HEADER ISOMERASE/DNA 03-JUN-15 5BTF
TITLE CRYSTAL STRUCTURE OF A TOPOISOMERASE II COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA GYRASE SUBUNIT A;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: GYRA 2-500 WITH IGSG C-TERMINAL TAG;
COMPND 5 EC: 5.99.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA GYRASE SUBUNIT B;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: GYRB 426-675 WITH N-TERMINAL SNA TAG;
COMPND 12 EC: 5.99.1.3;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: DNA SUBSTRATE 24-MER GGTCATGAATGACTATGCACGTAA;
COMPND 16 CHAIN: E, H;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: DNA SUBSTRATE 24-MER TTACGTGCATAGTCATTCATGACC;
COMPND 20 CHAIN: F, G;
COMPND 21 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 GENE: GYRA, RV0006, MTCY10H4.04;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-28B;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 14 H37RV);
SOURCE 15 ORGANISM_TAXID: 83332;
SOURCE 16 STRAIN: ATCC 25618 / H37RV;
SOURCE 17 GENE: GYRB, RV0005, MTCY10H4.03;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 83332;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 PLYSS;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PET-28B;
SOURCE 23 MOL_ID: 3;
SOURCE 24 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 25 ORGANISM_TAXID: 32630;
SOURCE 26 EXPRESSION_SYSTEM: SYNTHETIC CONSTRUCT;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 32630;
SOURCE 28 MOL_ID: 4;
SOURCE 29 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 30 ORGANISM_TAXID: 32630;
SOURCE 31 EXPRESSION_SYSTEM: SYNTHETIC CONSTRUCT;
SOURCE 32 EXPRESSION_SYSTEM_TAXID: 32630
KEYWDS PROTEIN-DNA COMPLEX, TOPOISOMERASE II, ISOMERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.R.BLOWER,B.H.WILLIAMSON,R.J.KERNS,J.M.BERGER
REVDAT 5 15-NOV-23 5BTF 1 REMARK
REVDAT 4 27-SEP-23 5BTF 1 LINK
REVDAT 3 04-DEC-19 5BTF 1 REMARK
REVDAT 2 20-SEP-17 5BTF 1 JRNL REMARK
REVDAT 1 02-MAR-16 5BTF 0
JRNL AUTH T.R.BLOWER,B.H.WILLIAMSON,R.J.KERNS,J.M.BERGER
JRNL TITL CRYSTAL STRUCTURE AND STABILITY OF GYRASE-FLUOROQUINOLONE
JRNL TITL 2 CLEAVED COMPLEXES FROM MYCOBACTERIUM TUBERCULOSIS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 1706 2016
JRNL REFN ESSN 1091-6490
JRNL PMID 26792525
JRNL DOI 10.1073/PNAS.1525047113
REMARK 2
REMARK 2 RESOLUTION. 2.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.090
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 125149
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 6310
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.7848 - 8.0991 0.90 3799 210 0.1744 0.1980
REMARK 3 2 8.0991 - 6.4329 0.93 3925 185 0.1854 0.2317
REMARK 3 3 6.4329 - 5.6210 0.91 3871 205 0.1971 0.2579
REMARK 3 4 5.6210 - 5.1076 0.91 3874 188 0.1832 0.2094
REMARK 3 5 5.1076 - 4.7418 0.91 3835 177 0.1638 0.1966
REMARK 3 6 4.7418 - 4.4624 0.91 3849 214 0.1693 0.1920
REMARK 3 7 4.4624 - 4.2391 0.91 3782 238 0.1751 0.2063
REMARK 3 8 4.2391 - 4.0546 0.87 3681 200 0.1830 0.1982
REMARK 3 9 4.0546 - 3.8986 0.92 3848 212 0.2026 0.2339
REMARK 3 10 3.8986 - 3.7641 0.94 3974 219 0.2067 0.2627
REMARK 3 11 3.7641 - 3.6465 0.95 4005 178 0.2169 0.2419
REMARK 3 12 3.6465 - 3.5423 0.96 3999 229 0.2317 0.2498
REMARK 3 13 3.5423 - 3.4490 0.96 4055 230 0.2441 0.3004
REMARK 3 14 3.4490 - 3.3649 0.97 4046 226 0.2604 0.3020
REMARK 3 15 3.3649 - 3.2884 0.97 4168 186 0.2687 0.3519
REMARK 3 16 3.2884 - 3.2185 0.98 4078 226 0.2767 0.3277
REMARK 3 17 3.2185 - 3.1541 0.95 4051 208 0.3098 0.2915
REMARK 3 18 3.1541 - 3.0946 0.93 3882 233 0.3045 0.3421
REMARK 3 19 3.0946 - 3.0393 0.96 4013 225 0.3097 0.3323
REMARK 3 20 3.0393 - 2.9878 0.97 4081 186 0.3173 0.3216
REMARK 3 21 2.9878 - 2.9396 0.97 4143 240 0.3205 0.3376
REMARK 3 22 2.9396 - 2.8944 0.97 4036 235 0.3291 0.3532
REMARK 3 23 2.8944 - 2.8518 0.97 4112 230 0.3222 0.3338
REMARK 3 24 2.8518 - 2.8117 0.97 4044 231 0.3379 0.3872
REMARK 3 25 2.8117 - 2.7737 0.97 4053 198 0.3513 0.3633
REMARK 3 26 2.7737 - 2.7377 0.97 4196 179 0.3618 0.3723
REMARK 3 27 2.7377 - 2.7034 0.98 4091 204 0.3672 0.3924
REMARK 3 28 2.7034 - 2.6709 0.98 4202 198 0.3779 0.3727
REMARK 3 29 2.6709 - 2.6398 0.98 4074 210 0.3903 0.4202
REMARK 3 30 2.6398 - 2.6102 0.73 3072 210 0.4100 0.3903
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.470
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.650
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 13646
REMARK 3 ANGLE : 0.699 18761
REMARK 3 CHIRALITY : 0.030 2116
REMARK 3 PLANARITY : 0.003 2179
REMARK 3 DIHEDRAL : 15.478 5307
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 4
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 5824
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 2980
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN E
REMARK 3 SELECTION : CHAIN H
REMARK 3 ATOM PAIRS NUMBER : 408
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN F
REMARK 3 SELECTION : CHAIN G
REMARK 3 ATOM PAIRS NUMBER : 402
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5BTF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210515.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0 TO 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI 220 FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 224023
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.610
REMARK 200 RESOLUTION RANGE LOW (A) : 49.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.14490
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 1.06000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.860
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: 5BS8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, 13-15% PEG 4000, 200
REMARK 280 MM MGCL2, 6.25% PEG 400, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
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 42.00950
REMARK 290 SMTRY3 2 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 DOUBLE-STRANDED DNAS ARE SUPERPOSED COPIES OF EACH
REMARK 300 OTHER, OVERLAID IN OPPOSITE ORIENTATIONS (BECAUSE DIRECTIONALITY
REMARK 300 COULD NOT BE RESOLVED). THEREFORE IN REALITY, RATHER THAN IN THE
REMARK 300 MODEL, THE BIOLOGICAL ASSEMBLY WOULD IN FACT BE HEXAMERIC - FOUR
REMARK 300 PROTEINS AND ONE DOUBLE-STRANDED DNA.
