HEADER RECOMBINATION,VIRAL PROTEIN/DNA 23-SEP-10 3OYH
TITLE CRYSTAL STRUCTURE OF THE PROTOTYPE FOAMY VIRUS (PFV) INTASOME IN
TITLE 2 COMPLEX WITH MAGNESIUM AND THE INSTI MK0536
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PFV INTEGRASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 752 TO 1143;
COMPND 5 SYNONYM: P42IN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-
COMPND 9 D(*AP*TP*TP*GP*TP*CP*AP*TP*GP*GP*AP*AP*TP*TP*TP*CP*GP*CP*A)-3');
COMPND 10 CHAIN: C;
COMPND 11 ENGINEERED: YES;
COMPND 12 OTHER_DETAILS: 19 NUCLEOTIDE PREPROCESSED PFV DONOR DNA (NON-
COMPND 13 TRANSFERRED STRAND);
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: DNA (5'-
COMPND 16 D(*TP*GP*CP*GP*AP*AP*AP*TP*TP*CP*CP*AP*TP*GP*AP*CP*A)-3');
COMPND 17 CHAIN: D;
COMPND 18 ENGINEERED: YES;
COMPND 19 OTHER_DETAILS: 17 NUCLEOTIDE PREPROCESSED PFV DONOR DNA (TRANSFERRED
COMPND 20 STRAND)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN SPUMARETROVIRUS;
SOURCE 3 ORGANISM_COMMON: SFVCPZ(HU);
SOURCE 4 ORGANISM_TAXID: 11963;
SOURCE 5 STRAIN: HSRV2;
SOURCE 6 GENE: POL;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: PC2;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PSSH6P-PFV-INFL;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 OTHER_DETAILS: DONOR DNA NON-TRANSFERRED STRAND;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 OTHER_DETAILS: DONOR DNA TRANSFERRED STRAND
KEYWDS PROTEIN-DNA COMPLEX, TETRAMER, DNA INTEGRATION, ENDONUCLEASE, METAL-
KEYWDS 2 BINDING, MULTIFUNCTIONAL ENZYME, NUCLEASE, NUCLEOTIDYLTRANSFERASE,
KEYWDS 3 NUCLEUS, TRANSFERASE, VIRAL NUCLEOPROTEIN, VIRION, DNA-BINDING, ZINC
KEYWDS 4 BINDING, HHCC MOTIF, VIRAL PROTEIN, RECOMBINATION, INHIBITOR, DNA-
KEYWDS 5 BINDING PROTEIN-DNA COMPLEX, VIRAL PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HARE,P.CHEREPANOV
REVDAT 4 06-SEP-23 3OYH 1 REMARK SEQADV LINK
REVDAT 3 30-MAR-11 3OYH 1 REMARK
REVDAT 2 01-DEC-10 3OYH 1 JRNL
REVDAT 1 17-NOV-10 3OYH 0
JRNL AUTH S.HARE,A.M.VOS,R.F.CLAYTON,J.W.THURING,M.D.CUMMINGS,
JRNL AUTH 2 P.CHEREPANOV
JRNL TITL MOLECULAR MECHANISMS OF RETROVIRAL INTEGRASE INHIBITION AND
JRNL TITL 2 THE EVOLUTION OF VIRAL RESISTANCE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 20057 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 21030679
JRNL DOI 10.1073/PNAS.1010246107
REMARK 2
REMARK 2 RESOLUTION. 2.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 41736
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2098
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) : 2.74
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.81
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2910
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.3550
REMARK 3 BIN FREE R VALUE SET COUNT : 152
REMARK 3 BIN FREE R VALUE : 0.3860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4343
REMARK 3 NUCLEIC ACID ATOMS : 732
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 162
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.99000
REMARK 3 B22 (A**2) : 1.99000
REMARK 3 B33 (A**2) : -3.98000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.241
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.193
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.853
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5342 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7439 ; 1.580 ; 2.155
