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Database: PDB
Entry: 1TEL
LinkDB: 1TEL
Original site: 1TEL 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   25-MAY-04   1TEL              
TITLE     CRYSTAL STRUCTURE OF A RUBISCO-LIKE PROTEIN FROM CHLOROBIUM           
TITLE    2 TEPIDUM                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE, LARGE SUBUNIT;          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHLOROBIUM TEPIDUM TLS;                         
SOURCE   3 ORGANISM_TAXID: 194439;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    STRUCTURAL GENOMICS, RUBISCO-LIKE PROTEIN, UNKNOWN FUNCTION,          
KEYWDS   2 NYSGXRC, TARGET 1798, PSI, PROTEIN STRUCTURE INITIATIVE,             
KEYWDS   3 NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.FEDOROV,E.V.FEDOROV,H.J.IMKER,J.A.GERLT,S.C.ALMO,                 
AUTHOR   2 S.K.BURLEY,NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL               
AUTHOR   3 GENOMICS (NYSGXRC)                                                   
REVDAT   3   24-FEB-09 1TEL    1       VERSN                                    
REVDAT   2   25-JAN-05 1TEL    1       AUTHOR KEYWDS REMARK                     
REVDAT   1   05-OCT-04 1TEL    0                                                
JRNL        AUTH   A.A.FEDOROV,E.V.FEDOROV,H.J.IMKER,J.A.GERLT,                 
JRNL        AUTH 2 S.C.ALMO                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF A RUBISCO-LIKE PROTEIN FROM             
JRNL        TITL 2 CHLOROBIUM TEPIDUM                                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 24718                          
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 SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1198                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6604                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 47                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.52                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.89                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.85                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : CIS_PEPTIDE.PARAM                              
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1TEL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022588.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 110.0                              
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X9A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97938, 0.97919, 0.96408          
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24718                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, TRIS HCL, MAGNESIUM            
REMARK 280  CHLORIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE        
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       38.85400            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER                           
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A  1085                                                      
REMARK 465     SER A  1086                                                      
REMARK 465     GLU A  1087                                                      
REMARK 465     THR A  1088                                                      
REMARK 465     SER A  1429                                                      
REMARK 465     LEU A  1430                                                      
REMARK 465     LEU A  1431                                                      
REMARK 465     LYS A  1432                                                      
REMARK 465     LYS A  1433                                                      
REMARK 465     GLN A  1434                                                      
REMARK 465     ASP A  1435                                                      
REMARK 465     SER B  2429                                                      
REMARK 465     LEU B  2430                                                      
