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Database: PDB
Entry: 2OAY
LinkDB: 2OAY
Original site: 2OAY 
HEADER    IMMUNE SYSTEM,HYDROLASE INHIBITOR       18-DEC-06   2OAY              
TITLE     CRYSTAL STRUCTURE OF LATENT HUMAN C1-INHIBITOR                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLASMA PROTEASE C1 INHIBITOR;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SERPIN DOMAIN;                                             
COMPND   5 SYNONYM: C1-INHIBITOR; C1 INH; C1INH; C1 ESTERASE INHIBITOR; C1-     
COMPND   6 INHIBITING FACTOR;                                                   
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SERPING1, C1IN, C1NH;                                          
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: GS115;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPIC9K                                    
KEYWDS    LATENT SERPIN; RCL INSERTION, IMMUNE SYSTEM, HYDROLASE INHIBITOR      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.HARMAT,L.BEINROHR,P.GAL,J.DOBO                                      
REVDAT   6   29-JUL-20 2OAY    1       COMPND REMARK SEQADV HETNAM              
REVDAT   6 2                   1       LINK   SITE                              
REVDAT   5   18-OCT-17 2OAY    1       REMARK                                   
REVDAT   4   13-JUL-11 2OAY    1       VERSN                                    
REVDAT   3   24-FEB-09 2OAY    1       VERSN                                    
REVDAT   2   07-AUG-07 2OAY    1       JRNL                                     
REVDAT   1   01-MAY-07 2OAY    0                                                
JRNL        AUTH   L.BEINROHR,V.HARMAT,J.DOBO,Z.LORINCZ,P.GAL,P.ZAVODSZKY       
JRNL        TITL   C1 INHIBITOR SERPIN DOMAIN STRUCTURE REVEALS THE LIKELY      
JRNL        TITL 2 MECHANISM OF HEPARIN POTENTIATION AND CONFORMATIONAL DISEASE 
JRNL        REF    J.BIOL.CHEM.                  V. 282 21100 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17488724                                                     
JRNL        DOI    10.1074/JBC.M700841200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 84.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20803                          
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1125                            
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) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1546                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 78                           
REMARK   3   BIN FREE R VALUE                    : 0.3200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2845                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 70                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 32.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.29000                                              
REMARK   3    B22 (A**2) : 0.29000                                              
REMARK   3    B33 (A**2) : -0.43000                                             
REMARK   3    B12 (A**2) : 0.14000                                              
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): 0.239         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.197         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.154         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.574         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2952 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2693 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4015 ; 1.764 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6265 ; 0.804 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   370 ; 7.479 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   481 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3204 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   558 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   599 ; 0.216 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3056 ; 0.256 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1927 ; 0.100 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   148 ; 0.187 ; 0.500       
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):    13 ; 0.273 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    45 ; 0.390 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.186 ; 0.500       
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):  1852 ; 2.070 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3006 ; 3.238 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1100 ; 2.123 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1006 ; 3.367 ; 3.000       
