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Database: PDB
Entry: 5CSA
LinkDB: 5CSA
Original site: 5CSA 
HEADER    LIGASE                                  23-JUL-15   5CSA              
TITLE     CRYSTAL STRUCTURE OF DOMAINS BT-BCCP-AC1-AC5 OF YEAST ACETYL-COA      
TITLE    2 CARBOXYLASE                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYL-COA CARBOXYLASE;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACC,FATTY ACID SYNTHETASE 3,MRNA TRANSPORT-DEFECTIVE PROTEIN
COMPND   5 7;                                                                   
COMPND   6 EC: 6.4.1.2,6.3.4.14;                                                
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   3 S288C);                                                              
SOURCE   4 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 559292;                                              
SOURCE   6 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   7 GENE: ACC1, ABP2, FAS3, MTR7, YNR016C, N3175;                        
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ACETYL-COA CARBOXYLASE, LIGASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.WEI,L.TONG                                                          
REVDAT   3   20-SEP-17 5CSA    1       JRNL   REMARK                            
REVDAT   2   11-NOV-15 5CSA    1       JRNL                                     
REVDAT   1   28-OCT-15 5CSA    0                                                
JRNL        AUTH   J.WEI,L.TONG                                                 
JRNL        TITL   CRYSTAL STRUCTURE OF THE 500-KDA YEAST ACETYL-COA            
JRNL        TITL 2 CARBOXYLASE HOLOENZYME DIMER.                                
JRNL        REF    NATURE                        V. 526   723 2015              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26458104                                                     
JRNL        DOI    10.1038/NATURE15375                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 42803                          
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) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2290                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5917                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 296                          
REMARK   3   BIN FREE R VALUE                    : 0.4100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13675                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.27000                                              
REMARK   3    B22 (A**2) : 0.62000                                              
REMARK   3    B33 (A**2) : -0.80000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.69000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.502         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.406         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.047        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.916                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.876                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13967 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 13753 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18913 ; 1.315 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 31705 ; 0.780 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1721 ; 6.008 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   621 ;34.105 ;24.525       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2547 ;17.074 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    81 ;18.022 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2180 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15528 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3037 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3                                                                      
REMARK   3   TENTATIVE SEGMENT.                                                 
REMARK   3   THE ACTUAL RESIDUE ASSIGNMENT FOR SEGMENT 1154-1161 IN CHAIN A     
REMARK   3   IS TENTATIVE DUE TO NO LARGE SIDE CHAINS                           
REMARK   4                                                                      
REMARK   4 5CSA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212108.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-14                          
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               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45742                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: AC1-2, AC3-5                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 80 MM HEPES (PH 7.5), 9.6% (W/V)         
REMARK 280  PEG6000, 1.6% (V/V) MPD, 60 MM SODIUM CITRATE, AND 80 MM NAI,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 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       74.83350            
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 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 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     LYS A   569                                                      
REMARK 465     MET A   570                                                      
REMARK 465     THR A   571                                                      
REMARK 465     ALA A   572                                                      
REMARK 465     GLU A  1122                                                      
REMARK 465     GLY A  1123                                                      
REMARK 465     VAL A  1124                                                      
REMARK 465     THR A  1125                                                      
