HEADER HYDROLASE 15-OCT-12 2YNI
TITLE HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH INHIBITOR GSK952
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REVERSE TRANSCRIPTASE/RIBONUCLEASE H;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EXORIBONUCLEASE H, P66 RT;
COMPND 5 EC: 2.7.7.49, 2.7.7.7, 3.1.26.13, 3.1.13.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: P51 RT;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES 588-1015;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HIV-1 M\:B_HXB2R;
SOURCE 3 ORGANISM_COMMON: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (HXB2 ISOLATE);
SOURCE 4 ORGANISM_TAXID: 11706;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKK233-2 VARIANT;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HIV-1 M\:B_HXB2R;
SOURCE 12 ORGANISM_COMMON: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (HXB2 ISOLATE);
SOURCE 13 ORGANISM_TAXID: 11706;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PKK233-2 VARIANT
KEYWDS HYDROLASE, NNRTI
EXPDTA X-RAY DIFFRACTION
AUTHOR P.CHONG,P.SEBAHAR,M.YOUNGMAN,D.GARRIDO,H.ZHANG,E.L.STEWART,R.T.NOLTE,
AUTHOR 2 L.WANG,R.G.FERRIS,M.EDELSTEIN,K.WEAVER,A.MATHIS,A.PEAT
REVDAT 3 20-DEC-23 2YNI 1 REMARK LINK
REVDAT 2 18-DEC-13 2YNI 1 TITLE
REVDAT 1 09-JAN-13 2YNI 0
JRNL AUTH P.CHONG,P.SEBAHAR,M.YOUNGMAN,D.GARRIDO,H.ZHANG,E.L.STEWART,
JRNL AUTH 2 R.T.NOLTE,L.WANG,R.G.FERRIS,M.EDELSTEIN,K.WEAVER,A.MATHIS,
JRNL AUTH 3 A.PEAT
JRNL TITL RATIONAL DESIGN OF POTENT NON-NUCLEOSIDE INHIBITORS OF HIV-1
JRNL TITL 2 REVERSE TRANSCRIPTASE.
JRNL REF J.MED.CHEM. V. 55 10601 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 23137340
JRNL DOI 10.1021/JM301294G
REMARK 2
REMARK 2 RESOLUTION. 2.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 48835
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1576
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) : 2.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3348
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 109
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7815
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 378
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : -0.98000
REMARK 3 B33 (A**2) : 0.92000
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): 0.369
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.263
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.192
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.656
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8104 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 5539 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11040 ; 1.053 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13592 ; 0.767 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 967 ; 5.460 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 361 ;36.136 ;25.125
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1420 ;13.675 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;15.855 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1203 ; 0.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8823 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1557 ; 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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2YNI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1290054485.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : DCM WITH CRYO-COOLED 1ST CRYSTAL
REMARK 200 SAGITTALLY BENT 2ND
REMARK 200 OPTICS : VERTICALLY FOCUSING MIRROR.
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50530
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.490
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.960
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 2YNG
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH 7.5, 10MM SPERMIDINE,
REMARK 280 1.1M SODIUM POTASSIUM TARTRATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.20300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.20300
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 59.24850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.28850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 59.24850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.28850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.20300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 59.24850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.28850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 78.20300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 59.24850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 77.28850
