HEADER TRANSFERASE 10-AUG-00 1FKO
TITLE CRYSTAL STRUCTURE OF NNRTI RESISTANT K103N MUTANT HIV-1 REVERSE
TITLE 2 TRANSCRIPTASE IN COMPLEX WITH DMP-266(EFAVIRENZ)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 RT, A-CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: P66;
COMPND 5 EC: 2.7.7.49;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: COMPLEXED WITH DMP-266(EFAVIRENZ);
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: HIV-1 RT, B-CHAIN;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: P51;
COMPND 13 EC: 2.7.7.49;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 STRAIN: HXB2 ISOLATE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 9 ORGANISM_TAXID: 11676;
SOURCE 10 STRAIN: HXB2 ISOLATE;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HIV-1 REVERSE TRANSCRIPTASE, AIDS, NON-NUCLEOSIDE INHIBITOR, DMP-266,
KEYWDS 2 EFAVIRENZ, DRUG RESISTANCE MUTATION, DRUG DESIGN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.REN,J.MILTON,K.L.WEAVER,S.A.SHORT,D.I.STUART,D.K.STAMMERS
REVDAT 8 14-MAR-18 1FKO 1 SEQADV
REVDAT 7 31-JAN-18 1FKO 1 JRNL
REVDAT 6 18-JUL-12 1FKO 1 HETSYN VERSN
REVDAT 5 24-FEB-09 1FKO 1 VERSN
REVDAT 4 28-DEC-04 1FKO 1 HETATM REMARK
REVDAT 3 06-JAN-04 1FKO 1 SOURCE JRNL REMARK MODRES
REVDAT 2 28-FEB-01 1FKO 3 ATOM REMARK
REVDAT 1 03-NOV-00 1FKO 0
JRNL AUTH J.REN,J.MILTON,K.L.WEAVER,S.A.SHORT,D.I.STUART,D.K.STAMMERS
JRNL TITL STRUCTURAL BASIS FOR THE RESILIENCE OF EFAVIRENZ (DMP-266)
JRNL TITL 2 TO DRUG RESISTANCE MUTATIONS IN HIV-1 REVERSE TRANSCRIPTASE.
JRNL REF STRUCTURE FOLD.DES. V. 8 1089 2000
JRNL REFN ISSN 0969-2126
JRNL PMID 11080630
JRNL DOI 10.1016/S0969-2126(00)00513-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.REN,C.NICHOLS,L.E.BIRD,T.FUJIWARA,H.SUGINOTO,D.I.STUART,
REMARK 1 AUTH 2 D.K.STAMMERS
REMARK 1 TITL BINDING OF THE SECOND GENERATTION NON-NUCLEOSIDE INHIBITOR
REMARK 1 TITL 2 S-1153 TO HIV-1 REVERSE TRANSCRIPTASE INVOLVES EXTENSIVE
REMARK 1 TITL 3 MAIN CHAIN HYDROGEN BONDING
REMARK 1 REF J.BIOL.CHEM. V. 275 14316 2000
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.275.19.14316
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.REN,J.DIPROSE,J.WARREN,R.M.ESNOUF,L.E.BIRD,S.IKEMIZU,
REMARK 1 AUTH 2 M.SLATER,J.MILTON,J.BALZARINI,D.I.STUART,D.K.STAMMERS
REMARK 1 TITL PHENETHYLTHIAZOLYLTHIOUREA (PETT) NON-NUCLEOSIDE INHIBITORS
REMARK 1 TITL 2 OF HIV-1 AND HIV-2 REVERSE TRANSCRIPTASES: STRUCTURAL AND
REMARK 1 TITL 3 BIOCHEMICAL ANALYSES
REMARK 1 REF J.BIOL.CHEM. V. 275 5633 2000
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.275.8.5633
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.REN,R.M.ESNOUF,A.L.HOPKINS,D.I.STUART,D.K.STAMMERS
REMARK 1 TITL CRYSTALLOGRAPHIC ANALYSIS OF THE BINDING MODES OF
REMARK 1 TITL 2 NON-NUCLEOSIDE THIAZOLOISOINDOLINONE INHIBITORS TO HIV-1
REMARK 1 TITL 3 REVERSE TRANSCRIPTASE AND COMPARISON WITH MODELING STUDIES
REMARK 1 REF J.MED.CHEM. V. 42 3845 1999
REMARK 1 REFN ISSN 0022-2623
REMARK 1 DOI 10.1021/JM990275T
REMARK 1 REFERENCE 4
REMARK 1 AUTH A.L.HOPKINS,J.REN,H.TANAKA,M.BABA,M.OKAMATO,D.I.STUART,
REMARK 1 AUTH 2 D.K.STAMMERS
REMARK 1 TITL DESIGN OF MKC-442 (EMIVIRINE) ANALOGUES WITH IMPROVED
REMARK 1 TITL 2 ACTIVITY AGAINST DRUG-RESISTANT HIV MUTANTS
REMARK 1 REF J.MED.CHEM. V. 42 4500 1999
REMARK 1 REFN ISSN 0022-2623
REMARK 1 DOI 10.1021/JM990192C
REMARK 1 REFERENCE 5
REMARK 1 AUTH J.REN,R.M.ESNOUF,A.L.HOPKINS,J.WARREN,J.BALZARINI,
REMARK 1 AUTH 2 D.I.STUART,D.K.STAMMERS
REMARK 1 TITL CRYSTAL STRUCTURES OF REVERSE TRANSCRIPTASE IN COMPLEX WITH
REMARK 1 TITL 2 CARBOXANILIDE DERIVATIVES
REMARK 1 REF BIOCHEMISTRY V. 37 14394 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI981309M
REMARK 1 REFERENCE 6