REMARK 465     VAL A  1126                                                      
REMARK 465     ALA A  1139                                                      
REMARK 465     PHE A  1140                                                      
REMARK 465     SER A  1141                                                      
REMARK 465     THR A  1142                                                      
REMARK 465     PHE A  1143                                                      
REMARK 465     PRO A  1144                                                      
REMARK 465     THR A  1145                                                      
REMARK 465     VAL A  1146                                                      
REMARK 465     LYS A  1147                                                      
REMARK 465     SER A  1148                                                      
REMARK 465     LYS A  1149                                                      
REMARK 465     MET A  1150                                                      
REMARK 465     GLY A  1151                                                      
REMARK 465     MET A  1152                                                      
REMARK 465     ASN A  1153                                                      
REMARK 465     SER A  1162                                                      
REMARK 465     TYR A  1163                                                      
REMARK 465     VAL A  1164                                                      
REMARK 465     ALA A  1165                                                      
REMARK 465     ASN A  1166                                                      
REMARK 465     SER A  1167                                                      
REMARK 465     GLN A  1168                                                      
REMARK 465     SER A  1169                                                      
REMARK 465     SER A  1170                                                      
REMARK 465     PRO A  1198                                                      
REMARK 465     ARG A  1199                                                      
REMARK 465     HIS A  1200                                                      
REMARK 465     GLN A  1201                                                      
REMARK 465     SER A  1202                                                      
REMARK 465     SER A  1203                                                      
REMARK 465     SER A  1204                                                      
REMARK 465     ASN A  1205                                                      
REMARK 465     GLY A  1206                                                      
REMARK 465     PRO A  1207                                                      
REMARK 465     ALA A  1208                                                      
REMARK 465     PRO A  1209                                                      
REMARK 465     ASP A  1210                                                      
REMARK 465     ARG A  1211                                                      
REMARK 465     SER A  1212                                                      
REMARK 465     GLY A  1213                                                      
REMARK 465     SER A  1214                                                      
REMARK 465     SER A  1215                                                      
REMARK 465     ALA A  1216                                                      
REMARK 465     SER A  1217                                                      
REMARK 465     GLN A  1494                                                      
REMARK 465     HIS A  1495                                                      
REMARK 465     HIS A  1496                                                      
REMARK 465     HIS A  1497                                                      
REMARK 465     HIS A  1498                                                      
REMARK 465     HIS A  1499                                                      
REMARK 465     HIS A  1500                                                      
REMARK 465     LYS B   569                                                      
REMARK 465     MET B   570                                                      
REMARK 465     THR B   571                                                      
REMARK 465     ALA B   572                                                      
REMARK 465     GLU B   573                                                      
REMARK 465     ASN B   941                                                      
REMARK 465     GLY B   942                                                      
REMARK 465     PRO B   943                                                      
REMARK 465     ASN B   944                                                      
REMARK 465     VAL B   945                                                      
REMARK 465     ARG B   946                                                      
REMARK 465     LYS B  1054                                                      
REMARK 465     VAL B  1055                                                      
REMARK 465     LYS B  1063                                                      
REMARK 465     ARG B  1064                                                      
REMARK 465     LEU B  1135                                                      
REMARK 465     PRO B  1136                                                      
REMARK 465     SER B  1137                                                      
REMARK 465     ALA B  1138                                                      
