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Database: PDB
Entry: 3VPC
LinkDB: 3VPC
Original site: 3VPC 
HEADER    LIGASE                                  29-FEB-12   3VPC              
TITLE     ARGX FROM SULFOLOBUS TOKODAII COMPLEXED WITH ADP                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE ACETYLORNITHINE DEACETYLASE;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: STARGX;                                                     
COMPND   5 EC: 3.5.1.16;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SULFOLOBUS TOKODAII;                            
SOURCE   3 ORGANISM_TAXID: 111955;                                              
SOURCE   4 STRAIN: DSM 16993, JCM 10545, NBRC 100140, 7;                        
SOURCE   5 GENE: ARGX;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 273063;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21CODONPLUS(DE3);                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-STARGX                                
KEYWDS    ATP-DEPENDENET AMINE/THIOL LIGASE FAMILY, ATP-DEPENDENET AMINE/THIOL  
KEYWDS   2 LIGASE, LIGASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.TOMITA,A.HORIE,T.KUZUYAMA,M.NISHIYAMA                               
REVDAT   2   31-JUL-13 3VPC    1       JRNL                                     
REVDAT   1   27-FEB-13 3VPC    0                                                
JRNL        AUTH   T.OUCHI,T.TOMITA,A.HORIE,A.YOSHIDA,K.TAKAHASHI,H.NISHIDA,    
JRNL        AUTH 2 K.LASSAK,H.TAKA,R.MINEKI,T.FUJIMURA,S.KOSONO,C.NISHIYAMA,    
JRNL        AUTH 3 R.MASUI,S.KURAMITSU,S.V.ALBERS,T.KUZUYAMA,M.NISHIYAMA        
JRNL        TITL   LYSINE AND ARGININE BIOSYNTHESES MEDIATED BY A COMMON        
JRNL        TITL 2 CARRIER PROTEIN IN SULFOLOBUS.                               
JRNL        REF    NAT.CHEM.BIOL.                V.   9   277 2013              
JRNL        REFN                   ISSN 1552-4450                               
JRNL        PMID   23434852                                                     
JRNL        DOI    10.1038/NCHEMBIO.1200                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.87 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
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) : 1.87                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 89452                          
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) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4707                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.86                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5671                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.74                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 270                          
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8841                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 108                                     
REMARK   3   SOLVENT ATOMS            : 956                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : -0.02000                                             
REMARK   3    B13 (A**2) : -0.01000                                             
