HEADER HYDROLASE 07-MAR-14 4PSA
TITLE MYCOBACTERIUM TUBERCULOSIS RECA GLYCEROL BOUND LOW TEMPERATURE
TITLE 2 STRUCTURE IIC-N1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN RECA, 1ST PART, 2ND PART;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RECOMBINASE A;
COMPND 5 EC: 3.1.-.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: MT2806, MTV002.02C, RECA, RV2737C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: KM4104;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PEJ135
KEYWDS HOMOLOGOUS RECOMBINATION, DNA REPAIR, ATPASE, RECOMBINASE, DNA
KEYWDS 2 BINDING PROTEIN, PLOOP CONTAINING NTPASE FOLD, ATP BINDING,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.V.CHANDRAN,J.R.PRABU,N.K.PATIL,K.MUNIYAPPA,M.VIJAYAN
REVDAT 3 08-NOV-23 4PSA 1 REMARK LINK
REVDAT 2 16-AUG-17 4PSA 1 SOURCE REMARK
REVDAT 1 18-MAR-15 4PSA 0
JRNL AUTH A.V.CHANDRAN,J.R.PRABU,A.NAUTIYAL,K.N.PATIL,K.MUNIYAPPA,
JRNL AUTH 2 M.VIJAYAN
JRNL TITL STRUCTURAL STUDIES ON MYCOBACTERIUM TUBERCULOSIS RECA:
JRNL TITL 2 MOLECULAR PLASTICITY AND INTERSPECIES VARIABILITY
JRNL REF J.BIOSCI. V. 40 13 2015
JRNL REFN ISSN 0250-4774
JRNL PMID 25740138
JRNL DOI 10.1007/S12038-014-9497-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.R.PRABU,G.P.MANJUNATH,N.R.CHANDRA,K.MUNIYAPPA,M.VIJAYAN
REMARK 1 TITL FUNCTIONALLY IMPORTANT MOVEMENTS IN RECA MOLECULES AND
REMARK 1 TITL 2 FILAMENTS: STUDIES INVOLVING MUTATION AND ENVIRONMENTAL
REMARK 1 TITL 3 CHANGES
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 64 1146 2008
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 19020353
REMARK 1 DOI 10.1107/S0907444908028448
REMARK 1 REFERENCE 2
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 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 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 5
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 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 12200
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1380
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) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 889
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2241
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 74
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.34000
REMARK 3 B22 (A**2) : -0.34000
REMARK 3 B33 (A**2) : 1.09000
REMARK 3 B12 (A**2) : -0.34000
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): 0.477
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.294
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.192
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.175
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2290 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2239 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3076 ; 0.982 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5127 ; 0.686 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 307 ; 5.089 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 88 ;32.754 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 380 ;16.197 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;20.134 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 359 ; 0.057 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2619 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 467 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4PSA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085157.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
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 : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54179
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13606
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 70.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 11.90
REMARK 200 R MERGE (I) : 0.15400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 11.20
