HEADER DNA BINDING PROTEIN 28-MAY-06 2H5X
TITLE RUVA FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOLLIDAY JUNCTION ATP-DEPENDENT DNA HELICASE RUVA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.6.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: RUVA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28
KEYWDS RECOMBINATION, RUVA, HOLLIDAY JUNCTION BINDING, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.PRABU,S.THAMOTHARAN,J.S.KHANDUJA,E.Z.ALIPIO,C.Y.KIM,G.S.WALDO,
AUTHOR 2 T.C.TERWILLIGER,B.SEGELKE,T.LEKIN,D.TOPPANI,L.W.HUNG,M.YU,E.BURSEY,
AUTHOR 3 K.MUNIYAPPA,N.R.CHANDRA,M.VIJAYAN
REVDAT 4 30-AUG-23 2H5X 1 REMARK
REVDAT 3 13-JUL-11 2H5X 1 VERSN
REVDAT 2 24-FEB-09 2H5X 1 VERSN
REVDAT 1 15-AUG-06 2H5X 0
JRNL AUTH J.R.PRABU,S.THAMOTHARAN,J.S.KHANDUJA,E.Z.ALIPIO,C.Y.KIM,
JRNL AUTH 2 G.S.WALDO,T.C.TERWILLIGER,B.SEGELKE,T.LEKIN,D.TOPPANI,
JRNL AUTH 3 L.W.HUNG,M.YU,E.BURSEY,K.MUNIYAPPA,N.R.CHANDRA,M.VIJAYAN
JRNL TITL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RUVA, A PROTEIN
JRNL TITL 2 INVOLVED IN RECOMBINATION.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 62 731 2006
JRNL REFN ESSN 1744-3091
JRNL PMID 16880543
JRNL DOI 10.1107/S1744309106024791
REMARK 2
REMARK 2 RESOLUTION. 2.70 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2661258.690
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 23897
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) : 0.233
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1157
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3634
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE : 0.3730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 189
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5265
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.28000
REMARK 3 B22 (A**2) : -7.28000
REMARK 3 B33 (A**2) : 14.55000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.44
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) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.57
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.370
REMARK 3 BOND ANGLES (DEGREES) : 3.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.670
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 48.40
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 2 : GOL_XPLOR_PAR.TXT
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : GOL_XPLOR_TOP.TXT
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MLF FUNCTION THROUGHOUT THE REFINEMENT
REMARK 4
REMARK 4 2H5X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000037969.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL, CYLINDRICALLY
REMARK 200 BENT, SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23937
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.90
REMARK 200 R MERGE FOR SHELL (I) : 0.51200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB 1BVS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN STOCK WAS BUFFERED IN 20 MM
REMARK 280 TRIS-HCL AT PH 8.0 WITH 100 MM SODIUM CHLORIDE AND 10 MM B-ME.