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, E, F, G, H
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 THR A 2
REMARK 465 ASP A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 LEU A 6
REMARK 465 PRO A 7
REMARK 465 PRO A 8
REMARK 465 ASP A 9
REMARK 465 ASP A 10
REMARK 465 SER A 11
REMARK 465 LEU A 12
REMARK 465 ASP A 13
REMARK 465 ARG A 14
REMARK 465 GLY A 502
REMARK 465 SER A 503
REMARK 465 GLY A 504
REMARK 465 SER B 423
REMARK 465 ASN B 424
REMARK 465 SER B 431
REMARK 465 ALA B 432
REMARK 465 THR B 433
REMARK 465 ASP B 434
REMARK 465 ILE B 435
REMARK 465 GLY B 436
REMARK 465 THR C 2
REMARK 465 ASP C 3
REMARK 465 THR C 4
REMARK 465 THR C 5
REMARK 465 LEU C 6
REMARK 465 PRO C 7
REMARK 465 PRO C 8
REMARK 465 ASP C 9
REMARK 465 ASP C 10
REMARK 465 SER C 11
REMARK 465 LEU C 12
REMARK 465 ASP C 13
REMARK 465 ARG C 14
REMARK 465 GLY C 502
REMARK 465 SER C 503
REMARK 465 GLY C 504
REMARK 465 SER D 423
REMARK 465 ALA D 432
REMARK 465 THR D 433
REMARK 465 ASP D 434
REMARK 465 ILE D 435
REMARK 465 GLY D 436
REMARK 465 DG E 1
REMARK 465 DG E 2
REMARK 465 DA E 24
REMARK 465 DT F 1
REMARK 465 DT F 2
REMARK 465 DC F 24
REMARK 465 DT G 1
REMARK 465 DT G 2
REMARK 465 DC G 24
REMARK 465 DG H 1
REMARK 465 DG H 2
REMARK 465 DA H 24
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 DG E 11 P OP1 OP2 O5'
REMARK 470 DA E 23 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DA E 23 N9 C8 N7 C5 C6 N6 N1
REMARK 470 DA E 23 C2 N3 C4
REMARK 470 DA F 11 P OP1 OP2 O5'
REMARK 470 DC F 23 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DC F 23 N1 C2 O2 N3 C4 N4 C5
REMARK 470 DC F 23 C6
REMARK 470 DA G 11 P OP1 OP2 O5'
REMARK 470 DC G 23 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DC G 23 N1 C2 O2 N3 C4 N4 C5
REMARK 470 DC G 23 C6
REMARK 470 DG H 11 P OP1 OP2 O5'
REMARK 470 DA H 23 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DA H 23 N9 C8 N7 C5 C6 N6 N1
REMARK 470 DA H 23 C2 N3 C4
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP C 293 O HOH C 701 0.57
REMARK 500 CG ASP C 293 O HOH C 701 0.97
REMARK 500 OD2 ASP C 293 O HOH C 701 1.67
REMARK 500 O3P PTR C 129 C5' DA G 11 2.04
REMARK 500 O3P PTR A 129 C5' DG H 11 2.10
REMARK 500 NH1 ARG C 98 OP1 DG F 7 2.12
REMARK 500 O GLY D 653 NH2 ARG D 659 2.13
REMARK 500 OD2 ASP D 534 O HOH D 801 2.19
REMARK 500 O3P PTR A 129 C5' DA F 11 2.19
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 ARG A 39 -65.60 -160.38
REMARK 500 TYR A 84 -44.33 -130.21
REMARK 500 ASN A 155 -165.49 -73.68
REMARK 500 SER A 168 72.41 50.30
REMARK 500 PRO A 171 84.71 -65.08
REMARK 500 ALA A 182 -145.46 -108.09
REMARK 500 ASN A 188 80.93 -158.08
REMARK 500 ASN A 207 59.99 -95.48
REMARK 500 ALA A 231 -127.90 58.15
REMARK 500 ARG A 313 83.13 -163.30
REMARK 500 ASP A 321 41.77 -92.69
REMARK 500 ASP A 426 75.01 57.65
REMARK 500 ASP A 428 -179.63 -69.19
REMARK 500 HIS B 514 -120.34 56.21
REMARK 500 MET B 552 53.29 -141.86
REMARK 500 GLU B 604 -73.25 -100.59
REMARK 500 THR B 624 -27.44 -141.03
REMARK 500 ASP B 639 -80.85 -86.19
REMARK 500 ARG C 39 -65.50 -160.29
REMARK 500 TYR C 84 -45.26 -130.61
REMARK 500 ASN C 155 -164.48 -72.99
REMARK 500 SER C 168 72.21 50.30
REMARK 500 PRO C 171 84.99 -65.28
