HEADER ISOMERASE 30-JAN-18 6FM4
TITLE THE CRYSTAL STRUCTURE OF S. AUREUS GYRASE COMPLEX WITH ID-130 AND DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA GYRASE SUBUNIT B,DNA GYRASE SUBUNIT B,DNA GYRASE
COMPND 3 SUBUNIT A;
COMPND 4 CHAIN: B, D;
COMPND 5 EC: 5.99.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: C-TERMINUS GYRB (640) FUSED TO N-TERMINUS GYRA (1010).
COMPND 9 DOMAIN 544-579 DELETED AND REPLACED WITH TWO RESIDUES TG.;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: DNA (5'-
COMPND 12 5UA*D(P*GP*CP*CP*GP*TP*AP*GP*GP*GP*CP*CP*CP*TP*AP*CP*GP*GP*CP*T)-3');
COMPND 13 CHAIN: E;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: DNA (5'-
COMPND 17 5UA*D(P*GP*CP*CP*GP*TP*AP*GP*GP*GP*CP*CP*CP*TP*AP*CP*GP*GP*C)-3');
COMPND 18 CHAIN: F;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS (STRAIN N315);
SOURCE 3 ORGANISM_TAXID: 158879;
SOURCE 4 GENE: GYRB, SA0005, GYRA, SA0006;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 10 ORGANISM_TAXID: 32630;
SOURCE 11 MOL_ID: 3;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630
KEYWDS NBTIS, BACTERIAL TOPOISOMERASE, GYRASE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.OMBRATO,B.GAROFALO,G.MANGANO,F.MANCINI
REVDAT 5 17-JAN-24 6FM4 1 REMARK
REVDAT 4 04-SEP-19 6FM4 1 JRNL
REVDAT 3 07-AUG-19 6FM4 1 JRNL
REVDAT 2 17-JUL-19 6FM4 1 JRNL
REVDAT 1 10-JUL-19 6FM4 0
JRNL AUTH G.MAGARO,F.PRATI,B.GAROFALO,G.CORSO,G.FURLOTTI,C.APICELLA,
JRNL AUTH 2 G.MANGANO,N.D'ATANASIO,D.ROBINSON,F.P.DI GIORGIO,R.OMBRATO
JRNL TITL VIRTUAL SCREENING APPROACH AND INVESTIGATION OF
JRNL TITL 2 STRUCTURE-ACTIVITY RELATIONSHIPS TO DISCOVER NOVEL BACTERIAL
JRNL TITL 3 TOPOISOMERASE INHIBITORS TARGETING GRAM-POSITIVE AND
JRNL TITL 4 GRAM-NEGATIVE PATHOGENS.
JRNL REF J.MED.CHEM. V. 62 7445 2019
JRNL REFN ISSN 0022-2623
JRNL PMID 31276392
JRNL DOI 10.1021/ACS.JMEDCHEM.9B00394
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 51255
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) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.300
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2750
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3767
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 201
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10606
REMARK 3 NUCLEIC ACID ATOMS : 758
REMARK 3 HETEROGEN ATOMS : 73
REMARK 3 SOLVENT ATOMS : 62
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.80000
REMARK 3 B22 (A**2) : -0.80000
REMARK 3 B33 (A**2) : 2.58000
REMARK 3 B12 (A**2) : -0.80000
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): 0.911
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.391
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.324
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.544
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.885
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.794