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -2
REMARK 465 VAL A 559
REMARK 465 LEU A 560
REMARK 465 MET B -18
REMARK 465 ALA B -17
REMARK 465 GLY B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 GLY B -9
REMARK 465 SER B -8
REMARK 465 ALA B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY B 0
REMARK 465 PRO B 1
REMARK 465 ILE B 2
REMARK 465 SER B 3
REMARK 465 PRO B 4
REMARK 465 LYS B 66
REMARK 465 ASP B 67
REMARK 465 THR B 216
REMARK 465 PRO B 217
REMARK 465 ASP B 218
REMARK 465 LYS B 219
REMARK 465 LYS B 220
REMARK 465 HIS B 221
REMARK 465 GLN B 222
REMARK 465 LYS B 223
REMARK 465 GLU B 224
REMARK 465 PRO B 225
REMARK 465 PRO B 226
REMARK 465 PHE B 227
REMARK 465 LEU B 228
REMARK 465 MET B 357
REMARK 465 ARG B 358
REMARK 465 GLY B 359
REMARK 465 ALA B 360
REMARK 465 HIS B 361
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 GLU A 36 CG CD OE1 OE2
REMARK 470 LYS A 65 CG CD CE NZ
REMARK 470 LYS A 66 CG CD CE NZ
REMARK 470 LYS A 70 CG CD CE NZ
REMARK 470 LYS A 101 CG CD CE NZ
REMARK 470 LYS A 173 CD CE NZ
REMARK 470 LYS A 219 CD CE NZ
REMARK 470 LYS A 223 CD CE NZ
REMARK 470 LYS A 263 CE NZ
REMARK 470 LYS A 287 CG CD CE NZ
REMARK 470 LEU A 289 CG CD1 CD2
REMARK 470 GLU A 291 CG CD OE1 OE2
REMARK 470 GLN A 334 CG CD OE1 NE2
REMARK 470 LYS A 550 CG CD CE NZ
REMARK 470 LYS A 558 CG CD CE NZ
REMARK 470 LYS B 11 CG CD CE NZ
REMARK 470 LYS B 13 CG CD CE NZ
REMARK 470 LYS B 22 CD CE NZ
REMARK 470 LYS B 65 CG CD CE NZ
REMARK 470 LYS B 70 CG CD CE NZ
REMARK 470 TYR B 232 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 281 CG CD CE NZ
REMARK 470 GLN B 334 CG CD OE1 NE2
REMARK 470 LYS B 347 CD CE NZ
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 85 157.77 -47.07
REMARK 500 MET A 184 -127.54 47.56
REMARK 500 LYS A 287 -139.94 68.86
REMARK 500 ALA A 288 117.07 110.91
REMARK 500 PHE A 346 58.29 -118.66
REMARK 500 ALA A 355 48.97 -152.84
REMARK 500 PRO A 412 -179.82 -68.54
REMARK 500 GLU A 413 119.63 -37.34
REMARK 500 MET B 184 -122.31 51.95
REMARK 500 PHE B 346 -14.78 75.04
REMARK 500 PRO B 420 -179.13 -61.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR B 419 PRO B 420 -147.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2158 DISTANCE = 5.94 ANGSTROMS
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 A1559 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 443 OD1
REMARK 620 2 ASP A 498 OD1 99.5
REMARK 620 3 HOH A2191 O 103.8 130.9
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 MG A 1559
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR A 1560
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CXD A 1561
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A30 RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE COMPLEXED WITH A TRIPEPTIDE INHIBITOR
REMARK 900 RELATED ID: 1BV7 RELATED DB: PDB
REMARK 900 COUNTERACTING HIV-1 PROTEASE DRUG RESISTANCE: STRUCTURAL ANALYSIS
REMARK 900 OF MUTANT PROTEASES COMPLEXED WITH XV638 AND SD146, CYCLIC UREA
REMARK 900 AMIDES WITH BROAD SPECIFICITIES
REMARK 900 RELATED ID: 1BV9 RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE (I84V) COMPLEXED WITH XV638 OF DUPONT PHARMACEUTICALS
REMARK 900 RELATED ID: 1BVE RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE-DMP323 COMPLEX IN SOLUTION, NMR, 28 STRUCTURES
REMARK 900 RELATED ID: 1BVG RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE-DMP323 COMPLEX IN SOLUTION, NMR MINIMIZED AVERAGE
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 1BWA RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE (V82F/I84V) DOUBLE MUTANT COMPLEXED WITH XV638 OF
REMARK 900 DUPONT PHARMACEUTICALS
REMARK 900 RELATED ID: 1BWB RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE (V82F/I84V) DOUBLE MUTANT COMPLEXED WITH SD146 OF
REMARK 900 DUPONT PHARMACEUTICALS
REMARK 900 RELATED ID: 1C0T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH BM+
REMARK 900 21.1326
REMARK 900 RELATED ID: 1C0U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH BM+
REMARK 900 50.0934
REMARK 900 RELATED ID: 1C1B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH
REMARK 900 GCA- 186
REMARK 900 RELATED ID: 1C1C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH
REMARK 900 TNK- 6123
REMARK 900 RELATED ID: 1DMP RELATED DB: PDB