REMARK 500 ALA C 182 -146.00 -107.43
REMARK 500 ASN C 188 81.24 -158.08
REMARK 500 ALA C 231 -127.83 58.31
REMARK 500 VAL C 291 -62.37 -104.96
REMARK 500 LEU C 296 60.88 -116.53
REMARK 500 ARG C 313 82.95 -163.09
REMARK 500 ASP C 321 43.23 -92.41
REMARK 500 ASP C 426 71.35 55.09
REMARK 500 HIS D 514 -120.23 57.18
REMARK 500 MET D 552 54.18 -142.11
REMARK 500 GLU D 604 -73.70 -100.62
REMARK 500 THR D 624 -27.47 -141.20
REMARK 500 ASP D 639 -80.33 -86.55
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 MG B 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 532 OD2
REMARK 620 2 ASP B 534 OD2 103.2
REMARK 620 3 HOH B 801 O 92.8 73.7
REMARK 620 4 HOH B 802 O 82.3 98.4 169.6
REMARK 620 5 HOH B 808 O 175.8 76.9 83.3 101.8
REMARK 620 6 HOH B 821 O 88.6 167.5 101.7 87.4 91.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH F 202 O
REMARK 620 2 GFN G 101 O20 80.8
REMARK 620 3 GFN G 101 O22 74.6 72.9
REMARK 620 4 HOH G 202 O 79.6 140.2 68.6
REMARK 620 5 HOH G 204 O 153.8 104.9 82.6 80.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 532 OD2
REMARK 620 2 ASP D 534 OD2 109.7
REMARK 620 3 HOH D 801 O 84.9 63.6
REMARK 620 4 HOH D 804 O 158.8 73.5 77.9
REMARK 620 5 HOH D 809 O 96.2 102.8 165.6 103.5
REMARK 620 6 HOH D 810 O 82.9 150.6 92.3 85.6 102.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 101 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E 202 O
REMARK 620 2 HOH E 203 O 135.4
REMARK 620 3 GFN F 101 O20 75.2 99.2
REMARK 620 4 GFN F 101 O22 68.0 68.7 69.6
REMARK 620 5 HOH F 203 O 79.9 78.4 141.1 73.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GFN F 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GFN G 101
DBREF 5BTF A 2 500 UNP P9WG47 GYRA_MYCTU 2 500
DBREF 5BTF B 426 675 UNP P9WG45 GYRB_MYCTU 426 675
DBREF 5BTF C 2 500 UNP P9WG47 GYRA_MYCTU 2 500
DBREF 5BTF D 426 675 UNP P9WG45 GYRB_MYCTU 426 675
DBREF 5BTF E 1 24 PDB 5BTF 5BTF 1 24
DBREF 5BTF F 1 24 PDB 5BTF 5BTF 1 24
DBREF 5BTF G 1 24 PDB 5BTF 5BTF 1 24
DBREF 5BTF H 1 24 PDB 5BTF 5BTF 1 24
SEQADV 5BTF SER A 90 UNP P9WG47 ALA 90 ENGINEERED MUTATION
SEQADV 5BTF ILE A 501 UNP P9WG47 EXPRESSION TAG
SEQADV 5BTF GLY A 502 UNP P9WG47 EXPRESSION TAG
SEQADV 5BTF SER A 503 UNP P9WG47 EXPRESSION TAG
SEQADV 5BTF GLY A 504 UNP P9WG47 EXPRESSION TAG
SEQADV 5BTF SER B 423 UNP P9WG45 EXPRESSION TAG
SEQADV 5BTF ASN B 424 UNP P9WG45 EXPRESSION TAG
SEQADV 5BTF ALA B 425 UNP P9WG45 EXPRESSION TAG
SEQADV 5BTF SER C 90 UNP P9WG47 ALA 90 ENGINEERED MUTATION
SEQADV 5BTF ILE C 501 UNP P9WG47 EXPRESSION TAG
SEQADV 5BTF GLY C 502 UNP P9WG47 EXPRESSION TAG
SEQADV 5BTF SER C 503 UNP P9WG47 EXPRESSION TAG
SEQADV 5BTF GLY C 504 UNP P9WG47 EXPRESSION TAG
SEQADV 5BTF SER D 423 UNP P9WG45 EXPRESSION TAG
SEQADV 5BTF ASN D 424 UNP P9WG45 EXPRESSION TAG
SEQADV 5BTF ALA D 425 UNP P9WG45 EXPRESSION TAG
SEQRES 1 A 503 THR ASP THR THR LEU PRO PRO ASP ASP SER LEU ASP ARG
SEQRES 2 A 503 ILE GLU PRO VAL ASP ILE GLU GLN GLU MET GLN ARG SER
SEQRES 3 A 503 TYR ILE ASP TYR ALA MET SER VAL ILE VAL GLY ARG ALA
SEQRES 4 A 503 LEU PRO GLU VAL ARG ASP GLY LEU LYS PRO VAL HIS ARG
SEQRES 5 A 503 ARG VAL LEU TYR ALA MET PHE ASP SER GLY PHE ARG PRO