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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   101        A   476                          
REMARK   3    RESIDUE RANGE :   A   500        A   500                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.7946  71.6738  -0.6784              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1060 T22:   0.0380                                     
REMARK   3      T33:   0.1121 T12:   0.0229                                     
REMARK   3      T13:  -0.0025 T23:   0.0519                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5314 L22:   2.5613                                     
REMARK   3      L33:   2.8210 L12:   0.1233                                     
REMARK   3      L13:   0.1272 L23:   1.5387                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0220 S12:  -0.0272 S13:   0.0470                       
REMARK   3      S21:  -0.0132 S22:  -0.0308 S23:  -0.0146                       
REMARK   3      S31:  -0.1414 S32:  -0.2032 S33:   0.0528                       
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   : 1.40                                          
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 2OAY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000040907.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAY-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8162                             
REMARK 200  MONOCHROMATOR                  : SI [111]                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21930                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 84.520                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 14.60                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.2900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.54                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.890                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: ENSEMBLE OF TRUNCATED SERPIN STRUCTURES. PDB         
REMARK 200  CODES: 4CAA, 1QMB, 1E05, 1DVM, 1C8O, 1JTI, 1JJO, 1MTP, 1HLE, 1JRR   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.85 M NAH2PO4, 0.85 M KH2PO4, 0.1 M     
REMARK 280  HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.12267            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.56133            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       47.34200            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       15.78067            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       78.90333            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     TYR A    89                                                      
REMARK 465     VAL A    90                                                      
REMARK 465     HIS A    91                                                      
REMARK 465     HIS A    92                                                      
REMARK 465     HIS A    93                                                      
REMARK 465     HIS A    94                                                      
REMARK 465     HIS A    95                                                      
REMARK 465     HIS A    96                                                      
REMARK 465     THR A    97                                                      
REMARK 465     GLY A    98                                                      
REMARK 465     SER A    99                                                      
REMARK 465     PHE A   100                                                      
REMARK 465     GLY A   103                                                      
REMARK 465     PRO A   104                                                      
REMARK 465     MET A   138                                                      
REMARK 465     LYS A   139                                                      
REMARK 465     LYS A   140                                                      
REMARK 465     VAL A   141                                                      
REMARK 465     LYS A   294                                                      
REMARK 465     ASN A   295                                                      
REMARK 465     ARG A   477                                                      
REMARK 465     ALA A   478                                                      
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     THR A 106    CB   OG1  CG2                                       
REMARK 470     LEU A 107    CG   CD1  CD2                                       
