HEADER TRANSFERASE 07-MAY-01 1IKV
TITLE K103N MUTANT HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH EFIVARENZ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POL POLYPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: REVERSE TRANSCRIPTASE;
COMPND 5 EC: 2.7.7.49;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: POL POLYPROTEIN;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: REVERSE TRANSCRIPTASE;
COMPND 12 EC: 2.7.7.49;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 GENE: BH10;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PETD;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 11 ORGANISM_TAXID: 11676;
SOURCE 12 GENE: BH10;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PETD
KEYWDS HETERODIMER, PROTEIN-INHIBITOR COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LINDBERG,T.UNGE
REVDAT 8 07-FEB-24 1IKV 1 REMARK
REVDAT 7 27-OCT-21 1IKV 1 REMARK SEQADV
REVDAT 6 07-MAR-18 1IKV 1 REMARK
REVDAT 5 18-JUL-12 1IKV 1 HETSYN
REVDAT 4 31-AUG-11 1IKV 1 HETATM VERSN
REVDAT 3 24-FEB-09 1IKV 1 VERSN
REVDAT 2 17-APR-02 1IKV 1 JRNL
REVDAT 1 06-JUN-01 1IKV 0
JRNL AUTH J.LINDBERG,S.SIGURDSSON,S.LOWGREN,H.O.ANDERSSON,C.SAHLBERG,
JRNL AUTH 2 R.NOREEN,K.FRIDBORG,H.ZHANG,T.UNGE
JRNL TITL STRUCTURAL BASIS FOR THE INHIBITORY EFFICACY OF EFAVIRENZ
JRNL TITL 2 (DMP-266), MSC194 AND PNU142721 TOWARDS THE HIV-1 RT K103N
JRNL TITL 3 MUTANT.
JRNL REF EUR.J.BIOCHEM. V. 269 1670 2002
JRNL REFN ISSN 0014-2956
JRNL PMID 11895437
JRNL DOI 10.1046/J.1432-1327.2002.02811.X
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2624691.460
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.3
REMARK 3 NUMBER OF REFLECTIONS : 25992
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1309
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4034
REMARK 3 BIN R VALUE (WORKING SET) : 0.3480
REMARK 3 BIN FREE R VALUE : 0.4010
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 197
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.029
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7851
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.70000
REMARK 3 B22 (A**2) : 1.14000
REMARK 3 B33 (A**2) : 6.56000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM SIGMAA (A) : 0.64
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.49
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.65
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.950
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.150 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.660 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.780 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.000 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.25
REMARK 3 BSOL : 14.43
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : SUS.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : SUS.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IKV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000013374.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-00
REMARK 200 TEMPERATURE (KELVIN) : 270
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 4
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.02320
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29152
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 24.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : 0.15200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 24.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.63000
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, PH 7.2, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 78.07450
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 78.07450
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 59.81650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 78.58400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 59.81650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 78.58400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.07450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 59.81650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 78.58400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 78.07450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 59.81650
