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Database: PDB
Entry: 3VPD
LinkDB: 3VPD
Original site: 3VPD 
HEADER    LIGASE                                  29-FEB-12   3VPD              
TITLE     LYSX FROM THERMUS THERMOPHILUS COMPLEXED WITH AMP-PNP                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN;                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TTLYSX, RIMK;                                               
COMPND   5 EC: 6.3.2.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   3 ORGANISM_TAXID: 274;                                                 
SOURCE   4 GENE: LYSX, RIMK;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21CODONPLUS(DE3);                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-TTLYSX                                
KEYWDS    ATP-DEPENDENET AMINE/THIOL LIGASE FAMILY, ATP-DEPENDENET AMINE/THIOL  
KEYWDS   2 LIGASE, LIGASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.TOMITA,T.OUCHI,T.KUZUYAMA,M.NISHIYAMA                               
REVDAT   2   31-JUL-13 3VPD    1       JRNL                                     
REVDAT   1   27-FEB-13 3VPD    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.    1.95 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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 52342                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2800                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3846                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 199                          
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4236                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 87                                      
REMARK   3   SOLVENT ATOMS            : 418                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.143         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.390         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4433 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6029 ; 1.467 ; 1.999       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   554 ; 5.591 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   191 ;35.548 ;22.670       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   734 ;16.167 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;21.395 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   678 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3338 ; 0.006 ; 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):  2736 ; 0.873 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4386 ; 1.644 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1697 ; 2.471 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1639 ; 4.248 ; 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 3VPD 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 RCSB095333.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 7.5                                
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-NE3A                            
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                  : MIRROR                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55332                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
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     (%) : 99.7                               
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) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
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   (%): 60.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5% PEG 400, 1.0M AMMONIUM CITRATE,     
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       25.80767            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       51.61533            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       51.61533            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       25.80767            
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: 14600 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       25.80767            
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     ARG B   195                                                      
REMARK 465     SER B   196                                                      
REMARK 465     ALA B   197                                                      
REMARK 465     HIS B   198                                                      