REMARK 465     LEU B  2431                                                      
REMARK 465     LYS B  2432                                                      
REMARK 465     LYS B  2433                                                      
REMARK 465     GLN B  2434                                                      
REMARK 465     ASP B  2435                                                      
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    ALA A1003      -54.00    -25.62                                   
REMARK 500    LYS A1007      -39.64    -35.76                                   
REMARK 500    MET A1018       -8.33    -54.33                                   
REMARK 500    SER A1046     -111.29   -143.05                                   
REMARK 500    ASP A1069      148.90    174.06                                   
REMARK 500    PRO A1082       78.64    -63.21                                   
REMARK 500    PRO A1107       47.76    -79.06                                   
REMARK 500    CYS A1117       52.00   -161.07                                   
REMARK 500    ASN A1174      -85.43    -95.90                                   
REMARK 500    ILE A1175     -105.03    -32.40                                   
REMARK 500    LEU A1203      -85.48    -77.85                                   
REMARK 500    ALA A1204     -166.23     59.45                                   
REMARK 500    SER A1209       95.98   -163.97                                   
REMARK 500    ASP A1244      -19.40    -47.75                                   
REMARK 500    PHE A1290      -33.58     81.18                                   
REMARK 500    PHE A1324       10.05    -64.49                                   
REMARK 500    ASP A1326       -2.58    163.56                                   
REMARK 500    MET A1329       43.22     39.97                                   
REMARK 500    ARG A1348      -14.28     76.64                                   
REMARK 500    SER A1359       43.31   -152.79                                   
REMARK 500    VAL A1380       77.91   -119.69                                   
REMARK 500    VAL A1385      -76.29   -108.24                                   
REMARK 500    ALA B2003      -53.71    -26.47                                   
REMARK 500    LYS B2007      -39.62    -36.05                                   
REMARK 500    MET B2018       -8.70    -54.02                                   
REMARK 500    SER B2046     -109.40   -141.18                                   
REMARK 500    ASP B2069      149.84    174.17                                   
REMARK 500    PRO B2082       77.61    -63.91                                   
REMARK 500    GLU B2087      152.02    -41.62                                   
REMARK 500    PRO B2107       47.52    -78.04                                   
REMARK 500    CYS B2117       51.59   -160.64                                   
REMARK 500    ASN B2174      -85.02    -95.28                                   
REMARK 500    ILE B2175     -104.92    -33.09                                   
REMARK 500    LEU B2203      -84.58    -78.24                                   
REMARK 500    ALA B2204     -165.41     58.76                                   
REMARK 500    SER B2209       96.11   -164.30                                   
REMARK 500    ASP B2244      -19.55    -48.23                                   
REMARK 500    PHE B2290      -34.78     80.86                                   
REMARK 500    PHE B2324        9.11    -64.81                                   
REMARK 500    ASP B2326       -2.40    164.18                                   
REMARK 500    ARG B2348      -15.78     77.03                                   
REMARK 500    SER B2359       43.71   -152.07                                   
REMARK 500    VAL B2385      -75.36   -107.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-T1798   RELATED DB: TARGETDB                     
DBREF  1TEL A 1001  1435  UNP    Q8KBL4   Q8KBL4_CHLTE     1    435             