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 550 ; 6.091 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 183 ;33.757 ;23.716
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 724 ;16.848 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;17.887 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 838 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3785 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2777 ; 0.748 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4530 ; 1.431 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2565 ; 1.729 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2909 ; 2.958 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3OYH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000061730.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98011
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41844
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740
REMARK 200 RESOLUTION RANGE LOW (A) : 39.923
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.88000
REMARK 200 R SYM FOR SHELL (I) : 0.88000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3OYB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.35 M AMMONIUM SULFATE, 25% (V/V)
REMARK 280 GLYCEROL, 4.8% (V/V) 1,6-HEXANEDIOL, 50 MM MES-NAOH, 1MM EDTA,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 61.86500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 79.51500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 79.51500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.93250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 79.51500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 79.51500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 92.79750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 79.51500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 79.51500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 30.93250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 79.51500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 79.51500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 92.79750
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 61.86500
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 27710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -253.0 KCAL/MOL
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 -61.86500
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 GLY A -2
REMARK 465 PRO A -1
REMARK 465 GLY A 0
REMARK 465 CYS A 1
REMARK 465 ASN A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 LYS A 5
REMARK 465 PRO A 6
REMARK 465 ASN A 7
REMARK 465 ASN A 376
REMARK 465 GLY A 377
REMARK 465 THR A 378
REMARK 465 THR A 379
REMARK 465 ASN A 380
REMARK 465 ASP A 381
REMARK 465 THR A 382
REMARK 465 ALA A 383
REMARK 465 THR A 384
REMARK 465 MET A 385
REMARK 465 ASP A 386
REMARK 465 HIS A 387
REMARK 465 LEU A 388
REMARK 465 GLU A 389
REMARK 465 LYS A 390
REMARK 465 ASN A 391
REMARK 465 GLU A 392
REMARK 465 GLY B -2
REMARK 465 PRO B -1
REMARK 465 GLY B 0
REMARK 465 CYS B 1
REMARK 465 ASN B 2
REMARK 465 THR B 3
REMARK 465 LYS B 4
REMARK 465 LYS B 5
REMARK 465 PRO B 6
REMARK 465 ASN B 7
REMARK 465 LEU B 8
REMARK 465 ASP B 9
REMARK 465 ALA B 10
REMARK 465 GLU B 11
REMARK 465 LEU B 12
REMARK 465 ASP B 13