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 78.58400
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HETERODIMER
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: 5740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 85800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 390.37250
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 ASN A 103
REMARK 465 LYS A 558
REMARK 465 ILE A 559
REMARK 465 LEU A 560
REMARK 465 PRO B 1001
REMARK 465 ILE B 1002
REMARK 465 SER B 1003
REMARK 465 PRO B 1004
REMARK 465 ASN B 1103
REMARK 465 ASP B 1218
REMARK 465 LYS B 1219
REMARK 465 LYS B 1220
REMARK 465 HIS B 1221
REMARK 465 GLN B 1222
REMARK 465 LYS B 1223
REMARK 465 GLU B 1224
REMARK 465 PRO B 1225
REMARK 465 PRO B 1226
REMARK 465 PHE B 1227
REMARK 465 LEU B 1228
REMARK 465 TRP B 1229
REMARK 465 MET B 1230
REMARK 465 MET B 1357
REMARK 465 ARG B 1358
REMARK 465 GLY B 1359
REMARK 465 ALA B 1360
REMARK 465 HIS B 1361
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 ILE A 556 CG1 CG2 CD1
REMARK 470 ARG A 557 CG CD NE CZ NH1 NH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASN A 136 ND2
REMARK 480 ASN A 137 ND2
REMARK 480 ASP B 1113 CG OD1 OD2
REMARK 480 ASP B 1121 CG OD1 OD2
REMARK 480 ARG B 1199 CG CD NE CZ NH1 NH2
REMARK 480 THR B 1253 OG1 CG2
REMARK 480 ILE B 1270 CG1 CG2 CD1
REMARK 480 GLN B 1278 CG CD OE1 NE2
REMARK 480 LYS B 1281 CG CD CE NZ
REMARK 480 THR B 1362 OG1 CG2
REMARK 480 ASN B 1363 CG OD1 ND2
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 PRO A 14 C - N - CA ANGL. DEV. = 9.2 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 ILE A 2 87.42 -163.13
REMARK 500 SER A 3 126.99 -33.54
REMARK 500 ILE A 5 134.54 -22.20
REMARK 500 GLU A 6 159.27 -47.92
REMARK 500 PRO A 14 -69.16 -26.03
REMARK 500 LYS A 20 40.80 -144.58
REMARK 500 THR A 27 170.78 -59.37
REMARK 500 PRO A 52 5.11 -64.08
REMARK 500 GLU A 53 41.34 -94.65
REMARK 500 PRO A 55 -2.40 -55.49
REMARK 500 PRO A 59 152.83 -43.77
REMARK 500 LYS A 66 105.48 -32.58
REMARK 500 ASP A 67 -10.87 68.01
REMARK 500 SER A 68 12.13 100.36
REMARK 500 ASP A 76 90.83 -51.86
REMARK 500 ARG A 78 -41.69 -29.90
REMARK 500 LYS A 82 -9.81 -56.61
REMARK 500 GLU A 89 143.13 -38.80
REMARK 500 VAL A 111 109.47 -57.80
REMARK 500 ALA A 114 -73.60 -55.77
REMARK 500 ASP A 123 -3.70 -49.51
REMARK 500 THR A 128 46.51 -90.82
REMARK 500 PHE A 130 -169.17 -111.83
REMARK 500 ILE A 135 80.52 4.73
REMARK 500 ASN A 136 60.28 70.09
REMARK 500 ASN A 137 54.50 33.45
REMARK 500 GLU A 138 -88.32 -102.27
REMARK 500 GLN A 151 -104.65 -73.05
REMARK 500 PRO A 176 6.91 -68.22
REMARK 500 MET A 184 -130.42 49.69
REMARK 500 ILE A 195 -25.27 -38.76
REMARK 500 PRO A 217 164.37 -45.35
REMARK 500 ASP A 218 -63.86 -107.12
REMARK 500 LYS A 220 34.18 -89.69
REMARK 500 GLN A 222 -7.18 62.10
REMARK 500 LYS A 223 -79.53 -32.80
REMARK 500 GLU A 224 70.30 6.86
REMARK 500 PRO A 226 172.17 -33.90
REMARK 500 MET A 230 39.95 29.44
REMARK 500 GLU A 248 86.21 56.54
REMARK 500 ASP A 250 -88.66 -63.44
REMARK 500 SER A 268 0.77 -53.71
REMARK 500 LEU A 283 39.90 -85.99
REMARK 500 THR A 286 98.21 -44.06
REMARK 500 ALA A 288 153.43 -48.59
REMARK 500 GLN A 332 -117.47 -80.93
REMARK 500 PRO A 345 103.30 -32.33
REMARK 500 PHE A 346 0.91 83.51
REMARK 500 LYS A 350 149.01 -171.32
REMARK 500 THR A 351 -166.89 -114.08
REMARK 500
REMARK 500 THIS ENTRY HAS 117 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EFZ A 2000
DBREF 1IKV A 1 560 UNP P03366 POL_HV1B1 168 727
DBREF 1IKV B 1001 1427 UNP P03366 POL_HV1B1 168 594
SEQADV 1IKV ASN A 103 UNP P03366 LYS 270 ENGINEERED MUTATION
SEQADV 1IKV GLN A 478 UNP P03366 GLU 645 ENGINEERED MUTATION
SEQADV 1IKV ASN B 1103 UNP P03366 LYS 270 ENGINEERED MUTATION
SEQRES 1 A 560 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 A 560 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 A 560 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 A 560 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 A 560 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 A 560 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 A 560 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 A 560 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS ASN LYS