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11668 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10993 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15885 ; 1.674 ; 1.915
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25231 ; 0.971 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1338 ; 6.844 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 534 ;35.129 ;23.670
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2001 ;15.439 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 118 ;16.980 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1748 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12718 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2656 ; 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 : NULL
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 U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6FM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1200008356.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51255
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 43.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.6800
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) : 2.77
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 2XCS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 5000 MME, 0.1 M BISTRIS PH
REMARK 280 6.5, PH 6.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295.15K
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 135.67667
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 271.35333
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 203.51500
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 339.19167
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 67.83833
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, E, F
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 B 409
REMARK 465 ASP B 410
REMARK 465 VAL B 411
REMARK 465 ALA B 412
REMARK 465 SER B 413
REMARK 465 LEU B 414
REMARK 465 PRO B 415
REMARK 465 GLY B 416
REMARK 465 ASN B 998
REMARK 465 LEU B 999
REMARK 465 ASP B 1000
REMARK 465 PHE B 1001
REMARK 465 ALA B 1002
REMARK 465 GLU B 1003
REMARK 465 LEU B 1004
REMARK 465 PRO B 1005
REMARK 465 GLN B 1006
REMARK 465 SER B 1007
REMARK 465 ARG B 1008
REMARK 465 ILE B 1009
REMARK 465 MET D 409
REMARK 465 ASP D 410
REMARK 465 VAL D 411
REMARK 465 ALA D 412
REMARK 465 SER D 413
REMARK 465 LEU D 414
REMARK 465 PRO D 415
REMARK 465 GLY D 416
REMARK 465 ALA D 997
REMARK 465 ASN D 998
REMARK 465 LEU D 999
REMARK 465 ASP D 1000
REMARK 465 PHE D 1001
REMARK 465 ALA D 1002
REMARK 465 GLU D 1003
REMARK 465 LEU D 1004
REMARK 465 PRO D 1005
REMARK 465 GLN D 1006
REMARK 465 SER D 1007
REMARK 465 ARG D 1008
REMARK 465 ILE D 1009
REMARK 465 GLY D 1491
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 LYS B 417 CG CD CE NZ
REMARK 470 LYS B 581 CG CD CE NZ
REMARK 470 LYS D 417 CG CD CE NZ
REMARK 470 LYS D 424 CG CD CE NZ
