     1555   1555  2.50  
LINK         OD1 ASP X1503                CA    CA X2002     1555   1555  2.50  
LINK         OD2 ASP Y1561                CA    CA Y2003     1555   1555  2.50  
LINK         OD1 ASP Y1543                CA    CA Y2003     1555   1555  2.51  
LINK         OD2 ASP Y1521                CA    CA Y2002     1555   1555  2.51  
LINK         OD2 ASP X1518                CA    CA X2002     1555   1555  2.54  
LINK         OD2 ASP X1476                CA    CA X2001     1555   1555  2.58  
LINK         OD2 ASP X1479                CA    CA X2001     1555   1555  2.59  
LINK         OD1 ASP X1518                CA    CA X2002     1555   1555  2.59  
LINK         OD1 ASP Y1558                CA    CA Y2003     1555   1555  2.61  
LINK         O   ASP X1458                CA    CA X2001     1555   1555  2.61  
LINK         OD2 ASP Y1518                CA    CA Y2002     1555   1555  2.66  
LINK         OD1 ASP X1558                CA    CA X2003     1555   1555  2.68  
LINK         OD2 ASP X1558                CA    CA X2003     1555   1555  2.76  
LINK         OD2 ASP Y1476                CA    CA Y2001     1555   1555  2.80  
CISPEP   1 SER A    7    PRO A    8          0        -3.10                     
CISPEP   2 TYR A  140    PRO A  141          0        -0.46                     
CISPEP   3 PHE B  146    PRO B  147          0        -9.98                     
CISPEP   4 GLU B  148    PRO B  149          0        -4.93                     
CISPEP   5 SER L    7    PRO L    8          0        -9.74                     
CISPEP   6 TYR L  140    PRO L  141          0         2.88                     
CISPEP   7 PHE H  146    PRO H  147          0        -0.45                     
CISPEP   8 GLU H  148    PRO H  149          0        -4.30                     
SITE     1 AC1  6 PHE B  27  THR B  28  TYR B  32  GLY X1447                    
SITE     2 AC1  6 SER X1448  VAL X1727                                          
SITE     1 AC2  5 ASP X1458  ASN X1461  VAL X1463  ASP X1476                    
SITE     2 AC2  5 ASP X1479                                                     
SITE     1 AC3  6 TYR X1500  ASP X1503  HIS X1505  ASP X1507                    
SITE     2 AC3  6 ASP X1518  ASP X1521                                          
SITE     1 AC4  6 HIS X1540  ASP X1543  HIS X1545  ASP X1547                    
SITE     2 AC4  6 ASP X1558  ASP X1561                                          
SITE     1 AC5  7 HOH X  79  LYS X1489  ASN X1490  SER X1696                    
SITE     2 AC5  7 THR X1698  ASP X1699  NAG X2005                               
SITE     1 AC6  1 NAG X2004                                                     
SITE     1 AC7  4 ASN Y1461  VAL Y1463  SER Y1465  ASP Y1476                    
SITE     1 AC8  6 TYR Y1500  ASP Y1503  HIS Y1505  ASP Y1507                    
SITE     2 AC8  6 ASP Y1518  ASP Y1521                                          
SITE     1 AC9  6 HIS Y1540  ASP Y1543  HIS Y1545  ASP Y1547                    
SITE     2 AC9  6 ASP Y1558  ASP Y1561                                          
CRYST1   46.254  163.934  179.620  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      0.021620  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006100  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005567        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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