SEQRES 6 A 503 ASP ARG SER HIS ALA LYS SER ALA ARG SER VAL ALA GLU
SEQRES 7 A 503 THR MET GLY ASN TYR HIS PRO HIS GLY ASP SER SER ILE
SEQRES 8 A 503 TYR ASP SER LEU VAL ARG MET ALA GLN PRO TRP SER LEU
SEQRES 9 A 503 ARG TYR PRO LEU VAL ASP GLY GLN GLY ASN PHE GLY SER
SEQRES 10 A 503 PRO GLY ASN ASP PRO PRO ALA ALA MET ARG PTR THR GLU
SEQRES 11 A 503 ALA ARG LEU THR PRO LEU ALA MET GLU MET LEU ARG GLU
SEQRES 12 A 503 ILE ASP GLU GLU THR VAL ASP PHE ILE PRO ASN TYR ASP
SEQRES 13 A 503 GLY ARG VAL GLN GLU PRO THR VAL LEU PRO SER ARG PHE
SEQRES 14 A 503 PRO ASN LEU LEU ALA ASN GLY SER GLY GLY ILE ALA VAL
SEQRES 15 A 503 GLY MET ALA THR ASN ILE PRO PRO HIS ASN LEU ARG GLU
SEQRES 16 A 503 LEU ALA ASP ALA VAL PHE TRP ALA LEU GLU ASN HIS ASP
SEQRES 17 A 503 ALA ASP GLU GLU GLU THR LEU ALA ALA VAL MET GLY ARG
SEQRES 18 A 503 VAL LYS GLY PRO ASP PHE PRO THR ALA GLY LEU ILE VAL
SEQRES 19 A 503 GLY SER GLN GLY THR ALA ASP ALA TYR LYS THR GLY ARG
SEQRES 20 A 503 GLY SER ILE ARG MET ARG GLY VAL VAL GLU VAL GLU GLU
SEQRES 21 A 503 ASP SER ARG GLY ARG THR SER LEU VAL ILE THR GLU LEU
SEQRES 22 A 503 PRO TYR GLN VAL ASN HIS ASP ASN PHE ILE THR SER ILE
SEQRES 23 A 503 ALA GLU GLN VAL ARG ASP GLY LYS LEU ALA GLY ILE SER
SEQRES 24 A 503 ASN ILE GLU ASP GLN SER SER ASP ARG VAL GLY LEU ARG
SEQRES 25 A 503 ILE VAL ILE GLU ILE LYS ARG ASP ALA VAL ALA LYS VAL
SEQRES 26 A 503 VAL ILE ASN ASN LEU TYR LYS HIS THR GLN LEU GLN THR
SEQRES 27 A 503 SER PHE GLY ALA ASN MET LEU ALA ILE VAL ASP GLY VAL
SEQRES 28 A 503 PRO ARG THR LEU ARG LEU ASP GLN LEU ILE ARG TYR TYR
SEQRES 29 A 503 VAL ASP HIS GLN LEU ASP VAL ILE VAL ARG ARG THR THR
SEQRES 30 A 503 TYR ARG LEU ARG LYS ALA ASN GLU ARG ALA HIS ILE LEU
SEQRES 31 A 503 ARG GLY LEU VAL LYS ALA LEU ASP ALA LEU ASP GLU VAL
SEQRES 32 A 503 ILE ALA LEU ILE ARG ALA SER GLU THR VAL ASP ILE ALA
SEQRES 33 A 503 ARG ALA GLY LEU ILE GLU LEU LEU ASP ILE ASP GLU ILE
SEQRES 34 A 503 GLN ALA GLN ALA ILE LEU ASP MET GLN LEU ARG ARG LEU
SEQRES 35 A 503 ALA ALA LEU GLU ARG GLN ARG ILE ILE ASP ASP LEU ALA
SEQRES 36 A 503 LYS ILE GLU ALA GLU ILE ALA ASP LEU GLU ASP ILE LEU
SEQRES 37 A 503 ALA LYS PRO GLU ARG GLN ARG GLY ILE VAL ARG ASP GLU
SEQRES 38 A 503 LEU ALA GLU ILE VAL ASP ARG HIS GLY ASP ASP ARG ARG
SEQRES 39 A 503 THR ARG ILE ILE ALA ILE GLY SER GLY
SEQRES 1 B 253 SER ASN ALA LEU VAL ARG ARG LYS SER ALA THR ASP ILE
SEQRES 2 B 253 GLY GLY LEU PRO GLY LYS LEU ALA ASP CYS ARG SER THR
SEQRES 3 B 253 ASP PRO ARG LYS SER GLU LEU TYR VAL VAL GLU GLY ASP
SEQRES 4 B 253 SER ALA GLY GLY SER ALA LYS SER GLY ARG ASP SER MET
SEQRES 5 B 253 PHE GLN ALA ILE LEU PRO LEU ARG GLY LYS ILE ILE ASN
SEQRES 6 B 253 VAL GLU LYS ALA ARG ILE ASP ARG VAL LEU LYS ASN THR
SEQRES 7 B 253 GLU VAL GLN ALA ILE ILE THR ALA LEU GLY THR GLY ILE
SEQRES 8 B 253 HIS ASP GLU PHE ASP ILE GLY LYS LEU ARG TYR HIS LYS
SEQRES 9 B 253 ILE VAL LEU MET ALA ASP ALA ASP VAL ASP GLY GLN HIS
SEQRES 10 B 253 ILE SER THR LEU LEU LEU THR LEU LEU PHE ARG PHE MET
SEQRES 11 B 253 ARG PRO LEU ILE GLU ASN GLY HIS VAL PHE LEU ALA GLN
SEQRES 12 B 253 PRO PRO LEU TYR LYS LEU LYS TRP GLN ARG SER ASP PRO
SEQRES 13 B 253 GLU PHE ALA TYR SER ASP ARG GLU ARG ASP GLY LEU LEU