REMARK   3    B23 (A**2) : 0.02000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.172         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.163         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.880         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9259 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12607 ; 1.452 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1162 ; 6.342 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   410 ;40.366 ;24.585       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1667 ;16.800 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;17.057 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1445 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6875 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  5658 ; 0.782 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9221 ; 1.425 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3601 ; 1.960 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3364 ; 3.252 ; 4.500       
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3VPC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-MAR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB095332.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 98303                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.870                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
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) : 1.87                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.8                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1UC8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)H2PO4, 10% PEG 3350, PH 4.6,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14980 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     ASN C   202                                                      
REMARK 465     VAL C   203                                                      
REMARK 465     ALA C   204                                                      
REMARK 465     LEU C   205                                                      
REMARK 465     GLY C   206                                                      
REMARK 465     GLY C   207                                                      
REMARK 465     THR C   208                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ILE D   130     O    HOH D   695              2.10            
REMARK 500   O2B  ADP B   500     O    HOH B   620              2.15            
REMARK 500   OD2  ASP A   176     O3'  ADP A   500              2.16            
REMARK 500   OE1  GLU A   250     O    HOH A   823              2.18            
REMARK 500   O    HOH B   704     O    HOH B   807              2.19            
REMARK 500   OE1  GLU D   250     O    HOH D   760              2.19            
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    ASP A   8      -57.20   -132.81                                   
REMARK 500    SER A 132       31.58    177.60                                   
REMARK 500    SER A 159     -168.83     66.32                                   
REMARK 500    TYR A 172      -67.35   -136.40                                   
REMARK 500    PRO A 196      -31.05    -38.19                                   
REMARK 500    VAL A 203       94.35   -162.88                                   
REMARK 500    ALA A 204      -90.54     40.21                                   
REMARK 500    PHE A 257        2.91   -152.49                                   
REMARK 500    ASP B   8      -52.89   -128.65                                   
REMARK 500    SER B 132       33.51   -171.63                                   
REMARK 500    TYR B 172      -72.66   -156.90                                   
REMARK 500    LEU B 205       72.51   -116.66                                   
REMARK 500    PHE B 257        2.45   -153.82                                   
REMARK 500    ASP C   8      -60.39   -134.71                                   
REMARK 500    SER C 132       29.26   -156.54                                   