DBREF  1TEL B 2001  2435  UNP    Q8KBL4   Q8KBL4_CHLTE     1    435             
SEQRES   1 A  435  MET ASN ALA GLU ASP VAL LYS GLY PHE PHE ALA SER ARG          
SEQRES   2 A  435  GLU SER LEU ASP MET GLU GLN TYR LEU VAL LEU ASP TYR          
SEQRES   3 A  435  TYR LEU GLU SER VAL GLY ASP ILE GLU THR ALA LEU ALA          
SEQRES   4 A  435  HIS PHE CYS SER GLU GLN SER THR ALA GLN TRP LYS ARG          
SEQRES   5 A  435  VAL GLY VAL ASP GLU ASP PHE ARG LEU VAL HIS ALA ALA          
SEQRES   6 A  435  LYS VAL ILE ASP TYR GLU VAL ILE GLU GLU LEU GLU GLN          
SEQRES   7 A  435  LEU SER TYR PRO VAL LYS HIS SER GLU THR GLY LYS ILE          
SEQRES   8 A  435  HIS ALA CYS ARG VAL THR ILE ALA HIS PRO HIS CYS ASN          
SEQRES   9 A  435  PHE GLY PRO LYS ILE PRO ASN LEU LEU THR ALA VAL CYS          
SEQRES  10 A  435  GLY GLU GLY THR TYR PHE THR PRO GLY VAL PRO VAL VAL          
SEQRES  11 A  435  LYS LEU MET ASP ILE HIS PHE PRO ASP THR TYR LEU ALA          
SEQRES  12 A  435  ASP PHE GLU GLY PRO LYS PHE GLY ILE GLU GLY LEU ARG          
SEQRES  13 A  435  ASP ILE LEU ASN ALA HIS GLY ARG PRO ILE PHE PHE GLY          
SEQRES  14 A  435  VAL VAL LYS PRO ASN ILE GLY LEU SER PRO GLY GLU PHE          
SEQRES  15 A  435  ALA GLU ILE ALA TYR GLN SER TRP LEU GLY GLY LEU ASP          
SEQRES  16 A  435  ILE ALA LYS ASP ASP GLU MET LEU ALA ASP VAL THR TRP          
SEQRES  17 A  435  SER SER ILE GLU GLU ARG ALA ALA HIS LEU GLY LYS ALA          
SEQRES  18 A  435  ARG ARG LYS ALA GLU ALA GLU THR GLY GLU PRO LYS ILE          
SEQRES  19 A  435  TYR LEU ALA ASN ILE THR ASP GLU VAL ASP SER LEU MET          
SEQRES  20 A  435  GLU LYS HIS ASP VAL ALA VAL ARG ASN GLY ALA ASN ALA          
SEQRES  21 A  435  LEU LEU ILE ASN ALA LEU PRO VAL GLY LEU SER ALA VAL          
SEQRES  22 A  435  ARG MET LEU SER ASN TYR THR GLN VAL PRO LEU ILE GLY          
SEQRES  23 A  435  HIS PHE PRO PHE ILE ALA SER PHE SER ARG MET GLU LYS          
SEQRES  24 A  435  TYR GLY ILE HIS SER LYS VAL MET THR LYS LEU GLN ARG          
SEQRES  25 A  435  LEU ALA GLY LEU ASP ALA VAL ILE MET PRO GLY PHE GLY          
SEQRES  26 A  435  ASP ARG MET MET THR PRO GLU GLU GLU VAL LEU GLU ASN          
SEQRES  27 A  435  VAL ILE GLU CYS THR LYS PRO MET GLY ARG ILE LYS PRO          
SEQRES  28 A  435  CYS LEU PRO VAL PRO GLY GLY SER ASP SER ALA LEU THR          
SEQRES  29 A  435  LEU GLN THR VAL TYR GLU LYS VAL GLY ASN VAL ASP PHE          
SEQRES  30 A  435  GLY PHE VAL PRO GLY ARG GLY VAL PHE GLY HIS PRO MET          
SEQRES  31 A  435  GLY PRO LYS ALA GLY ALA LYS SER ILE ARG GLN ALA TRP          
SEQRES  32 A  435  GLU ALA ILE GLU GLN GLY ILE SER ILE GLU THR TRP ALA          
SEQRES  33 A  435  GLU THR HIS PRO GLU LEU GLN ALA MET VAL ASP GLN SER          
SEQRES  34 A  435  LEU LEU LYS LYS GLN ASP                                      
SEQRES   1 B  435  MET ASN ALA GLU ASP VAL LYS GLY PHE PHE ALA SER ARG          
SEQRES   2 B  435  GLU SER LEU ASP MET GLU GLN TYR LEU VAL LEU ASP TYR          
SEQRES   3 B  435  TYR LEU GLU SER VAL GLY ASP ILE GLU THR ALA LEU ALA          
SEQRES   4 B  435  HIS PHE CYS SER GLU GLN SER THR ALA GLN TRP LYS ARG          
SEQRES   5 B  435  VAL GLY VAL ASP GLU ASP PHE ARG LEU VAL HIS ALA ALA          
SEQRES   6 B  435  LYS VAL ILE ASP TYR GLU VAL ILE GLU GLU LEU GLU GLN          
SEQRES   7 B  435  LEU SER TYR PRO VAL LYS HIS SER GLU THR GLY LYS ILE          
SEQRES   8 B  435  HIS ALA CYS ARG VAL THR ILE ALA HIS PRO HIS CYS ASN          
SEQRES   9 B  435  PHE GLY PRO LYS ILE PRO ASN LEU LEU THR ALA VAL CYS          
SEQRES  10 B  435  GLY GLU GLY THR TYR PHE THR PRO GLY VAL PRO VAL VAL          
SEQRES  11 B  435  LYS LEU MET ASP ILE HIS PHE PRO ASP THR TYR LEU ALA          
SEQRES  12 B  435  ASP PHE GLU GLY PRO LYS PHE GLY ILE GLU GLY LEU ARG          
SEQRES  13 B  435  ASP ILE LEU ASN ALA HIS GLY ARG PRO ILE PHE PHE GLY          
SEQRES  14 B  435  VAL VAL LYS PRO ASN ILE GLY LEU SER PRO GLY GLU PHE          
SEQRES  15 B  435  ALA GLU ILE ALA TYR GLN SER TRP LEU GLY GLY LEU ASP          