REMARK 200 R MERGE FOR SHELL (I) : 0.85200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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: PDB ENTRY 1G19
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 10% PEG 5000 MME, 0.2M
REMARK 280 AMMONIUM ACETATE, 0.1M SODIUM CITRATE, PH 5.8, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
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 23.64333
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 47.28667
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 35.46500
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 59.10833
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 11.82167
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 THR A 2
REMARK 465 GLN A 3
REMARK 465 THR A 4
REMARK 465 MET A 160
REMARK 465 GLY A 161
REMARK 465 ASP A 162
REMARK 465 SER A 163
REMARK 465 ARG A 197
REMARK 465 ASP A 198
REMARK 465 LYS A 199
REMARK 465 ILE A 200
REMARK 465 GLY A 201
REMARK 465 VAL A 202
REMARK 465 MET A 203
REMARK 465 PHE A 204
REMARK 465 GLY A 205
REMARK 465 SER A 206
REMARK 465 PRO A 207
REMARK 465 GLU A 208
REMARK 465 GLY A 331
REMARK 465 ALA A 332
REMARK 465 VAL A 333
REMARK 465 VAL A 334
REMARK 465 THR A 335
REMARK 465 ASP A 336
REMARK 465 ASP A 337
REMARK 465 PRO A 338
REMARK 465 SER A 339
REMARK 465 ASN A 340
REMARK 465 ASP A 341
REMARK 465 GLY A 342
REMARK 465 VAL A 343
REMARK 465 LEU A 344
REMARK 465 PRO A 345
REMARK 465 ALA A 346
REMARK 465 PRO A 347
REMARK 465 VAL A 348
REMARK 465 ASP A 349
REMARK 465 PHE A 350
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 PRO A 5 CB CG CD
REMARK 470 GLU A 8 CG CD OE1 OE2
REMARK 470 LYS A 9 CG CD CE NZ
REMARK 470 GLU A 12 CG CD OE1 OE2
REMARK 470 LYS A 20 CG CD CE NZ
REMARK 470 LYS A 24 CG CD CE NZ
REMARK 470 ARG A 35 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 69 CG CD OE1 OE2
REMARK 470 ARG A 153 CZ NH1 NH2
REMARK 470 HIS A 164 CB CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 165 CB CG1 CG2
REMARK 470 THR A 210 OG1 CG2
REMARK 470 THR A 211 CB OG1 CG2
REMARK 470 LYS A 233 CG CD CE NZ
REMARK 470 THR A 236 OG1 CG2
REMARK 470 ASN A 237 CG OD1 ND2
REMARK 470 ARG A 286 NE CZ NH1 NH2
REMARK 470 LYS A 287 CE NZ
REMARK 470 LYS A 303 CG CD CE NZ
REMARK 470 ASN A 308 CG OD1 ND2
REMARK 470 LYS A 322 CG CD CE NZ
REMARK 470 ILE A 330 CG1 CG2 CD1
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 THR A 211 50.34 79.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 557 O
REMARK 620 2 HOH A 558 O 98.7
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 409
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OQF RELATED DB: PDB
REMARK 900 RELATED ID: 4PO1 RELATED DB: PDB
REMARK 900 RELATED ID: 4PO8 RELATED DB: PDB
REMARK 900 RELATED ID: 4PO9 RELATED DB: PDB
REMARK 900 RELATED ID: 4POA RELATED DB: PDB
REMARK 900 RELATED ID: 4PPF RELATED DB: PDB
REMARK 900 RELATED ID: 4PPG RELATED DB: PDB
REMARK 900 RELATED ID: 4PPN RELATED DB: PDB
REMARK 900 RELATED ID: 4PPQ RELATED DB: PDB
REMARK 900 RELATED ID: 4PQF RELATED DB: PDB
REMARK 900 RELATED ID: 4PQR RELATED DB: PDB
REMARK 900 RELATED ID: 4PQY RELATED DB: PDB
REMARK 900 RELATED ID: 4PR0 RELATED DB: PDB
REMARK 900 RELATED ID: 4PSK RELATED DB: PDB
REMARK 900 RELATED ID: 4PSV RELATED DB: PDB
REMARK 900 RELATED ID: 4PTL RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PROTEIN IS EXPRESSED AS A 790 AMINO ACID RESIDUE PRECURSOR
REMARK 999 (UNIPROT P0A5U4). ONCE IT IS RELEASED INTO THE CELL, THE CHAIN MTU
REMARK 999 RECA INTEIN (RESIDUES 252-691) IS CLEAVED OFF, CHAINS 1ST PART
REMARK 999 (RESIDUES 1-251) AND 2ND PART (RESIDUES 692-790) JOIN TOGETHER TO
REMARK 999 FORM THE MATURE PROTEIN.
DBREF 4PSA A 1 251 UNP P0A5U4 RECA_MYCTU 1 251
DBREF 4PSA A 252 350 UNP P0A5U4 RECA_MYCTU 692 790
SEQRES 1 A 350 MET THR GLN THR PRO ASP ARG GLU LYS ALA LEU GLU LEU
SEQRES 2 A 350 ALA VAL ALA GLN ILE GLU LYS SER TYR GLY LYS GLY SER
SEQRES 3 A 350 VAL MET ARG LEU GLY ASP GLU ALA ARG GLN PRO ILE SER