REMARK 500    TYR C 172      -70.15   -136.32                                   
REMARK 500    PHE C 257       16.14   -148.70                                   
REMARK 500    ASP D   8      -63.38   -127.54                                   
REMARK 500    SER D 132       17.60   -166.88                                   
REMARK 500    LEU D 155       30.05    -99.52                                   
REMARK 500    TYR D 172      -79.27   -163.17                                   
REMARK 500    TRP D 199       -0.20   -150.29                                   
REMARK 500    PHE D 257        6.22   -151.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG B 135        20.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE D 130        24.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 797        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH A 804        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH A 805        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH A 812        DISTANCE =  7.55 ANGSTROMS                       
REMARK 525    HOH A 813        DISTANCE =  7.90 ANGSTROMS                       
REMARK 525    HOH B 768        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH B 799        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH B 849        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH C 604        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH C 783        DISTANCE =  7.38 ANGSTROMS                       
REMARK 525    HOH C 784        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH C 795        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH C 796        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH C 798        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH D 816        DISTANCE =  5.47 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 500                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VPB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VPD   RELATED DB: PDB                                   
DBREF  3VPC A    1   282  UNP    Q970U6   Q970U6_SULTO     1    282             
DBREF  3VPC B    1   282  UNP    Q970U6   Q970U6_SULTO     1    282             
DBREF  3VPC C    1   282  UNP    Q970U6   Q970U6_SULTO     1    282             
DBREF  3VPC D    1   282  UNP    Q970U6   Q970U6_SULTO     1    282             
SEQRES   1 A  282  MET ARG VAL VAL LEU ILE VAL ASP ILE VAL ARG GLN GLU          
SEQRES   2 A  282  GLU LYS LEU ILE ALA LYS ALA LEU GLU GLU ASN LYS VAL          
SEQRES   3 A  282  GLN TYR ASP ILE ILE ASN VAL ALA GLN GLU PRO LEU PRO          
SEQRES   4 A  282  PHE ASN LYS ALA LEU GLY ARG TYR ASP VAL ALA ILE ILE          
SEQRES   5 A  282  ARG PRO VAL SER MET TYR ARG ALA LEU TYR SER SER ALA          
SEQRES   6 A  282  VAL LEU GLU ALA ALA GLY VAL HIS THR ILE ASN SER SER          
SEQRES   7 A  282  ASP VAL ILE ASN VAL CYS GLY ASP LYS ILE LEU THR TYR          
SEQRES   8 A  282  SER LYS LEU TYR ARG GLU GLY ILE PRO ILE PRO ASP SER          
SEQRES   9 A  282  ILE ILE ALA LEU SER ALA GLU ALA ALA LEU LYS ALA TYR          
SEQRES  10 A  282  GLU GLN ARG GLY PHE PRO LEU ILE ASP LYS PRO PRO ILE          
SEQRES  11 A  282  GLY SER TRP GLY ARG LEU VAL SER LEU ILE ARG ASP VAL          
SEQRES  12 A  282  PHE GLU GLY LYS THR ILE ILE GLU HIS ARG GLU LEU MET          
SEQRES  13 A  282  GLY ASN SER ALA LEU LYS ALA HIS ILE VAL GLN GLU TYR          
SEQRES  14 A  282  ILE GLN TYR LYS GLY ARG ASP ILE ARG CYS ILE ALA ILE          
SEQRES  15 A  282  GLY GLU GLU LEU LEU GLY CYS TYR ALA ARG ASN ILE PRO          
SEQRES  16 A  282  PRO ASN GLU TRP ARG ALA ASN VAL ALA LEU GLY GLY THR          