REMARK 465 GLN B 14
REMARK 465 LEU B 15
REMARK 465 LEU B 16
REMARK 465 GLN B 17
REMARK 465 GLY B 18
REMARK 465 HIS B 19
REMARK 465 TYR B 20
REMARK 465 ILE B 21
REMARK 465 LYS B 22
REMARK 465 GLY B 23
REMARK 465 TYR B 24
REMARK 465 PRO B 25
REMARK 465 LYS B 26
REMARK 465 GLN B 27
REMARK 465 TYR B 28
REMARK 465 THR B 29
REMARK 465 TYR B 30
REMARK 465 PHE B 31
REMARK 465 LEU B 32
REMARK 465 GLU B 33
REMARK 465 ASP B 34
REMARK 465 GLY B 35
REMARK 465 LYS B 36
REMARK 465 VAL B 37
REMARK 465 LYS B 38
REMARK 465 VAL B 39
REMARK 465 SER B 40
REMARK 465 ARG B 41
REMARK 465 PRO B 42
REMARK 465 GLU B 43
REMARK 465 GLY B 44
REMARK 465 VAL B 45
REMARK 465 LYS B 46
REMARK 465 ILE B 47
REMARK 465 ILE B 48
REMARK 465 PRO B 49
REMARK 465 PRO B 50
REMARK 465 GLN B 51
REMARK 465 SER B 52
REMARK 465 ASP B 53
REMARK 465 ARG B 54
REMARK 465 GLN B 55
REMARK 465 LYS B 56
REMARK 465 ILE B 57
REMARK 465 VAL B 58
REMARK 465 LEU B 59
REMARK 465 GLN B 60
REMARK 465 ALA B 61
REMARK 465 HIS B 62
REMARK 465 ASN B 63
REMARK 465 LEU B 64
REMARK 465 ALA B 65
REMARK 465 HIS B 66
REMARK 465 THR B 67
REMARK 465 GLY B 68
REMARK 465 ARG B 69
REMARK 465 GLU B 70
REMARK 465 ALA B 71
REMARK 465 THR B 72
REMARK 465 LEU B 73
REMARK 465 LEU B 74
REMARK 465 LYS B 75
REMARK 465 ILE B 76
REMARK 465 ALA B 77
REMARK 465 ASN B 78
REMARK 465 LEU B 79
REMARK 465 TYR B 80
REMARK 465 TRP B 81
REMARK 465 TRP B 82
REMARK 465 PRO B 83
REMARK 465 ASN B 84
REMARK 465 MET B 85
REMARK 465 ARG B 86
REMARK 465 LYS B 87
REMARK 465 ASP B 88
REMARK 465 VAL B 89
REMARK 465 VAL B 90
REMARK 465 LYS B 91
REMARK 465 GLN B 92
REMARK 465 LEU B 93
REMARK 465 GLY B 94
REMARK 465 ARG B 95
REMARK 465 CYS B 96
REMARK 465 GLN B 97
REMARK 465 GLN B 98
REMARK 465 CYS B 99
REMARK 465 LEU B 100
REMARK 465 ILE B 101
REMARK 465 THR B 102
REMARK 465 ASN B 103
REMARK 465 ALA B 104
REMARK 465 SER B 105
REMARK 465 ASN B 106
REMARK 465 LYS B 107
REMARK 465 ALA B 108
REMARK 465 SER B 109
REMARK 465 GLY B 110
REMARK 465 PRO B 111
REMARK 465 ILE B 112
REMARK 465 LEU B 113
REMARK 465 ARG B 114
REMARK 465 PRO B 115
REMARK 465 THR B 300
REMARK 465 SER B 301
REMARK 465 LEU B 302
REMARK 465 TYR B 303
REMARK 465 HIS B 304
REMARK 465 PRO B 305
REMARK 465 SER B 306
REMARK 465 THR B 307
REMARK 465 PRO B 308
REMARK 465 PRO B 309
REMARK 465 ALA B 310
REMARK 465 SER B 311
REMARK 465 SER B 312
REMARK 465 ARG B 313
REMARK 465 SER B 314
REMARK 465 TRP B 315
REMARK 465 SER B 316
REMARK 465 PRO B 317
REMARK 465 VAL B 318
REMARK 465 VAL B 319
REMARK 465 GLY B 320
REMARK 465 GLN B 321
REMARK 465 LEU B 322
REMARK 465 VAL B 323
REMARK 465 GLN B 324
REMARK 465 GLU B 325
REMARK 465 ARG B 326
REMARK 465 VAL B 327
REMARK 465 ALA B 328
REMARK 465 ARG B 329
REMARK 465 PRO B 330
REMARK 465 ALA B 331
REMARK 465 SER B 332
REMARK 465 LEU B 333
REMARK 465 ARG B 334
REMARK 465 PRO B 335
REMARK 465 ARG B 336
REMARK 465 TRP B 337
REMARK 465 HIS B 338
REMARK 465 LYS B 339
REMARK 465 PRO B 340
REMARK 465 SER B 341
REMARK 465 THR B 342
REMARK 465 VAL B 343
REMARK 465 LEU B 344
REMARK 465 LYS B 345
REMARK 465 VAL B 346
REMARK 465 LEU B 347
REMARK 465 ASN B 348
REMARK 465 PRO B 349
REMARK 465 ARG B 350
REMARK 465 THR B 351
REMARK 465 VAL B 352
REMARK 465 VAL B 353
REMARK 465 ILE B 354
REMARK 465 LEU B 355
REMARK 465 ASP B 356
REMARK 465 HIS B 357
REMARK 465 LEU B 358
