HEADER RECOMBINATION 01-JAN-07 2OES
TITLE MSRECA-NATIVE-SSB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN RECA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RECOMBINASE A;
COMPND 5 EC: 3.4.99.37;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE 3 ORGANISM_TAXID: 1772;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JC10289;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTHIOA
KEYWDS RECOMBINATION, DNA-REPAIR, SOS RESPONCE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.KRISHNA,J.RAJAN PRABU,G.P.MANJUNATH,S.DATTA,N.R.CHANDRA,
AUTHOR 2 K.MUNIYAPPA,M.VIJAYAN
REVDAT 3 25-OCT-23 2OES 1 REMARK
REVDAT 2 24-FEB-09 2OES 1 VERSN
REVDAT 1 19-JUN-07 2OES 0
JRNL AUTH R.KRISHNA,J.R.PRABU,G.P.MANJUNATH,S.DATTA,N.R.CHANDRA,
JRNL AUTH 2 K.MUNIYAPPA,M.VIJAYAN
JRNL TITL SNAPSHOTS OF RECA PROTEIN INVOLVING MOVEMENT OF THE C-DOMAIN
JRNL TITL 2 AND DIFFERENT CONFORMATIONS OF THE DNA-BINDING LOOPS:
JRNL TITL 3 CRYSTALLOGRAPHIC AND COMPARATIVE ANALYSIS OF 11 STRUCTURES
JRNL TITL 4 OF MYCOBACTERIUM SMEGMATIS RECA
JRNL REF J.MOL.BIOL. V. 367 1130 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17306300
JRNL DOI 10.1016/J.JMB.2007.01.058
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.DATTA,M.M.PRABU,M.B.VAZE,N.GANESH,N.R.CHANDRA,K.MUNIYAPPA,
REMARK 1 AUTH 2 M.VIJAYAN
REMARK 1 TITL CRYSTAL STRUCTURES OF MYCOBACTERIUM TUBERCULOSIS RECA AND
REMARK 1 TITL 2 ITS COMPLEX WITH ADP-ALF(4): IMPLICATIONS FOR DECREASED
REMARK 1 TITL 3 ATPASE ACTIVITY AND MOLECULAR AGGREGATION
REMARK 1 REF NUCLEIC ACIDS RES. V. 28 4964 2000
REMARK 1 REFN ISSN 0305-1048
REMARK 1 PMID 11121488
REMARK 1 DOI 10.1093/NAR/28.24.4964
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.DATTA,N.GANESH,N.R.CHANDRA,K.MUNIYAPPA,M.VIJAYAN
REMARK 1 TITL STRUCTURAL STUDIES ON MTRECA-NUCLEOTIDE COMPLEXES: INSIGHTS
REMARK 1 TITL 2 INTO DNA AND NUCLEOTIDE BINDING AND THE STRUCTURAL SIGNATURE
REMARK 1 TITL 3 OF NTP RECOGNITION
REMARK 1 REF PROTEINS V. 50 474 2003
REMARK 1 REFN ISSN 0887-3585
REMARK 1 PMID 12557189
REMARK 1 DOI 10.1002/PROT.10315
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.DATTA,R.KRISHNA,N.GANESH,N.R.CHANDRA,K.MUNIYAPPA,M.VIJAYAN
REMARK 1 TITL CRYSTAL STRUCTURES OF MYCOBACTERIUM SMEGMATIS RECA AND ITS
REMARK 1 TITL 2 NUCLEOTIDE COMPLEXES
REMARK 1 REF J.BACTERIOL. V. 185 4280 2003
REMARK 1 REFN ISSN 0021-9193
REMARK 1 PMID 12837805
REMARK 1 DOI 10.1128/JB.185.14.4280-4284.2003
REMARK 1 REFERENCE 4
REMARK 1 AUTH R.KRISHNA,G.P.MANJUNATH,P.KUMAR,A.SUROLIA,N.R.CHANDRA,
REMARK 1 AUTH 2 K.MUNIYAPPA,M.VIJAYAN
REMARK 1 TITL CRYSTALLOGRAPHIC IDENTIFICATION OF AN ORDERED C-TERMINAL
REMARK 1 TITL 2 DOMAIN AND A SECOND NUCLEOTIDE-BINDING SITE IN RECA: NEW
REMARK 1 TITL 3 INSIGHTS INTO ALLOSTERY
REMARK 1 REF NUCLEIC ACIDS RES. V. 34 2186 2006
REMARK 1 REFN ISSN 0305-1048
REMARK 1 PMID 16648362
REMARK 1 DOI 10.1093/NAR/GKL107
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 704850.550
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 5286
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.600
REMARK 3 FREE R VALUE TEST SET COUNT : 562
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.012
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.72
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 723