REMARK 465     ALA B  1139                                                      
REMARK 465     PHE B  1140                                                      
REMARK 465     SER B  1141                                                      
REMARK 465     THR B  1142                                                      
REMARK 465     PHE B  1143                                                      
REMARK 465     PRO B  1144                                                      
REMARK 465     THR B  1145                                                      
REMARK 465     VAL B  1146                                                      
REMARK 465     LYS B  1147                                                      
REMARK 465     SER B  1148                                                      
REMARK 465     LYS B  1149                                                      
REMARK 465     MET B  1150                                                      
REMARK 465     GLY B  1151                                                      
REMARK 465     MET B  1152                                                      
REMARK 465     ASN B  1153                                                      
REMARK 465     ARG B  1154                                                      
REMARK 465     ALA B  1155                                                      
REMARK 465     VAL B  1156                                                      
REMARK 465     SER B  1157                                                      
REMARK 465     VAL B  1158                                                      
REMARK 465     SER B  1159                                                      
REMARK 465     ASP B  1160                                                      
REMARK 465     LEU B  1161                                                      
REMARK 465     SER B  1162                                                      
REMARK 465     TYR B  1163                                                      
REMARK 465     VAL B  1164                                                      
REMARK 465     ALA B  1165                                                      
REMARK 465     ASN B  1166                                                      
REMARK 465     SER B  1167                                                      
REMARK 465     GLN B  1168                                                      
REMARK 465     SER B  1169                                                      
REMARK 465     SER B  1170                                                      
REMARK 465     PRO B  1171                                                      
REMARK 465     LEU B  1172                                                      
REMARK 465     PRO B  1198                                                      
REMARK 465     ARG B  1199                                                      
REMARK 465     HIS B  1200                                                      
REMARK 465     GLN B  1201                                                      
REMARK 465     SER B  1202                                                      
REMARK 465     SER B  1203                                                      
REMARK 465     SER B  1204                                                      
REMARK 465     ASN B  1205                                                      
REMARK 465     GLY B  1206                                                      
REMARK 465     PRO B  1207                                                      
REMARK 465     ALA B  1208                                                      
REMARK 465     PRO B  1209                                                      
REMARK 465     ASP B  1210                                                      
REMARK 465     ARG B  1211                                                      
REMARK 465     SER B  1212                                                      
REMARK 465     GLY B  1213                                                      
REMARK 465     SER B  1214                                                      
REMARK 465     SER B  1215                                                      
REMARK 465     ALA B  1216                                                      
REMARK 465     SER B  1217                                                      
REMARK 465     GLN B  1494                                                      
REMARK 465     HIS B  1495                                                      
REMARK 465     HIS B  1496                                                      
REMARK 465     HIS B  1497                                                      
REMARK 465     HIS B  1498                                                      
REMARK 465     HIS B  1499                                                      
REMARK 465     HIS B  1500                                                      
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   OD2  ASP A  1431     OG1  THR A  1434              1.89            
REMARK 500   OD2  ASP B  1431     OG1  THR B  1434              2.00            
REMARK 500   OE1  GLU B  1455     OH   TYR B  1457              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CD   LYS A  1474     CE1  TYR B  1450     2546     1.72            
REMARK 500   CE   LYS A  1474     CE1  TYR B  1450     2546     1.85            
REMARK 500   CE   LYS A  1474     OH   TYR B  1450     2546     2.05            
REMARK 500   CE   LYS A  1474     CZ   TYR B  1450     2546     2.09            
REMARK 500   NZ   LYS A  1474     CE1  TYR B  1450     2546     2.10            
REMARK 500   CD   LYS A  1474     CZ   TYR B  1450     2546     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B 602   CD    GLU B 602   OE1     0.077                       