REMARK 1 AUTH J.REN,R.M.ESNOUF,A.L.HOPKINS,E.Y.JONES,I.KIRBY,J.KEELING,
REMARK 1 AUTH 2 C.K.ROSS,B.A.LARDER,D.I.STUART,D.K.STAMMERS
REMARK 1 TITL 3'-AZIDO-3'-DEOXYTHYMIDINE DRUG RESISTANCE MUTATIONS IN
REMARK 1 TITL 2 HIV-1 REVERSE TRANSCRIPTASE CAN INDUCE LONG RANGE
REMARK 1 TITL 3 CONFORMATIONAL CHANGES
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 95 9518 1998
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.95.16.9518
REMARK 1 REFERENCE 7
REMARK 1 AUTH R.M.ESNOUF,J.REN,E.GARMAN,D.O.SOMERS,C.K.ROSS,E.Y.JONES,
REMARK 1 AUTH 2 D.K STAMMERS,D.I.STUART
REMARK 1 TITL CONTINUOUS AND DISCONTINUOUS CHANGES IN THE UNIT CELL OF
REMARK 1 TITL 2 HIV-1 REVERSE TRANSCRIPTASE CRYSTALS ON DEHYDRATION
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 54 938 1998
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444998004284
REMARK 1 REFERENCE 8
REMARK 1 AUTH R.M.ESNOUF,J.REN,A.L.HOPKINS,C.K.ROSS,E.Y.JONES,
REMARK 1 AUTH 2 D.K.STAMMERS,D.I.STUART
REMARK 1 TITL UNIQUE FEATURES IN THE STRUCTURE OF THE COMPLEX BETWEEN
REMARK 1 TITL 2 HIV-1 REVERSE TRANSCRIPTASE AND THE
REMARK 1 TITL 3 BIS(HETEROARYL)PIPERAZINE (BHAP) U-90152 EXPLAIN RESISTANCE
REMARK 1 TITL 4 MUTATIONS FOR THIS NON-NUCLEOSIDE INHIBITOR
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 94 3984 1997
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.94.8.3984
REMARK 1 REFERENCE 9
REMARK 1 AUTH A.L HOPKINS,J.REN,R.M.ESNOUF,B.E.WILLCOX,E.Y.JONES,C.K.ROSS,
REMARK 1 AUTH 2 T.MIYASAKA,R.T.WALKER,H.TANAKA,D.K.STAMMERS,D.I.STUART
REMARK 1 TITL COMPLEXES OF HIV-1 REVERSE TRANSCRIPTASE WITH INHIBITORS OF
REMARK 1 TITL 2 THE HEPT SERIES REVEAL CONFORMATIONAL CHANGES RELEVANT TO
REMARK 1 TITL 3 THE DESIGN OF POTENT NON-NUCLEOSIDE INHIBITORS
REMARK 1 REF J.MED.CHEM. V. 39 1589 1996
REMARK 1 REFN ISSN 0022-2623
REMARK 1 DOI 10.1021/JM960056X
REMARK 1 REFERENCE 10
REMARK 1 AUTH J.REN,R.M.ESNOUF,A.L.HOPKINS,C.K.ROSS,E.Y.JONES,
REMARK 1 AUTH 2 D.K STAMMERS,D.I.STUART
REMARK 1 TITL THE STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE COMPLEXED WITH
REMARK 1 TITL 2 9-CHLORO-TIBO: LESSONS FOR INHIBITOR DESIGN
REMARK 1 REF STRUCTURE V. 3 915 1995
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 11
REMARK 1 AUTH J.REN,R.M.ESNOUF,E.GARMAN,D.O.SOMERS,C.K.ROSS,I.KIRBY,
REMARK 1 AUTH 2 J.KEELING,G.DARBY,E.Y.JONES,D.I.STUART,D.K.STAMMERS
REMARK 1 TITL HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR
REMARK 1 TITL 2 RT-INHIBITOR COMPLEXES
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 293 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 12
REMARK 1 AUTH R.M.ESNOUF,J.REN,C.K.ROSS,E.Y.JONES,D.K.STAMMERS,D.I.STUART
REMARK 1 TITL MECHANISM OF INHIBITION OF HIV-1 REVERSE TRANSCRIPTASE BY
REMARK 1 TITL 2 NON-NUCLEOSIDE INHIBITORS
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 303 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 13
REMARK 1 AUTH D.K.STAMMERS,D.O.SOMERS,C.K.ROSS,I.KIRBY,P.H.RAY,J.E.WILSON,
REMARK 1 AUTH 2 M.NORMAN,J.REN,R.M.ESNOUF,E.GARMAN,E.Y.JONES,D.I.STUART
REMARK 1 TITL CRYSTALS OF HIV-1 REVERSE TRANSCRIPTASE DIFFRACTING TO 2.2
REMARK 1 TITL 2 ANGSTROM RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 242 586 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1994.1604
REMARK 2
REMARK 2 RESOLUTION. 2.90 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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.2
REMARK 3 NUMBER OF REFLECTIONS : 23338
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1541
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7756
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) : 55.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