SEQRES  17 A  282  PRO SER ASN ILE GLU VAL ASP GLU LYS LEU LYS GLU THR          
SEQRES  18 A  282  VAL VAL LYS ALA VAL SER ILE VAL HIS GLY GLU PHE VAL          
SEQRES  19 A  282  SER ILE ASP ILE LEU GLU HIS PRO ASN LYS GLY TYR VAL          
SEQRES  20 A  282  VAL ASN GLU LEU ASN ASP VAL PRO GLU PHE LYS GLY PHE          
SEQRES  21 A  282  MET VAL ALA THR ASN ILE ASN VAL ALA GLN LYS LEU VAL          
SEQRES  22 A  282  GLU TYR ILE LYS GLU ASN TYR SER LYS                          
SEQRES   1 B  282  MET ARG VAL VAL LEU ILE VAL ASP ILE VAL ARG GLN GLU          
SEQRES   2 B  282  GLU LYS LEU ILE ALA LYS ALA LEU GLU GLU ASN LYS VAL          
SEQRES   3 B  282  GLN TYR ASP ILE ILE ASN VAL ALA GLN GLU PRO LEU PRO          
SEQRES   4 B  282  PHE ASN LYS ALA LEU GLY ARG TYR ASP VAL ALA ILE ILE          
SEQRES   5 B  282  ARG PRO VAL SER MET TYR ARG ALA LEU TYR SER SER ALA          
SEQRES   6 B  282  VAL LEU GLU ALA ALA GLY VAL HIS THR ILE ASN SER SER          
SEQRES   7 B  282  ASP VAL ILE ASN VAL CYS GLY ASP LYS ILE LEU THR TYR          
SEQRES   8 B  282  SER LYS LEU TYR ARG GLU GLY ILE PRO ILE PRO ASP SER          
SEQRES   9 B  282  ILE ILE ALA LEU SER ALA GLU ALA ALA LEU LYS ALA TYR          
SEQRES  10 B  282  GLU GLN ARG GLY PHE PRO LEU ILE ASP LYS PRO PRO ILE          
SEQRES  11 B  282  GLY SER TRP GLY ARG LEU VAL SER LEU ILE ARG ASP VAL          
SEQRES  12 B  282  PHE GLU GLY LYS THR ILE ILE GLU HIS ARG GLU LEU MET          
SEQRES  13 B  282  GLY ASN SER ALA LEU LYS ALA HIS ILE VAL GLN GLU TYR          
SEQRES  14 B  282  ILE GLN TYR LYS GLY ARG ASP ILE ARG CYS ILE ALA ILE          
SEQRES  15 B  282  GLY GLU GLU LEU LEU GLY CYS TYR ALA ARG ASN ILE PRO          
SEQRES  16 B  282  PRO ASN GLU TRP ARG ALA ASN VAL ALA LEU GLY GLY THR          
SEQRES  17 B  282  PRO SER ASN ILE GLU VAL ASP GLU LYS LEU LYS GLU THR          
SEQRES  18 B  282  VAL VAL LYS ALA VAL SER ILE VAL HIS GLY GLU PHE VAL          
SEQRES  19 B  282  SER ILE ASP ILE LEU GLU HIS PRO ASN LYS GLY TYR VAL          
SEQRES  20 B  282  VAL ASN GLU LEU ASN ASP VAL PRO GLU PHE LYS GLY PHE          
SEQRES  21 B  282  MET VAL ALA THR ASN ILE ASN VAL ALA GLN LYS LEU VAL          
SEQRES  22 B  282  GLU TYR ILE LYS GLU ASN TYR SER LYS                          
SEQRES   1 C  282  MET ARG VAL VAL LEU ILE VAL ASP ILE VAL ARG GLN GLU          
SEQRES   2 C  282  GLU LYS LEU ILE ALA LYS ALA LEU GLU GLU ASN LYS VAL          
SEQRES   3 C  282  GLN TYR ASP ILE ILE ASN VAL ALA GLN GLU PRO LEU PRO          
SEQRES   4 C  282  PHE ASN LYS ALA LEU GLY ARG TYR ASP VAL ALA ILE ILE          
SEQRES   5 C  282  ARG PRO VAL SER MET TYR ARG ALA LEU TYR SER SER ALA          
SEQRES   6 C  282  VAL LEU GLU ALA ALA GLY VAL HIS THR ILE ASN SER SER          
SEQRES   7 C  282  ASP VAL ILE ASN VAL CYS GLY ASP LYS ILE LEU THR TYR          
SEQRES   8 C  282  SER LYS LEU TYR ARG GLU GLY ILE PRO ILE PRO ASP SER          
SEQRES   9 C  282  ILE ILE ALA LEU SER ALA GLU ALA ALA LEU LYS ALA TYR          
SEQRES  10 C  282  GLU GLN ARG GLY PHE PRO LEU ILE ASP LYS PRO PRO ILE          
SEQRES  11 C  282  GLY SER TRP GLY ARG LEU VAL SER LEU ILE ARG ASP VAL          
SEQRES  12 C  282  PHE GLU GLY LYS THR ILE ILE GLU HIS ARG GLU LEU MET          
SEQRES  13 C  282  GLY ASN SER ALA LEU LYS ALA HIS ILE VAL GLN GLU TYR          
SEQRES  14 C  282  ILE GLN TYR LYS GLY ARG ASP ILE ARG CYS ILE ALA ILE          
SEQRES  15 C  282  GLY GLU GLU LEU LEU GLY CYS TYR ALA ARG ASN ILE PRO          
SEQRES  16 C  282  PRO ASN GLU TRP ARG ALA ASN VAL ALA LEU GLY GLY THR          
SEQRES  17 C  282  PRO SER ASN ILE GLU VAL ASP GLU LYS LEU LYS GLU THR          