REMARK 500    GLU B 602   CD    GLU B 602   OE2     0.077                       
REMARK 500    TYR B1450   CE1   TYR B1450   CZ      0.165                       
REMARK 500    GLU B1466   CD    GLU B1466   OE1     0.080                       
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    LYS A1474   CD  -  CE  -  NZ  ANGL. DEV. =  17.2 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    HIS A 625      -80.61    -93.01                                   
REMARK 500    GLU A 626      -73.62    -95.68                                   
REMARK 500    ILE A 667       54.06   -106.34                                   
REMARK 500    GLU A 697      136.75    -37.73                                   
REMARK 500    LEU A 715       31.85    -95.99                                   
REMARK 500    LYS A 724      137.82    -39.95                                   
REMARK 500    LYS A 735      -28.72     63.70                                   
REMARK 500    ASN A 818       75.18   -101.80                                   
REMARK 500    ALA A 874       52.56   -143.73                                   
REMARK 500    ASN A 891      109.77   -168.95                                   
REMARK 500    LYS A 913      -51.04    -28.04                                   
REMARK 500    ARG A 946       78.82   -111.07                                   
REMARK 500    SER A 976      -58.95    -24.66                                   
REMARK 500    SER A1015      152.33    179.87                                   
REMARK 500    ASP A1068       96.93    -68.55                                   
REMARK 500    TYR A1110       36.92    -98.94                                   
REMARK 500    PHE A1133      164.69    179.70                                   
REMARK 500    LEU A1135      162.52    -49.07                                   
REMARK 500    SER A1157     -176.37    -67.33                                   
REMARK 500    ILE A1289       48.81   -103.88                                   
REMARK 500    THR A1377       56.81   -104.19                                   
REMARK 500    SER A1378      -81.39    -60.19                                   
REMARK 500    ASP A1381      -59.30   -138.80                                   
REMARK 500    LEU A1382       62.83   -111.32                                   
REMARK 500    LYS A1470       94.78   -161.11                                   
REMARK 500    LEU A1472      -77.19    -90.07                                   
REMARK 500    HIS A1479      -72.06    -60.42                                   
REMARK 500    LEU A1480       48.19   -108.24                                   
REMARK 500    THR A1485      109.53    -49.23                                   
REMARK 500    TRP A1492      -17.40   -151.29                                   
REMARK 500    LEU B 610      -89.33    -89.61                                   
REMARK 500    SER B 611      147.30   -172.49                                   
REMARK 500    HIS B 625      -73.68    -94.01                                   
REMARK 500    GLU B 626      -71.87   -109.78                                   
REMARK 500    LYS B 631       79.34   -117.45                                   
REMARK 500    ILE B 646     -103.95   -122.48                                   
REMARK 500    ARG B 656      133.90   -171.51                                   
REMARK 500    VAL B 680      -75.15    -39.29                                   
REMARK 500    SER B 686       88.74   -155.34                                   
REMARK 500    VAL B 712      -67.43   -104.56                                   
REMARK 500    MET B 734       77.12     40.66                                   
REMARK 500    LYS B 735      -67.52     67.47                                   
REMARK 500    HIS B 777       99.47    -62.55                                   
REMARK 500    VAL B 792      -92.54    -98.69                                   
REMARK 500    ASN B 818       77.01   -103.72                                   
REMARK 500    LEU B 850       -0.90   -144.53                                   
REMARK 500    PRO B 855      152.99    -49.00                                   
REMARK 500    LEU B 939       16.28    -67.64                                   
REMARK 500    SER B1051        1.54    -63.69                                   
REMARK 500    SER B1060     -112.93   -116.95                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5CS0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CS4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CSK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CSL   RELATED DB: PDB                                   
DBREF  5CSA A  569  1494  UNP    Q00955   ACAC_YEAST     569   1494             
DBREF  5CSA B  569  1494  UNP    Q00955   ACAC_YEAST     569   1494             
SEQADV 5CSA HIS A 1495  UNP  Q00955              EXPRESSION TAG                 
SEQADV 5CSA HIS A 1496  UNP  Q00955              EXPRESSION TAG                 
SEQADV 5CSA HIS A 1497  UNP  Q00955              EXPRESSION TAG                 
SEQADV 5CSA HIS A 1498  UNP  Q00955              EXPRESSION TAG                 
SEQADV 5CSA HIS A 1499  UNP  Q00955              EXPRESSION TAG                 
SEQADV 5CSA HIS A 1500  UNP  Q00955              EXPRESSION TAG                 
SEQADV 5CSA HIS B 1495  UNP  Q00955              EXPRESSION TAG                 
SEQADV 5CSA HIS B 1496  UNP  Q00955              EXPRESSION TAG                 
SEQADV 5CSA HIS B 1497  UNP  Q00955              EXPRESSION TAG                 
SEQADV 5CSA HIS B 1498  UNP  Q00955              EXPRESSION TAG                 
SEQADV 5CSA HIS B 1499  UNP  Q00955              EXPRESSION TAG                 