REMARK 280 0.1 M SODIUM SUCCINATE AT PH 5.5 AND 1.7 M AMMONIUM SULFATE WAS
REMARK 280 USED AS A PRECIPITANT, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 68.82100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 68.82100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 44.48500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 68.82100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 68.82100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.48500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 68.82100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 68.82100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 44.48500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 68.82100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 68.82100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 44.48500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A OCTAMER GENERATED FROM THE
REMARK 300 TETRAMER IN THE ASYMMETRIC UNIT BY THE FOLLOWING SYMMETRY
REMARK 300 OPERATION. SYMMETRY: Y,X,-Z+1
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: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 88.97000
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 ALA A 134
REMARK 465 ALA A 135
REMARK 465 THR A 136
REMARK 465 GLY A 137
REMARK 465 GLY A 138
REMARK 465 ALA A 139
REMARK 465 LEU A 140
REMARK 465 SER A 141
REMARK 465 THR A 142
REMARK 465 ASN A 143
REMARK 465 GLY A 144
REMARK 465 HIS A 145
REMARK 465 ARG A 196
REMARK 465 ALA B 135
REMARK 465 THR B 136
REMARK 465 GLY B 137
REMARK 465 GLY B 138
REMARK 465 ALA B 139
REMARK 465 LEU B 140
REMARK 465 SER B 141
REMARK 465 THR B 142
REMARK 465 ASN B 143
REMARK 465 GLY B 144
REMARK 465 HIS B 145
REMARK 465 ALA B 195
REMARK 465 ARG B 196
REMARK 465 ALA C 134
REMARK 465 ALA C 135
REMARK 465 THR C 136
REMARK 465 GLY C 137
REMARK 465 GLY C 138
REMARK 465 ALA C 139
REMARK 465 LEU C 140
REMARK 465 SER C 141
REMARK 465 THR C 142
REMARK 465 ASN C 143
REMARK 465 GLY C 144
REMARK 465 HIS C 145
REMARK 465 ALA C 195
REMARK 465 ARG C 196
REMARK 465 VAL D 133
REMARK 465 ALA D 134
REMARK 465 ALA D 135
REMARK 465 THR D 136
REMARK 465 GLY D 137
REMARK 465 GLY D 138
REMARK 465 ALA D 139
REMARK 465 LEU D 140
REMARK 465 SER D 141
REMARK 465 THR D 142
REMARK 465 ASN D 143
REMARK 465 GLY D 144
REMARK 465 HIS D 145
REMARK 465 ARG D 196
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 99 CG CD OE1 NE2
REMARK 470 LYS A 117 CG CD CE NZ
REMARK 470 ASP A 129 CG OD1 OD2
REMARK 470 ASP A 178 CG OD1 OD2
REMARK 470 LYS B 117 CG CD CE NZ
REMARK 470 VAL B 133 CG1 CG2
REMARK 470 LYS B 163 CG CD CE NZ
REMARK 470 ASP B 178 CG OD1 OD2
REMARK 470 LYS C 163 CG CD CE NZ
REMARK 470 THR C 180 OG1 CG2
REMARK 470 LYS C 194 CG CD CE NZ
REMARK 470 LYS D 117 CG CD CE NZ
REMARK 470 LYS D 163 CG CD CE NZ
REMARK 470 THR D 180 OG1 CG2
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 ASN A 105 90.79 -60.60
REMARK 500 LYS A 130 18.70 -141.12
REMARK 500 VAL A 147 -78.18 27.27