REMARK 465 GLY B 359
REMARK 465 ASN B 360
REMARK 465 ASN B 361
REMARK 465 ARG B 362
REMARK 465 THR B 363
REMARK 465 VAL B 364
REMARK 465 SER B 365
REMARK 465 ILE B 366
REMARK 465 ASP B 367
REMARK 465 ASN B 368
REMARK 465 LEU B 369
REMARK 465 LYS B 370
REMARK 465 PRO B 371
REMARK 465 THR B 372
REMARK 465 SER B 373
REMARK 465 HIS B 374
REMARK 465 GLN B 375
REMARK 465 ASN B 376
REMARK 465 GLY B 377
REMARK 465 THR B 378
REMARK 465 THR B 379
REMARK 465 ASN B 380
REMARK 465 ASP B 381
REMARK 465 THR B 382
REMARK 465 ALA B 383
REMARK 465 THR B 384
REMARK 465 MET B 385
REMARK 465 ASP B 386
REMARK 465 HIS B 387
REMARK 465 LEU B 388
REMARK 465 GLU B 389
REMARK 465 LYS B 390
REMARK 465 ASN B 391
REMARK 465 GLU B 392
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 LEU A 8 CG CD1 CD2
REMARK 470 LYS A 26 CG CD CE NZ
REMARK 470 LYS A 241 CG CD CE NZ
REMARK 470 ARG A 329 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 197 CG CD OE1 OE2
REMARK 470 HIS B 213 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 241 CG CD CE NZ
REMARK 470 LYS B 262 CG CD CE NZ
REMARK 470 GLN B 281 CG CD OE1 NE2
REMARK 470 LEU B 292 CG CD1 CD2
REMARK 470 LEU B 294 CG CD1 CD2
REMARK 470 LEU B 295 CG CD1 CD2
REMARK 470 GLN B 296 CG CD OE1 NE2
REMARK 470 GLU B 297 CG CD OE1 OE2
REMARK 470 ILE B 298 CG1 CG2 CD1
REMARK 470 ARG B 299 CG CD NE CZ NH1 NH2
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 MG MG A 396 OAG ZYN A 398 1.66
REMARK 500 O HOH A 410 O HOH A 509 2.04
REMARK 500 OE1 GLN A 98 O HOH A 439 2.04
REMARK 500 O HOH A 492 O HOH A 493 2.07
REMARK 500 O HOH A 493 O HOH A 494 2.09
REMARK 500 O SER B 258 O LEU B 261 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 DT D 9 O3' DT D 9 C3' -0.040
REMARK 500 DC D 11 O3' DC D 11 C3' -0.038
REMARK 500 DC D 16 O3' DC D 16 C3' -0.041
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 DA C 1 C3' - O3' - P ANGL. DEV. = 7.3 DEGREES
REMARK 500 DT C 3 O4' - C1' - N1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 DT C 3 C5 - C4 - O4 ANGL. DEV. = -5.0 DEGREES
REMARK 500 DG C 4 O4' - C1' - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DT C 5 O4' - C1' - N1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 DT C 8 O4' - C4' - C3' ANGL. DEV. = -3.1 DEGREES
REMARK 500 DG C 9 O5' - C5' - C4' ANGL. DEV. = -5.1 DEGREES
REMARK 500 DG C 17 O5' - C5' - C4' ANGL. DEV. = -5.5 DEGREES
REMARK 500 DG C 17 O4' - C1' - N9 ANGL. DEV. = -5.4 DEGREES
REMARK 500 DC C 18 O4' - C4' - C3' ANGL. DEV. = -3.3 DEGREES
REMARK 500 DT D 1 C3' - O3' - P ANGL. DEV. = 9.7 DEGREES
REMARK 500 DG D 2 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DC D 11 O5' - C5' - C4' ANGL. DEV. = -5.6 DEGREES
REMARK 500 DC D 11 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DA D 12 O4' - C1' - N9 ANGL. DEV. = -6.3 DEGREES
REMARK 500 DA D 15 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC D 16 O4' - C4' - C3' ANGL. DEV. = -2.7 DEGREES
REMARK 500 DA D 17 C3' - C2' - C1' ANGL. DEV. = -6.3 DEGREES
REMARK 500 DA D 17 C8 - N9 - C4 ANGL. DEV. = 2.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 17 23.75 -77.25
REMARK 500 PHE A 31 -169.15 -106.79
REMARK 500 GLU A 33 136.02 -178.20
REMARK 500 ASP A 34 25.98 48.42
REMARK 500 GLN A 51 -35.66 -39.21
REMARK 500 ARG A 69 -75.26 -54.94
REMARK 500 PHE A 122 -2.46 79.07
REMARK 500 GLN A 137 29.46 46.78