REMARK 470     GLU A 165    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 168    CE   NZ                                             
REMARK 470     LYS A 179    CG   CD   CE   NZ                                   
REMARK 470     GLU A 238    CG   CD   OE1  OE2                                  
REMARK 470     SER A 261    OG                                                  
REMARK 470     LYS A 276    NZ                                                  
REMARK 470     LYS A 278    CD   CE   NZ                                        
REMARK 470     LYS A 285    CE   NZ                                             
REMARK 470     ARG A 287    CD   NE   CZ   NH1  NH2                             
REMARK 470     SER A 296    CB   OG                                             
REMARK 470     LYS A 306    CE   NZ                                             
REMARK 470     LYS A 307    CD   CE   NZ                                        
REMARK 470     GLN A 316    CD   OE1  NE2                                       
REMARK 470     LYS A 319    CE   NZ                                             
REMARK 470     LYS A 342    CG   CD   CE   NZ                                   
REMARK 470     LYS A 368    CG   CD   CE   NZ                                   
REMARK 470     ASP A 413    CG   OD1  OD2                                       
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    THR A   193     O    HOH A    18              2.12            
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    VAL A 184   CB  -  CA  -  C   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    ASP A 212   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP A 234   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    LEU A 456   CA  -  CB  -  CG  ANGL. DEV. =  16.9 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    THR A 106       79.90     65.40                                   
REMARK 500    PHE A 396      -82.89    -87.06                                   
REMARK 500    LEU A 405       43.66   -108.59                                   
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 ASP A  180     PHE A  181                 -147.98                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2OAY A   97   478  UNP    P05155   IC1_HUMAN      119    500             
SEQADV 2OAY TYR A   89  UNP  P05155              EXPRESSION TAG                 
SEQADV 2OAY VAL A   90  UNP  P05155              EXPRESSION TAG                 
SEQADV 2OAY HIS A   91  UNP  P05155              EXPRESSION TAG                 
SEQADV 2OAY HIS A   92  UNP  P05155              EXPRESSION TAG                 
SEQADV 2OAY HIS A   93  UNP  P05155              EXPRESSION TAG                 
SEQADV 2OAY HIS A   94  UNP  P05155              EXPRESSION TAG                 
SEQADV 2OAY HIS A   95  UNP  P05155              EXPRESSION TAG                 
SEQADV 2OAY HIS A   96  UNP  P05155              EXPRESSION TAG                 
SEQADV 2OAY MET A  458  UNP  P05155    VAL   480 VARIANT                        
SEQRES   1 A  390  TYR VAL HIS HIS HIS HIS HIS HIS THR GLY SER PHE CYS          
SEQRES   2 A  390  PRO GLY PRO VAL THR LEU CYS SER ASP LEU GLU SER HIS          
SEQRES   3 A  390  SER THR GLU ALA VAL LEU GLY ASP ALA LEU VAL ASP PHE          
SEQRES   4 A  390  SER LEU LYS LEU TYR HIS ALA PHE SER ALA MET LYS LYS          
SEQRES   5 A  390  VAL GLU THR ASN MET ALA PHE SER PRO PHE SER ILE ALA          
SEQRES   6 A  390  SER LEU LEU THR GLN VAL LEU LEU GLY ALA GLY GLU ASN          
SEQRES   7 A  390  THR LYS THR ASN LEU GLU SER ILE LEU SER TYR PRO LYS          
SEQRES   8 A  390  ASP PHE THR CYS VAL HIS GLN ALA LEU LYS GLY PHE THR          
SEQRES   9 A  390  THR LYS GLY VAL THR SER VAL SER GLN ILE PHE HIS SER          
SEQRES  10 A  390  PRO ASP LEU ALA ILE ARG ASP THR PHE VAL ASN ALA SER          
SEQRES  11 A  390  ARG THR LEU TYR SER SER SER PRO ARG VAL LEU SER ASN          
SEQRES  12 A  390  ASN SER ASP ALA ASN LEU GLU LEU ILE ASN THR TRP VAL          
SEQRES  13 A  390  ALA LYS ASN THR ASN ASN LYS ILE SER ARG LEU LEU ASP          
SEQRES  14 A  390  SER LEU PRO SER ASP THR ARG LEU VAL LEU LEU ASN ALA          
SEQRES  15 A  390  ILE TYR LEU SER ALA LYS TRP LYS THR THR PHE ASP PRO          
SEQRES  16 A  390  LYS LYS THR ARG MET GLU PRO PHE HIS PHE LYS ASN SER          
SEQRES  17 A  390  VAL ILE LYS VAL PRO MET MET ASN SER LYS LYS TYR PRO          
SEQRES  18 A  390  VAL ALA HIS PHE ILE ASP GLN THR LEU LYS ALA LYS VAL          
SEQRES  19 A  390  GLY GLN LEU GLN LEU SER HIS ASN LEU SER LEU VAL ILE          