REMARK 500 ARG A 148 -73.84 -46.50
REMARK 500 LYS A 163 13.74 -64.37
REMARK 500 ASP A 178 -4.82 -44.29
REMARK 500 LYS A 194 96.50 47.77
REMARK 500 SER B 4 146.42 -171.42
REMARK 500 ALA B 13 -166.05 -111.66
REMARK 500 ASN B 105 65.78 -61.85
REMARK 500 ARG B 128 -52.29 170.93
REMARK 500 VAL B 133 -48.27 170.22
REMARK 500 VAL B 147 -34.09 -135.74
REMARK 500 HIS B 177 -86.71 12.06
REMARK 500 ALA B 179 -110.80 -137.27
REMARK 500 SER B 182 -72.29 -56.01
REMARK 500 THR C 37 1.13 -65.36
REMARK 500 LYS C 117 -89.18 -19.13
REMARK 500 ASP C 129 31.77 -70.62
REMARK 500 LYS C 130 64.22 -177.42
REMARK 500 VAL C 131 -46.07 -146.45
REMARK 500 VAL C 151 -34.73 -38.97
REMARK 500 ALA C 161 -110.90 -57.40
REMARK 500 ALA C 162 -48.71 -163.47
REMARK 500 HIS C 177 -69.70 -0.59
REMARK 500 ASP C 178 111.14 171.11
REMARK 500 ALA C 179 -159.54 -140.26
REMARK 500 THR C 180 139.98 -37.55
REMARK 500 THR D 37 3.67 -59.77
REMARK 500 ARG D 128 -54.71 -24.99
REMARK 500 LYS D 130 9.09 -55.17
REMARK 500 VAL D 147 -35.92 -136.48
REMARK 500 GLU D 167 -1.85 -58.55
REMARK 500 HIS D 177 -66.12 -92.03
REMARK 500 ASP D 178 94.09 -68.83
REMARK 500 LYS D 194 -141.38 -45.09
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 GOL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 504
DBREF 2H5X A 1 196 UNP P66744 RUVA_MYCTU 1 196
DBREF 2H5X B 1 196 UNP P66744 RUVA_MYCTU 1 196
DBREF 2H5X C 1 196 UNP P66744 RUVA_MYCTU 1 196
DBREF 2H5X D 1 196 UNP P66744 RUVA_MYCTU 1 196
SEQRES 1 A 196 MET ILE ALA SER VAL ARG GLY GLU VAL LEU GLU VAL ALA
SEQRES 2 A 196 LEU ASP HIS VAL VAL ILE GLU ALA ALA GLY VAL GLY TYR
SEQRES 3 A 196 ARG VAL ASN ALA THR PRO ALA THR LEU ALA THR LEU ARG
SEQRES 4 A 196 GLN GLY THR GLU ALA ARG LEU ILE THR ALA MET ILE VAL
SEQRES 5 A 196 ARG GLU ASP SER MET THR LEU TYR GLY PHE PRO ASP GLY
SEQRES 6 A 196 GLU THR ARG ASP LEU PHE LEU THR LEU LEU SER VAL SER
SEQRES 7 A 196 GLY VAL GLY PRO ARG LEU ALA MET ALA ALA LEU ALA VAL
SEQRES 8 A 196 HIS ASP ALA PRO ALA LEU ARG GLN VAL LEU ALA ASP GLY
SEQRES 9 A 196 ASN VAL ALA ALA LEU THR ARG VAL PRO GLY ILE GLY LYS
SEQRES 10 A 196 ARG GLY ALA GLU ARG MET VAL LEU GLU LEU ARG ASP LYS
SEQRES 11 A 196 VAL GLY VAL ALA ALA THR GLY GLY ALA LEU SER THR ASN
SEQRES 12 A 196 GLY HIS ALA VAL ARG SER PRO VAL VAL GLU ALA LEU VAL
SEQRES 13 A 196 GLY LEU GLY PHE ALA ALA LYS GLN ALA GLU GLU ALA THR
SEQRES 14 A 196 ASP THR VAL LEU ALA ALA ASN HIS ASP ALA THR THR SER
SEQRES 15 A 196 SER ALA LEU ARG SER ALA LEU SER LEU LEU GLY LYS ALA
SEQRES 16 A 196 ARG
SEQRES 1 B 196 MET ILE ALA SER VAL ARG GLY GLU VAL LEU GLU VAL ALA
SEQRES 2 B 196 LEU ASP HIS VAL VAL ILE GLU ALA ALA GLY VAL GLY TYR
SEQRES 3 B 196 ARG VAL ASN ALA THR PRO ALA THR LEU ALA THR LEU ARG
SEQRES 4 B 196 GLN GLY THR GLU ALA ARG LEU ILE THR ALA MET ILE VAL
SEQRES 5 B 196 ARG GLU ASP SER MET THR LEU TYR GLY PHE PRO ASP GLY
SEQRES 6 B 196 GLU THR ARG ASP LEU PHE LEU THR LEU LEU SER VAL SER
SEQRES 7 B 196 GLY VAL GLY PRO ARG LEU ALA MET ALA ALA LEU ALA VAL
SEQRES 8 B 196 HIS ASP ALA PRO ALA LEU ARG GLN VAL LEU ALA ASP GLY