SEQRES  18 C  282  VAL VAL LYS ALA VAL SER ILE VAL HIS GLY GLU PHE VAL          
SEQRES  19 C  282  SER ILE ASP ILE LEU GLU HIS PRO ASN LYS GLY TYR VAL          
SEQRES  20 C  282  VAL ASN GLU LEU ASN ASP VAL PRO GLU PHE LYS GLY PHE          
SEQRES  21 C  282  MET VAL ALA THR ASN ILE ASN VAL ALA GLN LYS LEU VAL          
SEQRES  22 C  282  GLU TYR ILE LYS GLU ASN TYR SER LYS                          
SEQRES   1 D  282  MET ARG VAL VAL LEU ILE VAL ASP ILE VAL ARG GLN GLU          
SEQRES   2 D  282  GLU LYS LEU ILE ALA LYS ALA LEU GLU GLU ASN LYS VAL          
SEQRES   3 D  282  GLN TYR ASP ILE ILE ASN VAL ALA GLN GLU PRO LEU PRO          
SEQRES   4 D  282  PHE ASN LYS ALA LEU GLY ARG TYR ASP VAL ALA ILE ILE          
SEQRES   5 D  282  ARG PRO VAL SER MET TYR ARG ALA LEU TYR SER SER ALA          
SEQRES   6 D  282  VAL LEU GLU ALA ALA GLY VAL HIS THR ILE ASN SER SER          
SEQRES   7 D  282  ASP VAL ILE ASN VAL CYS GLY ASP LYS ILE LEU THR TYR          
SEQRES   8 D  282  SER LYS LEU TYR ARG GLU GLY ILE PRO ILE PRO ASP SER          
SEQRES   9 D  282  ILE ILE ALA LEU SER ALA GLU ALA ALA LEU LYS ALA TYR          
SEQRES  10 D  282  GLU GLN ARG GLY PHE PRO LEU ILE ASP LYS PRO PRO ILE          
SEQRES  11 D  282  GLY SER TRP GLY ARG LEU VAL SER LEU ILE ARG ASP VAL          
SEQRES  12 D  282  PHE GLU GLY LYS THR ILE ILE GLU HIS ARG GLU LEU MET          
SEQRES  13 D  282  GLY ASN SER ALA LEU LYS ALA HIS ILE VAL GLN GLU TYR          
SEQRES  14 D  282  ILE GLN TYR LYS GLY ARG ASP ILE ARG CYS ILE ALA ILE          
SEQRES  15 D  282  GLY GLU GLU LEU LEU GLY CYS TYR ALA ARG ASN ILE PRO          
SEQRES  16 D  282  PRO ASN GLU TRP ARG ALA ASN VAL ALA LEU GLY GLY THR          
SEQRES  17 D  282  PRO SER ASN ILE GLU VAL ASP GLU LYS LEU LYS GLU THR          
SEQRES  18 D  282  VAL VAL LYS ALA VAL SER ILE VAL HIS GLY GLU PHE VAL          
SEQRES  19 D  282  SER ILE ASP ILE LEU GLU HIS PRO ASN LYS GLY TYR VAL          
SEQRES  20 D  282  VAL ASN GLU LEU ASN ASP VAL PRO GLU PHE LYS GLY PHE          
SEQRES  21 D  282  MET VAL ALA THR ASN ILE ASN VAL ALA GLN LYS LEU VAL          
SEQRES  22 D  282  GLU TYR ILE LYS GLU ASN TYR SER LYS                          
HET    ADP  A 500      27                                                       
HET    ADP  B 500      27                                                       
HET    ADP  C 500      27                                                       
HET    ADP  D 500      27                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   5  ADP    4(C10 H15 N5 O10 P2)                                         
FORMUL   9  HOH   *956(H2 O)                                                    
HELIX    1   1 ARG A   11  ASN A   24  1                                  14    
HELIX    2   2 LYS A   42  TYR A   47  5                                   6    
HELIX    3   3 SER A   56  ALA A   70  1                                  15    
HELIX    4   4 SER A   77  GLY A   85  1                                   9    
HELIX    5   5 ASP A   86  GLY A   98  1                                  13    
HELIX    6   6 SER A  109  GLY A  121  1                                  13    
HELIX    7   7 ASP A  142  LEU A  155  1                                  14    
HELIX    8   8 SER A  159  ALA A  163  5                                   5    
HELIX    9   9 ASP A  215  HIS A  230  1                                  16    
HELIX   10  10 PHE A  257  ASN A  265  1                                   9    
HELIX   11  11 ASN A  267  SER A  281  1                                  15    
HELIX   12  12 ARG B   11  ASN B   24  1                                  14    
