HEADER ASPARTYL PROTEASE 21-NOV-96 1UWB
TITLE TYR 181 CYS HIV-1 RT/8-CL TIBO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REVERSE TRANSCRIPTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.7.49;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: REVERSE TRANSCRIPTASE;
COMPND 9 CHAIN: B;
COMPND 10 EC: 2.7.7.49;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 STRAIN: BH10;
SOURCE 5 CELL_LINE: 293;
SOURCE 6 ATCC: 1065288;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: 293;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 12 ORGANISM_TAXID: 11676;
SOURCE 13 STRAIN: BH10;
SOURCE 14 CELL_LINE: 293;
SOURCE 15 ATCC: 1065288;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: 293
KEYWDS AIDS, POLYPROTEIN, HYDROLASE, ASPARTYL PROTEASE, ENDONUCLEASE, RNA-
KEYWDS 2 DIRECTED DNA POLYMERASE, TYR181CYS HIV-1 RT/8-CL TIBO, DRUG-
KEYWDS 3 RESISTANT MUTANT
EXPDTA X-RAY DIFFRACTION
AUTHOR K.DAS,J.DING,Y.HSIOU,E.ARNOLD
REVDAT 5 14-FEB-24 1UWB 1 REMARK
REVDAT 4 03-NOV-21 1UWB 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1UWB 1 VERSN
REVDAT 2 01-APR-03 1UWB 1 JRNL
REVDAT 1 15-MAY-97 1UWB 0
JRNL AUTH K.DAS,J.DING,Y.HSIOU,A.D.CLARK JR.,H.MOEREELS,L.KOYMANS,
JRNL AUTH 2 K.ANDRIES,R.PAUWELS,P.A.JANSSEN,P.L.BOYER,P.CLARK,
JRNL AUTH 3 R.H.SMITH JR.,M.B.KROEGER SMITH,C.J.MICHEJDA,S.H.HUGHES,
JRNL AUTH 4 E.ARNOLD
JRNL TITL CRYSTAL STRUCTURES OF 8-CL AND 9-CL TIBO COMPLEXED WITH
JRNL TITL 2 WILD-TYPE HIV-1 RT AND 8-CL TIBO COMPLEXED WITH THE
JRNL TITL 3 TYR181CYS HIV-1 RT DRUG-RESISTANT MUTANT.
JRNL REF J.MOL.BIOL. V. 264 1085 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 9000632
JRNL DOI 10.1006/JMBI.1996.0698
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.ARNOLD,K.DAS,J.DING,P.N.YADAV,Y.HSIOU,P.L.BOYER,S.H.HUGHES
REMARK 1 TITL TARGETING HIV REVERSE TRANSCRIPTASE FOR ANTI-AIDS DRUG
REMARK 1 TITL 2 DESIGN: STRUCTURAL AND BIOLOGICAL CONSIDERATIONS FOR
REMARK 1 TITL 3 CHEMOTHERAPEUTIC STRATEGIES
REMARK 1 REF DRUG DES.DISCOVERY V. 13 29 1996
REMARK 1 REFN ISSN 1055-9612
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.HSIOU,J.DING,K.DAS,A.D.CLARK JUNIOR,S.H.HUGHES,E.ARNOLD
REMARK 1 TITL STRUCTURE OF UNLIGANDED HIV-1 REVERSE TRANSCRIPTASE AT 2.7 A
REMARK 1 TITL 2 RESOLUTION: IMPLICATIONS OF CONFORMATIONAL CHANGES FOR
REMARK 1 TITL 3 POLYMERIZATION AND INHIBITION MECHANISMS
REMARK 1 REF STRUCTURE V. 4 853 1996
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 3
REMARK 1 AUTH P.H.PATEL,A.JACOBO-MOLINA,J.DING,C.TANTILLO,
REMARK 1 AUTH 2 A.D.CLARK JUNIOR,R.RAAG,R.G.NANNI,S.H.HUGHES,E.ARNOLD
REMARK 1 TITL INSIGHTS INTO DNA POLYMERIZATION MECHANISMS FROM STRUCTURE
REMARK 1 TITL 2 AND FUNCTION ANALYSIS OF HIV-1 REVERSE TRANSCRIPTASE
REMARK 1 REF BIOCHEMISTRY V. 34 5351 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.DING,K.DAS,C.TANTILLO,W.ZHANG,A.D.CLARK JUNIOR,S.JESSEN,
REMARK 1 AUTH 2 X.LU,Y.HSIOU,A.JACOBO-MOLINA,K.ANDRIES,ET AL.