SEQRES 9 A 560 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 A 560 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 A 560 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 A 560 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 A 560 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 A 560 PRO PHE LYS LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 A 560 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 A 560 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 A 560 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 A 560 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 A 560 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 A 560 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 A 560 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 A 560 ILE LYS VAL ARG GLN LEU CYS LYS LEU LEU ARG GLY THR
SEQRES 23 A 560 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 A 560 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 A 560 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 A 560 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 A 560 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 A 560 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 A 560 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 A 560 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 A 560 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 A 560 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 A 560 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU
SEQRES 34 A 560 GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE TYR VAL
SEQRES 35 A 560 ASP GLY ALA ALA ASN ARG GLU THR LYS LEU GLY LYS ALA
SEQRES 36 A 560 GLY TYR VAL THR ASN LYS GLY ARG GLN LYS VAL VAL PRO
SEQRES 37 A 560 LEU THR ASN THR THR ASN GLN LYS THR GLN LEU GLN ALA
SEQRES 38 A 560 ILE TYR LEU ALA LEU GLN ASP SER GLY LEU GLU VAL ASN
SEQRES 39 A 560 ILE VAL THR ASP SER GLN TYR ALA LEU GLY ILE ILE GLN
SEQRES 40 A 560 ALA GLN PRO ASP LYS SER GLU SER GLU LEU VAL ASN GLN
SEQRES 41 A 560 ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS VAL TYR LEU
SEQRES 42 A 560 ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY GLY ASN GLU
SEQRES 43 A 560 GLN VAL ASP LYS LEU VAL SER ALA GLY ILE ARG LYS ILE
SEQRES 44 A 560 LEU
SEQRES 1 B 427 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 B 427 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 B 427 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 B 427 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 B 427 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 B 427 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 B 427 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 B 427 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS ASN LYS
SEQRES 9 B 427 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 B 427 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 B 427 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 B 427 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 B 427 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 B 427 PRO PHE LYS LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 B 427 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 B 427 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 B 427 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 B 427 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 B 427 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 B 427 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 B 427 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 B 427 ILE LYS VAL ARG GLN LEU CYS LYS LEU LEU ARG GLY THR