REMARK 500 GLN A 186 31.36 -94.56
REMARK 500 GLU A 201 -27.17 -37.91
REMARK 500 HIS A 213 71.40 -158.38
REMARK 500 THR A 240 68.74 -65.88
REMARK 500 THR A 307 123.30 -38.74
REMARK 500 ASP A 356 32.14 -93.96
REMARK 500 HIS A 357 -12.79 66.86
REMARK 500 PRO B 135 122.40 -39.46
REMARK 500 GLN B 186 35.41 -94.96
REMARK 500 TYR B 212 -19.54 70.13
REMARK 500 HIS B 213 77.95 -113.93
REMARK 500 SER B 216 -107.02 -121.33
REMARK 500 PHE B 278 76.18 -111.85
REMARK 500 ASN B 280 82.35 -66.87
REMARK 500 LEU B 284 -7.34 63.00
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 ZN A 393 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 62 NE2
REMARK 620 2 HIS A 66 ND1 107.1
REMARK 620 3 CYS A 96 SG 113.5 102.6
REMARK 620 4 CYS A 99 SG 101.7 117.1 115.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 396 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 128 OD1
REMARK 620 2 ASP A 185 OD1 90.8
REMARK 620 3 ZYN A 398 OAH 89.2 102.9
REMARK 620 4 HOH A 400 O 87.9 92.5 164.4
REMARK 620 5 HOH A 497 O 98.6 168.6 83.6 81.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 397 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 128 OD2
REMARK 620 2 GLU A 221 OE1 94.0
REMARK 620 3 GLU A 221 OE2 89.3 66.4
REMARK 620 4 ZYN A 398 OAH 92.4 157.3 91.9
REMARK 620 5 ZYN A 398 OAF 167.4 94.4 85.4 76.3
REMARK 620 6 HOH A 399 O 89.3 119.2 174.3 82.6 94.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 394 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 128 OD1
REMARK 620 2 ASP B 185 OD1 99.0
REMARK 620 3 HOH B 395 O 82.4 167.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 393
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 393
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 A 395
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 396
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 397
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZYN A 398
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DLR RELATED DB: PDB
REMARK 900 CATALYTIC CORE DOMAIN OF PFV INTEGRASE
REMARK 900 RELATED ID: 3L2Q RELATED DB: PDB
REMARK 900 PFV INTASOME IN APO FORM
REMARK 900 RELATED ID: 3L2R RELATED DB: PDB
REMARK 900 PFV INTASOME IN COMPLEX WITH MAGNESIUM
REMARK 900 RELATED ID: 3L2U RELATED DB: PDB
REMARK 900 PFV INTASOME IN COMPLEX WITH MAGNESIUM AND ELVITEGRAVIR
REMARK 900 RELATED ID: 3L2V RELATED DB: PDB
REMARK 900 PFV INTASOME IN COMPLEX WITH MANGANESE AND RALTEGRAVIR
REMARK 900 RELATED ID: 3L2W RELATED DB: PDB
REMARK 900 PFV INTASOME IN COMPLEX WITH MANGANESE AND ELVITEGRAVIR
REMARK 900 RELATED ID: 3OY9 RELATED DB: PDB
REMARK 900 PFV INTASOME IN COMPLEX WITH MANGANESE
REMARK 900 RELATED ID: 3OYA RELATED DB: PDB
REMARK 900 PFV INTASOME IN COMPLEX WITH MAGNESIUM AND RALTEGRAVIR
REMARK 900 RELATED ID: 3OYB RELATED DB: PDB
REMARK 900 PFV INTASOME IN COMPLEX WITH MAGNESIUM AND MK2048
REMARK 900 RELATED ID: 3OYC RELATED DB: PDB
REMARK 900 PFV INTASOME IN COMPLEX WITH MAGNESIUM AND PICA
REMARK 900 RELATED ID: 3OYD RELATED DB: PDB
REMARK 900 PFV INTASOME IN COMPLEX WITH MAGNESIUM AND GS9160
REMARK 900 RELATED ID: 3OYE RELATED DB: PDB
REMARK 900 PFV INTASOME IN COMPLEX WITH MAGNESIUM AND COMPOUND2
REMARK 900 RELATED ID: 3OYF RELATED DB: PDB
REMARK 900 PFV INTASOME IN COMPLEX WITH MAGNESIUM AND L870810
REMARK 900 RELATED ID: 3OYG RELATED DB: PDB