SEQRES 9 B 196 ASN VAL ALA ALA LEU THR ARG VAL PRO GLY ILE GLY LYS
SEQRES 10 B 196 ARG GLY ALA GLU ARG MET VAL LEU GLU LEU ARG ASP LYS
SEQRES 11 B 196 VAL GLY VAL ALA ALA THR GLY GLY ALA LEU SER THR ASN
SEQRES 12 B 196 GLY HIS ALA VAL ARG SER PRO VAL VAL GLU ALA LEU VAL
SEQRES 13 B 196 GLY LEU GLY PHE ALA ALA LYS GLN ALA GLU GLU ALA THR
SEQRES 14 B 196 ASP THR VAL LEU ALA ALA ASN HIS ASP ALA THR THR SER
SEQRES 15 B 196 SER ALA LEU ARG SER ALA LEU SER LEU LEU GLY LYS ALA
SEQRES 16 B 196 ARG
SEQRES 1 C 196 MET ILE ALA SER VAL ARG GLY GLU VAL LEU GLU VAL ALA
SEQRES 2 C 196 LEU ASP HIS VAL VAL ILE GLU ALA ALA GLY VAL GLY TYR
SEQRES 3 C 196 ARG VAL ASN ALA THR PRO ALA THR LEU ALA THR LEU ARG
SEQRES 4 C 196 GLN GLY THR GLU ALA ARG LEU ILE THR ALA MET ILE VAL
SEQRES 5 C 196 ARG GLU ASP SER MET THR LEU TYR GLY PHE PRO ASP GLY
SEQRES 6 C 196 GLU THR ARG ASP LEU PHE LEU THR LEU LEU SER VAL SER
SEQRES 7 C 196 GLY VAL GLY PRO ARG LEU ALA MET ALA ALA LEU ALA VAL
SEQRES 8 C 196 HIS ASP ALA PRO ALA LEU ARG GLN VAL LEU ALA ASP GLY
SEQRES 9 C 196 ASN VAL ALA ALA LEU THR ARG VAL PRO GLY ILE GLY LYS
SEQRES 10 C 196 ARG GLY ALA GLU ARG MET VAL LEU GLU LEU ARG ASP LYS
SEQRES 11 C 196 VAL GLY VAL ALA ALA THR GLY GLY ALA LEU SER THR ASN
SEQRES 12 C 196 GLY HIS ALA VAL ARG SER PRO VAL VAL GLU ALA LEU VAL
SEQRES 13 C 196 GLY LEU GLY PHE ALA ALA LYS GLN ALA GLU GLU ALA THR
SEQRES 14 C 196 ASP THR VAL LEU ALA ALA ASN HIS ASP ALA THR THR SER
SEQRES 15 C 196 SER ALA LEU ARG SER ALA LEU SER LEU LEU GLY LYS ALA
SEQRES 16 C 196 ARG
SEQRES 1 D 196 MET ILE ALA SER VAL ARG GLY GLU VAL LEU GLU VAL ALA
SEQRES 2 D 196 LEU ASP HIS VAL VAL ILE GLU ALA ALA GLY VAL GLY TYR
SEQRES 3 D 196 ARG VAL ASN ALA THR PRO ALA THR LEU ALA THR LEU ARG
SEQRES 4 D 196 GLN GLY THR GLU ALA ARG LEU ILE THR ALA MET ILE VAL
SEQRES 5 D 196 ARG GLU ASP SER MET THR LEU TYR GLY PHE PRO ASP GLY
SEQRES 6 D 196 GLU THR ARG ASP LEU PHE LEU THR LEU LEU SER VAL SER
SEQRES 7 D 196 GLY VAL GLY PRO ARG LEU ALA MET ALA ALA LEU ALA VAL
SEQRES 8 D 196 HIS ASP ALA PRO ALA LEU ARG GLN VAL LEU ALA ASP GLY
SEQRES 9 D 196 ASN VAL ALA ALA LEU THR ARG VAL PRO GLY ILE GLY LYS
SEQRES 10 D 196 ARG GLY ALA GLU ARG MET VAL LEU GLU LEU ARG ASP LYS
SEQRES 11 D 196 VAL GLY VAL ALA ALA THR GLY GLY ALA LEU SER THR ASN
SEQRES 12 D 196 GLY HIS ALA VAL ARG SER PRO VAL VAL GLU ALA LEU VAL
SEQRES 13 D 196 GLY LEU GLY PHE ALA ALA LYS GLN ALA GLU GLU ALA THR
SEQRES 14 D 196 ASP THR VAL LEU ALA ALA ASN HIS ASP ALA THR THR SER
SEQRES 15 D 196 SER ALA LEU ARG SER ALA LEU SER LEU LEU GLY LYS ALA
SEQRES 16 D 196 ARG
HET GOL A 501 6
HET GOL B 502 6
HET GOL C 503 6
HET GOL D 504 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 HOH *270(H2 O)
HELIX 1 1 THR A 31 THR A 37 1 7
HELIX 2 2 ASP A 64 SER A 76 1 13
HELIX 3 3 GLY A 81 HIS A 92 1 12
HELIX 4 4 ASP A 93 ASP A 103 1 11
HELIX 5 5 ASN A 105 VAL A 112 1 8
HELIX 6 6 GLY A 116 LEU A 127 1 12
HELIX 7 7 VAL A 147 LEU A 158 1 12
HELIX 8 8 ALA A 161 ASN A 176 1 16