SEQADV 5CSA HIS B 1500  UNP  Q00955              EXPRESSION TAG                 
SEQRES   1 A  932  LYS MET THR ALA GLU LYS PRO ASP PRO THR LEU ALA VAL          
SEQRES   2 A  932  ILE CYS GLY ALA ALA THR LYS ALA PHE LEU ALA SER GLU          
SEQRES   3 A  932  GLU ALA ARG HIS LYS TYR ILE GLU SER LEU GLN LYS GLY          
SEQRES   4 A  932  GLN VAL LEU SER LYS ASP LEU LEU GLN THR MET PHE PRO          
SEQRES   5 A  932  VAL ASP PHE ILE HIS GLU GLY LYS ARG TYR LYS PHE THR          
SEQRES   6 A  932  VAL ALA LYS SER GLY ASN ASP ARG TYR THR LEU PHE ILE          
SEQRES   7 A  932  ASN GLY SER LYS CYS ASP ILE ILE LEU ARG GLN LEU SER          
SEQRES   8 A  932  ASP GLY GLY LEU LEU ILE ALA ILE GLY GLY LYS SER HIS          
SEQRES   9 A  932  THR ILE TYR TRP LYS GLU GLU VAL ALA ALA THR ARG LEU          
SEQRES  10 A  932  SER VAL ASP SER MET THR THR LEU LEU GLU VAL GLU ASN          
SEQRES  11 A  932  ASP PRO THR GLN LEU ARG THR PRO SER PRO GLY LYS LEU          
SEQRES  12 A  932  VAL LYS PHE LEU VAL GLU ASN GLY GLU HIS ILE ILE LYS          
SEQRES  13 A  932  GLY GLN PRO TYR ALA GLU ILE GLU VAL MET LYS MET GLN          
SEQRES  14 A  932  MET PRO LEU VAL SER GLN GLU ASN GLY ILE VAL GLN LEU          
SEQRES  15 A  932  LEU LYS GLN PRO GLY SER THR ILE VAL ALA GLY ASP ILE          
SEQRES  16 A  932  MET ALA ILE MET THR LEU ASP ASP PRO SER LYS VAL LYS          
SEQRES  17 A  932  HIS ALA LEU PRO PHE GLU GLY MET LEU PRO ASP PHE GLY          
SEQRES  18 A  932  SER PRO VAL ILE GLU GLY THR LYS PRO ALA TYR LYS PHE          
SEQRES  19 A  932  LYS SER LEU VAL SER THR LEU GLU ASN ILE LEU LYS GLY          
SEQRES  20 A  932  TYR ASP ASN GLN VAL ILE MET ASN ALA SER LEU GLN GLN          
SEQRES  21 A  932  LEU ILE GLU VAL LEU ARG ASN PRO LYS LEU PRO TYR SER          
SEQRES  22 A  932  GLU TRP LYS LEU HIS ILE SER ALA LEU HIS SER ARG LEU          
SEQRES  23 A  932  PRO ALA LYS LEU ASP GLU GLN MET GLU GLU LEU VAL ALA          
SEQRES  24 A  932  ARG SER LEU ARG ARG GLY ALA VAL PHE PRO ALA ARG GLN          
SEQRES  25 A  932  LEU SER LYS LEU ILE ASP MET ALA VAL LYS ASN PRO GLU          
SEQRES  26 A  932  TYR ASN PRO ASP LYS LEU LEU GLY ALA VAL VAL GLU PRO          
SEQRES  27 A  932  LEU ALA ASP ILE ALA HIS LYS TYR SER ASN GLY LEU GLU          
SEQRES  28 A  932  ALA HIS GLU HIS SER ILE PHE VAL HIS PHE LEU GLU GLU          
SEQRES  29 A  932  TYR TYR GLU VAL GLU LYS LEU PHE ASN GLY PRO ASN VAL          
SEQRES  30 A  932  ARG GLU GLU ASN ILE ILE LEU LYS LEU ARG ASP GLU ASN          
SEQRES  31 A  932  PRO LYS ASP LEU ASP LYS VAL ALA LEU THR VAL LEU SER          
SEQRES  32 A  932  HIS SER LYS VAL SER ALA LYS ASN ASN LEU ILE LEU ALA          
SEQRES  33 A  932  ILE LEU LYS HIS TYR GLN PRO LEU CYS LYS LEU SER SER          
SEQRES  34 A  932  LYS VAL SER ALA ILE PHE SER THR PRO LEU GLN HIS ILE          
SEQRES  35 A  932  VAL GLU LEU GLU SER LYS ALA THR ALA LYS VAL ALA LEU          
SEQRES  36 A  932  GLN ALA ARG GLU ILE LEU ILE GLN GLY ALA LEU PRO SER          
SEQRES  37 A  932  VAL LYS GLU ARG THR GLU GLN ILE GLU HIS ILE LEU LYS          
SEQRES  38 A  932  SER SER VAL VAL LYS VAL ALA TYR GLY SER SER ASN PRO          
SEQRES  39 A  932  LYS ARG SER GLU PRO ASP LEU ASN ILE LEU LYS ASP LEU          
SEQRES  40 A  932  ILE ASP SER ASN TYR VAL VAL PHE ASP VAL LEU LEU GLN          
SEQRES  41 A  932  PHE LEU THR HIS GLN ASP PRO VAL VAL THR ALA ALA ALA          
SEQRES  42 A  932  ALA GLN VAL TYR ILE ARG ARG ALA TYR ARG ALA TYR THR          
SEQRES  43 A  932  ILE GLY ASP ILE ARG VAL HIS GLU GLY VAL THR VAL PRO          
SEQRES  44 A  932  ILE VAL GLU TRP LYS PHE GLN LEU PRO SER ALA ALA PHE          
SEQRES  45 A  932  SER THR PHE PRO THR VAL LYS SER LYS MET GLY MET ASN          
SEQRES  46 A  932  ARG ALA VAL SER VAL SER ASP LEU SER TYR VAL ALA ASN          
SEQRES  47 A  932  SER GLN SER SER PRO LEU ARG GLU GLY ILE LEU MET ALA          
SEQRES  48 A  932  VAL ASP HIS LEU ASP ASP VAL ASP GLU ILE LEU SER GLN          
SEQRES  49 A  932  SER LEU GLU VAL ILE PRO ARG HIS GLN SER SER SER ASN          
SEQRES  50 A  932  GLY PRO ALA PRO ASP ARG SER GLY SER SER ALA SER LEU          
SEQRES  51 A  932  SER ASN VAL ALA ASN VAL CYS VAL ALA SER THR GLU GLY          
SEQRES  52 A  932  PHE GLU SER GLU GLU GLU ILE LEU VAL ARG LEU ARG GLU          
SEQRES  53 A  932  ILE LEU ASP LEU ASN LYS GLN GLU LEU ILE ASN ALA SER          
SEQRES  54 A  932  ILE ARG ARG ILE THR PHE MET PHE GLY PHE LYS ASP GLY          
SEQRES  55 A  932  SER TYR PRO LYS TYR TYR THR PHE ASN GLY PRO ASN TYR          
SEQRES  56 A  932  ASN GLU ASN GLU THR ILE ARG HIS ILE GLU PRO ALA LEU          
SEQRES  57 A  932  ALA PHE GLN LEU GLU LEU GLY ARG LEU SER ASN PHE ASN          
SEQRES  58 A  932  ILE LYS PRO ILE PHE THR ASP ASN ARG ASN ILE HIS VAL          
SEQRES  59 A  932  TYR GLU ALA VAL SER LYS THR SER PRO LEU ASP LYS ARG          
SEQRES  60 A  932  PHE PHE THR ARG GLY ILE ILE ARG THR GLY HIS ILE ARG          
SEQRES  61 A  932  ASP ASP ILE SER ILE GLN GLU TYR LEU THR SER GLU ALA          
SEQRES  62 A  932  ASN ARG LEU MET SER ASP ILE LEU ASP ASN LEU GLU VAL          
SEQRES  63 A  932  THR ASP THR SER ASN SER ASP LEU ASN HIS ILE PHE ILE          
SEQRES  64 A  932  ASN PHE ILE ALA VAL PHE ASP ILE SER PRO GLU ASP VAL          
SEQRES  65 A  932  GLU ALA ALA PHE GLY GLY PHE LEU GLU ARG PHE GLY LYS          
SEQRES  66 A  932  ARG LEU LEU ARG LEU ARG VAL SER SER ALA GLU ILE ARG          
SEQRES  67 A  932  ILE ILE ILE LYS ASP PRO GLN THR GLY ALA PRO VAL PRO          
SEQRES  68 A  932  LEU ARG ALA LEU ILE ASN ASN VAL SER GLY TYR VAL ILE          
SEQRES  69 A  932  LYS THR GLU MET TYR THR GLU VAL LYS ASN ALA LYS GLY          
SEQRES  70 A  932  GLU TRP VAL PHE LYS SER LEU GLY LYS PRO GLY SER MET          