REMARK 470 LYS D 607 CG CD CE NZ
REMARK 470 ASN D1010 CG OD1 ND2
REMARK 470 LYS D1227 CG CD CE NZ
REMARK 470 LEU D1490 CG CD1 CD2
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 OD2 ASP B 508 MN MN E 101 0.76
REMARK 500 OD2 ASP D 508 MN MN F 1501 0.92
REMARK 500 P DG E 2 O3' 5UA E 102 1.39
REMARK 500 OE2 GLU B 435 MN MN E 101 1.56
REMARK 500 OE2 GLU D 435 MN MN F 1501 1.57
REMARK 500 OP1 DG E 9 MN MN E 101 1.60
REMARK 500 OP2 DG F 2 O3' 5UA F 1502 1.62
REMARK 500 OE2 GLU B 435 OD2 ASP B 508 1.81
REMARK 500 OP2 DG F 2 C3' 5UA F 1502 1.94
REMARK 500 OE2 GLU D 435 OD2 ASP D 508 1.99
REMARK 500 O LEU D 462 O HOH D 1601 2.08
REMARK 500 OP1 DG E 2 O3' 5UA E 102 2.09
REMARK 500 OD2 ASP B 508 OP1 DG E 9 2.10
REMARK 500 O5' DG F 2 O3' 5UA F 1502 2.11
REMARK 500 O LEU B 519 O HOH B 1601 2.15
REMARK 500 OG SER D 1297 OG1 THR D 1300 2.16
REMARK 500 OG1 THR B 1129 OG1 THR B 1132 2.17
REMARK 500 O LEU B 1321 OG1 THR B 1325 2.18
REMARK 500 O5' DG E 2 O3' 5UA E 102 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU D 1393 N1 5UA E 102 1655 2.09
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 ARG B1484 NE - CZ - NH2 ANGL. DEV. = -3.0 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 LYS B 424 71.20 -101.64
REMARK 500 PRO B 426 -54.73 -28.55
REMARK 500 LEU B 457 -154.37 -107.45
REMARK 500 ASP B 492 -35.55 -36.73
REMARK 500 PHE B 493 136.27 -30.53
REMARK 500 ALA B 509 37.97 -75.85
REMARK 500 MET B 528 40.39 -153.63
REMARK 500 THR B 595 -35.00 -137.20
REMARK 500 TYR B 639 86.85 -65.59
REMARK 500 ARG B1033 -84.18 -173.22
REMARK 500 GLN B1056 36.15 -95.60
REMARK 500 PRO B1080 46.55 -75.02
REMARK 500 ALA B1119 168.85 -46.77
REMARK 500 ALA B1162 65.67 69.67
REMARK 500 PRO B1165 80.14 -65.37
REMARK 500 ALA B1176 -149.58 -118.33
REMARK 500 ASN B1182 89.02 -158.34
REMARK 500 ASN B1201 75.81 -172.22
REMARK 500 ASP B1212 -74.45 -72.85
REMARK 500 ALA B1221 -138.10 46.03
REMARK 500 GLN B1267 34.56 72.11
REMARK 500 ASP B1291 145.15 -170.98
REMARK 500 ASP B1311 -14.01 80.49
REMARK 500 LEU B1327 -27.37 -35.30
REMARK 500 HIS B1390 31.47 -148.14
REMARK 500 ILE B1488 75.78 -113.90
REMARK 500 SER D 449 -19.33 -48.13
REMARK 500 LEU D 457 -158.92 -90.37
REMARK 500 MET D 506 77.60 -117.33
REMARK 500 ALA D 509 43.81 -79.86
REMARK 500 HIS D 600 -40.47 -130.08
REMARK 500 ALA D1032 45.95 -142.31
REMARK 500 ARG D1033 -72.62 -159.27
REMARK 500 TYR D1078 -53.69 -134.65
REMARK 500 PRO D1080 46.83 -71.56
REMARK 500 ASP D1116 118.30 -29.50
REMARK 500 LYS D1141 46.92 -93.57
REMARK 500 ASP D1142 48.53 25.33
REMARK 500 ASN D1149 -177.50 -59.47
REMARK 500 ALA D1172 148.77 168.10
REMARK 500 ALA D1176 -142.28 -90.03
REMARK 500 ALA D1221 -136.91 67.63
REMARK 500 ARG D1256 158.78 -44.60
REMARK 500 ASP D1311 -30.80 73.60
REMARK 500 ALA D1312 152.68 -48.95
REMARK 500 LEU D1327 -45.24 -29.28
REMARK 500 MET D1428 125.56 -37.91
REMARK 500 ARG D1431 -15.75 -43.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 MN B 1501