REMARK 900 PFV INTASOME IN COMPLEX WITH MAGNESIUM AND COMPOUND G
REMARK 900 RELATED ID: 3OYI RELATED DB: PDB
REMARK 900 S217Q PFV INTASOME IN COMPLEX WITH MANGANESE
REMARK 900 RELATED ID: 3OYJ RELATED DB: PDB
REMARK 900 S217Q PFV INTASOME IN COMPLEX WITH MAGNESIUM AND MK2048
REMARK 900 RELATED ID: 3OYK RELATED DB: PDB
REMARK 900 S217H PFV INTASOME IN COMPLEX WITH MANGANESE
REMARK 900 RELATED ID: 3OYL RELATED DB: PDB
REMARK 900 S217H PFV INTASOME IN COMPLEX WITH MAGNESIUM AND MK2048
REMARK 900 RELATED ID: 3OYM RELATED DB: PDB
REMARK 900 N224H PFV INTASOME IN COMPLEX WITH MANGANESE
REMARK 900 RELATED ID: 3OYN RELATED DB: PDB
REMARK 900 N224H PFV INTASOME IN COMPLEX WITH MAGNESIUM AND MK2048
DBREF 3OYH A 1 392 UNP P14350 POL_FOAMV 752 1143
DBREF 3OYH B 1 392 UNP P14350 POL_FOAMV 752 1143
DBREF 3OYH C 1 19 PDB 3OYH 3OYH 1 19
DBREF 3OYH D 1 17 PDB 3OYH 3OYH 1 17
SEQADV 3OYH GLY A -2 UNP P14350 EXPRESSION TAG
SEQADV 3OYH PRO A -1 UNP P14350 EXPRESSION TAG
SEQADV 3OYH GLY A 0 UNP P14350 EXPRESSION TAG
SEQADV 3OYH SER A 217 UNP P14350 GLY 968 VARIANT
SEQADV 3OYH GLY A 218 UNP P14350 SER 969 VARIANT
SEQADV 3OYH GLY B -2 UNP P14350 EXPRESSION TAG
SEQADV 3OYH PRO B -1 UNP P14350 EXPRESSION TAG
SEQADV 3OYH GLY B 0 UNP P14350 EXPRESSION TAG
SEQADV 3OYH SER B 217 UNP P14350 GLY 968 VARIANT
SEQADV 3OYH GLY B 218 UNP P14350 SER 969 VARIANT
SEQRES 1 A 395 GLY PRO GLY CYS ASN THR LYS LYS PRO ASN LEU ASP ALA
SEQRES 2 A 395 GLU LEU ASP GLN LEU LEU GLN GLY HIS TYR ILE LYS GLY
SEQRES 3 A 395 TYR PRO LYS GLN TYR THR TYR PHE LEU GLU ASP GLY LYS
SEQRES 4 A 395 VAL LYS VAL SER ARG PRO GLU GLY VAL LYS ILE ILE PRO
SEQRES 5 A 395 PRO GLN SER ASP ARG GLN LYS ILE VAL LEU GLN ALA HIS
SEQRES 6 A 395 ASN LEU ALA HIS THR GLY ARG GLU ALA THR LEU LEU LYS
SEQRES 7 A 395 ILE ALA ASN LEU TYR TRP TRP PRO ASN MET ARG LYS ASP
SEQRES 8 A 395 VAL VAL LYS GLN LEU GLY ARG CYS GLN GLN CYS LEU ILE
SEQRES 9 A 395 THR ASN ALA SER ASN LYS ALA SER GLY PRO ILE LEU ARG
SEQRES 10 A 395 PRO ASP ARG PRO GLN LYS PRO PHE ASP LYS PHE PHE ILE
SEQRES 11 A 395 ASP TYR ILE GLY PRO LEU PRO PRO SER GLN GLY TYR LEU
SEQRES 12 A 395 TYR VAL LEU VAL VAL VAL ASP GLY MET THR GLY PHE THR
SEQRES 13 A 395 TRP LEU TYR PRO THR LYS ALA PRO SER THR SER ALA THR
SEQRES 14 A 395 VAL LYS SER LEU ASN VAL LEU THR SER ILE ALA ILE PRO
SEQRES 15 A 395 LYS VAL ILE HIS SER ASP GLN GLY ALA ALA PHE THR SER
SEQRES 16 A 395 SER THR PHE ALA GLU TRP ALA LYS GLU ARG GLY ILE HIS
SEQRES 17 A 395 LEU GLU PHE SER THR PRO TYR HIS PRO GLN SER SER GLY
SEQRES 18 A 395 LYS VAL GLU ARG LYS ASN SER ASP ILE LYS ARG LEU LEU
SEQRES 19 A 395 THR LYS LEU LEU VAL GLY ARG PRO THR LYS TRP TYR ASP
SEQRES 20 A 395 LEU LEU PRO VAL VAL GLN LEU ALA LEU ASN ASN THR TYR
SEQRES 21 A 395 SER PRO VAL LEU LYS TYR THR PRO HIS GLN LEU LEU PHE
SEQRES 22 A 395 GLY ILE ASP SER ASN THR PRO PHE ALA ASN GLN ASP THR
SEQRES 23 A 395 LEU ASP LEU THR ARG GLU GLU GLU LEU SER LEU LEU GLN
SEQRES 24 A 395 GLU ILE ARG THR SER LEU TYR HIS PRO SER THR PRO PRO
SEQRES 25 A 395 ALA SER SER ARG SER TRP SER PRO VAL VAL GLY GLN LEU
SEQRES 26 A 395 VAL GLN GLU ARG VAL ALA ARG PRO ALA SER LEU ARG PRO
SEQRES 27 A 395 ARG TRP HIS LYS PRO SER THR VAL LEU LYS VAL LEU ASN
SEQRES 28 A 395 PRO ARG THR VAL VAL ILE LEU ASP HIS LEU GLY ASN ASN
SEQRES 29 A 395 ARG THR VAL SER ILE ASP ASN LEU LYS PRO THR SER HIS