REMARK 900 STRUCTURE OF HIV-1 PROTEASE COMPLEX
REMARK 900 RELATED ID: 1DTQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH
REMARK 900 PETT-1 (PETT131A94)
REMARK 900 RELATED ID: 1DTT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH
REMARK 900 PETT-2 (PETT130A94)
REMARK 900 RELATED ID: 1E6J RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 CAPSID PROTEIN (P24) IN COMPLEX WITH
REMARK 900 FAB13B5
REMARK 900 RELATED ID: 1EP4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH S-
REMARK 900 1153
REMARK 900 RELATED ID: 1ESK RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF NCP7 FROM HIV-1
REMARK 900 RELATED ID: 1EX4 RELATED DB: PDB
REMARK 900 HIV-1 INTEGRASE CATALYTIC CORE AND C-TERMINAL DOMAIN
REMARK 900 RELATED ID: 1EXQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HIV-1 INTEGRASE CATALYTIC COREDOMAIN
REMARK 900 RELATED ID: 1FB7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN IN VIVO HIV-1 PROTEASE MUTANT INCOMPLEX
REMARK 900 WITH SAQUINAVIR: INSIGHTS INTO THE MECHANISMS OFDRUG RESISTANCE
REMARK 900 RELATED ID: 1FK9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEXWITH DMP-
REMARK 900 266(EFAVIRENZ)
REMARK 900 RELATED ID: 1FKO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NNRTI RESISTANT K103N MUTANT HIV- 1REVERSE
REMARK 900 TRANSCRIPTASE IN COMPLEX WITH DMP-266(EFAVIRENZ )
REMARK 900 RELATED ID: 1FKP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NNRTI RESISTANT K103N MUTANT HIV- 1REVERSE
REMARK 900 TRANSCRIPTASE IN COMPLEX WITH NEVIRAPINE
REMARK 900 RELATED ID: 1G6L RELATED DB: PDB
REMARK 900 1.9A CRYSTAL STRUCTURE OF TETHERED HIV-1 PROTEASE
REMARK 900 RELATED ID: 1HIV RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE (HIV-1 PR) COMPLEX WITH U75875 (NOA- HIS-CHA-
REMARK 900 PSI[CH(OH)CH(OH)]VAL-ILE-APY)
REMARK 900 RELATED ID: 1HVH RELATED DB: PDB
REMARK 900 NONPEPTIDE CYCLIC CYANOGUANIDINES AS HIV PROTEASE INHIBITORS
REMARK 900 RELATED ID: 1HVR RELATED DB: PDB
REMARK 900 HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (HIV-1) PROTEASE COMPLEXED WITH
REMARK 900 XK263 OF DUPONT MERCK
REMARK 900 RELATED ID: 1HWR RELATED DB: PDB
REMARK 900 MOLECULAR RECOGNITION OF CYCLIC UREA HIV PROTEASE INHIBITORS
REMARK 900 RELATED ID: 1HXB RELATED DB: PDB
REMARK 900 HIV-1 PROTEINASE COMPLEXED WITH RO 31-8959
REMARK 900 RELATED ID: 1JKH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF Y181C MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH DMP-266(EFAVIRENZ)
REMARK 900 RELATED ID: 1JLA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF Y181C MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH TNK-651
REMARK 900 RELATED ID: 1JLB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF Y181C MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH NEVIRAPINE
REMARK 900 RELATED ID: 1JLC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF Y181C MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH PETT-2
REMARK 900 RELATED ID: 1JLE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF Y188C MUTANT HIV-1 REVERSETRANSCRIPTASE
REMARK 900 RELATED ID: 1JLF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF Y188C MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH NEVIRAPINE
REMARK 900 RELATED ID: 1JLG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF Y188C MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH UC-781
REMARK 900 RELATED ID: 1JLQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEXWITH
REMARK 900 739W94
REMARK 900 RELATED ID: 1KLM RELATED DB: PDB
REMARK 900 HIV-1 REVERSE TRANSCRIPTASE COMPLEXED WITH BHAP U- 90152
REMARK 900 RELATED ID: 1LV1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE NON-ACTIVE SITE MUTANT OFTETHERED
REMARK 900 HIV-1 PROTEASE TO 2.1A RESOLUTION
REMARK 900 RELATED ID: 1LW0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF T215Y MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH NEVIRAPINE
REMARK 900 RELATED ID: 1LW2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF T215Y MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH 1051U91
REMARK 900 RELATED ID: 1LWC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF M184V MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH NEVIRAPINE
REMARK 900 RELATED ID: 1LWE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF M41L/T215Y MUTANT HIV-1 REVERSETRANSCRIPTASE
REMARK 900 (RTMN) IN COMPLEX WITH NEVIRAPINE