REMARK 615 MN E 101
REMARK 615 5UA E 102
REMARK 615 MN F 1501
REMARK 615 5UA F 1502
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 MN E 101 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG E 8 O3'
REMARK 620 2 DG E 9 P 36.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN F1501 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG F 8 O3'
REMARK 620 2 DG F 9 OP1 63.9
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 DU5 E 103
DBREF 6FM4 B 409 543 UNP P66937 GYRB_STAAN 409 543
DBREF 6FM4 B 580 1001 UNP P66937 GYRB_STAAN 580 644
DBREF 6FM4 B 1002 1491 UNP Q99XG5 GYRA_STAAN 2 491
DBREF 6FM4 D 409 543 UNP P66937 GYRB_STAAN 409 543
DBREF 6FM4 D 580 1001 UNP P66937 GYRB_STAAN 580 644
DBREF 6FM4 D 1002 1491 UNP Q99XG5 GYRA_STAAN 2 491
DBREF 6FM4 E 2 20 PDB 6FM4 6FM4 2 20
DBREF 6FM4 F 2 19 PDB 6FM4 6FM4 2 19
SEQADV 6FM4 MET B 409 UNP P66937 LEU 409 CONFLICT
SEQADV 6FM4 THR B 544 UNP P66937 LINKER
SEQADV 6FM4 GLY B 545 UNP P66937 LINKER
SEQADV 6FM4 PHE B 1123 UNP Q99XG5 TYR 123 ENGINEERED MUTATION
SEQADV 6FM4 MET D 409 UNP P66937 LEU 409 CONFLICT
SEQADV 6FM4 THR D 544 UNP P66937 LINKER
SEQADV 6FM4 GLY D 545 UNP P66937 LINKER
SEQADV 6FM4 PHE D 1123 UNP Q99XG5 TYR 123 ENGINEERED MUTATION
SEQRES 1 B 692 MET ASP VAL ALA SER LEU PRO GLY LYS LEU ALA ASP CYS
SEQRES 2 B 692 SER SER LYS SER PRO GLU GLU CYS GLU ILE PHE LEU VAL
SEQRES 3 B 692 GLU GLY ASP SER ALA GLY GLY SER THR LYS SER GLY ARG
SEQRES 4 B 692 ASP SER ARG THR GLN ALA ILE LEU PRO LEU ARG GLY LYS
SEQRES 5 B 692 ILE LEU ASN VAL GLU LYS ALA ARG LEU ASP ARG ILE LEU
SEQRES 6 B 692 ASN ASN ASN GLU ILE ARG GLN MET ILE THR ALA PHE GLY
SEQRES 7 B 692 THR GLY ILE GLY GLY ASP PHE ASP LEU ALA LYS ALA ARG
SEQRES 8 B 692 TYR HIS LYS ILE VAL ILE MET THR ASP ALA ASP VAL ASP
SEQRES 9 B 692 GLY ALA HIS ILE ARG THR LEU LEU LEU THR PHE PHE TYR
SEQRES 10 B 692 ARG PHE MET ARG PRO LEU ILE GLU ALA GLY TYR VAL TYR
SEQRES 11 B 692 ILE ALA GLN PRO PRO THR GLY TYR LYS GLY LEU GLY GLU
SEQRES 12 B 692 MET ASN ALA ASP GLN LEU TRP GLU THR THR MET ASN PRO
SEQRES 13 B 692 GLU HIS ARG ALA LEU LEU GLN VAL LYS LEU GLU ASP ALA
SEQRES 14 B 692 ILE GLU ALA ASP GLN THR PHE GLU MET LEU MET GLY ASP
SEQRES 15 B 692 VAL VAL GLU ASN ARG ARG GLN PHE ILE GLU ASP ASN ALA
SEQRES 16 B 692 VAL TYR ALA ASN LEU ASP PHE ALA GLU LEU PRO GLN SER
SEQRES 17 B 692 ARG ILE ASN GLU ARG ASN ILE THR SER GLU MET ARG GLU
SEQRES 18 B 692 SER PHE LEU ASP TYR ALA MET SER VAL ILE VAL ALA ARG
SEQRES 19 B 692 ALA LEU PRO ASP VAL ARG ASP GLY LEU LYS PRO VAL HIS
SEQRES 20 B 692 ARG ARG ILE LEU TYR GLY LEU ASN GLU GLN GLY MET THR
SEQRES 21 B 692 PRO ASP LYS SER TYR LYS LYS SER ALA ARG ILE VAL GLY
SEQRES 22 B 692 ASP VAL MET GLY LYS TYR HIS PRO HIS GLY ASP SER SER
SEQRES 23 B 692 ILE TYR GLU ALA MET VAL ARG MET ALA GLN ASP PHE SER
SEQRES 24 B 692 TYR ARG TYR PRO LEU VAL ASP GLY GLN GLY ASN PHE GLY