SEQRES 30 A 395 GLN ASN GLY THR THR ASN ASP THR ALA THR MET ASP HIS
SEQRES 31 A 395 LEU GLU LYS ASN GLU
SEQRES 1 B 395 GLY PRO GLY CYS ASN THR LYS LYS PRO ASN LEU ASP ALA
SEQRES 2 B 395 GLU LEU ASP GLN LEU LEU GLN GLY HIS TYR ILE LYS GLY
SEQRES 3 B 395 TYR PRO LYS GLN TYR THR TYR PHE LEU GLU ASP GLY LYS
SEQRES 4 B 395 VAL LYS VAL SER ARG PRO GLU GLY VAL LYS ILE ILE PRO
SEQRES 5 B 395 PRO GLN SER ASP ARG GLN LYS ILE VAL LEU GLN ALA HIS
SEQRES 6 B 395 ASN LEU ALA HIS THR GLY ARG GLU ALA THR LEU LEU LYS
SEQRES 7 B 395 ILE ALA ASN LEU TYR TRP TRP PRO ASN MET ARG LYS ASP
SEQRES 8 B 395 VAL VAL LYS GLN LEU GLY ARG CYS GLN GLN CYS LEU ILE
SEQRES 9 B 395 THR ASN ALA SER ASN LYS ALA SER GLY PRO ILE LEU ARG
SEQRES 10 B 395 PRO ASP ARG PRO GLN LYS PRO PHE ASP LYS PHE PHE ILE
SEQRES 11 B 395 ASP TYR ILE GLY PRO LEU PRO PRO SER GLN GLY TYR LEU
SEQRES 12 B 395 TYR VAL LEU VAL VAL VAL ASP GLY MET THR GLY PHE THR
SEQRES 13 B 395 TRP LEU TYR PRO THR LYS ALA PRO SER THR SER ALA THR
SEQRES 14 B 395 VAL LYS SER LEU ASN VAL LEU THR SER ILE ALA ILE PRO
SEQRES 15 B 395 LYS VAL ILE HIS SER ASP GLN GLY ALA ALA PHE THR SER
SEQRES 16 B 395 SER THR PHE ALA GLU TRP ALA LYS GLU ARG GLY ILE HIS
SEQRES 17 B 395 LEU GLU PHE SER THR PRO TYR HIS PRO GLN SER SER GLY
SEQRES 18 B 395 LYS VAL GLU ARG LYS ASN SER ASP ILE LYS ARG LEU LEU
SEQRES 19 B 395 THR LYS LEU LEU VAL GLY ARG PRO THR LYS TRP TYR ASP
SEQRES 20 B 395 LEU LEU PRO VAL VAL GLN LEU ALA LEU ASN ASN THR TYR
SEQRES 21 B 395 SER PRO VAL LEU LYS TYR THR PRO HIS GLN LEU LEU PHE
SEQRES 22 B 395 GLY ILE ASP SER ASN THR PRO PHE ALA ASN GLN ASP THR
SEQRES 23 B 395 LEU ASP LEU THR ARG GLU GLU GLU LEU SER LEU LEU GLN
SEQRES 24 B 395 GLU ILE ARG THR SER LEU TYR HIS PRO SER THR PRO PRO
SEQRES 25 B 395 ALA SER SER ARG SER TRP SER PRO VAL VAL GLY GLN LEU
SEQRES 26 B 395 VAL GLN GLU ARG VAL ALA ARG PRO ALA SER LEU ARG PRO
SEQRES 27 B 395 ARG TRP HIS LYS PRO SER THR VAL LEU LYS VAL LEU ASN
SEQRES 28 B 395 PRO ARG THR VAL VAL ILE LEU ASP HIS LEU GLY ASN ASN
SEQRES 29 B 395 ARG THR VAL SER ILE ASP ASN LEU LYS PRO THR SER HIS
SEQRES 30 B 395 GLN ASN GLY THR THR ASN ASP THR ALA THR MET ASP HIS
SEQRES 31 B 395 LEU GLU LYS ASN GLU
SEQRES 1 C 19 DA DT DT DG DT DC DA DT DG DG DA DA DT
SEQRES 2 C 19 DT DT DC DG DC DA
SEQRES 1 D 17 DT DG DC DG DA DA DA DT DT DC DC DA DT
SEQRES 2 D 17 DG DA DC DA
HET ZN A 393 1
HET SO4 A 394 5
HET GOL A 801 6
HET GOL A 802 6
HET GOL A 803 6
HET GOL A 805 6
HET NH4 A 395 1
HET MG A 396 1
HET MG A 397 1
HET ZYN A 398 30
HET SO4 B 393 5
HET MG B 394 1
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM NH4 AMMONIUM ION
HETNAM MG MAGNESIUM ION
HETNAM ZYN 6-(3-CHLORO-4-FLUOROBENZYL)-4-HYDROXY-N,N-DIMETHYL-2-
HETNAM 2 ZYN (1-METHYLETHYL)-3,5-DIOXO-2,3,5,6,7,8-HEXAHYDRO-2,6-
HETNAM 3 ZYN NAPHTHYRIDINE-1-CARBOXAMIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 ZN ZN 2+
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 11 NH4 H4 N 1+
FORMUL 12 MG 3(MG 2+)
FORMUL 14 ZYN C21 H23 CL F N3 O4
FORMUL 17 HOH *162(H2 O)
HELIX 1 1 LEU A 8 GLN A 17 1 10
HELIX 2 2 PRO A 50 LEU A 64 1 15
HELIX 3 3 GLY A 68 TYR A 80 1 13
HELIX 4 4 ASN A 84 CYS A 96 1 13
HELIX 5 5 CYS A 96 ASN A 103 1 8
HELIX 6 6 SER A 162 SER A 175 1 14
HELIX 7 7 GLY A 187 SER A 192 1 6
HELIX 8 8 SER A 192 GLU A 201 1 10
HELIX 9 9 HIS A 213 SER A 216 5 4