HELIX   13  13 LYS B   42  TYR B   47  5                                   6    
HELIX   14  14 SER B   56  ALA B   70  1                                  15    
HELIX   15  15 SER B   77  GLY B   85  1                                   9    
HELIX   16  16 ASP B   86  GLY B   98  1                                  13    
HELIX   17  17 SER B  109  GLY B  121  1                                  13    
HELIX   18  18 ASP B  142  LEU B  155  1                                  14    
HELIX   19  19 ASN B  158  ALA B  163  5                                   6    
HELIX   20  20 ASP B  215  HIS B  230  1                                  16    
HELIX   21  21 PHE B  257  ASN B  265  1                                   9    
HELIX   22  22 ASN B  267  SER B  281  1                                  15    
HELIX   23  23 ARG C   11  ASN C   24  1                                  14    
HELIX   24  24 LYS C   42  TYR C   47  5                                   6    
HELIX   25  25 SER C   56  ALA C   70  1                                  15    
HELIX   26  26 SER C   77  GLY C   85  1                                   9    
HELIX   27  27 ASP C   86  GLY C   98  1                                  13    
HELIX   28  28 SER C  109  GLY C  121  1                                  13    
HELIX   29  29 ASP C  142  LEU C  155  1                                  14    
HELIX   30  30 SER C  159  ALA C  163  5                                   5    
HELIX   31  31 ASP C  215  HIS C  230  1                                  16    
HELIX   32  32 PHE C  257  ASN C  265  1                                   9    
HELIX   33  33 ASN C  267  SER C  281  1                                  15    
HELIX   34  34 ARG D   11  ASN D   24  1                                  14    
HELIX   35  35 LYS D   42  TYR D   47  5                                   6    
HELIX   36  36 SER D   56  ALA D   70  1                                  15    
HELIX   37  37 SER D   77  GLY D   85  1                                   9    
HELIX   38  38 ASP D   86  GLU D   97  1                                  12    
HELIX   39  39 SER D  109  GLY D  121  1                                  13    
HELIX   40  40 ASP D  142  LEU D  155  1                                  14    
HELIX   41  41 ASN D  158  ALA D  163  5                                   6    
HELIX   42  42 ASP D  215  VAL D  229  1                                  15    
HELIX   43  43 PHE D  257  ASN D  265  1                                   9    
HELIX   44  44 ASN D  267  SER D  281  1                                  15    
SHEET    1   A 4 GLN A  27  ASN A  32  0                                        
SHEET    2   A 4 ARG A   2  VAL A   7  1  N  LEU A   5   O  ASP A  29           
SHEET    3   A 4 VAL A  49  ILE A  52  1  O  ILE A  51   N  VAL A   4           
SHEET    4   A 4 HIS A  73  ILE A  75  1  O  ILE A  75   N  ALA A  50           
SHEET    1   B 5 LEU A  38  PRO A  39  0                                        
SHEET    2   B 5 SER B 104  ALA B 107 -1  O  ILE B 106   N  LEU A  38           
SHEET    3   B 5 HIS B 164  GLN B 167 -1  O  HIS B 164   N  ALA B 107           
SHEET    4   B 5 LEU B 124  LYS B 127 -1  N  ILE B 125   O  GLN B 167           
SHEET    5   B 5 SER B 138  ILE B 140 -1  O  SER B 138   N  ASP B 126           
SHEET    1   C 5 SER A 138  ILE A 140  0                                        
SHEET    2   C 5 LEU A 124  LYS A 127 -1  N  LEU A 124   O  ILE A 140           
SHEET    3   C 5 HIS A 164  GLU A 168 -1  O  GLN A 167   N  ILE A 125           
SHEET    4   C 5 SER A 104  ALA A 107 -1  N  ILE A 105   O  VAL A 166           
SHEET    5   C 5 LEU B  38  PRO B  39 -1  O  LEU B  38   N  ILE A 106           