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) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: POSITIONAL RESTRAINTS WERE APPLIED TO
REMARK 3 ALL ATOMS DISTANT FROM THE NNRTI-BINDING SITE (DEFINED AS
REMARK 3 GREATER THAN 25 ANSTROM FROM THE CA ATOM OF RESIDUE 188)
REMARK 3 THROUGHOUT THE REFINEMENT.
REMARK 4
REMARK 4 1FKO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011671.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-NOV-97
REMARK 200 TEMPERATURE (KELVIN) : 289
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23338
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.64100
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: NULL
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 (%): 50.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SEE REFERENCE 13, PH 5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 70.15000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.15000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.85000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: HIV-1 RT IS A HETERODIMER CONSISTING OF A P66 AND A P51
REMARK 300 SUBUNITS, THE P51 CONTAINS THE FIRST 440 RESIDUES OF THE P66.
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: 5920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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 PRO B 1
REMARK 465 ILE B 2
REMARK 465 TRP B 88
REMARK 465 GLU B 89
REMARK 465 VAL B 90
REMARK 465 GLN B 91
REMARK 465 LEU B 214
REMARK 465 THR B 215
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 TRP B 229
REMARK 465 MET B 230
REMARK 465 GLY B 231
REMARK 465 TYR B 232
REMARK 465 LEU B 429
REMARK 465 GLU B 430
REMARK 465 LYS B 431
REMARK 465 GLU B 432
REMARK 465 PRO B 433
REMARK 465 ILE B 434
REMARK 465 VAL B 435
REMARK 465 GLY B 436
REMARK 465 ALA B 437
REMARK 465 GLU B 438
REMARK 465 THR B 439
REMARK 465 PHE B 440
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 B 133 C - N - CA ANGL. DEV. = 10.9 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 PRO A 14 107.27 -41.72
REMARK 500 TRP A 24 140.71 -34.73
REMARK 500 GLU A 53 7.20 -69.43
REMARK 500 ASN A 57 147.81 -174.20
REMARK 500 ASP A 67 -22.48 91.56
REMARK 500 LEU A 74 134.23 -175.01
REMARK 500 PHE A 116 -3.58 -58.92
REMARK 500 THR A 128 31.35 -95.52
REMARK 500 GLU A 138 -78.00 -60.58
REMARK 500 THR A 139 -68.66 -145.60
REMARK 500 SER A 156 -63.16 -29.86
REMARK 500 ILE A 167 -14.85 -49.03
REMARK 500 ASN A 175 66.86 -112.49
REMARK 500 ASP A 177 -9.76 -59.55
REMARK 500 TYR A 183 113.76 -165.86
REMARK 500 MET A 184 -136.99 43.65
REMARK 500 MET A 230 87.00 8.15
REMARK 500 GLN A 242 94.51 -59.74
REMARK 500 PRO A 243 136.07 -32.71
REMARK 500 ASP A 250 -82.30 -64.66
REMARK 500 ARG A 284 115.76 -27.94
REMARK 500 THR A 286 122.71 -39.99
REMARK 500 LYS A 311 -75.12 -84.40
REMARK 500 GLU A 312 89.48 -57.02
REMARK 500 PRO A 321 -33.48 -36.67
REMARK 500 GLN A 332 -64.01 -91.53
REMARK 500 PRO A 345 134.90 -32.34
REMARK 500 PHE A 346 -15.03 69.45
REMARK 500 MET A 357 158.99 -44.12
REMARK 500 ARG A 358 -29.48 -36.92
REMARK 500 ALA A 360 -91.18 -125.19
REMARK 500 TRP A 410 147.29 -170.68
REMARK 500 ASN A 418 60.14 -66.54
REMARK 500 TYR A 427 161.32 165.55
REMARK 500 TYR A 441 78.25 -103.48
REMARK 500 ALA A 445 149.50 -172.99
REMARK 500 ASP A 488 14.57 -67.98
REMARK 500 SER A 489 -64.45 -93.19
REMARK 500 LEU A 491 -42.17 -26.02
REMARK 500 ALA A 508 36.55 -89.37
REMARK 500 GLN A 509 52.79 15.61
REMARK 500 GLN A 512 143.37 -173.37
REMARK 500 ILE A 542 -77.74 -95.53
REMARK 500 GLU B 44 0.13 -50.00
REMARK 500 GLU B 53 -9.55 -56.53
REMARK 500 PHE B 61 -169.36 -163.66
REMARK 500 SER B 68 121.33 151.19
REMARK 500 ASN B 103 156.65 -38.07
REMARK 500 PHE B 116 -6.49 -53.62
REMARK 500 GLU B 122 -75.19 -29.81
REMARK 500