REMARK 900 RELATED ID: 1LWF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A MUTANT HIV-1 REVERSE TRANSCRIPTASE(RTMQ+
REMARK 900 M184V: M41L/D67N/K70R/M184V/T215Y) IN COMPLEX WITHNEVIRAPINE
REMARK 900 RELATED ID: 1NCP RELATED DB: PDB
REMARK 900 RELATED ID: 1O1W RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE RNASE H DOMAIN OF THE HIV -1REVERSE
REMARK 900 TRANSCRIPTASE IN THE PRESENCE OF MAGNESIUM
REMARK 900 RELATED ID: 1ODW RELATED DB: PDB
REMARK 900 NATIVE HIV-1 PROTEINASE
REMARK 900 RELATED ID: 1ODY RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE COMPLEXED WITH AN INHIBITOR LP-130
REMARK 900 RELATED ID: 1QBR RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE INHIBITORS WIIH LOW NANOMOLAR POTENCY
REMARK 900 RELATED ID: 1QBS RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE INHIBITORS WIIH LOW NANOMOLAR POTENCY
REMARK 900 RELATED ID: 1QBT RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE INHIBITORS WIIH LOW NANOMOLAR POTENCY
REMARK 900 RELATED ID: 1QBU RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE INHIBITORS WIIH LOW NANOMOLAR POTENCY
REMARK 900 RELATED ID: 1REV RELATED DB: PDB
REMARK 900 HIV-1 REVERSE TRANSCRIPTASE
REMARK 900 RELATED ID: 1RT1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE COMPLEXED WITH MKC-
REMARK 900 442
REMARK 900 RELATED ID: 1RT2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE COMPLEXED WITH TNK-
REMARK 900 651
REMARK 900 RELATED ID: 1RT3 RELATED DB: PDB
REMARK 900 AZT DRUG RESISTANT HIV-1 REVERSE TRANSCRIPTASE COMPLEXED WITH
REMARK 900 1051U91
REMARK 900 RELATED ID: 1RT4 RELATED DB: PDB
REMARK 900 HIV-1 REVERSE TRANSCRIPTASE COMPLEXED WITH UC781
REMARK 900 RELATED ID: 1RT5 RELATED DB: PDB
REMARK 900 HIV-1 REVERSE TRANSCRIPTASE COMPLEXED WITH UC10
REMARK 900 RELATED ID: 1RT6 RELATED DB: PDB
REMARK 900 HIV-1 REVERSE TRANSCRIPTASE COMPLEXED WITH UC38
REMARK 900 RELATED ID: 1RT7 RELATED DB: PDB
REMARK 900 HIV-1 REVERSE TRANSCRIPTASE COMPLEXED WITH UC84
REMARK 900 RELATED ID: 1RTD RELATED DB: PDB
REMARK 900 STRUCTURE OF A CATALYTIC COMPLEX OF HIV-1 REVERSE TRANSCRIPTASE:
REMARK 900 IMPLICATIONS FOR NUCLEOSIDE ANALOG DRUG RESISTANCE
REMARK 900 RELATED ID: 1RTH RELATED DB: PDB
REMARK 900 RELATED ID: 1RTI RELATED DB: PDB
REMARK 900 RELATED ID: 1RTJ RELATED DB: PDB
REMARK 900 RELATED ID: 1S1T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF L100I MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH UC-781
REMARK 900 RELATED ID: 1S1U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF L100I MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH NEVIRAPINE
REMARK 900 RELATED ID: 1S1V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF L100I MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH TNK-651
REMARK 900 RELATED ID: 1S1W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF V106A MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH UC-781
REMARK 900 RELATED ID: 1S1X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF V108I MUTANT HIV-1 REVERSETRANSCRIPTASE IN
REMARK 900 COMPLEX WITH NEVIRAPINE
REMARK 900 RELATED ID: 1T05 RELATED DB: PDB
REMARK 900 HIV-1 REVERSE TRANSCRIPTASE CROSSLINKED TO TEMPLATE- PRIMERWITH
REMARK 900 TENOFOVIR-DIPHOSPHATE BOUND AS THE INCOMINGNUCLEOTIDE SUBSTRATE
REMARK 900 RELATED ID: 1TAM RELATED DB: PDB
REMARK 900 HUMAN IMMUNODEFICIENCY VIRUS, NMR, MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1TKT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEXWITH
REMARK 900 GW426318
REMARK 900 RELATED ID: 1TKX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEXWITH
REMARK 900 GW490745
REMARK 900 RELATED ID: 1TKZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEXWITH
REMARK 900 GW429576
REMARK 900 RELATED ID: 1TL1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEXWITH
REMARK 900 GW451211
REMARK 900 RELATED ID: 1TL3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEXWITH
REMARK 900 GW450557
REMARK 900 RELATED ID: 1VRT RELATED DB: PDB
REMARK 900 RELATED ID: 1VRU RELATED DB: PDB
REMARK 900 RELATED ID: 2WHH RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE TETHERED DIMER Q-PRODUCT COMPLEX ALONG WITH
REMARK 900 NUCLEOPHILIC WATER MOLECULE
REMARK 900 RELATED ID: 2WOM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF UK-453061 BOUND TO HIV-1 REVERSE TRANSCRIPTASE
REMARK 900 (K103N).
REMARK 900 RELATED ID: 2WON RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF UK-453061 BOUND TO HIV-1 REVERSE TRANSCRIPTASE
REMARK 900 (WILD-TYPE).