SHEET    1   D 5 PRO A 209  ASN A 211  0                                        
SHEET    2   D 5 GLU A 185  ASN A 193 -1  N  ALA A 191   O  SER A 210           
SHEET    3   D 5 ARG A 175  ILE A 182 -1  N  ASP A 176   O  ARG A 192           
SHEET    4   D 5 PHE A 233  HIS A 241 -1  O  ILE A 238   N  ILE A 177           
SHEET    5   D 5 GLY A 245  ASN A 252 -1  O  ASN A 249   N  ASP A 237           
SHEET    1   E 4 GLN B  27  ASN B  32  0                                        
SHEET    2   E 4 ARG B   2  VAL B   7  1  N  LEU B   5   O  ASP B  29           
SHEET    3   E 4 VAL B  49  ILE B  52  1  O  ILE B  51   N  VAL B   4           
SHEET    4   E 4 HIS B  73  ILE B  75  1  O  ILE B  75   N  ILE B  52           
SHEET    1   F 5 PRO B 209  ASN B 211  0                                        
SHEET    2   F 5 GLU B 185  ASN B 193 -1  N  ALA B 191   O  SER B 210           
SHEET    3   F 5 ARG B 175  ILE B 182 -1  N  ILE B 180   O  LEU B 187           
SHEET    4   F 5 PHE B 233  HIS B 241 -1  O  ILE B 238   N  ILE B 177           
SHEET    5   F 5 GLY B 245  ASN B 252 -1  O  GLU B 250   N  ASP B 237           
SHEET    1   G 4 GLN C  27  ASN C  32  0                                        
SHEET    2   G 4 ARG C   2  VAL C   7  1  N  LEU C   5   O  ASP C  29           
SHEET    3   G 4 VAL C  49  ILE C  52  1  O  ILE C  51   N  ILE C   6           
SHEET    4   G 4 HIS C  73  ILE C  75  1  O  ILE C  75   N  ILE C  52           
SHEET    1   H 5 LEU C  38  PRO C  39  0                                        
SHEET    2   H 5 SER D 104  ALA D 107 -1  O  ILE D 106   N  LEU C  38           
SHEET    3   H 5 HIS D 164  GLN D 167 -1  O  HIS D 164   N  ALA D 107           
SHEET    4   H 5 LEU D 124  LYS D 127 -1  N  ILE D 125   O  GLN D 167           
SHEET    5   H 5 SER D 138  ILE D 140 -1  O  SER D 138   N  ASP D 126           
SHEET    1   I 5 SER C 138  ILE C 140  0                                        
SHEET    2   I 5 LEU C 124  LYS C 127 -1  N  LEU C 124   O  ILE C 140           
SHEET    3   I 5 HIS C 164  GLU C 168 -1  O  GLN C 167   N  ILE C 125           
SHEET    4   I 5 SER C 104  ALA C 107 -1  N  ILE C 105   O  VAL C 166           
SHEET    5   I 5 LEU D  38  PRO D  39 -1  O  LEU D  38   N  ILE C 106           
SHEET    1   J 5 SER C 210  ASN C 211  0                                        
SHEET    2   J 5 GLU C 185  ASN C 193 -1  N  ALA C 191   O  SER C 210           
SHEET    3   J 5 ARG C 175  ILE C 182 -1  N  ASP C 176   O  ARG C 192           
SHEET    4   J 5 PHE C 233  HIS C 241 -1  O  ILE C 238   N  ILE C 177           
SHEET    5   J 5 GLY C 245  ASN C 252 -1  O  VAL C 247   N  LEU C 239           
SHEET    1   K 4 GLN D  27  ASN D  32  0                                        
SHEET    2   K 4 ARG D   2  VAL D   7  1  N  LEU D   5   O  ASP D  29           
SHEET    3   K 4 VAL D  49  ILE D  52  1  O  ILE D  51   N  VAL D   4           
SHEET    4   K 4 HIS D  73  ILE D  75  1  O  ILE D  75   N  ILE D  52           
SHEET    1   L 5 SER D 210  ASN D 211  0                                        
SHEET    2   L 5 GLU D 185  ASN D 193 -1  N  ALA D 191   O  SER D 210           
SHEET    3   L 5 ARG D 175  ILE D 182 -1  N  ILE D 180   O  LEU D 187           
SHEET    4   L 5 PHE D 233  HIS D 241 -1  O  ILE D 238   N  ILE D 177           
SHEET    5   L 5 GLY D 245  ASN D 252 -1  O  ASN D 249   N  ASP D 237           
SSBOND   1 CYS A  179    CYS A  189                          1555   1555  2.04  
SSBOND   2 CYS B  179    CYS B  189                          1555   1555  2.04  
SSBOND   3 CYS C  179    CYS C  189                          1555   1555  2.05  