REMARK 465     TRP B   199                                                      
REMARK 465     ILE B   200                                                      
REMARK 465     THR B   201                                                      
REMARK 465     ASN B   202                                                      
REMARK 465     THR B   203                                                      
REMARK 465     ALA B   204                                                      
REMARK 465     ARG B   205                                                      
REMARK 465     GLY B   206                                                      
REMARK 465     GLY B   207                                                      
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    MET A  37       76.96   -113.55                                   
REMARK 500    ARG A 205       30.72    -97.78                                   
REMARK 500    MET B  37       72.68   -114.32                                   
REMARK 500    PRO B 175       45.67    -80.78                                   
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 558        DISTANCE =  5.64 ANGSTROMS                       
REMARK 525    HOH A 559        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH A 587        DISTANCE =  7.38 ANGSTROMS                       
REMARK 525    HOH A 606        DISTANCE =  5.73 ANGSTROMS                       
REMARK 525    HOH A 617        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH B 559        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH B 570        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH B 572        DISTANCE =  7.65 ANGSTROMS                       
REMARK 525    HOH B 587        DISTANCE =  7.61 ANGSTROMS                       
REMARK 525    HOH B 588        DISTANCE =  7.33 ANGSTROMS                       
REMARK 525    HOH B 590        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH B 594        DISTANCE =  5.63 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BUA A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BUA B 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VPB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VPC   RELATED DB: PDB                                   
DBREF  3VPD A    1   281  UNP    O50144   O50144_THETH     1    281             
DBREF  3VPD B    1   281  UNP    O50144   O50144_THETH     1    281             
SEQRES   1 A  281  MET LEU ALA ILE LEU TYR ASP ARG ILE ARG PRO ASP GLU          
SEQRES   2 A  281  ARG MET LEU PHE GLU ARG ALA GLU ALA LEU GLY LEU PRO          
SEQRES   3 A  281  TYR LYS LYS VAL TYR VAL PRO ALA LEU PRO MET VAL LEU          
SEQRES   4 A  281  GLY GLU ARG PRO GLU ALA LEU GLU GLY VAL THR VAL ALA          
SEQRES   5 A  281  LEU GLU ARG CYS VAL SER GLN SER ARG GLY LEU ALA ALA          
SEQRES   6 A  281  ALA ARG TYR LEU THR ALA LEU GLY ILE PRO VAL VAL ASN          
SEQRES   7 A  281  ARG PRO GLU VAL ILE GLU ALA CYS GLY ASP LYS TRP ALA          
SEQRES   8 A  281  THR SER VAL ALA LEU ALA LYS ALA GLY LEU PRO GLN PRO          
SEQRES   9 A  281  LYS THR ALA LEU ALA THR ASP ARG GLU GLU ALA LEU ARG          
SEQRES  10 A  281  LEU MET GLU ALA PHE GLY TYR PRO VAL VAL LEU LYS PRO          
SEQRES  11 A  281  VAL ILE GLY SER TRP GLY ARG LEU LEU ALA LYS VAL THR          
SEQRES  12 A  281  ASP ARG ALA ALA ALA GLU ALA LEU LEU GLU HIS LYS GLU          
SEQRES  13 A  281  VAL LEU GLY GLY PHE GLN HIS GLN LEU PHE TYR ILE GLN          
SEQRES  14 A  281  GLU TYR VAL GLU LYS PRO GLY ARG ASP ILE ARG VAL PHE          
SEQRES  15 A  281  VAL VAL GLY GLU ARG ALA ILE ALA ALA ILE TYR ARG ARG          
SEQRES  16 A  281  SER ALA HIS TRP ILE THR ASN THR ALA ARG GLY GLY GLN          
SEQRES  17 A  281  ALA GLU ASN CYS PRO LEU THR GLU GLU ILE ALA ARG LEU          
SEQRES  18 A  281  SER VAL GLY ALA ALA GLU ALA VAL GLY GLY GLY VAL VAL          
SEQRES  19 A  281  ALA VAL ASP LEU PHE GLU SER GLU ARG GLY LEU LEU VAL          
SEQRES  20 A  281  ASN GLU VAL ASN HIS THR MET GLU PHE LYS ASN SER VAL          
SEQRES  21 A  281  HIS THR THR GLY VAL ASP ILE PRO GLY GLU ILE LEU ARG          
SEQRES  22 A  281  TYR ALA TRP GLU VAL ALA ARG GLY                              
SEQRES   1 B  281  MET LEU ALA ILE LEU TYR ASP ARG ILE ARG PRO ASP GLU          
SEQRES   2 B  281  ARG MET LEU PHE GLU ARG ALA GLU ALA LEU GLY LEU PRO          
SEQRES   3 B  281  TYR LYS LYS VAL TYR VAL PRO ALA LEU PRO MET VAL LEU          