SEQRES  16 B  435  ILE ALA LYS ASP ASP GLU MET LEU ALA ASP VAL THR TRP          
SEQRES  17 B  435  SER SER ILE GLU GLU ARG ALA ALA HIS LEU GLY LYS ALA          
SEQRES  18 B  435  ARG ARG LYS ALA GLU ALA GLU THR GLY GLU PRO LYS ILE          
SEQRES  19 B  435  TYR LEU ALA ASN ILE THR ASP GLU VAL ASP SER LEU MET          
SEQRES  20 B  435  GLU LYS HIS ASP VAL ALA VAL ARG ASN GLY ALA ASN ALA          
SEQRES  21 B  435  LEU LEU ILE ASN ALA LEU PRO VAL GLY LEU SER ALA VAL          
SEQRES  22 B  435  ARG MET LEU SER ASN TYR THR GLN VAL PRO LEU ILE GLY          
SEQRES  23 B  435  HIS PHE PRO PHE ILE ALA SER PHE SER ARG MET GLU LYS          
SEQRES  24 B  435  TYR GLY ILE HIS SER LYS VAL MET THR LYS LEU GLN ARG          
SEQRES  25 B  435  LEU ALA GLY LEU ASP ALA VAL ILE MET PRO GLY PHE GLY          
SEQRES  26 B  435  ASP ARG MET MET THR PRO GLU GLU GLU VAL LEU GLU ASN          
SEQRES  27 B  435  VAL ILE GLU CYS THR LYS PRO MET GLY ARG ILE LYS PRO          
SEQRES  28 B  435  CYS LEU PRO VAL PRO GLY GLY SER ASP SER ALA LEU THR          
SEQRES  29 B  435  LEU GLN THR VAL TYR GLU LYS VAL GLY ASN VAL ASP PHE          
SEQRES  30 B  435  GLY PHE VAL PRO GLY ARG GLY VAL PHE GLY HIS PRO MET          
SEQRES  31 B  435  GLY PRO LYS ALA GLY ALA LYS SER ILE ARG GLN ALA TRP          
SEQRES  32 B  435  GLU ALA ILE GLU GLN GLY ILE SER ILE GLU THR TRP ALA          
SEQRES  33 B  435  GLU THR HIS PRO GLU LEU GLN ALA MET VAL ASP GLN SER          
SEQRES  34 B  435  LEU LEU LYS LYS GLN ASP                                      
FORMUL   3  HOH   *47(H2 O)                                                     
HELIX    1   1 ASN A 1002  LYS A 1007  1                                   6    
HELIX    2   2 GLY A 1008  PHE A 1010  5                                   3    
HELIX    3   3 SER A 1012  LEU A 1016  5                                   5    
HELIX    4   4 ASP A 1017  GLU A 1019  5                                   3    
HELIX    5   5 ASP A 1033  SER A 1046  1                                  14    
HELIX    6   6 PHE A 1059  ALA A 1064  1                                   6    
HELIX    7   7 CYS A 1103  PHE A 1105  5                                   3    
HELIX    8   8 LYS A 1108  CYS A 1117  1                                  10    
HELIX    9   9 GLY A 1118  THR A 1124  1                                   7    
HELIX   10  10 PRO A 1138  ALA A 1143  1                                   6    
HELIX   11  11 PHE A 1150  ASN A 1160  1                                  11    
HELIX   12  12 SER A 1178  GLY A 1193  1                                  16    
HELIX   13  13 SER A 1210  GLY A 1230  1                                  21    
HELIX   14  14 GLU A 1242  ASP A 1244  5                                   3    
HELIX   15  15 SER A 1245  GLY A 1257  1                                  13    
HELIX   16  16 ALA A 1265  GLY A 1269  1                                   5    
HELIX   17  17 GLY A 1269  ASN A 1278  1                                  10    
HELIX   18  18 ILE A 1291  ARG A 1296  1                                   6    
HELIX   19  19 HIS A 1303  GLY A 1315  1                                  13    
HELIX   20  20 PRO A 1331  LYS A 1344  1                                  14    
HELIX   21  21 THR A 1364  GLY A 1373  1                                  10    
HELIX   22  22 GLY A 1391  GLN A 1408  1                                  18    
HELIX   23  23 SER A 1411  GLU A 1417  1                                   7    
HELIX   24  24 HIS A 1419  GLN A 1428  1                                  10    
HELIX   25  25 ASN B 2002  LYS B 2007  1                                   6    
HELIX   26  26 GLY B 2008  PHE B 2010  5                                   3    
HELIX   27  27 SER B 2012  LEU B 2016  5                                   5    
HELIX   28  28 ASP B 2017  GLU B 2019  5                                   3    
HELIX   29  29 ASP B 2033  SER B 2046  1                                  14    
HELIX   30  30 PHE B 2059  ALA B 2064  1                                   6    
HELIX   31  31 CYS B 2103  PHE B 2105  5                                   3    