REMARK 500 THIS ENTRY HAS 73 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 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RTV RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH NEVIRAPINE
REMARK 900 RELATED ID: 1RTH RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH 1051U91
REMARK 900 RELATED ID: 1VRU RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH ALPHA-APA
REMARK 900 RELATED ID: 1RTI RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH HEPT
REMARK 900 RELATED ID: 1RTJ RELATED DB: PDB
REMARK 900 HIV-1 RT
REMARK 900 RELATED ID: 1REV RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH 9-CL-TIBO
REMARK 900 RELATED ID: 1RT1 RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH MKC-442
REMARK 900 RELATED ID: 1RT2 RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH TNK-651
REMARK 900 RELATED ID: 1KLM RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH BHAP (U-90152)
REMARK 900 RELATED ID: 1RT3 RELATED DB: PDB
REMARK 900 AZT DRUG RESISTANT HIV-1 RT MUTANT (RTMC) COMPLEXED WITH 1051U91
REMARK 900 RELATED ID: 1RT4 RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH UC-781
REMARK 900 RELATED ID: 1RT5 RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH UC-10
REMARK 900 RELATED ID: 1RT6 RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH UC-38
REMARK 900 RELATED ID: 1RT7 RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH UC-84
REMARK 900 RELATED ID: 1C0T RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH BM+21.1326
REMARK 900 RELATED ID: 1C0U RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH BM+50.0934
REMARK 900 RELATED ID: 1C1B RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH GCA-186
REMARK 900 RELATED ID: 1C1C RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH TNK-6123
REMARK 900 RELATED ID: 1DTQ RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH PETT-1
REMARK 900 RELATED ID: 1DTT RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH PETT-2
REMARK 900 RELATED ID: 1EP4 RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH S-1153
REMARK 900 RELATED ID: 1FK9 RELATED DB: PDB
REMARK 900 HIV-1 RT COMPLEXED WITH DMP-266 (EFAVIRENZ)
REMARK 900 RELATED ID: 1FKP RELATED DB: PDB
REMARK 900 NNRTI RESISTANT K103N MUTANT HIV-1 RT COMPLEXED WITH NEVIRAPINE
DBREF 1FKO A 1 543 UNP P04585 POL_HV1H2 587 1129
DBREF 1FKO B 1 440 UNP P04585 POL_HV1H2 587 1026
SEQADV 1FKO ASN A 103 UNP P04585 LEU 258 ENGINEERED MUTATION
SEQADV 1FKO ASN B 103 UNP P04585 LEU 258 ENGINEERED MUTATION
SEQRES 1 A 543 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 A 543 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 A 543 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 A 543 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 A 543 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 A 543 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 A 543 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 A 543 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS ASN LYS
SEQRES 9 A 543 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 A 543 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 A 543 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 A 543 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 A 543 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 A 543 PRO PHE ARG LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 A 543 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 A 543 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 A 543 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 A 543 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 A 543 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 A 543 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 A 543 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 A 543 ILE LYS VAL ARG GLN LEU CSD LYS LEU LEU ARG GLY THR