SEQRES   4 B  281  GLY GLU ARG PRO GLU ALA LEU GLU GLY VAL THR VAL ALA          
SEQRES   5 B  281  LEU GLU ARG CYS VAL SER GLN SER ARG GLY LEU ALA ALA          
SEQRES   6 B  281  ALA ARG TYR LEU THR ALA LEU GLY ILE PRO VAL VAL ASN          
SEQRES   7 B  281  ARG PRO GLU VAL ILE GLU ALA CYS GLY ASP LYS TRP ALA          
SEQRES   8 B  281  THR SER VAL ALA LEU ALA LYS ALA GLY LEU PRO GLN PRO          
SEQRES   9 B  281  LYS THR ALA LEU ALA THR ASP ARG GLU GLU ALA LEU ARG          
SEQRES  10 B  281  LEU MET GLU ALA PHE GLY TYR PRO VAL VAL LEU LYS PRO          
SEQRES  11 B  281  VAL ILE GLY SER TRP GLY ARG LEU LEU ALA LYS VAL THR          
SEQRES  12 B  281  ASP ARG ALA ALA ALA GLU ALA LEU LEU GLU HIS LYS GLU          
SEQRES  13 B  281  VAL LEU GLY GLY PHE GLN HIS GLN LEU PHE TYR ILE GLN          
SEQRES  14 B  281  GLU TYR VAL GLU LYS PRO GLY ARG ASP ILE ARG VAL PHE          
SEQRES  15 B  281  VAL VAL GLY GLU ARG ALA ILE ALA ALA ILE TYR ARG ARG          
SEQRES  16 B  281  SER ALA HIS TRP ILE THR ASN THR ALA ARG GLY GLY GLN          
SEQRES  17 B  281  ALA GLU ASN CYS PRO LEU THR GLU GLU ILE ALA ARG LEU          
SEQRES  18 B  281  SER VAL GLY ALA ALA GLU ALA VAL GLY GLY GLY VAL VAL          
SEQRES  19 B  281  ALA VAL ASP LEU PHE GLU SER GLU ARG GLY LEU LEU VAL          
SEQRES  20 B  281  ASN GLU VAL ASN HIS THR MET GLU PHE LYS ASN SER VAL          
SEQRES  21 B  281  HIS THR THR GLY VAL ASP ILE PRO GLY GLU ILE LEU ARG          
SEQRES  22 B  281  TYR ALA TRP GLU VAL ALA ARG GLY                              
HET    ANP  A 301      31                                                       
HET    BUA  A 302       6                                                       
HET    CIT  A 303      13                                                       
HET    ANP  B 301      31                                                       
HET    BUA  B 302       6                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     BUA BUTANOIC ACID                                                    
HETNAM     CIT CITRIC ACID                                                      
FORMUL   3  ANP    2(C10 H17 N6 O12 P3)                                         
FORMUL   4  BUA    2(C4 H8 O2)                                                  
FORMUL   5  CIT    C6 H8 O7                                                     
FORMUL   8  HOH   *418(H2 O)                                                    
HELIX    1   1 ARG A   10  LEU A   23  1                                  14    
HELIX    2   2 PRO A   33  LEU A   35  5                                   3    
HELIX    3   3 PRO A   43  GLU A   47  5                                   5    
HELIX    4   4 SER A   58  LEU A   72  1                                  15    
HELIX    5   5 ARG A   79  ASP A   88  1                                  10    
HELIX    6   6 ASP A   88  GLY A  100  1                                  13    
HELIX    7   7 ASP A  111  GLY A  123  1                                  13    
HELIX    8   8 ASP A  144  GLY A  159  1                                  16    
HELIX    9   9 GLY A  160  LEU A  165  5                                   6    
HELIX   10  10 ASN A  202  GLY A  206  5                                   5    
HELIX   11  11 THR A  215  VAL A  229  1                                  15    
HELIX   12  12 ASN A  258  GLY A  264  1                                   7    
HELIX   13  13 ASP A  266  VAL A  278  1                                  13    
HELIX   14  14 ARG B   10  GLY B   24  1                                  15    
HELIX   15  15 PRO B   33  LEU B   35  5                                   3    
HELIX   16  16 PRO B   43  GLU B   47  5                                   5    
HELIX   17  17 SER B   58  LEU B   72  1                                  15    
HELIX   18  18 ARG B   79  ASP B   88  1                                  10    
HELIX   19  19 ASP B   88  ALA B   99  1                                  12    
HELIX   20  20 ASP B  111  GLY B  123  1                                  13    
HELIX   21  21 ASP B  144  GLY B  159  1                                  16    
HELIX   22  22 GLY B  160  LEU B  165  5                                   6    
HELIX   23  23 THR B  215  VAL B  229  1                                  15    
HELIX   24  24 PHE B  256  GLY B  264  1                                   9    
HELIX   25  25 ASP B  266  ALA B  279  1                                  14    