SEQRES 14 B 253 GLU ALA GLY LEU LYS ALA GLY LYS LYS ILE ASN LYS GLU
SEQRES 15 B 253 ASP GLY ILE GLN ARG TYR LYS GLY LEU GLY GLU MET ASP
SEQRES 16 B 253 ALA LYS GLU LEU TRP GLU THR THR MET ASP PRO SER VAL
SEQRES 17 B 253 ARG VAL LEU ARG GLN VAL THR LEU ASP ASP ALA ALA ALA
SEQRES 18 B 253 ALA ASP GLU LEU PHE SER ILE LEU MET GLY GLU ASP VAL
SEQRES 19 B 253 ASP ALA ARG ARG SER PHE ILE THR ARG ASN ALA LYS ASP
SEQRES 20 B 253 VAL ARG PHE LEU ASP VAL
SEQRES 1 C 503 THR ASP THR THR LEU PRO PRO ASP ASP SER LEU ASP ARG
SEQRES 2 C 503 ILE GLU PRO VAL ASP ILE GLU GLN GLU MET GLN ARG SER
SEQRES 3 C 503 TYR ILE ASP TYR ALA MET SER VAL ILE VAL GLY ARG ALA
SEQRES 4 C 503 LEU PRO GLU VAL ARG ASP GLY LEU LYS PRO VAL HIS ARG
SEQRES 5 C 503 ARG VAL LEU TYR ALA MET PHE ASP SER GLY PHE ARG PRO
SEQRES 6 C 503 ASP ARG SER HIS ALA LYS SER ALA ARG SER VAL ALA GLU
SEQRES 7 C 503 THR MET GLY ASN TYR HIS PRO HIS GLY ASP SER SER ILE
SEQRES 8 C 503 TYR ASP SER LEU VAL ARG MET ALA GLN PRO TRP SER LEU
SEQRES 9 C 503 ARG TYR PRO LEU VAL ASP GLY GLN GLY ASN PHE GLY SER
SEQRES 10 C 503 PRO GLY ASN ASP PRO PRO ALA ALA MET ARG PTR THR GLU
SEQRES 11 C 503 ALA ARG LEU THR PRO LEU ALA MET GLU MET LEU ARG GLU
SEQRES 12 C 503 ILE ASP GLU GLU THR VAL ASP PHE ILE PRO ASN TYR ASP
SEQRES 13 C 503 GLY ARG VAL GLN GLU PRO THR VAL LEU PRO SER ARG PHE
SEQRES 14 C 503 PRO ASN LEU LEU ALA ASN GLY SER GLY GLY ILE ALA VAL
SEQRES 15 C 503 GLY MET ALA THR ASN ILE PRO PRO HIS ASN LEU ARG GLU
SEQRES 16 C 503 LEU ALA ASP ALA VAL PHE TRP ALA LEU GLU ASN HIS ASP
SEQRES 17 C 503 ALA ASP GLU GLU GLU THR LEU ALA ALA VAL MET GLY ARG
SEQRES 18 C 503 VAL LYS GLY PRO ASP PHE PRO THR ALA GLY LEU ILE VAL
SEQRES 19 C 503 GLY SER GLN GLY THR ALA ASP ALA TYR LYS THR GLY ARG
SEQRES 20 C 503 GLY SER ILE ARG MET ARG GLY VAL VAL GLU VAL GLU GLU
SEQRES 21 C 503 ASP SER ARG GLY ARG THR SER LEU VAL ILE THR GLU LEU
SEQRES 22 C 503 PRO TYR GLN VAL ASN HIS ASP ASN PHE ILE THR SER ILE
SEQRES 23 C 503 ALA GLU GLN VAL ARG ASP GLY LYS LEU ALA GLY ILE SER
SEQRES 24 C 503 ASN ILE GLU ASP GLN SER SER ASP ARG VAL GLY LEU ARG
SEQRES 25 C 503 ILE VAL ILE GLU ILE LYS ARG ASP ALA VAL ALA LYS VAL
SEQRES 26 C 503 VAL ILE ASN ASN LEU TYR LYS HIS THR GLN LEU GLN THR
SEQRES 27 C 503 SER PHE GLY ALA ASN MET LEU ALA ILE VAL ASP GLY VAL
SEQRES 28 C 503 PRO ARG THR LEU ARG LEU ASP GLN LEU ILE ARG TYR TYR
SEQRES 29 C 503 VAL ASP HIS GLN LEU ASP VAL ILE VAL ARG ARG THR THR
SEQRES 30 C 503 TYR ARG LEU ARG LYS ALA ASN GLU ARG ALA HIS ILE LEU
SEQRES 31 C 503 ARG GLY LEU VAL LYS ALA LEU ASP ALA LEU ASP GLU VAL
SEQRES 32 C 503 ILE ALA LEU ILE ARG ALA SER GLU THR VAL ASP ILE ALA
SEQRES 33 C 503 ARG ALA GLY LEU ILE GLU LEU LEU ASP ILE ASP GLU ILE
SEQRES 34 C 503 GLN ALA GLN ALA ILE LEU ASP MET GLN LEU ARG ARG LEU
SEQRES 35 C 503 ALA ALA LEU GLU ARG GLN ARG ILE ILE ASP ASP LEU ALA
SEQRES 36 C 503 LYS ILE GLU ALA GLU ILE ALA ASP LEU GLU ASP ILE LEU
SEQRES 37 C 503 ALA LYS PRO GLU ARG GLN ARG GLY ILE VAL ARG ASP GLU
SEQRES 38 C 503 LEU ALA GLU ILE VAL ASP ARG HIS GLY ASP ASP ARG ARG
SEQRES 39 C 503 THR ARG ILE ILE ALA ILE GLY SER GLY
SEQRES 1 D 253 SER ASN ALA LEU VAL ARG ARG LYS SER ALA THR ASP ILE
SEQRES 2 D 253 GLY GLY LEU PRO GLY LYS LEU ALA ASP CYS ARG SER THR