SEQRES 25 B 692 SER MET ASP GLY ASP GLY ALA ALA ALA MET ARG PHE THR
SEQRES 26 B 692 GLU ALA ARG MET THR LYS ILE THR LEU GLU LEU LEU ARG
SEQRES 27 B 692 ASP ILE ASN LYS ASP THR ILE ASP PHE ILE ASP ASN TYR
SEQRES 28 B 692 ASP GLY ASN GLU ARG GLU PRO SER VAL LEU PRO ALA ARG
SEQRES 29 B 692 PHE PRO ASN LEU LEU ALA ASN GLY ALA SER GLY ILE ALA
SEQRES 30 B 692 VAL GLY MET ALA THR ASN ILE PRO PRO HIS ASN LEU THR
SEQRES 31 B 692 GLU LEU ILE ASN GLY VAL LEU SER LEU SER LYS ASN PRO
SEQRES 32 B 692 ASP ILE SER ILE ALA GLU LEU MET GLU ASP ILE GLU GLY
SEQRES 33 B 692 PRO ASP PHE PRO THR ALA GLY LEU ILE LEU GLY LYS SER
SEQRES 34 B 692 GLY ILE ARG ARG ALA TYR GLU THR GLY ARG GLY SER ILE
SEQRES 35 B 692 GLN MET ARG SER ARG ALA VAL ILE GLU GLU ARG GLY GLY
SEQRES 36 B 692 GLY ARG GLN ARG ILE VAL VAL THR GLU ILE PRO PHE GLN
SEQRES 37 B 692 VAL ASN LYS ALA ARG MET ILE GLU LYS ILE ALA GLU LEU
SEQRES 38 B 692 VAL ARG ASP LYS LYS ILE ASP GLY ILE THR ASP LEU ARG
SEQRES 39 B 692 ASP GLU THR SER LEU ARG THR GLY VAL ARG VAL VAL ILE
SEQRES 40 B 692 ASP VAL ARG LYS ASP ALA ASN ALA SER VAL ILE LEU ASN
SEQRES 41 B 692 ASN LEU TYR LYS GLN THR PRO LEU GLN THR SER PHE GLY
SEQRES 42 B 692 VAL ASN MET ILE ALA LEU VAL ASN GLY ARG PRO LYS LEU
SEQRES 43 B 692 ILE ASN LEU LYS GLU ALA LEU VAL HIS TYR LEU GLU HIS
SEQRES 44 B 692 GLN LYS THR VAL VAL ARG ARG ARG THR GLN TYR ASN LEU
SEQRES 45 B 692 ARG LYS ALA LYS ASP ARG ALA HIS ILE LEU GLU GLY LEU
SEQRES 46 B 692 ARG ILE ALA LEU ASP HIS ILE ASP GLU ILE ILE SER THR
SEQRES 47 B 692 ILE ARG GLU SER ASP THR ASP LYS VAL ALA MET GLU SER
SEQRES 48 B 692 LEU GLN GLN ARG PHE LYS LEU SER GLU LYS GLN ALA GLN
SEQRES 49 B 692 ALA ILE LEU ASP MET ARG LEU ARG ARG LEU THR GLY LEU
SEQRES 50 B 692 GLU ARG ASP LYS ILE GLU ALA GLU TYR ASN GLU LEU LEU
SEQRES 51 B 692 ASN TYR ILE SER GLU LEU GLU THR ILE LEU ALA ASP GLU
SEQRES 52 B 692 GLU VAL LEU LEU GLN LEU VAL ARG ASP GLU LEU THR GLU
SEQRES 53 B 692 ILE ARG ASP ARG PHE GLY ASP ASP ARG ARG THR GLU ILE
SEQRES 54 B 692 GLN LEU GLY
SEQRES 1 D 692 MET ASP VAL ALA SER LEU PRO GLY LYS LEU ALA ASP CYS
SEQRES 2 D 692 SER SER LYS SER PRO GLU GLU CYS GLU ILE PHE LEU VAL
SEQRES 3 D 692 GLU GLY ASP SER ALA GLY GLY SER THR LYS SER GLY ARG
SEQRES 4 D 692 ASP SER ARG THR GLN ALA ILE LEU PRO LEU ARG GLY LYS
SEQRES 5 D 692 ILE LEU ASN VAL GLU LYS ALA ARG LEU ASP ARG ILE LEU
SEQRES 6 D 692 ASN ASN ASN GLU ILE ARG GLN MET ILE THR ALA PHE GLY
SEQRES 7 D 692 THR GLY ILE GLY GLY ASP PHE ASP LEU ALA LYS ALA ARG
SEQRES 8 D 692 TYR HIS LYS ILE VAL ILE MET THR ASP ALA ASP VAL ASP
SEQRES 9 D 692 GLY ALA HIS ILE ARG THR LEU LEU LEU THR PHE PHE TYR
SEQRES 10 D 692 ARG PHE MET ARG PRO LEU ILE GLU ALA GLY TYR VAL TYR
SEQRES 11 D 692 ILE ALA GLN PRO PRO THR GLY TYR LYS GLY LEU GLY GLU
SEQRES 12 D 692 MET ASN ALA ASP GLN LEU TRP GLU THR THR MET ASN PRO
SEQRES 13 D 692 GLU HIS ARG ALA LEU LEU GLN VAL LYS LEU GLU ASP ALA