SEQRES 23 A 543 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 A 543 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 A 543 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 A 543 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 A 543 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 A 543 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 A 543 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 A 543 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 A 543 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 A 543 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 A 543 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU
SEQRES 34 A 543 GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE TYR VAL
SEQRES 35 A 543 ASP GLY ALA ALA ASN ARG GLU THR LYS LEU GLY LYS ALA
SEQRES 36 A 543 GLY TYR VAL THR ASN ARG GLY ARG GLN LYS VAL VAL THR
SEQRES 37 A 543 LEU THR ASP THR THR ASN GLN LYS THR GLU LEU GLN ALA
SEQRES 38 A 543 ILE TYR LEU ALA LEU GLN ASP SER GLY LEU GLU VAL ASN
SEQRES 39 A 543 ILE VAL THR ASP SER GLN TYR ALA LEU GLY ILE ILE GLN
SEQRES 40 A 543 ALA GLN PRO ASP GLN SER GLU SER GLU LEU VAL ASN GLN
SEQRES 41 A 543 ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS VAL TYR LEU
SEQRES 42 A 543 ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY
SEQRES 1 B 440 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 B 440 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 B 440 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 B 440 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 B 440 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 B 440 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 B 440 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 B 440 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS ASN LYS
SEQRES 9 B 440 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 B 440 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 B 440 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 B 440 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 B 440 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 B 440 PRO PHE ARG LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 B 440 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 B 440 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 B 440 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 B 440 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 B 440 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 B 440 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 B 440 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 B 440 ILE LYS VAL ARG GLN LEU CYS LYS LEU LEU ARG GLY THR
SEQRES 23 B 440 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 B 440 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 B 440 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 B 440 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 B 440 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 B 440 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 B 440 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 B 440 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 B 440 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 B 440 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 B 440 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU
SEQRES 34 B 440 GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE
MODRES 1FKO CSD A 280 CYS 3-SULFINOALANINE
HET CSD A 280 8
HET EFZ A 999 21
HETNAM CSD 3-SULFINOALANINE
HETNAM EFZ (-)-6-CHLORO-4-CYCLOPROPYLETHYNYL-4-TRIFLUOROMETHYL-1,