HELIX 10 10 SER A 217 LEU A 235 1 19
HELIX 11 11 LEU A 245 ASN A 255 1 11
HELIX 12 12 THR A 264 GLY A 271 1 8
HELIX 13 13 THR A 287 SER A 301 1 15
HELIX 14 14 SER B 162 THR B 174 1 13
HELIX 15 15 GLY B 187 SER B 192 1 6
HELIX 16 16 SER B 192 ARG B 202 1 11
HELIX 17 17 SER B 217 VAL B 236 1 20
HELIX 18 18 LYS B 241 ASN B 255 1 15
HELIX 19 19 THR B 264 GLY B 271 1 8
HELIX 20 20 THR B 287 SER B 293 1 7
SHEET 1 A 3 TYR A 30 GLU A 33 0
SHEET 2 A 3 LYS A 36 ARG A 41 -1 O LYS A 38 N PHE A 31
SHEET 3 A 3 GLY A 44 ILE A 47 -1 O GLY A 44 N ARG A 41
SHEET 1 B 2 ALA A 108 SER A 109 0
SHEET 2 B 2 SER A 314 TRP A 315 1 O TRP A 315 N ALA A 108
SHEET 1 C 5 THR A 153 THR A 158 0
SHEET 2 C 5 TYR A 141 ASP A 147 -1 N LEU A 143 O TYR A 156
SHEET 3 C 5 LYS A 124 ILE A 130 -1 N PHE A 126 O VAL A 146
SHEET 4 C 5 VAL A 181 SER A 184 1 O HIS A 183 N PHE A 125
SHEET 5 C 5 HIS A 205 PHE A 208 1 O GLU A 207 N ILE A 182
SHEET 1 D 5 ASN A 361 SER A 365 0
SHEET 2 D 5 THR A 351 LEU A 355 -1 N VAL A 352 O VAL A 364
SHEET 3 D 5 SER A 341 ASN A 348 -1 N LYS A 345 O VAL A 353
SHEET 4 D 5 LEU A 322 GLU A 325 -1 N VAL A 323 O SER A 341
SHEET 5 D 5 LEU A 369 PRO A 371 -1 O LYS A 370 N GLN A 324
SHEET 1 E 5 THR B 153 THR B 158 0
SHEET 2 E 5 TYR B 141 ASP B 147 -1 N LEU B 143 O TYR B 156
SHEET 3 E 5 PHE B 125 ILE B 130 -1 N ASP B 128 O VAL B 144
SHEET 4 E 5 VAL B 181 SER B 184 1 O HIS B 183 N PHE B 125
SHEET 5 E 5 HIS B 205 PHE B 208 1 O GLU B 207 N SER B 184
LINK NE2 HIS A 62 ZN ZN A 393 1555 1555 1.93
LINK ND1 HIS A 66 ZN ZN A 393 1555 1555 2.07
LINK SG CYS A 96 ZN ZN A 393 1555 1555 2.27
LINK SG CYS A 99 ZN ZN A 393 1555 1555 2.19
LINK OD1 ASP A 128 MG MG A 396 1555 1555 2.01
LINK OD2 ASP A 128 MG MG A 397 1555 1555 2.07
LINK OD1 ASP A 185 MG MG A 396 1555 1555 2.03
LINK OE1 GLU A 221 MG MG A 397 1555 1555 1.92
LINK OE2 GLU A 221 MG MG A 397 1555 1555 2.09
LINK MG MG A 396 OAH ZYN A 398 1555 1555 2.53
LINK MG MG A 396 O HOH A 400 1555 1555 2.23
LINK MG MG A 396 O HOH A 497 1555 1555 2.14
LINK MG MG A 397 OAH ZYN A 398 1555 1555 1.97
LINK MG MG A 397 OAF ZYN A 398 1555 1555 2.12
LINK MG MG A 397 O HOH A 399 1555 1555 2.18
LINK OD1 ASP B 128 MG MG B 394 1555 1555 2.26
LINK OD1 ASP B 185 MG MG B 394 1555 1555 2.16
LINK MG MG B 394 O HOH B 395 1555 1555 2.31
CISPEP 1 GLY A 131 PRO A 132 0 6.30
CISPEP 2 LEU A 358 GLY A 359 0 -4.84
CISPEP 3 GLY B 131 PRO B 132 0 7.15
SITE 1 AC1 4 HIS A 62 HIS A 66 CYS A 96 CYS A 99
SITE 1 AC2 5 LYS B 219 ARG B 222 SER B 258 PRO B 259
SITE 2 AC2 5 VAL B 260
SITE 1 AC3 3 HIS A 338 LYS A 339 HIS A 357
SITE 1 AC4 3 SER A 162 THR A 163 SER A 164
SITE 1 AC5 4 PRO A 135 SER A 136 GLN A 137 LYS A 241
SITE 1 AC6 4 GLN A 296 TYR B 263 GLN B 267 ASP B 273
SITE 1 AC7 4 GLN A 60 TYR A 80 PRO A 277 PHE A 278
SITE 1 AC8 1 ASP A 116
SITE 1 AC9 3 ASP A 128 ASP A 185 ZYN A 398
SITE 1 BC1 4 ASP A 128 GLU A 221 ASN A 224 ZYN A 398
SITE 1 BC2 3 ASP B 128 ASP B 185 DA C 19
SITE 1 BC3 11 ASP A 128 ASP A 185 TYR A 212 PRO A 214
SITE 2 BC3 11 GLN A 215 GLU A 221 MG A 396 MG A 397
SITE 3 BC3 11 DG C 4 DC D 16 DA D 17
CRYST1 159.030 159.030 123.730 90.00 90.00 90.00 P 41 21 2 16
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 0.006288 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006288 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008082 0.00000
(ATOM LINES ARE NOT SHOWN.)
END