SEQRES  20 A  390  LEU VAL PRO GLN ASN LEU LYS HIS ARG LEU GLU ASP MET          
SEQRES  21 A  390  GLU GLN ALA LEU SER PRO SER VAL PHE LYS ALA ILE MET          
SEQRES  22 A  390  GLU LYS LEU GLU MET SER LYS PHE GLN PRO THR LEU LEU          
SEQRES  23 A  390  THR LEU PRO ARG ILE LYS VAL THR THR SER GLN ASP MET          
SEQRES  24 A  390  LEU SER ILE MET GLU LYS LEU GLU PHE PHE ASP PHE SER          
SEQRES  25 A  390  TYR ASP LEU ASN LEU CYS GLY LEU THR GLU ASP PRO ASP          
SEQRES  26 A  390  LEU GLN VAL SER ALA MET GLN HIS GLN THR VAL LEU GLU          
SEQRES  27 A  390  LEU THR GLU THR GLY VAL GLU ALA ALA ALA ALA SER ALA          
SEQRES  28 A  390  ILE SER VAL ALA ARG THR LEU LEU VAL PHE GLU VAL GLN          
SEQRES  29 A  390  GLN PRO PHE LEU PHE MET LEU TRP ASP GLN GLN HIS LYS          
SEQRES  30 A  390  PHE PRO VAL PHE MET GLY ARG VAL TYR ASP PRO ARG ALA          
MODRES 2OAY ASN A  216  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 500      14                                                       
HET    GOL  A5001       6                                                       
HET    GOL  A5002       6                                                       
HET    GOL  A5003       6                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   3  GOL    3(C3 H8 O3)                                                  
FORMUL   6  HOH   *70(H2 O)                                                     
HELIX    1   1 GLU A  112  SER A  136  1                                  25    
HELIX    2   2 SER A  148  GLY A  162  1                                  15    
HELIX    3   3 GLY A  164  SER A  176  1                                  13    
HELIX    4   4 CYS A  183  GLY A  190  1                                   8    
HELIX    5   5 ARG A  211  SER A  223  1                                  13    
HELIX    6   6 ASN A  232  ASN A  247  1                                  16    
HELIX    7   7 ARG A  344  LEU A  352  1                                   9    
HELIX    8   8 SER A  353  MET A  366  1                                  14    
HELIX    9   9 MET A  387  GLU A  392  1                                   6    
HELIX   10  10 LYS A  393  GLU A  395  5                                   3    
HELIX   11  11 ASP A  398  LEU A  403  5                                   6    
SHEET    1   A 7 MET A 145  PHE A 147  0                                        
SHEET    2   A 7 PHE A 466  VAL A 473 -1  O  MET A 470   N  PHE A 147           
SHEET    3   A 7 PHE A 455  ASP A 461 -1  N  PHE A 455   O  VAL A 473           
SHEET    4   A 7 LEU A 331  PRO A 338 -1  N  SER A 332   O  TRP A 460           
SHEET    5   A 7 ALA A 320  GLN A 326 -1  N  LYS A 321   O  VAL A 337           
SHEET    6   A 7 ILE A 298  ASP A 315 -1  N  PHE A 313   O  VAL A 322           
SHEET    7   A 7 ARG A 287  PHE A 291 -1  N  GLU A 289   O  VAL A 300           
SHEET    1   B 7 MET A 145  PHE A 147  0                                        
SHEET    2   B 7 PHE A 466  VAL A 473 -1  O  MET A 470   N  PHE A 147           
SHEET    3   B 7 PHE A 455  ASP A 461 -1  N  PHE A 455   O  VAL A 473           
SHEET    4   B 7 LEU A 331  PRO A 338 -1  N  SER A 332   O  TRP A 460           
SHEET    5   B 7 ALA A 320  GLN A 326 -1  N  LYS A 321   O  VAL A 337           
SHEET    6   B 7 ILE A 298  ASP A 315 -1  N  PHE A 313   O  VAL A 322           
SHEET    7   B 7 PHE A 369  PRO A 377 -1  O  LEU A 374   N  SER A 305           
SHEET    1   C 7 ARG A 227  VAL A 228  0                                        
SHEET    2   C 7 VAL A 196  HIS A 204  1  N  ILE A 202   O  ARG A 227           
SHEET    3   C 7 LEU A 265  LYS A 276 -1  O  TYR A 272   N  THR A 197           
SHEET    4   C 7 GLY A 431  ILE A 440 -1  O  ALA A 436   N  ILE A 271           
SHEET    5   C 7 MET A 419  LEU A 427 -1  N  VAL A 424   O  ALA A 435           
SHEET    6   C 7 LYS A 380  ASP A 386 -1  N  VAL A 381   O  LEU A 425           
SHEET    7   C 7 LEU A 446  VAL A 448 -1  O  VAL A 448   N  THR A 382           
SSBOND   1 CYS A  101    CYS A  406                          1555   1555  2.02  
SSBOND   2 CYS A  108    CYS A  183                          1555   1555  2.05  
LINK         ND2 ASN A 216                 C1  NAG A 500     1555   1555  1.46  
CRYST1   98.903   98.903   94.684  90.00  90.00 120.00 P 65          6          
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      0.010111  0.005838  0.000000        0.00000                         
SCALE2      0.000000  0.011675  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010561        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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