HETNAM 2 EFZ 4-DIHYDRO-2H-3,1-BENZOXAZIN-2-ONE
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
HETSYN EFZ DMP-266; EFAVIRENZ
FORMUL 1 CSD C3 H7 N O4 S
FORMUL 3 EFZ C14 H9 CL F3 N O2
HELIX 1 1 THR A 27 GLY A 45 1 19
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 GLY A 112 VAL A 118 5 7
HELIX 5 5 PHE A 124 TYR A 127 5 4
HELIX 6 6 LYS A 154 ASN A 175 1 22
HELIX 7 7 GLU A 194 ARG A 211 1 18
HELIX 8 8 VAL A 254 GLN A 269 1 16
HELIX 9 9 THR A 296 LEU A 310 1 15
HELIX 10 10 ASN A 363 TRP A 383 1 21
HELIX 11 11 GLN A 394 THR A 403 1 10
HELIX 12 12 THR A 473 ASP A 488 1 16
HELIX 13 13 SER A 499 ALA A 508 1 10
HELIX 14 14 SER A 515 LYS A 528 1 14
HELIX 15 15 THR B 27 GLU B 44 1 18
HELIX 16 16 PHE B 77 ARG B 83 1 7
HELIX 17 17 GLY B 112 VAL B 118 5 7
HELIX 18 18 ASP B 121 LYS B 126 1 6
HELIX 19 19 TYR B 127 ALA B 129 5 3
HELIX 20 20 SER B 134 GLU B 138 5 5
HELIX 21 21 LYS B 154 PHE B 160 1 7
HELIX 22 22 PHE B 160 LYS B 173 1 14
HELIX 23 23 GLU B 194 GLY B 213 1 20
HELIX 24 24 VAL B 254 SER B 268 1 15
HELIX 25 25 VAL B 276 LEU B 283 1 8
HELIX 26 26 THR B 296 LEU B 310 1 15
HELIX 27 27 ASN B 363 GLY B 384 1 22
HELIX 28 28 GLN B 394 TRP B 406 1 13
HELIX 29 29 PRO B 420 GLN B 428 1 9
SHEET 1 A 3 ILE A 47 LYS A 49 0
SHEET 2 A 3 ILE A 142 TYR A 146 -1 O GLN A 145 N SER A 48
SHEET 3 A 3 ALA A 129 ILE A 132 -1 N PHE A 130 O TYR A 144
SHEET 1 B 2 VAL A 60 ILE A 63 0
SHEET 2 B 2 ARG A 72 VAL A 75 -1 O ARG A 72 N 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 O LEU A 187 N LEU A 109
SHEET 3 C 3 VAL A 179 TYR A 183 -1 N VAL A 179 O GLY A 190
SHEET 1 D 4 PHE A 227 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 TRP A 239 VAL A 241 -1 N THR A 240 O GLU A 233
SHEET 4 D 4 HIS A 315 GLY A 316 -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 ALA A 355 0
SHEET 2 F 5 GLN A 336 GLU A 344 -1 N TRP A 337 O TYR A 354
SHEET 3 F 5 ILE A 326 GLY A 333 -1 O ILE A 326 N 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 N GLU A 415 O PHE A 389
SHEET 1 G 2 HIS A 361 THR A 362 0
SHEET 2 G 2 GLN A 512 SER A 513 -1 O GLN A 512 N THR A 362
SHEET 1 H 3 GLU A 438 TYR A 441 0
SHEET 2 H 3 GLU A 492 THR A 497 1 O GLU A 492 N GLU A 438
SHEET 3 H 3 LYS A 530 TRP A 535 1 O LYS A 530 N VAL A 493
SHEET 1 I 3 ASP A 443 ALA A 446 0
SHEET 2 I 3 GLY A 453 VAL A 458 -1 N LYS A 454 O ALA A 445
SHEET 3 I 3 GLN A 464 LEU A 469 -1 O LYS A 465 N TYR A 457
SHEET 1 J 3 ILE B 47 LYS B 49 0
SHEET 2 J 3 ILE B 142 TYR B 146 -1 O GLN B 145 N SER B 48
SHEET 3 J 3 PHE B 130 ILE B 132 -1 O PHE B 130 N TYR B 144
SHEET 1 K 2 VAL B 60 ILE B 63 0
SHEET 2 K 2 ARG B 72 VAL B 75 -1 N ARG B 72 O ILE B 63
SHEET 1 L 3 SER B 105 ASP B 110 0
SHEET 2 L 3 ASP B 186 SER B 191 -1 O LEU B 187 N LEU B 109
SHEET 3 L 3 ILE B 178 TYR B 183 -1 O VAL B 179 N GLY B 190
SHEET 1 M 2 TRP B 252 THR B 253 0
SHEET 2 M 2 VAL B 292 ILE B 293 -1 N ILE B 293 O TRP B 252
SHEET 1 N 5 LYS B 347 ALA B 355 0
SHEET 2 N 5 GLN B 336 GLU B 344 -1 N TRP B 337 O TYR B 354
SHEET 3 N 5 ILE B 326 GLY B 333 -1 N ILE B 326 O TYR B 342
SHEET 4 N 5 LYS B 388 LEU B 391 1 O LYS B 388 N ALA B 327
SHEET 5 N 5 GLU B 413 PHE B 416 1 O GLU B 413 N PHE B 389
LINK C LEU A 279 N CSD A 280 1555 1555 1.33
LINK C CSD A 280 N LYS A 281 1555 1555 1.38
CISPEP 1 PRO A 225 PRO A 226 0 -0.62
CISPEP 2 PRO A 420 PRO A 421 0 0.13
SITE 1 AC1 11 LEU A 100 LYS A 101 ASN A 103 VAL A 179
SITE 2 AC1 11 TYR A 181 TYR A 188 VAL A 189 GLY A 190
SITE 3 AC1 11 PHE A 227 LEU A 234 TYR A 318
CRYST1 140.300 109.700 74.400 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007128 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009116 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013441 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
