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PDBsum entry 2rve

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Top Page protein dna_rna Protein-protein interface(s) links
Hydrolase/DNA PDB id
2rve
Jmol
Contents
Protein chains
213 a.a.
DNA/RNA
Waters ×68
HEADER    HYDROLASE/DNA                           19-MAR-91   2RVE
TITLE     THE CRYSTAL STRUCTURE OF ECORV ENDONUCLEASE AND OF ITS
TITLE    2 COMPLEXES WITH COGNATE AND NON-COGNATE DNA SEGMENTS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA (5'-D(*CP*GP*AP*GP*CP*TP*CP*G)-3');
COMPND   3 CHAIN: C, D, E, F;
COMPND   4 ENGINEERED: YES;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: PROTEIN (ECO RV (E.C.3.1.21.4));
COMPND   7 CHAIN: A, B;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 MOL_ID: 2;
SOURCE   4 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   5 ORGANISM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    PROTEIN-DNA COMPLEX, DOUBLE HELIX, HYDROLASE/DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    F.K.WINKLER,D.W.BANNER,C.OEFNER,D.TSERNOGLOU,R.S.BROWN,
AUTHOR   2 S.P.HEATHMAN,R.K.BRYAN,P.D.MARTIN,K.PETRATOS,K.S.WILSON
REVDAT   3   24-FEB-09 2RVE    1       VERSN
REVDAT   2   01-APR-03 2RVE    1       JRNL
REVDAT   1   15-JAN-92 2RVE    0
JRNL        AUTH   F.K.WINKLER,D.W.BANNER,C.OEFNER,D.TSERNOGLOU,
JRNL        AUTH 2 R.S.BROWN,S.P.HEATHMAN,R.K.BRYAN,P.D.MARTIN,
JRNL        AUTH 3 K.PETRATOS,K.S.WILSON
JRNL        TITL   THE CRYSTAL STRUCTURE OF ECORV ENDONUCLEASE AND OF
JRNL        TITL 2 ITS COMPLEXES WITH COGNATE AND NON-COGNATE DNA
JRNL        TITL 3 FRAGMENTS.
JRNL        REF    EMBO J.                       V.  12  1781 1993
JRNL        REFN                   ISSN 0261-4189
JRNL        PMID   8491171
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   F.K.WINKLER,A.D'ARCY,H.BLOECKER,R.FRANK,
REMARK   1  AUTH 2 J.H.VAN BOOM
REMARK   1  TITL   CRYSTALLIZATION OF COMPLEXES OF ECORV ENDONUCLEASE
REMARK   1  TITL 2 WITH COGNATE AND NON-COGNATE DNA FRAGMENTS
REMARK   1  REF    J.MOL.BIOL.                   V. 217   235 1991
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : TNT
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 11127
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178
REMARK   3   R VALUE            (WORKING SET) : NULL
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3528
REMARK   3   NUCLEIC ACID ATOMS       : 644
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 68
REMARK   3
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT
REMARK   3   BOND LENGTHS                 (A) : 0.014 ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : 1.740 ; NULL  ; NULL
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : NULL
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:  THE FOLLOWING PROTEIN SIDE CHAINS
REMARK   3  HAVE NO OR POORLY DEFINED DENSITY BUT HAVE NOT BEEN EXCLUDED
REMARK   3  FROM THIS ENTRY: A CHAIN: ASP 19, SER 35, LYS 67, LYS 85, LYS
REMARK   3  98, LYS 197, LYS 203, ASN 231 B CHAIN: GLU 27, LYS 85, LYS 164
REMARK   4
REMARK   4 2RVE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 6.00
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : ELLIOTT GX-21
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS-NICOLET X100
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12143
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