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 12.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 101
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.036
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2293
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 31
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -21.22000
REMARK 3 B22 (A**2) : -21.22000
REMARK 3 B33 (A**2) : 42.45000
REMARK 3 B12 (A**2) : 1.86000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.62
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.49
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.79
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 2.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.520
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 11.720; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 17.140; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 16.710; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 22.760; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.20
REMARK 3 BSOL : 41.97
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 3 : PHOS.PARAM
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 3 : PHOS.TOP
REMARK 3 TOPOLOGY FILE 4 : WATER.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OES COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000041044.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5789
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 29.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.54200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1UBC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CITRATE PHOSPHATE, SODIUM CITRATE, PEG
REMARK 280 4000, NACL, PH 7.50, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 24.13333
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 48.26667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 36.20000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 60.33333
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 12.06667
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLN A 3
REMARK 465 ASP A 163
REMARK 465 GLY A 202
REMARK 465 VAL A 203
REMARK 465 MET A 204
REMARK 465 PHE A 205
REMARK 465 GLY A 206
REMARK 465 SER A 207
REMARK 465 PRO A 208
REMARK 465 ILE A 331
REMARK 465 GLY A 332
REMARK 465 ALA A 333
REMARK 465 VAL A 334
REMARK 465 VAL A 335
REMARK 465 THR A 336
REMARK 465 ALA A 337
REMARK 465 GLU A 338
REMARK 465 ALA A 339
REMARK 465 ASP A 340
REMARK 465 ASP A 341
REMARK 465 VAL A 342
REMARK 465 LEU A 343
REMARK 465 PRO A 344
REMARK 465 ALA A 345
REMARK 465 PRO A 346
REMARK 465 VAL A 347
REMARK 465 ASP A 348
REMARK 465 PHE A 349
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 4 CG CD OE1 NE2
REMARK 470 LYS A 10 CG CD CE NZ
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 ILE A 39 CG1 CG2 CD1
REMARK 470 GLU A 104 CG CD OE1 OE2
REMARK 470 LYS A 107 CG CD CE NZ
REMARK 470 ARG A 154 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 160 CG CD OE1 OE2
REMARK 470 MET A 161 CG SD CE
REMARK 470 SER A 164 OG
REMARK 470 HIS A 165 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 166 CG1 CG2
REMARK 470 ASN A 185 CG OD1 ND2
REMARK 470 LEU A 197 CG CD1 CD2
REMARK 470 ARG A 198 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 199 CG CD OE1 OE2
REMARK 470 LYS A 200 CG CD CE NZ
REMARK 470 ILE A 201 CG1 CG2 CD1
REMARK 470 GLU A 209 CG CD OE1 OE2