SEQRES 23 B 427 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 B 427 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 B 427 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 B 427 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 B 427 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 B 427 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 B 427 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 B 427 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 B 427 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 B 427 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 B 427 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR
HET EFZ A2000 21
HETNAM EFZ (-)-6-CHLORO-4-CYCLOPROPYLETHYNYL-4-TRIFLUOROMETHYL-1,
HETNAM 2 EFZ 4-DIHYDRO-2H-3,1-BENZOXAZIN-2-ONE
HETSYN EFZ DMP-266; EFAVIRENZ
FORMUL 3 EFZ C14 H9 CL F3 N O2
HELIX 1 1 THR A 27 GLY A 45 1 19
HELIX 2 2 LYS A 66 THR A 69 5 4
HELIX 3 3 PHE A 77 THR A 84 1 8
HELIX 4 4 HIS A 96 LEU A 100 5 5
HELIX 5 5 ALA A 114 VAL A 118 5 5
HELIX 6 6 ASP A 121 LYS A 126 1 6
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 VAL A 254 SER A 268 1 15
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 THR A 403 1 10
HELIX 14 14 GLN A 475 GLN A 480 1 6
HELIX 15 15 GLN A 480 ASP A 488 1 9
HELIX 16 16 SER A 499 ALA A 508 1 10
HELIX 17 17 SER A 515 LYS A 528 1 14
HELIX 18 18 GLY A 544 ALA A 554 1 11
HELIX 19 19 THR B 1027 GLU B 1044 1 18
HELIX 20 20 PHE B 1077 ARG B 1083 1 7
HELIX 21 21 THR B 1084 VAL B 1090 1 7
HELIX 22 22 VAL B 1111 PHE B 1116 5 6
HELIX 23 23 PHE B 1124 ALA B 1129 5 6
HELIX 24 24 SER B 1134 GLU B 1138 5 5
HELIX 25 25 LYS B 1154 GLN B 1174 1 21
HELIX 26 26 GLU B 1194 ARG B 1211 1 18
HELIX 27 27 HIS B 1235 TRP B 1239 5 5
HELIX 28 28 THR B 1253 ALA B 1267 1 15
HELIX 29 29 THR B 1296 GLU B 1312 1 17
HELIX 30 30 ASN B 1363 TRP B 1383 1 21
HELIX 31 31 GLN B 1394 TRP B 1402 1 9
HELIX 32 32 THR B 1403 TYR B 1405 5 3
SHEET 1 A 3 ILE A 47 LYS A 49 0
SHEET 2 A 3 ILE A 142 TYR A 146 -1 N GLN A 145 O SER A 48
SHEET 3 A 3 PHE A 130 ILE A 132 -1 N PHE A 130 O TYR A 144
SHEET 1 B 2 PHE A 61 LYS A 64 0
SHEET 2 B 2 TRP A 71 LEU A 74 -1 N ARG A 72 O ILE A 63
SHEET 1 C 3 SER A 105 ASP A 110 0
SHEET 2 C 3 ASP A 186 SER A 191 -1 N LEU A 187 O LEU A 109
SHEET 3 C 3 ILE A 178 TYR A 181 -1 O VAL A 179 N GLY A 190
SHEET 1 D 4 LEU A 228 TRP A 229 0
SHEET 2 D 4 TYR A 232 LEU A 234 -1 N TYR A 232 O TRP A 229
SHEET 3 D 4 LYS A 238 VAL A 241 -1 O THR A 240 N GLU A 233
SHEET 4 D 4 GLY A 316 VAL A 317 -1 N GLY A 316 O TRP A 239
SHEET 1 E 2 TRP A 252 THR A 253 0
SHEET 2 E 2 VAL A 292 ILE A 293 -1 N ILE A 293 O TRP A 252
SHEET 1 F 5 LYS A 347 TYR A 354 0
SHEET 2 F 5 TRP A 337 GLU A 344 -1 O TRP A 337 N TYR A 354
SHEET 3 F 5 ILE A 326 LYS A 331 -1 N ILE A 326 O TYR A 342
SHEET 4 F 5 LYS A 388 LEU A 391 1 O LYS A 388 N ALA A 327
SHEET 5 F 5 TRP A 414 PHE A 416 1 O GLU A 415 N LEU A 391
SHEET 1 G 3 THR A 439 TYR A 441 0
SHEET 2 G 3 GLU A 492 THR A 497 1 O ASN A 494 N PHE A 440
SHEET 3 G 3 LYS A 530 TRP A 535 1 O LYS A 530 N VAL A 493
SHEET 1 H 2 LEU A 452 LYS A 454 0
SHEET 2 H 2 PRO A 468 THR A 470 -1 N LEU A 469 O GLY A 453
SHEET 1 I 3 ILE B1047 LYS B1049 0
SHEET 2 I 3 ILE B1142 TYR B1146 -1 O GLN B1145 N SER B1048
SHEET 3 I 3 PHE B1130 ILE B1132 -1 N PHE B1130 O TYR B1144
SHEET 1 J 2 VAL B1060 LYS B1064 0
SHEET 2 J 2 TRP B1071 VAL B1075 -1 N ARG B1072 O ILE B1063
SHEET 1 K 4 VAL B1179 TYR B1183 0
SHEET 2 K 4 ASP B1186 SER B1191 -1 O ASP B1186 N TYR B1183
SHEET 3 K 4 SER B1105 LEU B1109 -1 O SER B1105 N SER B1191
SHEET 4 K 4 GLU B1233 LEU B1234 -1 N LEU B1234 O VAL B1106
SHEET 1 L 5 ASN B1348 TYR B1354 0
SHEET 2 L 5 TRP B1337 TYR B1342 -1 N TRP B1337 O TYR B1354
SHEET 3 L 5 ILE B1326 LYS B1331 -1 O ILE B1326 N TYR B1342
SHEET 4 L 5 LYS B1388 LEU B1391 1 O LYS B1388 N ALA B1327
SHEET 5 L 5 GLU B1413 PHE B1416 1 O GLU B1413 N PHE B1389
CISPEP 1 PRO A 225 PRO A 226 0 0.51
CISPEP 2 PRO A 420 PRO A 421 0 0.90
SITE 1 AC1 12 LEU A 100 LYS A 101 VAL A 106 VAL A 179
SITE 2 AC1 12 TYR A 181 TYR A 188 GLY A 190 PHE A 227
SITE 3 AC1 12 TRP A 229 LEU A 234 HIS A 235 TYR A 318
CRYST1 119.633 157.168 156.149 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 0.008359 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006363 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006404 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