SEQRES 3 D 253 ASP PRO ARG LYS SER GLU LEU TYR VAL VAL GLU GLY ASP
SEQRES 4 D 253 SER ALA GLY GLY SER ALA LYS SER GLY ARG ASP SER MET
SEQRES 5 D 253 PHE GLN ALA ILE LEU PRO LEU ARG GLY LYS ILE ILE ASN
SEQRES 6 D 253 VAL GLU LYS ALA ARG ILE ASP ARG VAL LEU LYS ASN THR
SEQRES 7 D 253 GLU VAL GLN ALA ILE ILE THR ALA LEU GLY THR GLY ILE
SEQRES 8 D 253 HIS ASP GLU PHE ASP ILE GLY LYS LEU ARG TYR HIS LYS
SEQRES 9 D 253 ILE VAL LEU MET ALA ASP ALA ASP VAL ASP GLY GLN HIS
SEQRES 10 D 253 ILE SER THR LEU LEU LEU THR LEU LEU PHE ARG PHE MET
SEQRES 11 D 253 ARG PRO LEU ILE GLU ASN GLY HIS VAL PHE LEU ALA GLN
SEQRES 12 D 253 PRO PRO LEU TYR LYS LEU LYS TRP GLN ARG SER ASP PRO
SEQRES 13 D 253 GLU PHE ALA TYR SER ASP ARG GLU ARG ASP GLY LEU LEU
SEQRES 14 D 253 GLU ALA GLY LEU LYS ALA GLY LYS LYS ILE ASN LYS GLU
SEQRES 15 D 253 ASP GLY ILE GLN ARG TYR LYS GLY LEU GLY GLU MET ASP
SEQRES 16 D 253 ALA LYS GLU LEU TRP GLU THR THR MET ASP PRO SER VAL
SEQRES 17 D 253 ARG VAL LEU ARG GLN VAL THR LEU ASP ASP ALA ALA ALA
SEQRES 18 D 253 ALA ASP GLU LEU PHE SER ILE LEU MET GLY GLU ASP VAL
SEQRES 19 D 253 ASP ALA ARG ARG SER PHE ILE THR ARG ASN ALA LYS ASP
SEQRES 20 D 253 VAL ARG PHE LEU ASP VAL
SEQRES 1 E 24 DG DG DT DC DA DT DG DA DA DT DG DA DC
SEQRES 2 E 24 DT DA DT DG DC DA DC DG DT DA DA
SEQRES 1 F 24 DT DT DA DC DG DT DG DC DA DT DA DG DT
SEQRES 2 F 24 DC DA DT DT DC DA DT DG DA DC DC
SEQRES 1 G 24 DT DT DA DC DG DT DG DC DA DT DA DG DT
SEQRES 2 G 24 DC DA DT DT DC DA DT DG DA DC DC
SEQRES 1 H 24 DG DG DT DC DA DT DG DA DA DT DG DA DC
SEQRES 2 H 24 DT DA DT DG DC DA DC DG DT DA DA
MODRES 5BTF PTR A 129 TYR MODIFIED RESIDUE
MODRES 5BTF PTR C 129 TYR MODIFIED RESIDUE
HET PTR A 129 23
HET PTR C 129 23
HET MG B 701 1
HET MG C 601 1
HET MG D 701 1
HET MG E 101 1
HET GFN F 101 48
HET GFN G 101 48
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM MG MAGNESIUM ION
HETNAM GFN 1-CYCLOPROPYL-6-FLUORO-8-METHOXY-7-[(3S)-3-
HETNAM 2 GFN METHYLPIPERAZIN-1-YL]-4-OXO-1,4-DIHYDROQUINOLINE-3-
HETNAM 3 GFN CARBOXYLIC ACID
HETSYN PTR PHOSPHONOTYROSINE
HETSYN GFN GATIFLOXACIN
FORMUL 1 PTR 2(C9 H12 N O6 P)
FORMUL 9 MG 4(MG 2+)
FORMUL 13 GFN 2(C19 H22 F N3 O4)
FORMUL 15 HOH *191(H2 O)
HELIX 1 AA1 ILE A 20 ARG A 39 1 20
HELIX 2 AA2 LYS A 49 GLY A 63 1 15
HELIX 3 AA3 SER A 73 TYR A 84 1 12
HELIX 4 AA4 GLY A 88 MET A 99 1 12
HELIX 5 AA5 THR A 135 LEU A 142 1 8
HELIX 6 AA6 GLU A 144 GLU A 148 5 5
HELIX 7 AA7 PRO A 171 GLY A 177 1 7
HELIX 8 AA8 ASN A 193 ASN A 207 1 15
HELIX 9 AA9 ASP A 211 VAL A 223 1 13
HELIX 10 AB1 SER A 237 GLY A 247 1 11
HELIX 11 AB2 ASN A 279 ASP A 293 1 15
HELIX 12 AB3 VAL A 323 THR A 335 1 13
HELIX 13 AB4 ARG A 357 ALA A 400 1 44
HELIX 14 AB5 ALA A 400 ALA A 410 1 11
HELIX 15 AB6 THR A 413 ASP A 426 1 14
HELIX 16 AB7 ASP A 428 ASP A 437 1 10
HELIX 17 AB8 GLN A 439 LEU A 443 5 5
HELIX 18 AB9 ALA A 444 LYS A 471 1 28
HELIX 19 AC1 LYS A 471 GLY A 491 1 21
HELIX 20 AC2 GLY B 460 ARG B 471 1 12
HELIX 21 AC3 ARG B 492 ASN B 499 1 8
HELIX 22 AC4 ASN B 499 GLY B 510 1 12
HELIX 23 AC5 ILE B 513 PHE B 517 5 5
HELIX 24 AC6 ASP B 518 LEU B 522 5 5
HELIX 25 AC7 ASP B 534 MET B 552 1 19
HELIX 26 AC8 ARG B 553 ASN B 558 1 6
HELIX 27 AC9 SER B 583 ALA B 597 1 15