SEQRES  71 A  932  HIS LEU ARG PRO ILE ALA THR PRO TYR PRO VAL LYS GLU          
SEQRES  72 A  932  TRP LEU GLN HIS HIS HIS HIS HIS HIS                          
SEQRES   1 B  932  LYS MET THR ALA GLU LYS PRO ASP PRO THR LEU ALA VAL          
SEQRES   2 B  932  ILE CYS GLY ALA ALA THR LYS ALA PHE LEU ALA SER GLU          
SEQRES   3 B  932  GLU ALA ARG HIS LYS TYR ILE GLU SER LEU GLN LYS GLY          
SEQRES   4 B  932  GLN VAL LEU SER LYS ASP LEU LEU GLN THR MET PHE PRO          
SEQRES   5 B  932  VAL ASP PHE ILE HIS GLU GLY LYS ARG TYR LYS PHE THR          
SEQRES   6 B  932  VAL ALA LYS SER GLY ASN ASP ARG TYR THR LEU PHE ILE          
SEQRES   7 B  932  ASN GLY SER LYS CYS ASP ILE ILE LEU ARG GLN LEU SER          
SEQRES   8 B  932  ASP GLY GLY LEU LEU ILE ALA ILE GLY GLY LYS SER HIS          
SEQRES   9 B  932  THR ILE TYR TRP LYS GLU GLU VAL ALA ALA THR ARG LEU          
SEQRES  10 B  932  SER VAL ASP SER MET THR THR LEU LEU GLU VAL GLU ASN          
SEQRES  11 B  932  ASP PRO THR GLN LEU ARG THR PRO SER PRO GLY LYS LEU          
SEQRES  12 B  932  VAL LYS PHE LEU VAL GLU ASN GLY GLU HIS ILE ILE LYS          
SEQRES  13 B  932  GLY GLN PRO TYR ALA GLU ILE GLU VAL MET LYS MET GLN          
SEQRES  14 B  932  MET PRO LEU VAL SER GLN GLU ASN GLY ILE VAL GLN LEU          
SEQRES  15 B  932  LEU LYS GLN PRO GLY SER THR ILE VAL ALA GLY ASP ILE          
SEQRES  16 B  932  MET ALA ILE MET THR LEU ASP ASP PRO SER LYS VAL LYS          
SEQRES  17 B  932  HIS ALA LEU PRO PHE GLU GLY MET LEU PRO ASP PHE GLY          
SEQRES  18 B  932  SER PRO VAL ILE GLU GLY THR LYS PRO ALA TYR LYS PHE          
SEQRES  19 B  932  LYS SER LEU VAL SER THR LEU GLU ASN ILE LEU LYS GLY          
SEQRES  20 B  932  TYR ASP ASN GLN VAL ILE MET ASN ALA SER LEU GLN GLN          
SEQRES  21 B  932  LEU ILE GLU VAL LEU ARG ASN PRO LYS LEU PRO TYR SER          
SEQRES  22 B  932  GLU TRP LYS LEU HIS ILE SER ALA LEU HIS SER ARG LEU          
SEQRES  23 B  932  PRO ALA LYS LEU ASP GLU GLN MET GLU GLU LEU VAL ALA          
SEQRES  24 B  932  ARG SER LEU ARG ARG GLY ALA VAL PHE PRO ALA ARG GLN          
SEQRES  25 B  932  LEU SER LYS LEU ILE ASP MET ALA VAL LYS ASN PRO GLU          
SEQRES  26 B  932  TYR ASN PRO ASP LYS LEU LEU GLY ALA VAL VAL GLU PRO          
SEQRES  27 B  932  LEU ALA ASP ILE ALA HIS LYS TYR SER ASN GLY LEU GLU          
SEQRES  28 B  932  ALA HIS GLU HIS SER ILE PHE VAL HIS PHE LEU GLU GLU          
SEQRES  29 B  932  TYR TYR GLU VAL GLU LYS LEU PHE ASN GLY PRO ASN VAL          
SEQRES  30 B  932  ARG GLU GLU ASN ILE ILE LEU LYS LEU ARG ASP GLU ASN          
SEQRES  31 B  932  PRO LYS ASP LEU ASP LYS VAL ALA LEU THR VAL LEU SER          
SEQRES  32 B  932  HIS SER LYS VAL SER ALA LYS ASN ASN LEU ILE LEU ALA          
SEQRES  33 B  932  ILE LEU LYS HIS TYR GLN PRO LEU CYS LYS LEU SER SER          
SEQRES  34 B  932  LYS VAL SER ALA ILE PHE SER THR PRO LEU GLN HIS ILE          
SEQRES  35 B  932  VAL GLU LEU GLU SER LYS ALA THR ALA LYS VAL ALA LEU          
SEQRES  36 B  932  GLN ALA ARG GLU ILE LEU ILE GLN GLY ALA LEU PRO SER          
SEQRES  37 B  932  VAL LYS GLU ARG THR GLU GLN ILE GLU HIS ILE LEU LYS          
SEQRES  38 B  932  SER SER VAL VAL LYS VAL ALA TYR GLY SER SER ASN PRO          
SEQRES  39 B  932  LYS ARG SER GLU PRO ASP LEU ASN ILE LEU LYS ASP LEU          
SEQRES  40 B  932  ILE ASP SER ASN TYR VAL VAL PHE ASP VAL LEU LEU GLN          
SEQRES  41 B  932  PHE LEU THR HIS GLN ASP PRO VAL VAL THR ALA ALA ALA          
SEQRES  42 B  932  ALA GLN VAL TYR ILE ARG ARG ALA TYR ARG ALA TYR THR          
SEQRES  43 B  932  ILE GLY ASP ILE ARG VAL HIS GLU GLY VAL THR VAL PRO          
SEQRES  44 B  932  ILE VAL GLU TRP LYS PHE GLN LEU PRO SER ALA ALA PHE          
SEQRES  45 B  932  SER THR PHE PRO THR VAL LYS SER LYS MET GLY MET ASN          
SEQRES  46 B  932  ARG ALA VAL SER VAL SER ASP LEU SER TYR VAL ALA ASN          
SEQRES  47 B  932  SER GLN SER SER PRO LEU ARG GLU GLY ILE LEU MET ALA          
SEQRES  48 B  932  VAL ASP HIS LEU ASP ASP VAL ASP GLU ILE LEU SER GLN          
SEQRES  49 B  932  SER LEU GLU VAL ILE PRO ARG HIS GLN SER SER SER ASN          
SEQRES  50 B  932  GLY PRO ALA PRO ASP ARG SER GLY SER SER ALA SER LEU          
SEQRES  51 B  932  SER ASN VAL ALA ASN VAL CYS VAL ALA SER THR GLU GLY          
SEQRES  52 B  932  PHE GLU SER GLU GLU GLU ILE LEU VAL ARG LEU ARG GLU          
SEQRES  53 B  932  ILE LEU ASP LEU ASN LYS GLN GLU LEU ILE ASN ALA SER          
SEQRES  54 B  932  ILE ARG ARG ILE THR PHE MET PHE GLY PHE LYS ASP GLY          
SEQRES  55 B  932  SER TYR PRO LYS TYR TYR THR PHE ASN GLY PRO ASN TYR          
SEQRES  56 B  932  ASN GLU ASN GLU THR ILE ARG HIS ILE GLU PRO ALA LEU          
SEQRES  57 B  932  ALA PHE GLN LEU GLU LEU GLY ARG LEU SER ASN PHE ASN          
SEQRES  58 B  932  ILE LYS PRO ILE PHE THR ASP ASN ARG ASN ILE HIS VAL          
SEQRES  59 B  932  TYR GLU ALA VAL SER LYS THR SER PRO LEU ASP LYS ARG          
SEQRES  60 B  932  PHE PHE THR ARG GLY ILE ILE ARG THR GLY HIS ILE ARG          
SEQRES  61 B  932  ASP ASP ILE SER ILE GLN GLU TYR LEU THR SER GLU ALA          
SEQRES  62 B  932  ASN ARG LEU MET SER ASP ILE LEU ASP ASN LEU GLU VAL          
SEQRES  63 B  932  THR ASP THR SER ASN SER ASP LEU ASN HIS ILE PHE ILE          
SEQRES  64 B  932  ASN PHE ILE ALA VAL PHE ASP ILE SER PRO GLU ASP VAL          
SEQRES  65 B  932  GLU ALA ALA PHE GLY GLY PHE LEU GLU ARG PHE GLY LYS          
SEQRES  66 B  932  ARG LEU LEU ARG LEU ARG VAL SER SER ALA GLU ILE ARG          
SEQRES  67 B  932  ILE ILE ILE LYS ASP PRO GLN THR GLY ALA PRO VAL PRO          
SEQRES  68 B  932  LEU ARG ALA LEU ILE ASN ASN VAL SER GLY TYR VAL ILE          
SEQRES  69 B  932  LYS THR GLU MET TYR THR GLU VAL LYS ASN ALA LYS GLY          