SEQRES 14 D 692 ILE GLU ALA ASP GLN THR PHE GLU MET LEU MET GLY ASP
SEQRES 15 D 692 VAL VAL GLU ASN ARG ARG GLN PHE ILE GLU ASP ASN ALA
SEQRES 16 D 692 VAL TYR ALA ASN LEU ASP PHE ALA GLU LEU PRO GLN SER
SEQRES 17 D 692 ARG ILE ASN GLU ARG ASN ILE THR SER GLU MET ARG GLU
SEQRES 18 D 692 SER PHE LEU ASP TYR ALA MET SER VAL ILE VAL ALA ARG
SEQRES 19 D 692 ALA LEU PRO ASP VAL ARG ASP GLY LEU LYS PRO VAL HIS
SEQRES 20 D 692 ARG ARG ILE LEU TYR GLY LEU ASN GLU GLN GLY MET THR
SEQRES 21 D 692 PRO ASP LYS SER TYR LYS LYS SER ALA ARG ILE VAL GLY
SEQRES 22 D 692 ASP VAL MET GLY LYS TYR HIS PRO HIS GLY ASP SER SER
SEQRES 23 D 692 ILE TYR GLU ALA MET VAL ARG MET ALA GLN ASP PHE SER
SEQRES 24 D 692 TYR ARG TYR PRO LEU VAL ASP GLY GLN GLY ASN PHE GLY
SEQRES 25 D 692 SER MET ASP GLY ASP GLY ALA ALA ALA MET ARG PHE THR
SEQRES 26 D 692 GLU ALA ARG MET THR LYS ILE THR LEU GLU LEU LEU ARG
SEQRES 27 D 692 ASP ILE ASN LYS ASP THR ILE ASP PHE ILE ASP ASN TYR
SEQRES 28 D 692 ASP GLY ASN GLU ARG GLU PRO SER VAL LEU PRO ALA ARG
SEQRES 29 D 692 PHE PRO ASN LEU LEU ALA ASN GLY ALA SER GLY ILE ALA
SEQRES 30 D 692 VAL GLY MET ALA THR ASN ILE PRO PRO HIS ASN LEU THR
SEQRES 31 D 692 GLU LEU ILE ASN GLY VAL LEU SER LEU SER LYS ASN PRO
SEQRES 32 D 692 ASP ILE SER ILE ALA GLU LEU MET GLU ASP ILE GLU GLY
SEQRES 33 D 692 PRO ASP PHE PRO THR ALA GLY LEU ILE LEU GLY LYS SER
SEQRES 34 D 692 GLY ILE ARG ARG ALA TYR GLU THR GLY ARG GLY SER ILE
SEQRES 35 D 692 GLN MET ARG SER ARG ALA VAL ILE GLU GLU ARG GLY GLY
SEQRES 36 D 692 GLY ARG GLN ARG ILE VAL VAL THR GLU ILE PRO PHE GLN
SEQRES 37 D 692 VAL ASN LYS ALA ARG MET ILE GLU LYS ILE ALA GLU LEU
SEQRES 38 D 692 VAL ARG ASP LYS LYS ILE ASP GLY ILE THR ASP LEU ARG
SEQRES 39 D 692 ASP GLU THR SER LEU ARG THR GLY VAL ARG VAL VAL ILE
SEQRES 40 D 692 ASP VAL ARG LYS ASP ALA ASN ALA SER VAL ILE LEU ASN
SEQRES 41 D 692 ASN LEU TYR LYS GLN THR PRO LEU GLN THR SER PHE GLY
SEQRES 42 D 692 VAL ASN MET ILE ALA LEU VAL ASN GLY ARG PRO LYS LEU
SEQRES 43 D 692 ILE ASN LEU LYS GLU ALA LEU VAL HIS TYR LEU GLU HIS
SEQRES 44 D 692 GLN LYS THR VAL VAL ARG ARG ARG THR GLN TYR ASN LEU
SEQRES 45 D 692 ARG LYS ALA LYS ASP ARG ALA HIS ILE LEU GLU GLY LEU
SEQRES 46 D 692 ARG ILE ALA LEU ASP HIS ILE ASP GLU ILE ILE SER THR
SEQRES 47 D 692 ILE ARG GLU SER ASP THR ASP LYS VAL ALA MET GLU SER
SEQRES 48 D 692 LEU GLN GLN ARG PHE LYS LEU SER GLU LYS GLN ALA GLN
SEQRES 49 D 692 ALA ILE LEU ASP MET ARG LEU ARG ARG LEU THR GLY LEU
SEQRES 50 D 692 GLU ARG ASP LYS ILE GLU ALA GLU TYR ASN GLU LEU LEU
SEQRES 51 D 692 ASN TYR ILE SER GLU LEU GLU THR ILE LEU ALA ASP GLU
SEQRES 52 D 692 GLU VAL LEU LEU GLN LEU VAL ARG ASP GLU LEU THR GLU
SEQRES 53 D 692 ILE ARG ASP ARG PHE GLY ASP ASP ARG ARG THR GLU ILE
SEQRES 54 D 692 GLN LEU GLY
SEQRES 1 E 19 DG DC DC DG DT DA DG DG DG DC DC DC DT
SEQRES 2 E 19 DA DC DG DG DC DT
SEQRES 1 F 18 DG DC DC DG DT DA DG DG DG DC DC DC DT