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   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.00, VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       39.80000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ASP A    13
REMARK 465     GLU A    14
REMARK 465     ASN A    15
REMARK 465     GLN A    16
REMARK 465     LYS A    17
REMARK 465     VAL A   141
REMARK 465     ALA A   142
REMARK 465     THR A   143
REMARK 465     ARG A   144
REMARK 465     LYS A   145
REMARK 465     SER A   146
REMARK 465     SER A   147
REMARK 465     LEU A   148
REMARK 465     LYS A   149
REMARK 465     GLY A   184
REMARK 465     ASN A   185
REMARK 465     THR A   186
REMARK 465     ARG A   221
REMARK 465     THR A   222
REMARK 465     SER A   223
REMARK 465     GLN A   224
REMARK 465     LEU A   225
REMARK 465     ARG A   226
REMARK 465     ASN A   227
REMARK 465     ASP A   228
REMARK 465     LYS A   229
REMARK 465     TYR A   241
REMARK 465     ARG A   242
REMARK 465     GLY A   243
REMARK 465     ARG A   244
REMARK 465     LYS A   245
REMARK 465     ASP B    13
REMARK 465     GLU B    14
REMARK 465     ASN B    15
REMARK 465     GLN B    16
REMARK 465     LYS B    17
REMARK 465     TYR B    18
REMARK 465     ASP B    19
REMARK 465     VAL B   141
REMARK 465     ALA B   142
REMARK 465     THR B   143
REMARK 465     ARG B   144
REMARK 465     LYS B   145
REMARK 465     SER B   146
REMARK 465     SER B   147
REMARK 465     LEU B   148
REMARK 465     LYS B   149
REMARK 465     GLY B   184
REMARK 465     ASN B   185
REMARK 465     THR B   186
REMARK 465     ARG B   221
REMARK 465     THR B   222
REMARK 465     SER B   223
REMARK 465     GLN B   224
REMARK 465     LEU B   225
REMARK 465     ARG B   226
REMARK 465     ASN B   227
REMARK 465     ASP B   228
REMARK 465     LYS B   229
REMARK 465     ARG B   242
REMARK 465     GLY B   243
REMARK 465     ARG B   244
REMARK 465     LYS B   245
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500     DC C   1   O3'    DC C   1   C3'    -0.038
REMARK 500     DC C   1   N1     DC C   1   C6     -0.042
REMARK 500     DA C   3   O3'    DA C   3   C3'    -0.056
REMARK 500     DC E   1   O3'    DC E   1   C3'    -0.057
REMARK 500     DC E   1   N1     DC E   1   C6     -0.040
REMARK 500     DG E   2   O3'    DG E   2   C3'    -0.038
REMARK 500     DC F   1   O3'    DC F   1   C3'    -0.037
REMARK 500     DA F   3   N3     DA F   3   C4     -0.037
REMARK 500     DC F   5   O3'    DC F   5   C3'    -0.052
REMARK 500    GLU A  27   CD    GLU A  27   OE2     0.069
REMARK 500    GLU A  45   CD    GLU A  45   OE2     0.072
REMARK 500    GLU A  57   CD    GLU A  57   OE2     0.079
REMARK 500    GLU A  82   CD    GLU A  82   OE2     0.067
REMARK 500    GLU A  99   CD    GLU A  99   OE2     0.068
REMARK 500    GLU A 158   CD    GLU A 158   OE2     0.080
REMARK 500    GLU A 201   CD    GLU A 201   OE2     0.070
REMARK 500    GLU B  27   CD    GLU B  27   OE2     0.077
REMARK 500    GLU B  45   CD    GLU B  45   OE2     0.066
REMARK 500    GLU B  57   CD    GLU B  57   OE2     0.071
REMARK 500    GLU B  64   CD    GLU B  64   OE2     0.075
REMARK 500    GLU B  65   CD    GLU B  65   OE2     0.071
REMARK 500    GLU B 101   CD    GLU B 101   OE2     0.070
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500     DC C   1   C6  -  N1  -  C1' ANGL. DEV. =   9.1 DEGREES
REMARK 500     DC C   1   C2  -  N1  -  C1' ANGL. DEV. = -10.7 DEGREES
REMARK 500     DG C   2   O4' -  C1' -  N9  ANGL. DEV. =   3.7 DEGREES