REMARK 1 TITL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN A COMPLEX WITH
REMARK 1 TITL 2 THE NON-NUCLEOSIDE INHIBITOR ALPHA-APA R 95845 AT 2.8 A
REMARK 1 TITL 3 RESOLUTION
REMARK 1 REF STRUCTURE V. 3 365 1995
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 5
REMARK 1 AUTH J.DING,K.DAS,H.MOEREELS,L.KOYMANS,K.ANDRIES,P.A.JANSSEN,
REMARK 1 AUTH 2 S.H.HUGHES,E.ARNOLD
REMARK 1 TITL STRUCTURE OF HIV-1 RT/TIBO R 86183 COMPLEX REVEALS
REMARK 1 TITL 2 SIMILARITY IN THE BINDING OF DIVERSE NONNUCLEOSIDE
REMARK 1 TITL 3 INHIBITORS
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 407 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 6
REMARK 1 AUTH C.TANTILLO,J.DING,A.JACOBO-MOLINA,R.G.NANNI,P.L.BOYER,
REMARK 1 AUTH 2 S.H.HUGHES,R.PAUWELS,K.ANDRIES,P.A.JANSSEN,E.ARNOLD
REMARK 1 TITL LOCATIONS OF ANTI-AIDS DRUG BINDING SITES AND RESISTANCE
REMARK 1 TITL 2 MUTATIONS IN THE THREE-DIMENSIONAL STRUCTURE OF HIV-1
REMARK 1 TITL 3 REVERSE TRANSCRIPTASE. IMPLICATIONS FOR MECHANISMS OF DRUG
REMARK 1 TITL 4 INHIBITION AND RESISTANCE
REMARK 1 REF J.MOL.BIOL. V. 243 369 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 7
REMARK 1 AUTH A.JACOBO-MOLINA,J.DING,R.G.NANNI,A.D.CLARK JUNIOR,X.LU,
REMARK 1 AUTH 2 C.TANTILLO,R.L.WILLIAMS,G.KAMER,A.L.FERRIS,P.CLARK,ET AL.
REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN IMMUNODEFICIENCY VIRUS TYPE 1
REMARK 1 TITL 2 REVERSE TRANSCRIPTASE COMPLEXED WITH DOUBLE-STRANDED DNA AT
REMARK 1 TITL 3 3.0 A RESOLUTION SHOWS BENT DNA
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 90 6320 1993
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 10.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.0
REMARK 3 NUMBER OF REFLECTIONS : 21825
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) : 0.274
REMARK 3 FREE R VALUE : 0.360
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1059
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.31
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1944
REMARK 3 BIN R VALUE (WORKING SET) : 0.3870
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 94
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.037
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7801
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) : 52.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.60
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) : 0.51
REMARK 3 ESD FROM SIGMAA (A) : 0.61
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.71
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.68
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.600
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) : 1.570 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.820 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.640 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.680 ; 2.500
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : TBO.PAR
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TBO.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1UWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176990.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAR-96
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 2.620
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 112.85000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 112.85000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.60000
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 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: 5620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48890 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 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 66 CG CD CE NZ