SEQRES 2 F 18 DA DC DG DG DC
HET MN B1501 1
HET MN E 101 1
HET 5UA E 102 21
HET DU5 E 103 56
HET MN F1501 1
HET 5UA F1502 21
HETNAM MN MANGANESE (II) ION
HETNAM 5UA 5'-O-CARBOXY-2'-DEOXYADENOSINE
HETNAM DU5 ~{N}-[3-(4-ISOQUINOLIN-1-YLPIPERAZIN-1-YL)
HETNAM 2 DU5 PROPYL]BENZAMIDE
FORMUL 5 MN 3(MN 2+)
FORMUL 7 5UA 2(C11 H13 N5 O5)
FORMUL 8 DU5 C23 H26 N4 O
FORMUL 11 HOH *62(H2 O)
HELIX 1 AA1 SER B 425 GLU B 428 5 4
HELIX 2 AA2 GLY B 436 SER B 445 1 10
HELIX 3 AA3 ARG B 468 ASN B 474 1 7
HELIX 4 AA4 ASN B 475 GLY B 486 1 12
HELIX 5 AA5 ASP B 510 MET B 528 1 19
HELIX 6 AA6 MET B 528 ALA B 534 1 7
HELIX 7 AA7 GLY B 582 MET B 586 5 5
HELIX 8 AA8 ASN B 587 MET B 596 1 10
HELIX 9 AA9 ASP B 610 GLY B 623 1 14
HELIX 10 AB1 VAL B 625 ALA B 637 1 13
HELIX 11 AB2 ILE B 1014 ALA B 1032 1 19
HELIX 12 AB3 LYS B 1043 GLN B 1056 1 14
HELIX 13 AB4 SER B 1067 TYR B 1078 1 12
HELIX 14 AB5 GLY B 1082 GLN B 1095 1 14
HELIX 15 AB6 THR B 1129 ARG B 1137 1 9
HELIX 16 AB7 PRO B 1165 ASN B 1170 1 6
HELIX 17 AB8 ASN B 1187 LYS B 1200 1 14
HELIX 18 AB9 SER B 1205 ILE B 1213 1 9
HELIX 19 AC1 LYS B 1227 GLY B 1237 1 11
HELIX 20 AC2 ASN B 1269 ASP B 1283 1 15
HELIX 21 AC3 ALA B 1314 THR B 1325 1 12
HELIX 22 AC4 ASN B 1347 ASP B 1389 1 43
HELIX 23 AC5 HIS B 1390 SER B 1401 1 12
HELIX 24 AC6 THR B 1403 LYS B 1416 1 14
HELIX 25 AC7 SER B 1418 ASP B 1427 1 10
HELIX 26 AC8 ARG B 1429 GLY B 1435 5 7
HELIX 27 AC9 LEU B 1436 LEU B 1459 1 24
HELIX 28 AD1 ASP B 1461 GLY B 1481 1 21
HELIX 29 AD2 GLY D 436 ARG D 447 1 12
HELIX 30 AD3 ASN D 463 ALA D 467 5 5
HELIX 31 AD4 ARG D 468 ASN D 475 1 8
HELIX 32 AD5 ASN D 475 GLY D 486 1 12
HELIX 33 AD6 ILE D 489 PHE D 493 5 5
HELIX 34 AD7 ASP D 494 ALA D 498 5 5
HELIX 35 AD8 ASP D 510 MET D 528 1 19
HELIX 36 AD9 MET D 528 ALA D 534 1 7
HELIX 37 AE1 GLY D 582 MET D 586 5 5
HELIX 38 AE2 ASN D 587 MET D 596 1 10
HELIX 39 AE3 ASP D 610 GLY D 623 1 14
HELIX 40 AE4 VAL D 625 ALA D 637 1 13
HELIX 41 AE5 ILE D 1014 ALA D 1032 1 19
HELIX 42 AE6 LYS D 1043 GLU D 1055 1 13
HELIX 43 AE7 SER D 1067 TYR D 1078 1 12
HELIX 44 AE8 GLY D 1082 MET D 1093 1 12
HELIX 45 AE9 ILE D 1131 ARG D 1137 1 7
HELIX 46 AF1 PRO D 1165 GLY D 1171 1 7
HELIX 47 AF2 ASN D 1187 LYS D 1200 1 14
HELIX 48 AF3 SER D 1205 ILE D 1213 1 9
HELIX 49 AF4 LYS D 1227 GLY D 1237 1 11
HELIX 50 AF5 ASN D 1269 ASP D 1283 1 15
HELIX 51 AF6 ASN D 1313 THR D 1325 1 13
HELIX 52 AF7 ASN D 1347 HIS D 1390 1 44
HELIX 53 AF8 HIS D 1390 GLU D 1400 1 11
HELIX 54 AF9 THR D 1403 LYS D 1416 1 14
HELIX 55 AG1 SER D 1418 MET D 1428 1 11
HELIX 56 AG2 ARG D 1429 LEU D 1433 5 5
HELIX 57 AG3 THR D 1434 ASP D 1461 1 28
HELIX 58 AG4 ASP D 1461 GLY D 1481 1 21
SHEET 1 AA1 6 GLN B 452 PRO B 456 0
SHEET 2 AA1 6 GLU B 430 VAL B 434 1 N PHE B 432 O ALA B 453
SHEET 3 AA1 6 LYS B 502 ILE B 505 1 O VAL B 504 N ILE B 431
SHEET 4 AA1 6 VAL B 537 ILE B 539 1 O TYR B 538 N ILE B 505