HELIX   32  32 LYS B 2108  CYS B 2117  1                                  10    
HELIX   33  33 GLY B 2118  THR B 2124  1                                   7    
HELIX   34  34 PRO B 2138  ALA B 2143  1                                   6    
HELIX   35  35 PHE B 2150  ASN B 2160  1                                  11    
HELIX   36  36 SER B 2178  GLY B 2193  1                                  16    
HELIX   37  37 SER B 2210  GLY B 2230  1                                  21    
HELIX   38  38 GLU B 2242  ASP B 2244  5                                   3    
HELIX   39  39 SER B 2245  GLY B 2257  1                                  13    
HELIX   40  40 ALA B 2265  GLY B 2269  1                                   5    
HELIX   41  41 GLY B 2269  ASN B 2278  1                                  10    
HELIX   42  42 ILE B 2291  ARG B 2296  1                                   6    
HELIX   43  43 HIS B 2303  GLY B 2315  1                                  13    
HELIX   44  44 PRO B 2331  LYS B 2344  1                                  14    
HELIX   45  45 THR B 2364  GLY B 2373  1                                  10    
HELIX   46  46 GLY B 2391  GLN B 2408  1                                  18    
HELIX   47  47 SER B 2411  GLU B 2417  1                                   7    
HELIX   48  48 HIS B 2419  GLN B 2428  1                                  10    
SHEET    1   A 5 LYS A1066  LEU A1076  0                                        
SHEET    2   A 5 ILE A1091  PRO A1101 -1  O  THR A1097   N  ASP A1069           
SHEET    3   A 5 TYR A1021  VAL A1031 -1  N  LEU A1028   O  CYS A1094           
SHEET    4   A 5 VAL A1129  HIS A1136 -1  O  MET A1133   N  ASP A1025           
SHEET    5   A 5 GLY A1301  ILE A1302  1  O  GLY A1301   N  VAL A1130           
SHEET    1   B 8 LEU A1353  GLY A1357  0                                        
SHEET    2   B 8 ALA A1318  PRO A1322  1  N  VAL A1319   O  VAL A1355           
SHEET    3   B 8 LEU A1284  HIS A1287  1  N  GLY A1286   O  ILE A1320           
SHEET    4   B 8 ALA A1260  ASN A1264  1  N  LEU A1261   O  ILE A1285           
SHEET    5   B 8 ILE A1234  ASN A1238  1  N  ALA A1237   O  LEU A1262           
SHEET    6   B 8 ILE A1196  LYS A1198  1  N  ALA A1197   O  LEU A1236           
SHEET    7   B 8 ILE A1166  VAL A1170  1  N  PHE A1167   O  ILE A1196           
SHEET    8   B 8 GLY A1378  PHE A1379  1  O  PHE A1379   N  ILE A1166           
SHEET    1   C 5 LYS B2066  LEU B2076  0                                        
SHEET    2   C 5 ILE B2091  PRO B2101 -1  O  THR B2097   N  ASP B2069           
SHEET    3   C 5 TYR B2021  VAL B2031 -1  N  LEU B2028   O  CYS B2094           
SHEET    4   C 5 VAL B2129  HIS B2136 -1  O  MET B2133   N  ASP B2025           
SHEET    5   C 5 GLY B2301  ILE B2302  1  O  GLY B2301   N  VAL B2130           
SHEET    1   D 8 LEU B2353  GLY B2357  0                                        
SHEET    2   D 8 ALA B2318  PRO B2322  1  N  VAL B2319   O  VAL B2355           
SHEET    3   D 8 LEU B2284  HIS B2287  1  N  GLY B2286   O  ILE B2320           
SHEET    4   D 8 ALA B2260  ASN B2264  1  N  LEU B2261   O  ILE B2285           
SHEET    5   D 8 ILE B2234  ASN B2238  1  N  ALA B2237   O  LEU B2262           
SHEET    6   D 8 ILE B2196  LYS B2198  1  N  ALA B2197   O  LEU B2236           
SHEET    7   D 8 ILE B2166  VAL B2170  1  N  PHE B2167   O  ILE B2196           
SHEET    8   D 8 GLY B2378  PHE B2379  1  O  PHE B2379   N  ILE B2166           
CISPEP   1 LYS A 1172    PRO A 1173          0        -0.48                     
CISPEP   2 LYS B 2172    PRO B 2173          0        -0.65                     
CRYST1   67.105   77.708   88.758  90.00  99.57  90.00 P 1 21 1      4          
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      0.014902  0.000000  0.002512        0.00000                         
SCALE2      0.000000  0.012869  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011426        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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