HELIX 28 AD1 GLY B 612 MET B 616 5 5
HELIX 29 AD2 ASP B 617 MET B 626 1 10
HELIX 30 AD3 ASP B 640 GLY B 653 1 14
HELIX 31 AD4 ASP B 655 ALA B 667 1 13
HELIX 32 AD5 LYS B 668 ASP B 674 5 7
HELIX 33 AD6 ILE C 20 ARG C 39 1 20
HELIX 34 AD7 LYS C 49 GLY C 63 1 15
HELIX 35 AD8 SER C 73 TYR C 84 1 12
HELIX 36 AD9 GLY C 88 MET C 99 1 12
HELIX 37 AE1 ALA C 126 PTR C 129 5 4
HELIX 38 AE2 THR C 135 LEU C 142 1 8
HELIX 39 AE3 GLU C 144 GLU C 148 5 5
HELIX 40 AE4 PRO C 171 GLY C 177 1 7
HELIX 41 AE5 ASN C 193 ASN C 207 1 15
HELIX 42 AE6 ASP C 211 VAL C 223 1 13
HELIX 43 AE7 SER C 237 GLY C 247 1 11
HELIX 44 AE8 ASN C 279 ASP C 293 1 15
HELIX 45 AE9 VAL C 323 THR C 335 1 13
HELIX 46 AF1 ARG C 357 ALA C 400 1 44
HELIX 47 AF2 ALA C 400 ALA C 410 1 11
HELIX 48 AF3 THR C 413 ASP C 426 1 14
HELIX 49 AF4 ASP C 428 MET C 438 1 11
HELIX 50 AF5 GLN C 439 LEU C 443 5 5
HELIX 51 AF6 ALA C 444 LYS C 471 1 28
HELIX 52 AF7 LYS C 471 GLY C 491 1 21
HELIX 53 AF8 GLY D 460 ARG D 471 1 12
HELIX 54 AF9 ARG D 492 ASN D 499 1 8
HELIX 55 AG1 ASN D 499 GLY D 510 1 12
HELIX 56 AG2 ILE D 513 PHE D 517 5 5
HELIX 57 AG3 ASP D 518 LEU D 522 5 5
HELIX 58 AG4 ASP D 534 MET D 552 1 19
HELIX 59 AG5 ARG D 553 ASN D 558 1 6
HELIX 60 AG6 SER D 583 ALA D 597 1 15
HELIX 61 AG7 GLY D 612 MET D 616 5 5
HELIX 62 AG8 ASP D 617 MET D 626 1 10
HELIX 63 AG9 ASP D 640 GLY D 653 1 14
HELIX 64 AH1 ASP D 655 ALA D 667 1 13
HELIX 65 AH2 LYS D 668 ASP D 674 5 7
SHEET 1 AA1 6 GLU A 16 ASP A 19 0
SHEET 2 AA1 6 LEU B 633 THR B 637 1 O THR B 637 N VAL A 18
SHEET 3 AA1 6 VAL B 561 ALA B 564 -1 N LEU B 563 O ARG B 634
SHEET 4 AA1 6 LYS B 526 MET B 530 1 N ILE B 527 O PHE B 562
SHEET 5 AA1 6 GLU B 454 GLU B 459 1 N LEU B 455 O LYS B 526
SHEET 6 AA1 6 GLN B 476 LEU B 481 1 O ALA B 477 N TYR B 456
SHEET 1 AA2 3 ALA A 71 LYS A 72 0
SHEET 2 AA2 3 GLU A 131 LEU A 134 -1 O ALA A 132 N ALA A 71
SHEET 3 AA2 3 VAL A 110 GLN A 113 -1 N ASP A 111 O ARG A 133
SHEET 1 AA3 2 PHE A 152 PRO A 154 0
SHEET 2 AA3 2 GLN A 161 PRO A 163 -1 O GLU A 162 N ILE A 153
SHEET 1 AA4 2 SER A 178 ILE A 181 0
SHEET 2 AA4 2 ALA A 186 ILE A 189 -1 O ILE A 189 N SER A 178
SHEET 1 AA5 4 GLN A 338 ASN A 344 0
SHEET 2 AA5 4 ARG A 248 ARG A 254 -1 N ILE A 251 O PHE A 341
SHEET 3 AA5 4 LEU A 233 VAL A 235 -1 N LEU A 233 O ARG A 254
SHEET 4 AA5 4 ARG A 497 ILE A 499 1 O ARG A 497 N ILE A 234
SHEET 1 AA6 4 VAL A 256 GLU A 260 0
SHEET 2 AA6 4 SER A 268 GLU A 273 -1 O SER A 268 N GLU A 260
SHEET 3 AA6 4 ILE A 314 ILE A 318 -1 O ILE A 316 N LEU A 269
SHEET 4 AA6 4 ILE A 299 ASP A 304 -1 N SER A 300 O GLU A 317
SHEET 1 AA7 2 LEU A 346 VAL A 349 0
SHEET 2 AA7 2 VAL A 352 THR A 355 -1 O VAL A 352 N VAL A 349
SHEET 1 AA8 3 GLU B 579 ALA B 581 0
SHEET 2 AA8 3 TYR B 569 LEU B 571 -1 N LEU B 571 O GLU B 579
SHEET 3 AA8 3 ILE B 607 ARG B 609 -1 O GLN B 608 N LYS B 570
SHEET 1 AA9 6 GLU C 16 ASP C 19 0
SHEET 2 AA9 6 LEU D 633 THR D 637 1 O THR D 637 N VAL C 18
SHEET 3 AA9 6 VAL D 561 ALA D 564 -1 N LEU D 563 O ARG D 634
SHEET 4 AA9 6 LYS D 526 MET D 530 1 N ILE D 527 O PHE D 562
SHEET 5 AA9 6 GLU D 454 GLU D 459 1 N LEU D 455 O LYS D 526
SHEET 6 AA9 6 GLN D 476 LEU D 481 1 O ALA D 477 N TYR D 456
SHEET 1 AB1 3 ALA C 71 LYS C 72 0