SHEET 5 AA1 6 LEU B 604 LYS B 607 -1 O LEU B 604 N ILE B 539
SHEET 6 AA1 6 GLU B1011 ASN B1013 1 O ARG B1012 N LYS B 607
SHEET 1 AA2 3 LYS B1065 LYS B1066 0
SHEET 2 AA2 3 GLU B1125 MET B1128 -1 O ALA B1126 N LYS B1065
SHEET 3 AA2 3 VAL B1104 GLN B1107 -1 N ASP B1105 O ARG B1127
SHEET 1 AA3 2 PHE B1146 ASP B1148 0
SHEET 2 AA3 2 ARG B1155 PRO B1157 -1 O GLU B1156 N ILE B1147
SHEET 1 AA4 2 ALA B1172 ILE B1175 0
SHEET 2 AA4 2 ALA B1180 ILE B1183 -1 O THR B1181 N GLY B1174
SHEET 1 AA5 4 GLN B1328 ASN B1334 0
SHEET 2 AA5 4 ARG B1238 ARG B1244 -1 N MET B1243 O THR B1329
SHEET 3 AA5 4 GLY B1222 ILE B1224 -1 N LEU B1223 O ARG B1244
SHEET 4 AA5 4 THR B1486 GLU B1487 1 O GLU B1487 N GLY B1222
SHEET 1 AA6 4 ARG B1246 GLU B1251 0
SHEET 2 AA6 4 GLN B1257 GLU B1263 -1 O ARG B1258 N GLU B1250
SHEET 3 AA6 4 VAL B1304 VAL B1308 -1 O VAL B1304 N VAL B1261
SHEET 4 AA6 4 ILE B1289 ASP B1294 -1 N ARG B1293 O VAL B1305
SHEET 1 AA7 2 ILE B1336 VAL B1339 0
SHEET 2 AA7 2 ARG B1342 LEU B1345 -1 O LYS B1344 N ALA B1337
SHEET 1 AA8 6 GLN D 452 PRO D 456 0
SHEET 2 AA8 6 GLU D 430 VAL D 434 1 N PHE D 432 O ALA D 453
SHEET 3 AA8 6 LYS D 502 ILE D 505 1 O VAL D 504 N LEU D 433
SHEET 4 AA8 6 VAL D 537 ILE D 539 1 O TYR D 538 N ILE D 503
SHEET 5 AA8 6 LEU D 604 LYS D 607 -1 O VAL D 606 N VAL D 537
SHEET 6 AA8 6 GLU D1011 ASN D1013 1 O ARG D1012 N LYS D 607
SHEET 1 AA9 3 LYS D1065 LYS D1066 0
SHEET 2 AA9 3 GLU D1125 MET D1128 -1 O ALA D1126 N LYS D1065
SHEET 3 AA9 3 VAL D1104 GLN D1107 -1 N GLN D1107 O GLU D1125
SHEET 1 AB1 2 PHE D1146 ASP D1148 0
SHEET 2 AB1 2 ARG D1155 PRO D1157 -1 O GLU D1156 N ILE D1147
SHEET 1 AB2 2 ALA D1172 ILE D1175 0
SHEET 2 AB2 2 ALA D1180 ILE D1183 -1 O ILE D1183 N ALA D1172
SHEET 1 AB3 4 GLN D1328 ASN D1334 0
SHEET 2 AB3 4 ARG D1238 ARG D1244 -1 N MET D1243 O THR D1329
SHEET 3 AB3 4 LEU D1223 LEU D1225 -1 N LEU D1223 O ARG D1244
SHEET 4 AB3 4 GLU D1487 GLN D1489 1 O GLU D1487 N ILE D1224
SHEET 1 AB4 4 ARG D1246 GLU D1251 0
SHEET 2 AB4 4 GLN D1257 GLU D1263 -1 O VAL D1260 N VAL D1248
SHEET 3 AB4 4 VAL D1304 VAL D1308 -1 O VAL D1304 N VAL D1261
SHEET 4 AB4 4 ILE D1289 ASP D1294 -1 N THR D1290 O ASP D1307
SHEET 1 AB5 2 ILE D1336 VAL D1339 0
SHEET 2 AB5 2 ARG D1342 LEU D1345 -1 O LYS D1344 N ALA D1337
LINK P DG F 2 O3' 5UA F1502 1555 1555 1.42
LINK O TYR B1322 MN MN B1501 1555 1555 2.74
LINK O3' DG E 8 MN MN E 101 1555 1555 2.53
LINK P DG E 9 MN MN E 101 1555 1555 2.57
LINK O3' DG F 8 MN MN F1501 1555 1555 2.62
LINK OP1 DG F 9 MN MN F1501 1555 1555 1.89
SITE 1 AC1 10 ALA B1068 MET B1075 ASP B1083 MET B1121
SITE 2 AC1 10 ASP D1083 MET D1121 DG E 10 DC E 11
SITE 3 AC1 10 DG F 10 DC F 11
CRYST1 92.951 92.951 407.030 90.00 90.00 120.00 P 61 12
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 0.010758 0.006211 0.000000 0.00000
SCALE2 0.000000 0.012423 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002457 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