REMARK 470 THR A 210 OG1 CG2
REMARK 470 THR A 211 OG1 CG2
REMARK 470 LYS A 215 CG CD CE NZ
REMARK 470 LYS A 234 CG CD CE NZ
REMARK 470 ASP A 235 CG OD1 OD2
REMARK 470 LYS A 288 CG CD CE NZ
REMARK 470 GLU A 298 CG CD OE1 OE2
REMARK 470 LYS A 309 CG CD CE NZ
REMARK 470 LEU A 312 CG CD1 CD2
REMARK 470 LYS A 323 CG CD CE NZ
REMARK 470 LYS A 324 CG CD CE NZ
REMARK 470 ILE A 325 CG1 CG2 CD1
REMARK 470 LYS A 326 CG CD CE NZ
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 LYS A 200 CA LYS A 200 CB -0.241
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 PRO A 6 CA - CB - CG ANGL. DEV. = -13.4 DEGREES
REMARK 500 PRO A 6 CA - C - N ANGL. DEV. = -21.6 DEGREES
REMARK 500 ASP A 7 N - CA - C ANGL. DEV. = -23.4 DEGREES
REMARK 500 VAL A 166 N - CA - C ANGL. DEV. = 25.0 DEGREES
REMARK 500 GLU A 199 CA - C - N ANGL. DEV. = -15.4 DEGREES
REMARK 500 GLU A 199 O - C - N ANGL. DEV. = 13.6 DEGREES
REMARK 500 LYS A 200 C - N - CA ANGL. DEV. = 27.5 DEGREES
REMARK 500 LYS A 200 N - CA - C ANGL. DEV. = 19.8 DEGREES
REMARK 500 LYS A 200 CA - C - N ANGL. DEV. = -13.8 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 PRO A 6 59.98 15.37
REMARK 500 ASP A 7 -56.91 -124.41
REMARK 500 ARG A 8 -83.29 -40.84
REMARK 500 LYS A 25 -74.51 -63.57
REMARK 500 VAL A 35 153.75 -13.55
REMARK 500 ARG A 36 -175.32 59.41
REMARK 500 GLN A 37 86.45 157.17
REMARK 500 VAL A 41 130.06 154.23
REMARK 500 LYS A 74 -83.11 -6.90
REMARK 500 ALA A 87 0.44 -58.68
REMARK 500 HIS A 99 52.76 39.52
REMARK 500 ALA A 100 79.08 -152.39
REMARK 500 ASP A 112 67.47 -100.08
REMARK 500 ASP A 132 -60.21 -90.71
REMARK 500 SER A 147 95.76 83.67
REMARK 500 LEU A 151 59.62 -95.66
REMARK 500 ALA A 155 -82.43 -58.59
REMARK 500 ILE A 157 0.50 -69.59
REMARK 500 MET A 161 -22.77 117.12
REMARK 500 HIS A 165 -87.18 -106.75
REMARK 500 VAL A 166 -49.29 125.36
REMARK 500 GLN A 169 -74.14 -61.41
REMARK 500 ALA A 170 73.20 -61.41
REMARK 500 ARG A 171 -65.86 176.05
REMARK 500 ASN A 195 -169.52 -113.03
REMARK 500 GLN A 196 -153.46 -127.04
REMARK 500 LEU A 197 118.34 -162.17
REMARK 500 GLU A 199 -73.55 -162.62
REMARK 500 LYS A 200 -61.80 32.66
REMARK 500 THR A 210 -14.31 -28.73
REMARK 500 THR A 211 -175.17 173.13
REMARK 500 THR A 212 -36.07 -146.74
REMARK 500 LYS A 215 -58.60 0.35
REMARK 500 ALA A 216 -71.20 -60.46
REMARK 500 THR A 237 -74.51 -69.63
REMARK 500 ASP A 238 -37.47 -153.51
REMARK 500 ALA A 239 141.69 179.36
REMARK 500 LYS A 252 -2.86 -56.98
REMARK 500 GLN A 259 146.70 -176.54
REMARK 500 GLN A 268 -30.51 -135.77
REMARK 500 PHE A 285 -6.57 -57.31
REMARK 500 SER A 291 -13.86 82.74
REMARK 500 GLU A 296 95.10 -1.89
REMARK 500 LEU A 300 -78.79 -75.39
REMARK 500 ASP A 316 -77.94 -31.85
REMARK 500 LEU A 329 -51.73 -150.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 200 ILE A 201 135.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LYS A 200 16.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 350
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UBC RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH DATP AND ATPGS.
REMARK 900 RELATED ID: 2ODN RELATED DB: PDB
REMARK 900 RELATED ID: 2ODW RELATED DB: PDB
REMARK 900 RELATED ID: 2OE2 RELATED DB: PDB
REMARK 900 RELATED ID: 2OEP RELATED DB: PDB
REMARK 900 RELATED ID: 2OFO RELATED DB: PDB
DBREF 2OES A 1 349 UNP Q59560 RECA_MYCSM 1 349
SEQRES 1 A 349 MET ALA GLN GLN ALA PRO ASP ARG GLU LYS ALA LEU GLU