REMARK 900 RELATED ID: 2YNF RELATED DB: PDB
REMARK 900 HIV-1 REVERSE TRANSCRIPTASE Y188L MUTANT IN COMPLEX WITH INHIBITOR
REMARK 900 GSK560
REMARK 900 RELATED ID: 2YNG RELATED DB: PDB
REMARK 900 HIV-1 REVERSE TRANSCRIPTASE MUTANT IN COMPLEX WITH INHIBITOR GSK560
REMARK 900 RELATED ID: 3PHV RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE (ISOLATE HXB2)
REMARK 900 RELATED ID: 4B3O RELATED DB: PDB
REMARK 900 STRUCTURES OF HIV-1 RT AND RNA-DNA COMPLEX REVEAL A UNIQUE RT
REMARK 900 CONFORMATION AND SUBSTRATE INTERFACE
REMARK 900 RELATED ID: 4B3P RELATED DB: PDB
REMARK 900 STRUCTURES OF HIV-1 RT AND RNA-DNA COMPLEX REVEAL A UNIQUE RT
REMARK 900 CONFORMATION AND SUBSTRATE INTERFACE
REMARK 900 RELATED ID: 4B3Q RELATED DB: PDB
REMARK 900 STRUCTURES OF HIV-1 RT AND RNA-DNA COMPLEX REVEAL A UNIQUE RT
REMARK 900 CONFORMATION AND SUBSTRATE INTERFACE
REMARK 900 RELATED ID: 2YNH RELATED DB: PDB
REMARK 900 HIV-1 REVERSE TRANSCRIPTASE MUTANT IN COMPLEX WITH INHIBITOR GSK500
DBREF 2YNI A 1 560 UNP P04585 POL_HV1H2 588 1147
DBREF 2YNI B 1 428 UNP P04585 POL_HV1H2 588 1015
SEQADV 2YNI MET A -2 UNP P04585 EXPRESSION TAG
SEQADV 2YNI ASN A -1 UNP P04585 EXPRESSION TAG
SEQADV 2YNI SER A 0 UNP P04585 EXPRESSION TAG
SEQADV 2YNI MET B -18 UNP P04585 EXPRESSION TAG
SEQADV 2YNI ALA B -17 UNP P04585 EXPRESSION TAG
SEQADV 2YNI GLY B -16 UNP P04585 EXPRESSION TAG
SEQADV 2YNI HIS B -15 UNP P04585 EXPRESSION TAG
SEQADV 2YNI HIS B -14 UNP P04585 EXPRESSION TAG
SEQADV 2YNI HIS B -13 UNP P04585 EXPRESSION TAG
SEQADV 2YNI HIS B -12 UNP P04585 EXPRESSION TAG
SEQADV 2YNI HIS B -11 UNP P04585 EXPRESSION TAG
SEQADV 2YNI HIS B -10 UNP P04585 EXPRESSION TAG
SEQADV 2YNI GLY B -9 UNP P04585 EXPRESSION TAG
SEQADV 2YNI SER B -8 UNP P04585 EXPRESSION TAG
SEQADV 2YNI ALA B -7 UNP P04585 EXPRESSION TAG
SEQADV 2YNI GLU B -6 UNP P04585 EXPRESSION TAG
SEQADV 2YNI ASN B -5 UNP P04585 EXPRESSION TAG
SEQADV 2YNI LEU B -4 UNP P04585 EXPRESSION TAG
SEQADV 2YNI TYR B -3 UNP P04585 EXPRESSION TAG
SEQADV 2YNI PHE B -2 UNP P04585 EXPRESSION TAG
SEQADV 2YNI GLN B -1 UNP P04585 EXPRESSION TAG
SEQADV 2YNI GLY B 0 UNP P04585 EXPRESSION TAG
SEQRES 1 A 563 MET ASN SER PRO ILE SER PRO ILE GLU THR VAL PRO VAL
SEQRES 2 A 563 LYS LEU LYS PRO GLY MET ASP GLY PRO LYS VAL LYS GLN
SEQRES 3 A 563 TRP PRO LEU THR GLU GLU LYS ILE LYS ALA LEU VAL GLU
SEQRES 4 A 563 ILE CYS THR GLU MET GLU LYS GLU GLY LYS ILE SER LYS
SEQRES 5 A 563 ILE GLY PRO GLU ASN PRO TYR ASN THR PRO VAL PHE ALA
SEQRES 6 A 563 ILE LYS LYS LYS ASP SER THR LYS TRP ARG LYS LEU VAL
SEQRES 7 A 563 ASP PHE ARG GLU LEU ASN LYS ARG THR GLN ASP PHE TRP
SEQRES 8 A 563 GLU VAL GLN LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS
SEQRES 9 A 563 LYS LYS LYS SER VAL THR VAL LEU ASP VAL GLY ASP ALA
SEQRES 10 A 563 TYR PHE SER VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR
SEQRES 11 A 563 THR ALA PHE THR ILE PRO SER ILE ASN ASN GLU THR PRO
SEQRES 12 A 563 GLY ILE ARG TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP
SEQRES 13 A 563 LYS GLY SER PRO ALA ILE PHE GLN SER SER MET THR LYS
SEQRES 14 A 563 ILE LEU GLU PRO PHE ARG LYS GLN ASN PRO ASP ILE VAL
SEQRES 15 A 563 ILE TYR GLN TYR MET ASP ASP LEU TYR VAL GLY SER ASP
SEQRES 16 A 563 LEU GLU ILE GLY GLN HIS ARG THR LYS ILE GLU GLU LEU
SEQRES 17 A 563 ARG GLN HIS LEU LEU ARG TRP GLY LEU THR THR PRO ASP
SEQRES 18 A 563 LYS LYS HIS GLN LYS GLU PRO PRO PHE LEU TRP MET GLY
SEQRES 19 A 563 TYR GLU LEU HIS PRO ASP LYS TRP THR VAL GLN PRO ILE
SEQRES 20 A 563 VAL LEU PRO GLU LYS ASP SER TRP THR VAL ASN ASP ILE
SEQRES 21 A 563 GLN LYS LEU VAL GLY LYS LEU ASN TRP ALA SER GLN ILE
SEQRES 22 A 563 TYR PRO GLY ILE LYS VAL ARG GLN LEU CYS LYS LEU LEU
SEQRES 23 A 563 ARG GLY THR LYS ALA LEU THR GLU VAL ILE PRO LEU THR
SEQRES 24 A 563 GLU GLU ALA GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE
SEQRES 25 A 563 LEU LYS GLU PRO VAL HIS GLY VAL TYR TYR ASP PRO SER
SEQRES 26 A 563 LYS ASP LEU ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY
SEQRES 27 A 563 GLN TRP THR TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN
SEQRES 28 A 563 LEU LYS THR GLY LYS TYR ALA ARG MET ARG GLY ALA HIS
SEQRES 29 A 563 THR ASN ASP VAL LYS GLN LEU THR GLU ALA VAL GLN LYS
SEQRES 30 A 563 ILE THR THR GLU SER ILE VAL ILE TRP GLY LYS THR PRO
SEQRES 31 A 563 LYS PHE LYS LEU PRO ILE GLN LYS GLU THR TRP GLU THR
SEQRES 32 A 563 TRP TRP THR GLU TYR TRP GLN ALA THR TRP ILE PRO GLU
SEQRES 33 A 563 TRP GLU PHE VAL ASN THR PRO PRO LEU VAL LYS LEU TRP
SEQRES 34 A 563 TYR GLN LEU GLU LYS GLU PRO ILE VAL GLY ALA GLU THR
SEQRES 35 A 563 PHE TYR VAL ASP GLY ALA ALA ASN ARG GLU THR LYS LEU
SEQRES 36 A 563 GLY LYS ALA GLY TYR VAL THR ASN ARG GLY ARG GLN LYS
SEQRES 37 A 563 VAL VAL THR LEU THR ASP THR THR ASN GLN LYS THR GLU
SEQRES 38 A 563 LEU GLN ALA ILE TYR LEU ALA LEU GLN ASP SER GLY LEU
SEQRES 39 A 563 GLU VAL ASN ILE VAL THR ASP SER GLN TYR ALA LEU GLY
SEQRES 40 A 563 ILE ILE GLN ALA GLN PRO ASP GLN SER GLU SER GLU LEU
SEQRES 41 A 563 VAL ASN GLN ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS
SEQRES 42 A 563 VAL TYR LEU ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY
SEQRES 43 A 563 GLY ASN GLU GLN VAL ASP LYS LEU VAL SER ALA GLY ILE
SEQRES 44 A 563 ARG LYS VAL LEU
SEQRES 1 B 447 MET ALA GLY HIS HIS HIS HIS HIS HIS GLY SER ALA GLU
SEQRES 2 B 447 ASN LEU TYR PHE GLN GLY PRO ILE SER PRO ILE GLU THR
SEQRES 3 B 447 VAL PRO VAL LYS LEU LYS PRO GLY MET ASP GLY PRO LYS
SEQRES 4 B 447 VAL LYS GLN TRP PRO LEU THR GLU GLU LYS ILE LYS ALA
SEQRES 5 B 447 LEU VAL GLU ILE CYS THR GLU MET GLU LYS GLU GLY LYS
SEQRES 6 B 447 ILE SER LYS ILE GLY PRO GLU ASN PRO TYR ASN THR PRO
SEQRES 7 B 447 VAL PHE ALA ILE LYS LYS LYS ASP SER THR LYS TRP ARG
SEQRES 8 B 447 LYS LEU VAL ASP PHE ARG GLU LEU ASN LYS ARG THR GLN
SEQRES 9 B 447 ASP PHE TRP GLU VAL GLN LEU GLY ILE PRO HIS PRO ALA
SEQRES 10 B 447 GLY LEU LYS LYS LYS LYS SER VAL THR VAL LEU ASP VAL
SEQRES 11 B 447 GLY ASP ALA TYR PHE SER VAL PRO LEU ASP GLU ASP PHE