SEQRES 4 A 350 VAL ILE PRO THR GLY SER ILE ALA LEU ASP VAL ALA LEU
SEQRES 5 A 350 GLY ILE GLY GLY LEU PRO ARG GLY ARG VAL ILE GLU ILE
SEQRES 6 A 350 TYR GLY PRO GLU SER SER GLY LYS THR THR VAL ALA LEU
SEQRES 7 A 350 HIS ALA VAL ALA ASN ALA GLN ALA ALA GLY GLY VAL ALA
SEQRES 8 A 350 ALA PHE ILE ASP ALA GLU HIS ALA LEU ASP PRO ASP TYR
SEQRES 9 A 350 ALA LYS LYS LEU GLY VAL ASP THR ASP SER LEU LEU VAL
SEQRES 10 A 350 SER GLN PRO ASP THR GLY GLU GLN ALA LEU GLU ILE ALA
SEQRES 11 A 350 ASP MET LEU ILE ARG SER GLY ALA LEU ASP ILE VAL VAL
SEQRES 12 A 350 ILE ASP SER VAL ALA ALA LEU VAL PRO ARG ALA GLU LEU
SEQRES 13 A 350 GLU GLY GLU MET GLY ASP SER HIS VAL GLY LEU GLN ALA
SEQRES 14 A 350 ARG LEU MET SER GLN ALA LEU ARG LYS MET THR GLY ALA
SEQRES 15 A 350 LEU ASN ASN SER GLY THR THR ALA ILE PHE ILE ASN GLN
SEQRES 16 A 350 LEU ARG ASP LYS ILE GLY VAL MET PHE GLY SER PRO GLU
SEQRES 17 A 350 THR THR THR GLY GLY LYS ALA LEU LYS PHE TYR ALA SER
SEQRES 18 A 350 VAL ARG MET ASP VAL ARG ARG VAL GLU THR LEU LYS ASP
SEQRES 19 A 350 GLY THR ASN ALA VAL GLY ASN ARG THR ARG VAL LYS VAL
SEQRES 20 A 350 VAL LYS ASN LYS CYS SER PRO PRO PHE LYS GLN ALA GLU
SEQRES 21 A 350 PHE ASP ILE LEU TYR GLY LYS GLY ILE SER ARG GLU GLY
SEQRES 22 A 350 SER LEU ILE ASP MET GLY VAL ASP GLN GLY LEU ILE ARG
SEQRES 23 A 350 LYS SER GLY ALA TRP PHE THR TYR GLU GLY GLU GLN LEU
SEQRES 24 A 350 GLY GLN GLY LYS GLU ASN ALA ARG ASN PHE LEU VAL GLU
SEQRES 25 A 350 ASN ALA ASP VAL ALA ASP GLU ILE GLU LYS LYS ILE LYS
SEQRES 26 A 350 GLU LYS LEU GLY ILE GLY ALA VAL VAL THR ASP ASP PRO
SEQRES 27 A 350 SER ASN ASP GLY VAL LEU PRO ALA PRO VAL ASP PHE
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET NA A 404 1
HET EDO A 405 4
HET EDO A 406 4
HET GOL A 407 6
HET EDO A 408 4
HET EDO A 409 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 EDO 7(C2 H6 O2)
FORMUL 5 NA NA 1+
FORMUL 8 GOL C3 H8 O3
FORMUL 11 HOH *74(H2 O)
HELIX 1 1 PRO A 5 GLY A 23 1 19
HELIX 2 2 SER A 45 LEU A 52 1 8
HELIX 3 3 GLY A 72 ALA A 87 1 16
HELIX 4 4 ASP A 101 GLY A 109 1 9
HELIX 5 5 THR A 122 SER A 136 1 15
HELIX 6 6 PRO A 152 GLU A 157 1 6
HELIX 7 7 GLY A 166 GLY A 187 1 22
HELIX 8 8 GLY A 212 ALA A 220 1 9
HELIX 9 9 SER A 270 GLN A 282 1 13
HELIX 10 10 GLY A 302 ASN A 313 1 12
HELIX 11 11 ASN A 313 GLY A 329 1 17
SHEET 1 A 9 LEU A 116 SER A 118 0
SHEET 2 A 9 ALA A 91 ASP A 95 1 N ASP A 95 O SER A 118
SHEET 3 A 9 ILE A 141 ASP A 145 1 O VAL A 143 N ILE A 94
SHEET 4 A 9 THR A 189 GLN A 195 1 O ILE A 191 N ILE A 144
SHEET 5 A 9 VAL A 62 GLY A 67 1 N ILE A 63 O PHE A 192
SHEET 6 A 9 VAL A 222 ASP A 234 1 O VAL A 226 N TYR A 66
SHEET 7 A 9 ASN A 237 ASN A 250 -1 O LYS A 246 N ASP A 225
SHEET 8 A 9 GLN A 258 LEU A 264 -1 O PHE A 261 N THR A 243
SHEET 9 A 9 GLY A 268 ILE A 269 -1 O GLY A 268 N LEU A 264
SHEET 1 B 3 ARG A 286 SER A 288 0
SHEET 2 B 3 TRP A 291 TYR A 294 -1 O THR A 293 N ARG A 286
SHEET 3 B 3 GLU A 297 GLN A 301 -1 O LEU A 299 N PHE A 292
LINK NA NA A 404 O HOH A 557 1555 1555 2.62
LINK NA NA A 404 O HOH A 558 1555 1555 2.37
CISPEP 1 ASP A 145 SER A 146 0 -2.60
SITE 1 AC1 2 GLY A 166 ALA A 169
SITE 1 AC2 5 ASP A 121 PHE A 218 TYR A 219 LYS A 251
SITE 2 AC2 5 EDO A 406
SITE 1 AC3 7 PRO A 42 THR A 43 GLY A 44 ASP A 49
SITE 2 AC3 7 ARG A 271 GLU A 321 HOH A 533
SITE 1 AC4 3 ASP A 101 HOH A 557 HOH A 558
SITE 1 AC5 3 ARG A 7 ALA A 87 ASP A 140
SITE 1 AC6 4 GLU A 157 PHE A 218 TYR A 219 EDO A 402
SITE 1 AC7 8 SER A 70 SER A 71 GLY A 72 LYS A 73
SITE 2 AC7 8 THR A 74 THR A 75 HOH A 560 HOH A 574
SITE 1 AC8 3 ALA A 47 GLN A 258 EDO A 409
SITE 1 AC9 4 ALA A 47 ALA A 259 GLU A 260 EDO A 408
CRYST1 107.100 107.100 70.930 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 0.009337 0.005391 0.000000 0.00000
SCALE2 0.000000 0.010782 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014098 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