REMARK 500     DC D   1   C2  -  N1  -  C1' ANGL. DEV. =  -7.5 DEGREES
REMARK 500     DG D   4   O4' -  C1' -  C2' ANGL. DEV. =  -5.3 DEGREES
REMARK 500     DC D   7   O4' -  C1' -  N1  ANGL. DEV. =   4.6 DEGREES
REMARK 500     DC E   1   C6  -  N1  -  C1' ANGL. DEV. =  17.5 DEGREES
REMARK 500     DC E   1   C2  -  N1  -  C1' ANGL. DEV. = -19.2 DEGREES
REMARK 500     DG E   2   C8  -  N9  -  C1' ANGL. DEV. =  12.6 DEGREES
REMARK 500     DG E   2   C4  -  N9  -  C1' ANGL. DEV. = -12.7 DEGREES
REMARK 500     DC E   7   O4' -  C1' -  N1  ANGL. DEV. =   4.2 DEGREES
REMARK 500     DC F   1   C6  -  N1  -  C1' ANGL. DEV. =  13.3 DEGREES
REMARK 500     DC F   1   C2  -  N1  -  C1' ANGL. DEV. = -14.1 DEGREES
REMARK 500     DG F   2   O4' -  C1' -  C2' ANGL. DEV. =  -5.5 DEGREES
REMARK 500     DG F   4   P   -  O5' -  C5' ANGL. DEV. = -10.9 DEGREES
REMARK 500     DC F   5   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES
REMARK 500     DT F   6   C6  -  N1  -  C1' ANGL. DEV. =  10.8 DEGREES
REMARK 500     DT F   6   C2  -  N1  -  C1' ANGL. DEV. = -11.2 DEGREES
REMARK 500    ASP A   6   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP A  19   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ASP A 126   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ARG A 140   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ASP A 172   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP A 172   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    ASP A 179   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ASP A 198   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ASP A 207   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP A 207   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ASP A 214   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ASP B  36   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ASP B  74   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ASP B 172   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP B 198   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP B 198   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES
REMARK 500    ASP B 207   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    ASP B 210   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ASP B 214   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP B 214   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ALA A  26      -35.02    -39.29
REMARK 500    LEU A  33     -159.60    -90.23
REMARK 500    PHE A  44       -9.39    -59.30
REMARK 500    HIS A  59       17.66   -148.41
REMARK 500    ASN A  70       33.77     76.16
REMARK 500    PRO A  80      -38.59    -31.26
REMARK 500    LYS A  98     -162.94   -112.81
REMARK 500    LYS A 104      134.68   -171.87
REMARK 500    SER A 112     -126.42    -73.86
REMARK 500    ASN A 117      -28.72     69.43
REMARK 500    PHE A 125      -36.18    -31.33
REMARK 500    GLU A 155        4.26    -68.46
REMARK 500    TYR A 163      154.84    175.02
REMARK 500    HIS A 193       70.56   -113.26
REMARK 500    ALA A 194     -167.82   -117.56
REMARK 500    SER A 208      171.22    177.21
REMARK 500    TRP A 239        3.38    -55.34
REMARK 500    ASN B  70       45.96     74.17
REMARK 500    TYR B  78      139.41   -179.90
REMARK 500    GLU B  82       66.47   -106.09
REMARK 500    LYS B  85       63.09   -118.72
REMARK 500    ASN B 100       11.84     80.63
REMARK 500    LYS B 102       98.92    -68.66