SEQRES 2 A 349 LEU ALA MET ALA GLN ILE ASP LYS ASN PHE GLY LYS GLY
SEQRES 3 A 349 SER VAL MET ARG LEU GLY GLU GLU VAL ARG GLN PRO ILE
SEQRES 4 A 349 SER VAL ILE PRO THR GLY SER ILE SER LEU ASP VAL ALA
SEQRES 5 A 349 LEU GLY ILE GLY GLY LEU PRO ARG GLY ARG VAL ILE GLU
SEQRES 6 A 349 ILE TYR GLY PRO GLU SER SER GLY LYS THR THR VAL ALA
SEQRES 7 A 349 LEU HIS ALA VAL ALA ASN ALA GLN ALA ALA GLY GLY ILE
SEQRES 8 A 349 ALA ALA PHE ILE ASP ALA GLU HIS ALA LEU ASP PRO GLU
SEQRES 9 A 349 TYR ALA LYS LYS LEU GLY VAL ASP THR ASP SER LEU LEU
SEQRES 10 A 349 VAL SER GLN PRO ASP THR GLY GLU GLN ALA LEU GLU ILE
SEQRES 11 A 349 ALA ASP MET LEU VAL ARG SER GLY ALA LEU ASP ILE ILE
SEQRES 12 A 349 VAL ILE ASP SER VAL ALA ALA LEU VAL PRO ARG ALA GLU
SEQRES 13 A 349 ILE GLU GLY GLU MET GLY ASP SER HIS VAL GLY LEU GLN
SEQRES 14 A 349 ALA ARG LEU MET SER GLN ALA LEU ARG LYS MET THR GLY
SEQRES 15 A 349 ALA LEU ASN ASN SER GLY THR THR ALA ILE PHE ILE ASN
SEQRES 16 A 349 GLN LEU ARG GLU LYS ILE GLY VAL MET PHE GLY SER PRO
SEQRES 17 A 349 GLU THR THR THR GLY GLY LYS ALA LEU LYS PHE TYR ALA
SEQRES 18 A 349 SER VAL ARG LEU ASP VAL ARG ARG ILE GLU THR LEU LYS
SEQRES 19 A 349 ASP GLY THR ASP ALA VAL GLY ASN ARG THR ARG VAL LYS
SEQRES 20 A 349 VAL VAL LYS ASN LYS VAL SER PRO PRO PHE LYS GLN ALA
SEQRES 21 A 349 GLU PHE ASP ILE LEU TYR GLY GLN GLY ILE SER ARG GLU
SEQRES 22 A 349 GLY SER LEU ILE ASP MET GLY VAL GLU HIS GLY PHE ILE
SEQRES 23 A 349 ARG LYS SER GLY SER TRP PHE THR TYR GLU GLY GLU GLN
SEQRES 24 A 349 LEU GLY GLN GLY LYS GLU ASN ALA ARG LYS PHE LEU LEU
SEQRES 25 A 349 GLU ASN THR ASP VAL ALA ASN GLU ILE GLU LYS LYS ILE
SEQRES 26 A 349 LYS GLU LYS LEU GLY ILE GLY ALA VAL VAL THR ALA GLU
SEQRES 27 A 349 ALA ASP ASP VAL LEU PRO ALA PRO VAL ASP PHE
HET PO4 A 350 5
HETNAM PO4 PHOSPHATE ION
FORMUL 2 PO4 O4 P 3-
FORMUL 3 HOH *31(H2 O)
HELIX 1 1 ASP A 7 GLY A 24 1 18
HELIX 2 2 LYS A 25 VAL A 28 5 4
HELIX 3 3 SER A 46 LEU A 53 1 8
HELIX 4 4 GLY A 73 ALA A 88 1 16
HELIX 5 5 ASP A 102 GLY A 110 1 9
HELIX 6 6 ASP A 112 LEU A 116 5 5
HELIX 7 7 THR A 123 SER A 137 1 15
HELIX 8 8 VAL A 148 LEU A 151 5 4
HELIX 9 9 LEU A 168 GLY A 188 1 21
HELIX 10 10 GLY A 214 ALA A 221 1 8
HELIX 11 11 SER A 271 HIS A 283 1 13
HELIX 12 12 GLY A 303 ASN A 314 1 12
HELIX 13 13 ASN A 314 LYS A 328 1 15
SHEET 1 A 9 LEU A 117 SER A 119 0
SHEET 2 A 9 ILE A 91 ASP A 96 1 N PHE A 94 O LEU A 117
SHEET 3 A 9 LEU A 140 ASP A 146 1 O ASP A 146 N ILE A 95
SHEET 4 A 9 THR A 190 ILE A 194 1 O ILE A 192 N ILE A 143
SHEET 5 A 9 VAL A 63 TYR A 67 1 N ILE A 64 O ALA A 191
SHEET 6 A 9 VAL A 223 GLU A 231 1 O LEU A 225 N GLU A 65
SHEET 7 A 9 GLY A 241 ASN A 251 -1 O ARG A 243 N GLU A 231
SHEET 8 A 9 GLN A 259 LEU A 265 -1 O PHE A 262 N THR A 244
SHEET 9 A 9 GLY A 269 ILE A 270 -1 O GLY A 269 N LEU A 265
SHEET 1 B 3 ILE A 286 LYS A 288 0
SHEET 2 B 3 TRP A 292 TYR A 295 -1 O THR A 294 N ARG A 287
SHEET 3 B 3 GLN A 299 GLN A 302 -1 O LEU A 300 N PHE A 293
SITE 1 AC1 5 SER A 71 SER A 72 GLY A 73 LYS A 74
SITE 2 AC1 5 THR A 75
CRYST1 103.672 103.672 72.400 90.00 90.00 120.00 P 61 6
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 0.009646 0.005569 0.000000 0.00000
SCALE2 0.000000 0.011138 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013812 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