HELIX 9 9 THR A 180 GLY A 193 1 14
HELIX 10 10 THR B 31 THR B 37 1 7
HELIX 11 11 ASP B 64 LEU B 75 1 12
HELIX 12 12 GLY B 81 HIS B 92 1 12
HELIX 13 13 ASP B 93 ASP B 103 1 11
HELIX 14 14 ASN B 105 VAL B 112 1 8
HELIX 15 15 GLY B 116 LEU B 127 1 12
HELIX 16 16 VAL B 147 LEU B 158 1 12
HELIX 17 17 ALA B 161 ASN B 176 1 16
HELIX 18 18 THR B 180 GLY B 193 1 14
HELIX 19 19 THR C 31 THR C 37 1 7
HELIX 20 20 ASP C 64 LEU C 75 1 12
HELIX 21 21 GLY C 81 HIS C 92 1 12
HELIX 22 22 ASP C 93 ASP C 103 1 11
HELIX 23 23 ASN C 105 THR C 110 1 6
HELIX 24 24 GLY C 116 ARG C 128 1 13
HELIX 25 25 ASP C 129 VAL C 131 5 3
HELIX 26 26 VAL C 147 LEU C 158 1 12
HELIX 27 27 ALA C 162 ASN C 176 1 15
HELIX 28 28 THR C 180 LYS C 194 1 15
HELIX 29 29 THR D 31 THR D 37 1 7
HELIX 30 30 ASP D 64 SER D 76 1 13
HELIX 31 31 GLY D 81 HIS D 92 1 12
HELIX 32 32 ASP D 93 ASP D 103 1 11
HELIX 33 33 ASN D 105 ARG D 111 1 7
HELIX 34 34 GLY D 116 ARG D 128 1 13
HELIX 35 35 VAL D 147 GLY D 157 1 11
HELIX 36 36 ALA D 161 ALA D 174 1 14
HELIX 37 37 THR D 180 GLY D 193 1 14
SHEET 1 A 7 VAL A 24 ASN A 29 0
SHEET 2 A 7 HIS A 16 ALA A 21 -1 N ALA A 21 O VAL A 24
SHEET 3 A 7 ILE A 2 VAL A 12 -1 N LEU A 10 O VAL A 18
SHEET 4 A 7 GLU A 43 ARG A 53 -1 O ALA A 44 N GLY A 7
SHEET 5 A 7 SER A 56 PHE A 62 -1 O THR A 58 N ILE A 51
SHEET 6 A 7 VAL A 24 ASN A 29 1 N ASN A 29 O LEU A 59
SHEET 7 A 7 ILE B 2 VAL B 12 -1 O ALA B 3 N GLY A 25
SHEET 1 B 7 VAL B 24 ASN B 29 0
SHEET 2 B 7 HIS B 16 ALA B 21 -1 N ILE B 19 O TYR B 26
SHEET 3 B 7 ILE B 2 VAL B 12 -1 N GLU B 8 O GLU B 20
SHEET 4 B 7 GLU B 43 ARG B 53 -1 O ALA B 44 N GLY B 7
SHEET 5 B 7 SER B 56 PHE B 62 -1 O SER B 56 N ARG B 53
SHEET 6 B 7 VAL B 24 ASN B 29 1 N ASN B 29 O GLY B 61
SHEET 7 B 7 ILE C 2 VAL C 12 -1 O ALA C 3 N GLY B 25
SHEET 1 C 7 VAL C 24 ASN C 29 0
SHEET 2 C 7 SER C 56 PHE C 62 1 O LEU C 59 N ASN C 29
SHEET 3 C 7 GLU C 43 ARG C 53 -1 N ILE C 51 O THR C 58
SHEET 4 C 7 ILE C 2 VAL C 12 -1 N ALA C 3 O THR C 48
SHEET 5 C 7 HIS C 16 ALA C 21 -1 O GLU C 20 N GLU C 8
SHEET 6 C 7 VAL C 24 ASN C 29 -1 O VAL C 28 N VAL C 17
SHEET 7 C 7 ILE D 2 VAL D 12 -1 O ALA D 3 N GLY C 25
SHEET 1 D 7 VAL D 24 ASN D 29 0
SHEET 2 D 7 HIS D 16 ALA D 21 -1 N VAL D 17 O VAL D 28
SHEET 3 D 7 ILE D 2 VAL D 12 -1 N GLU D 8 O GLU D 20
SHEET 4 D 7 GLU D 43 ARG D 53 -1 O ALA D 44 N GLY D 7
SHEET 5 D 7 SER D 56 PHE D 62 -1 O SER D 56 N ARG D 53
SHEET 6 D 7 VAL D 24 ASN D 29 1 N ASN D 29 O GLY D 61
SHEET 7 D 7 ILE A 2 VAL A 12 -1 N SER A 4 O GLY D 25
SITE 1 AC1 5 GLY A 81 PRO A 82 ARG A 83 LEU A 84
SITE 2 AC1 5 HOH A 771
SITE 1 AC2 5 GLY B 79 GLY B 81 PRO B 82 ARG B 83
SITE 2 AC2 5 LEU B 84
SITE 1 AC3 4 GLY C 81 ARG C 83 LEU C 84 HOH C 709
SITE 1 AC4 4 GLY D 81 PRO D 82 ARG D 83 LEU D 84
CRYST1 137.642 137.642 88.970 90.00 90.00 90.00 P 42 21 2 32
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 0.007265 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007265 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011240 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