SHEET    1   A 4 TYR A  27  TYR A  31  0                                        
SHEET    2   A 4 LEU A   2  TYR A   6  1  N  ILE A   4   O  VAL A  30           
SHEET    3   A 4 VAL A  51  GLU A  54  1  O  LEU A  53   N  ALA A   3           
SHEET    4   A 4 VAL A  76  VAL A  77  1  O  VAL A  77   N  GLU A  54           
SHEET    1   B 5 MET A  37  VAL A  38  0                                        
SHEET    2   B 5 THR B 106  ALA B 109 -1  O  LEU B 108   N  MET A  37           
SHEET    3   B 5 PHE B 166  GLU B 170 -1  O  PHE B 166   N  ALA B 109           
SHEET    4   B 5 VAL B 126  LYS B 129 -1  N  VAL B 127   O  GLN B 169           
SHEET    5   B 5 ALA B 140  VAL B 142 -1  O  VAL B 142   N  VAL B 126           
SHEET    1   C 5 ALA A 140  VAL A 142  0                                        
SHEET    2   C 5 VAL A 126  LYS A 129 -1  N  VAL A 126   O  VAL A 142           
SHEET    3   C 5 PHE A 166  GLU A 170 -1  O  GLN A 169   N  VAL A 127           
SHEET    4   C 5 THR A 106  ALA A 109 -1  N  ALA A 109   O  PHE A 166           
SHEET    5   C 5 MET B  37  VAL B  38 -1  O  MET B  37   N  LEU A 108           
SHEET    1   D 5 GLN A 208  ASN A 211  0                                        
SHEET    2   D 5 ARG A 187  ARG A 195 -1  N  TYR A 193   O  GLU A 210           
SHEET    3   D 5 ARG A 177  VAL A 184 -1  N  PHE A 182   O  ALA A 190           
SHEET    4   D 5 VAL A 233  SER A 241 -1  O  VAL A 236   N  VAL A 181           
SHEET    5   D 5 GLY A 244  ASN A 251 -1  O  ASN A 251   N  ALA A 235           
SHEET    1   E 4 TYR B  27  TYR B  31  0                                        
SHEET    2   E 4 LEU B   2  TYR B   6  1  N  ILE B   4   O  VAL B  30           
SHEET    3   E 4 VAL B  51  GLU B  54  1  O  LEU B  53   N  LEU B   5           
SHEET    4   E 4 VAL B  76  VAL B  77  1  O  VAL B  77   N  ALA B  52           
SHEET    1   F 5 GLU B 210  ASN B 211  0                                        
SHEET    2   F 5 ARG B 187  ARG B 194 -1  N  TYR B 193   O  GLU B 210           
SHEET    3   F 5 ASP B 178  VAL B 184 -1  N  VAL B 184   O  ARG B 187           
SHEET    4   F 5 VAL B 233  SER B 241 -1  O  VAL B 236   N  VAL B 181           
SHEET    5   F 5 GLY B 244  ASN B 251 -1  O  ASN B 248   N  ASP B 237           
CISPEP   1 VAL A   77    ASN A   78          0        -1.19                     
CISPEP   2 TYR A  124    PRO A  125          0        -3.45                     
CISPEP   3 VAL B   77    ASN B   78          0         0.30                     
CISPEP   4 TYR B  124    PRO B  125          0         3.92                     
CISPEP   5 SER B  134    TRP B  135          0        19.05                     
SITE     1 AC1 20 VAL A 127  LYS A 129  TRP A 135  GLY A 136                    
SITE     2 AC1 20 LEU A 139  GLN A 169  GLU A 170  VAL A 172                    
SITE     3 AC1 20 LYS A 174  ASP A 178  ARG A 180  ARG A 194                    
SITE     4 AC1 20 TRP A 199  ILE A 200  THR A 201  ASP A 237                    
SITE     5 AC1 20 PHE A 239  ASN A 248  GLU A 249  ASN A 251                    
SITE     1 AC2  6 THR A 203  PHE A 256  LYS A 257  ASN A 258                    
SITE     2 AC2  6 SER A 259  HOH A 608                                          
SITE     1 AC3  9 VAL A  57  SER A  58  GLN A  59  SER A  60                    
SITE     2 AC3  9 GLY A 133  TRP A 135  HOH A 585  HOH A 597                    
SITE     3 AC3  9 PHE B 161                                                     
SITE     1 AC4 17 VAL B 127  LYS B 129  GLN B 169  GLU B 170                    
SITE     2 AC4 17 TYR B 171  VAL B 172  LYS B 174  ASP B 178                    
SITE     3 AC4 17 ARG B 180  ARG B 194  PHE B 239  ASN B 248                    
SITE     4 AC4 17 GLU B 249  HOH B 426  HOH B 496  HOH B 532                    
SITE     5 AC4 17 HOH B 575                                                     
SITE     1 AC5  5 GLU B 255  PHE B 256  LYS B 257  ASN B 258                    
SITE     2 AC5  5 SER B 259                                                     
CRYST1  130.339  130.339   77.423  90.00  90.00 120.00 P 31 2 1     12          
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      0.007672  0.004430  0.000000        0.00000                         
SCALE2      0.000000  0.008859  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012916        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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