SEQRES  70 B  932  GLU TRP VAL PHE LYS SER LEU GLY LYS PRO GLY SER MET          
SEQRES  71 B  932  HIS LEU ARG PRO ILE ALA THR PRO TYR PRO VAL LYS GLU          
SEQRES  72 B  932  TRP LEU GLN HIS HIS HIS HIS HIS HIS                          
HELIX    1 AA1 ASP A  576  LYS A  606  1                                  31    
HELIX    2 AA2 SER A  611  GLN A  616  5                                   6    
HELIX    3 AA3 ASP A  771  VAL A  775  5                                   5    
HELIX    4 AA4 THR A  796  LYS A  814  1                                  19    
HELIX    5 AA5 ALA A  824  ARG A  834  1                                  11    
HELIX    6 AA6 PRO A  836  HIS A  851  1                                  16    
HELIX    7 AA7 SER A  852  LEU A  854  5                                   3    
HELIX    8 AA8 PRO A  855  GLY A  873  1                                  19    
HELIX    9 AA9 PRO A  877  LYS A  890  1                                  14    
HELIX   10 AB1 LEU A  899  TYR A  914  1                                  16    
HELIX   11 AB2 ASN A  916  LYS A  938  1                                  23    
HELIX   12 AB3 LEU A  939  ASN A  941  5                                   3    
HELIX   13 AB4 ARG A  946  ASN A  958  1                                  13    
HELIX   14 AB5 ASP A  961  LYS A  974  1                                  14    
HELIX   15 AB6 LYS A  974  SER A  996  1                                  23    
HELIX   16 AB7 SER A  996  VAL A 1011  1                                  16    
HELIX   17 AB8 THR A 1018  LEU A 1034  1                                  17    
HELIX   18 AB9 SER A 1036  VAL A 1052  1                                  17    
HELIX   19 AC1 ASP A 1068  ASP A 1077  1                                  10    
HELIX   20 AC2 VAL A 1082  LEU A 1087  1                                   6    
HELIX   21 AC3 GLN A 1088  HIS A 1092  5                                   5    
HELIX   22 AC4 ASP A 1094  TYR A 1110  1                                  17    
HELIX   23 AC5 HIS A 1182  ASP A 1184  5                                   3    
HELIX   24 AC6 ASP A 1185  LEU A 1194  1                                  10    
HELIX   25 AC7 GLU A 1195  ILE A 1197  5                                   3    
HELIX   26 AC8 SER A 1234  ALA A 1256  1                                  23    
HELIX   27 AC9 GLU A 1293  GLU A 1301  1                                   9    
HELIX   28 AD1 LEU A 1302  SER A 1306  5                                   5    
HELIX   29 AD2 SER A 1352  THR A 1375  1                                  24    
HELIX   30 AD3 SER A 1396  PHE A 1404  1                                   9    
HELIX   31 AD4 GLY A 1406  ARG A 1419  1                                  14    
HELIX   32 AD5 ASP B  576  GLN B  605  1                                  30    
HELIX   33 AD6 SER B  611  GLN B  616  5                                   6    
HELIX   34 AD7 THR B  796  LEU B  813  1                                  18    
HELIX   35 AD8 ALA B  824  ARG B  834  1                                  11    
HELIX   36 AD9 PRO B  836  ALA B  849  1                                  14    
HELIX   37 AE1 PRO B  855  GLY B  873  1                                  19    
HELIX   38 AE2 PRO B  877  ASN B  891  1                                  15    
HELIX   39 AE3 LEU B  899  VAL B  904  1                                   6    
HELIX   40 AE4 VAL B  904  TYR B  914  1                                  11    
HELIX   41 AE5 GLY B  917  LYS B  938  1                                  22    
HELIX   42 AE6 GLU B  948  ASN B  958  1                                  11    
HELIX   43 AE7 LEU B  962  LYS B  974  1                                  13    
HELIX   44 AE8 LYS B  974  SER B  996  1                                  23    
HELIX   45 AE9 SER B  996  PHE B 1003  1                                   8    
HELIX   46 AF1 PHE B 1003  VAL B 1011  1                                   9    
HELIX   47 AF2 THR B 1018  LEU B 1034  1                                  17    
HELIX   48 AF3 SER B 1036  SER B 1051  1                                  16    
HELIX   49 AF4 ASP B 1068  SER B 1078  1                                  11    
HELIX   50 AF5 VAL B 1082  LEU B 1087  1                                   6    
HELIX   51 AF6 GLN B 1088  HIS B 1092  5                                   5    
HELIX   52 AF7 ASP B 1094  TYR B 1110  1                                  17    
HELIX   53 AF8 ARG B 1111  TYR B 1113  5                                   3    
HELIX   54 AF9 HIS B 1182  ASP B 1184  5                                   3    
HELIX   55 AG1 ASP B 1185  LEU B 1194  1                                  10    
HELIX   56 AG2 SER B 1234  ALA B 1256  1                                  23    
HELIX   57 AG3 GLU B 1293  SER B 1306  5                                  14    
HELIX   58 AG4 SER B 1352  THR B 1375  1                                  24    
HELIX   59 AG5 SER B 1396  PHE B 1404  1                                   9    
HELIX   60 AG6 GLY B 1406  LEU B 1418  1                                  13    
SHEET    1 AA1 8 GLU A 678  GLU A 679  0                                        
SHEET    2 AA1 8 ALA A 682  VAL A 687 -1  O  ALA A 682   N  GLU A 679           
SHEET    3 AA1 8 SER A 671  TYR A 675 -1  N  TYR A 675   O  SER A 686           
SHEET    4 AA1 8 LEU A 663  ALA A 666 -1  N  LEU A 663   O  ILE A 674           
SHEET    5 AA1 8 LYS A 650  GLN A 657 -1  N  ARG A 656   O  LEU A 664           
SHEET    6 AA1 8 ARG A 641  PHE A 645 -1  N  TYR A 642   O  ILE A 653           
SHEET    7 AA1 8 LYS A 628  LYS A 636 -1  N  ALA A 635   O  THR A 643           
SHEET    8 AA1 8 LEU A 779  PRO A 780  1  O  LEU A 779   N  ARG A 629           