SHEET 2 AB1 3 GLU C 131 LEU C 134 -1 O ALA C 132 N ALA C 71
SHEET 3 AB1 3 VAL C 110 GLN C 113 -1 N ASP C 111 O ARG C 133
SHEET 1 AB2 2 PHE C 152 PRO C 154 0
SHEET 2 AB2 2 GLN C 161 PRO C 163 -1 O GLU C 162 N ILE C 153
SHEET 1 AB3 2 SER C 178 ILE C 181 0
SHEET 2 AB3 2 ALA C 186 ILE C 189 -1 O ILE C 189 N SER C 178
SHEET 1 AB4 4 GLN C 338 ASN C 344 0
SHEET 2 AB4 4 ARG C 248 ARG C 254 -1 N ILE C 251 O PHE C 341
SHEET 3 AB4 4 LEU C 233 VAL C 235 -1 N LEU C 233 O ARG C 254
SHEET 4 AB4 4 ARG C 497 ILE C 499 1 O ARG C 497 N ILE C 234
SHEET 1 AB5 4 VAL C 256 GLU C 261 0
SHEET 2 AB5 4 THR C 267 GLU C 273 -1 O SER C 268 N GLU C 260
SHEET 3 AB5 4 ILE C 314 ILE C 318 -1 O ILE C 316 N LEU C 269
SHEET 4 AB5 4 ILE C 299 ASP C 304 -1 N SER C 300 O GLU C 317
SHEET 1 AB6 2 LEU C 346 VAL C 349 0
SHEET 2 AB6 2 VAL C 352 THR C 355 -1 O VAL C 352 N VAL C 349
SHEET 1 AB7 3 GLU D 579 ALA D 581 0
SHEET 2 AB7 3 TYR D 569 LEU D 571 -1 N LEU D 571 O GLU D 579
SHEET 3 AB7 3 ILE D 607 ARG D 609 -1 O GLN D 608 N LYS D 570
LINK C ARG A 128 N PTR A 129 1555 1555 1.33
LINK C PTR A 129 N THR A 130 1555 1555 1.33
LINK C ARG C 128 N PTR C 129 1555 1555 1.33
LINK C PTR C 129 N THR C 130 1555 1555 1.33
LINK OD2 ASP B 532 MG MG B 701 1555 1555 2.10
LINK OD2 ASP B 534 MG MG B 701 1555 1555 2.14
LINK MG MG B 701 O HOH B 801 1555 1555 2.06
LINK MG MG B 701 O HOH B 802 1555 1555 2.08
LINK MG MG B 701 O HOH B 808 1555 1555 2.08
LINK MG MG B 701 O HOH B 821 1555 1555 2.08
LINK MG MG C 601 O HOH F 202 1555 1555 2.08
LINK MG MG C 601 O20 GFN G 101 1555 1555 2.20
LINK MG MG C 601 O22 GFN G 101 1555 1555 2.21
LINK MG MG C 601 O HOH G 202 1555 1555 2.10
LINK MG MG C 601 O HOH G 204 1555 1555 2.07
LINK OD2 ASP D 532 MG MG D 701 1555 1555 2.03
LINK OD2 ASP D 534 MG MG D 701 1555 1555 2.11
LINK MG MG D 701 O HOH D 801 1555 1555 2.05
LINK MG MG D 701 O HOH D 804 1555 1555 2.10
LINK MG MG D 701 O HOH D 809 1555 1555 2.08
LINK MG MG D 701 O HOH D 810 1555 1555 2.03
LINK MG MG E 101 O HOH E 202 1555 1555 2.09
LINK MG MG E 101 O HOH E 203 1555 1555 2.09
LINK MG MG E 101 O20 GFN F 101 1555 1555 2.19
LINK MG MG E 101 O22 GFN F 101 1555 1555 2.31
LINK MG MG E 101 O HOH F 203 1555 1555 2.08
SITE 1 AC1 6 ASP B 532 ASP B 534 HOH B 801 HOH B 802
SITE 2 AC1 6 HOH B 808 HOH B 821
SITE 1 AC2 4 HOH F 202 GFN G 101 HOH G 202 HOH G 204
SITE 1 AC3 7 GLU D 459 ASP D 532 ASP D 534 HOH D 801
SITE 2 AC3 7 HOH D 804 HOH D 809 HOH D 810
SITE 1 AC4 4 HOH E 202 HOH E 203 GFN F 101 HOH F 203
SITE 1 AC5 18 SER A 90 ARG B 482 GLY B 483 ARG C 128
SITE 2 AC5 18 DT E 10 DG E 11 MG E 101 HOH E 202
SITE 3 AC5 18 HOH E 203 DC F 14 DA F 15 HOH F 203
SITE 4 AC5 18 HOH F 204 HOH F 205 DT G 10 DA G 11
SITE 5 AC5 18 DT H 14 DA H 15
SITE 1 AC6 16 ARG A 128 SER C 90 MG C 601 ARG D 482
SITE 2 AC6 16 GLY D 483 DT E 14 DA E 15 DT F 10
SITE 3 AC6 16 DA F 11 HOH F 202 DC G 14 DA G 15
SITE 4 AC6 16 HOH G 202 HOH G 204 DT H 10 DG H 11
CRYST1 108.955 84.019 130.590 90.00 108.87 90.00 P 1 21 1 4
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 0.009178 0.000000 0.003137 0.00000
SCALE2 0.000000 0.011902 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008092 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