REMARK 500    LEU B 107       54.41   -115.90
REMARK 500    SER B 112     -119.71    -88.81
REMARK 500    ASN B 117      -33.10     99.19
REMARK 500    ASP B 126       12.43    -68.28
REMARK 500    GLU B 155       43.19   -109.74
REMARK 500    ALA B 181      177.06    -57.16
REMARK 500    ALA B 194     -168.29   -122.68
REMARK 500    ASN B 231       33.05   -149.35
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 250        DISTANCE =  6.15 ANGSTROMS
DBREF  2RVE A    2   245  UNP    P04390   T2E5_ECOLI       1    244
DBREF  2RVE B    2   245  UNP    P04390   T2E5_ECOLI       1    244
DBREF  2RVE C    1     8  PDB    2RVE     2RVE             1      8
DBREF  2RVE D    1     8  PDB    2RVE     2RVE             1      8
DBREF  2RVE E    1     8  PDB    2RVE     2RVE             1      8
DBREF  2RVE F    1     8  PDB    2RVE     2RVE             1      8
SEQRES   1 C    8   DC  DG  DA  DG  DC  DT  DC  DG
SEQRES   1 D    8   DC  DG  DA  DG  DC  DT  DC  DG
SEQRES   1 E    8   DC  DG  DA  DG  DC  DT  DC  DG
SEQRES   1 F    8   DC  DG  DA  DG  DC  DT  DC  DG
SEQRES   1 A  244  SER LEU ARG SER ASP LEU ILE ASN ALA LEU TYR ASP GLU
SEQRES   2 A  244  ASN GLN LYS TYR ASP VAL CYS GLY ILE ILE SER ALA GLU
SEQRES   3 A  244  GLY LYS ILE TYR PRO LEU GLY SER ASP THR LYS VAL LEU
SEQRES   4 A  244  SER THR ILE PHE GLU LEU PHE SER ARG PRO ILE ILE ASN
SEQRES   5 A  244  LYS ILE ALA GLU LYS HIS GLY TYR ILE VAL GLU GLU PRO
SEQRES   6 A  244  LYS GLN GLN ASN HIS TYR PRO ASP PHE THR LEU TYR LYS
SEQRES   7 A  244  PRO SER GLU PRO ASN LYS LYS ILE ALA ILE ASP ILE LYS
SEQRES   8 A  244  THR THR TYR THR ASN LYS GLU ASN GLU LYS ILE LYS PHE
SEQRES   9 A  244  THR LEU GLY GLY TYR THR SER PHE ILE ARG ASN ASN THR
SEQRES  10 A  244  LYS ASN ILE VAL TYR PRO PHE ASP GLN TYR ILE ALA HIS
SEQRES  11 A  244  TRP ILE ILE GLY TYR VAL TYR THR ARG VAL ALA THR ARG
SEQRES  12 A  244  LYS SER SER LEU LYS THR TYR ASN ILE ASN GLU LEU ASN
SEQRES  13 A  244  GLU ILE PRO LYS PRO TYR LYS GLY VAL LYS VAL PHE LEU
SEQRES  14 A  244  GLN ASP LYS TRP VAL ILE ALA GLY ASP LEU ALA GLY SER
SEQRES  15 A  244  GLY ASN THR THR ASN ILE GLY SER ILE HIS ALA HIS TYR
SEQRES  16 A  244  LYS ASP PHE VAL GLU GLY LYS GLY ILE PHE ASP SER GLU
SEQRES  17 A  244  ASP GLU PHE LEU ASP TYR TRP ARG ASN TYR GLU ARG THR
SEQRES  18 A  244  SER GLN LEU ARG ASN ASP LYS TYR ASN ASN ILE SER GLU
SEQRES  19 A  244  TYR ARG ASN TRP ILE TYR ARG GLY ARG LYS
SEQRES   1 B  244  SER LEU ARG SER ASP LEU ILE ASN ALA LEU TYR ASP GLU
SEQRES   2 B  244  ASN GLN LYS TYR ASP VAL CYS GLY ILE ILE SER ALA GLU
SEQRES   3 B  244  GLY LYS ILE TYR PRO LEU GLY SER ASP THR LYS VAL LEU
SEQRES   4 B  244  SER THR ILE PHE GLU LEU PHE SER ARG PRO ILE ILE ASN
SEQRES   5 B  244  LYS ILE ALA GLU LYS HIS GLY TYR ILE VAL GLU GLU PRO
SEQRES   6 B  244  LYS GLN GLN ASN HIS TYR PRO ASP PHE THR LEU TYR LYS
SEQRES   7 B  244  PRO SER GLU PRO ASN LYS LYS ILE ALA ILE ASP ILE LYS
SEQRES   8 B  244  THR THR TYR THR ASN LYS GLU ASN GLU LYS ILE LYS PHE
SEQRES   9 B  244  THR LEU GLY GLY TYR THR SER PHE ILE ARG ASN ASN THR
SEQRES  10 B  244  LYS ASN ILE VAL TYR PRO PHE ASP GLN TYR ILE ALA HIS
SEQRES  11 B  244  TRP ILE ILE GLY TYR VAL TYR THR ARG VAL ALA THR ARG
SEQRES  12 B  244  LYS SER SER LEU LYS THR TYR ASN ILE ASN GLU LEU ASN
SEQRES  13 B  244  GLU ILE PRO LYS PRO TYR LYS GLY VAL LYS VAL PHE LEU
SEQRES  14 B  244  GLN ASP LYS TRP VAL ILE ALA GLY ASP LEU ALA GLY SER