SHEET    1 AA2 6 GLU A 678  GLU A 679  0                                        
SHEET    2 AA2 6 ALA A 682  VAL A 687 -1  O  ALA A 682   N  GLU A 679           
SHEET    3 AA2 6 MET A 690  GLU A 695 -1  O  LEU A 694   N  THR A 683           
SHEET    4 AA2 6 MET A 618  ILE A 624 -1  N  ILE A 624   O  GLU A 695           
SHEET    5 AA2 6 LYS A 628  LYS A 636 -1  O  VAL A 634   N  PHE A 619           
SHEET    6 AA2 6 LEU A 779  PRO A 780  1  O  LEU A 779   N  ARG A 629           
SHEET    1 AA3 4 GLN A 702  ARG A 704  0                                        
SHEET    2 AA3 4 ILE A 763  MET A 767 -1  O  MET A 764   N  LEU A 703           
SHEET    3 AA3 4 GLY A 746  LEU A 750 -1  N  GLN A 749   O  ILE A 766           
SHEET    4 AA3 4 HIS A 721  ILE A 722 -1  N  ILE A 722   O  GLY A 746           
SHEET    1 AA4 4 MET A 736  VAL A 741  0                                        
SHEET    2 AA4 4 PRO A 727  VAL A 733 -1  N  VAL A 733   O  MET A 736           
SHEET    3 AA4 4 GLY A 709  PHE A 714 -1  N  LYS A 710   O  GLU A 732           
SHEET    4 AA4 4 THR A 757  ILE A 758 -1  O  ILE A 758   N  GLY A 709           
SHEET    1 AA5 6 THR A1114  VAL A1120  0                                        
SHEET    2 AA5 6 ILE A1128  GLN A1134 -1  O  LYS A1132   N  GLY A1116           
SHEET    3 AA5 6 ARG A1173  VAL A1180 -1  O  LEU A1177   N  VAL A1129           
SHEET    4 AA5 6 ASN A1220  VAL A1226  1  O  CYS A1225   N  VAL A1180           
SHEET    5 AA5 6 ILE A1258  PHE A1265  1  O  THR A1262   N  VAL A1224           
SHEET    6 AA5 6 LYS A1274  PHE A1278 -1  O  PHE A1278   N  ILE A1261           
SHEET    1 AA6 5 ALA A1155  VAL A1156  0                                        
SHEET    2 AA6 5 ASN A1383  PHE A1393 -1  O  VAL A1392   N  VAL A1156           
SHEET    3 AA6 5 LYS A1334  ILE A1342  1  N  GLY A1340   O  PHE A1386           
SHEET    4 AA6 5 ILE A1320  SER A1327 -1  N  ALA A1325   O  ARG A1335           
SHEET    5 AA6 5 PHE A1308  ILE A1313 -1  N  ASN A1309   O  VAL A1326           
SHEET    1 AA7 5 ALA A1155  VAL A1156  0                                        
SHEET    2 AA7 5 ASN A1383  PHE A1393 -1  O  VAL A1392   N  VAL A1156           
SHEET    3 AA7 5 VAL A1420  LYS A1430  1  O  ILE A1428   N  PHE A1393           
SHEET    4 AA7 5 PRO A1437  ASN A1445 -1  O  LEU A1440   N  ILE A1427           
SHEET    5 AA7 5 GLU A1455  THR A1458 -1  O  GLU A1455   N  LEU A1443           
SHEET    1 AA8 2 VAL A1460  LYS A1461  0                                        
SHEET    2 AA8 2 TRP A1467  VAL A1468 -1  O  VAL A1468   N  VAL A1460           
SHEET    1 AA9 4 MET B 618  ILE B 624  0                                        
SHEET    2 AA9 4 LYS B 628  LYS B 636 -1  O  VAL B 634   N  PHE B 619           
SHEET    3 AA9 4 ARG B 641  PHE B 645 -1  O  THR B 643   N  ALA B 635           
SHEET    4 AA9 4 LYS B 650  ILE B 654 -1  O  CYS B 651   N  LEU B 644           
SHEET    1 AB1 3 MET B 618  ILE B 624  0                                        
SHEET    2 AB1 3 LYS B 628  LYS B 636 -1  O  VAL B 634   N  PHE B 619           
SHEET    3 AB1 3 LEU B 779  PRO B 780  1  O  LEU B 779   N  ARG B 629           
SHEET    1 AB2 2 LEU B 663  ALA B 666  0                                        
SHEET    2 AB2 2 SER B 671  ILE B 674 -1  O  HIS B 672   N  ILE B 665           
SHEET    1 AB3 3 LYS B 677  GLU B 678  0                                        
SHEET    2 AB3 3 THR B 683  VAL B 687 -1  O  ARG B 684   N  LYS B 677           
SHEET    3 AB3 3 MET B 690  LEU B 694 -1  O  LEU B 694   N  THR B 683           
SHEET    1 AB4 4 GLN B 702  ARG B 704  0                                        
SHEET    2 AB4 4 ILE B 763  LEU B 769 -1  O  ALA B 765   N  LEU B 703           
SHEET    3 AB4 4 GLY B 746  LEU B 750 -1  N  GLN B 749   O  ILE B 766           
SHEET    4 AB4 4 HIS B 721  ILE B 722 -1  N  ILE B 722   O  GLY B 746           
SHEET    1 AB5 4 GLN B 737  VAL B 741  0                                        
SHEET    2 AB5 4 PRO B 727  GLU B 732 -1  N  ILE B 731   O  MET B 738           
SHEET    3 AB5 4 GLY B 709  PHE B 714 -1  N  LYS B 713   O  GLU B 730           
SHEET    4 AB5 4 THR B 757  ILE B 758 -1  O  ILE B 758   N  GLY B 709           
SHEET    1 AB6 7 ILE B1115  HIS B1121  0                                        
SHEET    2 AB6 7 ILE B1128  PHE B1133 -1  O  ILE B1128   N  HIS B1121           
SHEET    3 AB6 7 GLU B1174  VAL B1180 -1  O  LEU B1177   N  VAL B1129           
SHEET    4 AB6 7 ASN B1220  VAL B1226  1  O  CYS B1225   N  MET B1178           
SHEET    5 AB6 7 ILE B1258  PHE B1265  1  O  MET B1264   N  VAL B1224           
SHEET    6 AB6 7 LYS B1274  PHE B1278 -1  O  PHE B1278   N  ILE B1261           
SHEET    7 AB6 7 GLU B1285  ASN B1286 -1  O  ASN B1286   N  THR B1277           
SHEET    1 AB7 8 PHE B1308  ILE B1313  0                                        
SHEET    2 AB7 8 ILE B1320  SER B1327 -1  O  GLU B1324   N  LYS B1311           
SHEET    3 AB7 8 LYS B1334  ILE B1342 -1  O  ARG B1335   N  ALA B1325           
SHEET    4 AB7 8 ASN B1383  PHE B1393  1  O  PHE B1386   N  GLY B1340           
SHEET    5 AB7 8 VAL B1420  LYS B1430  1  O  ARG B1426   N  PHE B1389           
SHEET    6 AB7 8 PRO B1437  ASN B1446 -1  O  VAL B1438   N  ILE B1429           
SHEET    7 AB7 8 ILE B1452  LYS B1461 -1  O  GLU B1455   N  LEU B1443           
SHEET    8 AB7 8 TRP B1467  SER B1471 -1  O  VAL B1468   N  VAL B1460           
CRYST1   93.329  149.667   95.437  90.00 118.39  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      0.010715  0.000000  0.005792        0.00000                         
SCALE2      0.000000  0.006681  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011911        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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