SEQRES 12 B 447 ARG LYS TYR THR ALA PHE THR ILE PRO SER ILE ASN ASN
SEQRES 13 B 447 GLU THR PRO GLY ILE ARG TYR GLN TYR ASN VAL LEU PRO
SEQRES 14 B 447 GLN GLY TRP LYS GLY SER PRO ALA ILE PHE GLN SER SER
SEQRES 15 B 447 MET THR LYS ILE LEU GLU PRO PHE ARG LYS GLN ASN PRO
SEQRES 16 B 447 ASP ILE VAL ILE TYR GLN TYR MET ASP ASP LEU TYR VAL
SEQRES 17 B 447 GLY SER ASP LEU GLU ILE GLY GLN HIS ARG THR LYS ILE
SEQRES 18 B 447 GLU GLU LEU ARG GLN HIS LEU LEU ARG TRP GLY LEU THR
SEQRES 19 B 447 THR PRO ASP LYS LYS HIS GLN LYS GLU PRO PRO PHE LEU
SEQRES 20 B 447 TRP MET GLY TYR GLU LEU HIS PRO ASP LYS TRP THR VAL
SEQRES 21 B 447 GLN PRO ILE VAL LEU PRO GLU LYS ASP SER TRP THR VAL
SEQRES 22 B 447 ASN ASP ILE GLN LYS LEU VAL GLY LYS LEU ASN TRP ALA
SEQRES 23 B 447 SER GLN ILE TYR PRO GLY ILE LYS VAL ARG GLN LEU CYS
SEQRES 24 B 447 LYS LEU LEU ARG GLY THR LYS ALA LEU THR GLU VAL ILE
SEQRES 25 B 447 PRO LEU THR GLU GLU ALA GLU LEU GLU LEU ALA GLU ASN
SEQRES 26 B 447 ARG GLU ILE LEU LYS GLU PRO VAL HIS GLY VAL TYR TYR
SEQRES 27 B 447 ASP PRO SER LYS ASP LEU ILE ALA GLU ILE GLN LYS GLN
SEQRES 28 B 447 GLY GLN GLY GLN TRP THR TYR GLN ILE TYR GLN GLU PRO
SEQRES 29 B 447 PHE LYS ASN LEU LYS THR GLY LYS TYR ALA ARG MET ARG
SEQRES 30 B 447 GLY ALA HIS THR ASN ASP VAL LYS GLN LEU THR GLU ALA
SEQRES 31 B 447 VAL GLN LYS ILE THR THR GLU SER ILE VAL ILE TRP GLY
SEQRES 32 B 447 LYS THR PRO LYS PHE LYS LEU PRO ILE GLN LYS GLU THR
SEQRES 33 B 447 TRP GLU THR TRP TRP THR GLU TYR TRP GLN ALA THR TRP
SEQRES 34 B 447 ILE PRO GLU TRP GLU PHE VAL ASN THR PRO PRO LEU VAL
SEQRES 35 B 447 LYS LEU TRP TYR GLN
HET MG A1559 1
HET TAR A1560 10
HET CXD A1561 28
HETNAM MG MAGNESIUM ION
HETNAM TAR D(-)-TARTARIC ACID
HETNAM CXD 4-CHLORANYL-N-[[4-CHLORANYL-3-(3-CHLORANYL-5-CYANO-
HETNAM 2 CXD PHENOXY)-2-FLUORANYL-PHENYL]METHYL]-1H-IMIDAZOLE-5-
HETNAM 3 CXD CARBOXAMIDE
FORMUL 3 MG MG 2+
FORMUL 4 TAR C4 H6 O6
FORMUL 5 CXD C18 H10 CL3 F N4 O2
FORMUL 6 HOH *378(H2 O)
HELIX 1 1 THR A 27 GLU A 44 1 18
HELIX 2 2 PHE A 77 THR A 84 1 8
HELIX 3 3 HIS A 96 LEU A 100 5 5
HELIX 4 4 ALA A 114 VAL A 118 5 5
HELIX 5 5 ASP A 121 LYS A 126 1 6
HELIX 6 6 TYR A 127 ALA A 129 5 3
HELIX 7 7 GLY A 155 ASN A 175 1 21
HELIX 8 8 GLU A 194 ARG A 211 1 18
HELIX 9 9 THR A 253 SER A 268 1 16
HELIX 10 10 VAL A 276 LEU A 282 1 7
HELIX 11 11 THR A 296 LYS A 311 1 16
HELIX 12 12 ASN A 363 GLY A 384 1 22
HELIX 13 13 GLN A 394 TYR A 405 1 12
HELIX 14 14 THR A 473 ASP A 488 1 16
HELIX 15 15 SER A 499 ALA A 508 1 10
HELIX 16 16 SER A 515 LYS A 528 1 14
HELIX 17 17 GLY A 544 ALA A 554 1 11
HELIX 18 18 THR B 27 GLU B 44 1 18
HELIX 19 19 PHE B 77 THR B 84 1 8
HELIX 20 20 THR B 84 VAL B 90 1 7
HELIX 21 21 GLY B 99 LYS B 103 5 5
HELIX 22 22 GLY B 112 VAL B 118 5 7
HELIX 23 23 PHE B 124 ALA B 129 5 6
HELIX 24 24 SER B 134 GLU B 138 5 5
HELIX 25 25 LYS B 154 ASN B 175 1 22
HELIX 26 26 GLU B 194 ARG B 211 1 18
HELIX 27 27 HIS B 235 TRP B 239 5 5
HELIX 28 28 THR B 253 TYR B 271 1 19