SSBOND   4 CYS D  179    CYS D  189                          1555   1555  2.05  
CISPEP   1 ILE A   75    ASN A   76          0        -2.89                     
CISPEP   2 PHE A  122    PRO A  123          0         2.06                     
CISPEP   3 MET A  156    GLY A  157          0       -13.92                     
CISPEP   4 ASN A  202    VAL A  203          0       -16.95                     
CISPEP   5 ILE B   75    ASN B   76          0        -2.74                     
CISPEP   6 PHE B  122    PRO B  123          0         1.72                     
CISPEP   7 PRO B  196    ASN B  197          0        -4.71                     
CISPEP   8 ALA B  204    LEU B  205          0        -5.59                     
CISPEP   9 GLY B  207    THR B  208          0         7.10                     
CISPEP  10 ILE C   75    ASN C   76          0        -4.16                     
CISPEP  11 PHE C  122    PRO C  123          0         3.18                     
CISPEP  12 GLY C  131    SER C  132          0        -8.65                     
CISPEP  13 PRO C  196    ASN C  197          0        -6.00                     
CISPEP  14 ILE D   75    ASN D   76          0        -6.03                     
CISPEP  15 PHE D  122    PRO D  123          0         0.82                     
SITE     1 AC1 22 LYS A  87  ILE A 125  LYS A 127  SER A 132                    
SITE     2 AC1 22 TRP A 133  GLY A 134  VAL A 137  GLN A 167                    
SITE     3 AC1 22 GLU A 168  TYR A 169  ILE A 170  ASP A 176                    
SITE     4 AC1 22 ARG A 200  ALA A 201  ASN A 202  ASN A 249                    
SITE     5 AC1 22 GLU A 250  HOH A 601  HOH A 624  HOH A 714                    
SITE     6 AC1 22 HOH A 756  HOH A 823                                          
SITE     1 AC2 22 LYS B  87  ILE B 125  LYS B 127  SER B 132                    
SITE     2 AC2 22 TRP B 133  GLY B 134  VAL B 137  GLN B 167                    
SITE     3 AC2 22 GLU B 168  TYR B 169  ILE B 170  ASP B 176                    
SITE     4 AC2 22 ARG B 200  ALA B 201  ASN B 202  ASN B 249                    
SITE     5 AC2 22 GLU B 250  HOH B 620  HOH B 706  HOH B 725                    
SITE     6 AC2 22 HOH B 796  HOH B 810                                          
SITE     1 AC3 22 LYS C  87  ILE C 125  LYS C 127  GLY C 131                    
SITE     2 AC3 22 SER C 132  TRP C 133  GLY C 134  ARG C 135                    
SITE     3 AC3 22 VAL C 137  GLN C 167  GLU C 168  TYR C 169                    
SITE     4 AC3 22 ILE C 170  ASP C 176  ARG C 200  ALA C 201                    
SITE     5 AC3 22 ASN C 249  GLU C 250  HOH C 638  HOH C 659                    
SITE     6 AC3 22 HOH C 664  HOH C 705                                          
SITE     1 AC4 21 LYS D  87  ILE D 125  LYS D 127  SER D 132                    
SITE     2 AC4 21 TRP D 133  GLY D 134  VAL D 137  GLN D 167                    
SITE     3 AC4 21 GLU D 168  ILE D 170  ASP D 176  ARG D 200                    
SITE     4 AC4 21 ALA D 201  ASN D 202  ASN D 249  GLU D 250                    
SITE     5 AC4 21 HOH D 618  HOH D 667  HOH D 714  HOH D 760                    
SITE     6 AC4 21 HOH D 810                                                     
CRYST1   63.266   67.845   80.032  87.77  75.29  67.03 P 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      0.015806 -0.006700 -0.004613        0.00000                         
SCALE2      0.000000  0.016009  0.001084        0.00000                         
SCALE3      0.000000  0.000000  0.012948        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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