SEQRES  15 B  244  GLY ASN THR THR ASN ILE GLY SER ILE HIS ALA HIS TYR
SEQRES  16 B  244  LYS ASP PHE VAL GLU GLY LYS GLY ILE PHE ASP SER GLU
SEQRES  17 B  244  ASP GLU PHE LEU ASP TYR TRP ARG ASN TYR GLU ARG THR
SEQRES  18 B  244  SER GLN LEU ARG ASN ASP LYS TYR ASN ASN ILE SER GLU
SEQRES  19 B  244  TYR ARG ASN TRP ILE TYR ARG GLY ARG LYS
FORMUL   7  HOH   *68(H2 O)
HELIX    1   1 SER A    2  TYR A   12  1                                  11
HELIX    2   2 LYS A   38  PHE A   47  1                                  10
HELIX    3   3 PHE A   47  LYS A   58  1                                  12
HELIX    4   4 SER A  112  ASN A  117  1                                   6
HELIX    5   5 PRO A  124  ASP A  126  5                                   3
HELIX    6   6 ASN A  154  ILE A  159  5                                   6
HELIX    7   7 LYS A  173  ILE A  176  1                                   4
HELIX    8   8 HIS A  195  GLY A  202  1                                   8
HELIX    9   9 SER A  208  ASN A  218  1                                  11
HELIX   10  10 ASN A  232  TRP A  239  1                                   8
HELIX   11  11 SER B    2  TYR B   12  1                                  11
HELIX   12  12 ASP B   36  HIS B   59  1                                  24
HELIX   13  13 PRO B  124  ASP B  126  5                                   3
HELIX   14  14 ASN B  154  ILE B  159  5                                   6
HELIX   15  15 LYS B  173  ALA B  177  1                                   5
HELIX   16  16 HIS B  195  GLY B  202  1                                   8
HELIX   17  17 SER B  208  TYR B  219  1                                  12
HELIX   18  18 ASN B  232  ILE B  240  1                                   9
SHEET    1   A 5 ILE A  30  PRO A  32  0
SHEET    2   A 5 VAL A  20  ILE A  24 -1  O  ILE A  23   N  TYR A  31
SHEET    3   A 5 ILE B  23  SER B  25 -1  O  ILE B  24   N  CYS A  21
SHEET    4   A 5 LYS B  29  TYR B  31 -1  O  LYS B  29   N  SER B  25
SHEET    5   A 5 TYR B 151  ASN B 152 -1  N  TYR B 151   O  ILE B  30
SHEET    1   B 5 ILE A  62  GLU A  64  0
SHEET    2   B 5 PHE A  75  LYS A  79 -1  O  THR A  76   N  GLU A  64
SHEET    3   B 5 GLU A  82  THR A  96 -1  N  GLU A  82   O  LYS A  79
SHEET    4   B 5 TYR A 128  THR A 139  1  N  ILE A 129   O  LYS A  86
SHEET    5   B 5 LYS A 164  ASP A 172 -1  N  LYS A 164   O  THR A 139
SHEET    1   C 3 THR A 106  GLY A 109  0
SHEET    2   C 3 ASN A 188  SER A 191 -1  N  ILE A 189   O  GLY A 108
SHEET    3   C 3 ALA A 177  ALA A 181 -1  N  GLY A 178   O  GLY A 190
SHEET    1   D 5 ILE B  62  GLU B  64  0
SHEET    2   D 5 PHE B  75  TYR B  78 -1  O  THR B  76   N  GLU B  64
SHEET    3   D 5 LYS B  86  THR B  96 -1  O  ILE B  87   N  LEU B  77
SHEET    4   D 5 TYR B 128  THR B 139  1  N  ILE B 129   O  LYS B  86
SHEET    5   D 5 LYS B 167  ASP B 172 -1  N  LYS B 167   O  VAL B 137
SHEET    1   E 2 THR B 106  GLY B 109  0
SHEET    2   E 2 ASN B 188  GLY B 190 -1  O  ILE B 189   N  LEU B 107
CISPEP   1 TYR A   72    PRO A   73          0        -0.28
CISPEP   2 TYR B   72    PRO B   73          0         2.61
CRYST1   68.500   79.600   66.400  90.00 104.60  90.00 P 1 21 1      8
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      0.014599  0.000000  0.003803        0.00000
SCALE2      0.000000  0.012563  0.000000        0.00000
SCALE3      0.000000  0.000000  0.015563        0.00000
      
PROCHECK
Go to PROCHECK summary
 References