HELIX 29 29 VAL B 276 ARG B 284 1 9
HELIX 30 30 THR B 296 GLU B 312 1 17
HELIX 31 31 ASN B 363 GLY B 384 1 22
HELIX 32 32 GLN B 394 TRP B 402 1 9
HELIX 33 33 THR B 403 TYR B 405 5 3
SHEET 1 AA 3 ILE A 47 LYS A 49 0
SHEET 2 AA 3 ILE A 142 TYR A 146 -1 O GLN A 145 N SER A 48
SHEET 3 AA 3 PHE A 130 ILE A 132 -1 O PHE A 130 N TYR A 144
SHEET 1 AB 2 VAL A 60 ILE A 63 0
SHEET 2 AB 2 ARG A 72 VAL A 75 -1 O ARG A 72 N ILE A 63
SHEET 1 AC 3 SER A 105 ASP A 110 0
SHEET 2 AC 3 ASP A 186 SER A 191 -1 O LEU A 187 N LEU A 109
SHEET 3 AC 3 VAL A 179 TYR A 183 -1 O VAL A 179 N GLY A 190
SHEET 1 AD 3 PHE A 227 TRP A 229 0
SHEET 2 AD 3 TYR A 232 LEU A 234 -1 O TYR A 232 N TRP A 229
SHEET 3 AD 3 TRP A 239 VAL A 241 -1 O THR A 240 N GLU A 233
SHEET 1 AE 5 LYS A 347 TYR A 354 0
SHEET 2 AE 5 GLN A 336 GLU A 344 -1 O TRP A 337 N TYR A 354
SHEET 3 AE 5 ILE A 326 GLY A 333 -1 O ILE A 326 N TYR A 342
SHEET 4 AE 5 LYS A 388 LEU A 391 1 O LYS A 388 N ALA A 327
SHEET 5 AE 5 TRP A 414 PHE A 416 1 O GLU A 415 N LEU A 391
SHEET 1 AF 2 HIS A 361 THR A 362 0
SHEET 2 AF 2 GLN A 512 SER A 513 -1 O GLN A 512 N THR A 362
SHEET 1 AG 5 GLN A 464 LEU A 469 0
SHEET 2 AG 5 GLY A 453 THR A 459 -1 O GLY A 453 N LEU A 469
SHEET 3 AG 5 THR A 439 ALA A 446 -1 O TYR A 441 N VAL A 458
SHEET 4 AG 5 GLU A 492 THR A 497 1 O ASN A 494 N PHE A 440
SHEET 5 AG 5 LYS A 530 TRP A 535 1 O LYS A 530 N VAL A 493
SHEET 1 BA 3 ILE B 47 LYS B 49 0
SHEET 2 BA 3 ILE B 142 TYR B 146 -1 O GLN B 145 N SER B 48
SHEET 3 BA 3 PHE B 130 ILE B 132 -1 O PHE B 130 N TYR B 144
SHEET 1 BB 2 VAL B 60 ILE B 63 0
SHEET 2 BB 2 ARG B 72 VAL B 75 -1 O ARG B 72 N ILE B 63
SHEET 1 BC 3 SER B 105 ASP B 110 0
SHEET 2 BC 3 ASP B 186 SER B 191 -1 O LEU B 187 N LEU B 109
SHEET 3 BC 3 VAL B 179 TYR B 183 -1 O VAL B 179 N GLY B 190
SHEET 1 BD 5 ASN B 348 ALA B 355 0
SHEET 2 BD 5 GLN B 336 TYR B 342 -1 O TRP B 337 N TYR B 354
SHEET 3 BD 5 ILE B 326 GLY B 333 -1 O ILE B 326 N TYR B 342
SHEET 4 BD 5 LYS B 388 LEU B 391 1 O LYS B 388 N ALA B 327
SHEET 5 BD 5 TRP B 414 PHE B 416 1 O GLU B 415 N LEU B 391
LINK OD1 ASP A 443 MG MG A1559 1555 1555 2.37
LINK OD1 ASP A 498 MG MG A1559 1555 1555 2.59
LINK MG MG A1559 O HOH A2191 1555 1555 2.08
CISPEP 1 PRO A 225 PRO A 226 0 2.28
CISPEP 2 PRO A 345 PHE A 346 0 -7.31
CISPEP 3 PRO A 420 PRO A 421 0 -5.11
CISPEP 4 PRO B 420 PRO B 421 0 -11.59
SITE 1 AC1 4 ASP A 443 GLY A 444 ASP A 498 HOH A2191
SITE 1 AC2 7 ARG A 211 GLY A 436 ALA A 437 ASN A 460
SITE 2 AC2 7 ARG A 461 HOH A2220 THR B 290
SITE 1 AC3 15 LEU A 100 LYS A 101 LYS A 102 LYS A 103
SITE 2 AC3 15 LYS A 104 VAL A 106 VAL A 108 TYR A 181
SITE 3 AC3 15 TYR A 188 PHE A 227 TRP A 229 LEU A 234
SITE 4 AC3 15 HIS A 235 PRO A 236 TYR A 318
CRYST1 118.497 154.577 156.406 90.00 90.00 90.00 C 2 2 21 8
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 0.008439 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006469 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006394 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