REMARK 470 TRP A 71 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 71 CZ3 CH2
REMARK 470 ARG A 72 CG CD NE CZ NH1 NH2
REMARK 470 SER A 134 OG
REMARK 470 ILE A 135 CG1 CG2 CD1
REMARK 470 ASN A 136 CG OD1 ND2
REMARK 470 ASN A 137 CG OD1 ND2
REMARK 470 GLU A 138 CG CD OE1 OE2
REMARK 470 THR A 139 OG1 CG2
REMARK 470 CYS A 181 SG
REMARK 470 ASP A 218 CG OD1 OD2
REMARK 470 LYS A 219 CG CD CE NZ
REMARK 470 LYS A 220 CG CD CE NZ
REMARK 470 HIS A 221 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 222 CG CD OE1 NE2
REMARK 470 LYS A 223 CG CD CE NZ
REMARK 470 LYS A 249 CG CD CE NZ
REMARK 470 LYS A 281 CG CD CE NZ
REMARK 470 LEU A 282 CG CD1 CD2
REMARK 470 LEU A 283 CG CD1 CD2
REMARK 470 ARG A 284 CG CD NE CZ NH1 NH2
REMARK 470 THR A 286 OG1 CG2
REMARK 470 LYS A 287 CG CD CE NZ
REMARK 470 LEU A 289 CG CD1 CD2
REMARK 470 THR A 290 OG1 CG2
REMARK 470 GLU A 291 CG CD OE1 OE2
REMARK 470 VAL A 292 CG1 CG2
REMARK 470 ILE A 293 CG1 CG2 CD1
REMARK 470 GLU A 297 CG CD OE1 OE2
REMARK 470 GLU A 298 CG CD OE1 OE2
REMARK 470 GLU A 300 CG CD OE1 OE2
REMARK 470 LEU A 301 CG CD1 CD2
REMARK 470 GLU A 302 CG CD OE1 OE2
REMARK 470 LYS A 311 CG CD CE NZ
REMARK 470 GLU A 312 CG CD OE1 OE2
REMARK 470 LYS A 323 CG CD CE NZ
REMARK 470 ARG A 356 CG CD NE CZ NH1 NH2
REMARK 470 MET A 357 CG SD CE
REMARK 470 ARG A 358 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 366 CG CD CE NZ
REMARK 470 LYS A 451 CG CD CE NZ
REMARK 470 ILE A 556 CG1 CG2 CD1
REMARK 470 ARG A 557 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 558 CG CD CE NZ
REMARK 470 LYS B 13 CG CD CE NZ
REMARK 470 ASP B 121 CG OD1 OD2
REMARK 470 GLN B 197 CG CD OE1 NE2
REMARK 470 ARG B 199 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 220 CG CD CE NZ
REMARK 470 GLN B 222 CG CD OE1 NE2
REMARK 470 LYS B 223 CG CD CE NZ
REMARK 470 GLU B 224 CG CD OE1 OE2
REMARK 470 PRO B 225 CG CD
REMARK 470 PRO B 226 CG CD
REMARK 470 PHE B 227 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 228 CG CD1 CD2
REMARK 470 TRP B 229 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 229 CZ3 CH2
REMARK 470 MET B 230 CG SD CE
REMARK 470 ILE B 270 CG1 CG2 CD1
REMARK 470 GLN B 278 CG CD OE1 NE2
REMARK 470 LYS B 281 CG CD CE NZ
REMARK 470 MET B 357 CG SD CE
REMARK 470 ARG B 358 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 361 CG ND1 CD2 CE1 NE2
REMARK 470 THR B 362 OG1 CG2
REMARK 470 ASN B 363 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 176 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 LYS A 287 N - CA - C ANGL. DEV. = 18.7 DEGREES
REMARK 500 PRO B 52 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO B 97 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 PRO B 133 C - N - CA ANGL. DEV. = 12.8 DEGREES
REMARK 500 PRO B 345 C - N - CA ANGL. DEV. = 9.4 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 4 27.35 -76.76
REMARK 500 GLU A 6 101.74 -59.12
REMARK 500 GLU A 28 -19.72 -47.43
REMARK 500 PRO A 52 -85.10 -51.95
REMARK 500 ASN A 54 105.70 -165.75
REMARK 500 TYR A 56 118.10 -39.30
REMARK 500 ILE A 63 -168.51 -165.25
REMARK 500 LYS A 65 -67.64 -104.18
REMARK 500 LYS A 66 -160.81 -105.48
REMARK 500 ASP A 67 -2.94 -45.07
REMARK 500 VAL A 75 116.03 -162.09
REMARK 500 PHE A 77 33.04 -98.68
REMARK 500 PHE A 87 -162.77 -107.85
REMARK 500 VAL A 90 -65.96 -29.73
REMARK 500 LEU A 100 171.39 -54.32
REMARK 500 THR A 107 161.27 175.08
REMARK 500 VAL A 111 46.40 -78.02
REMARK 500 ALA A 114 -70.64 -24.08
REMARK 500 SER A 134 -88.05 -70.01
REMARK 500 ILE A 135 -140.54 -104.35
REMARK 500 ASN A 137 -54.24 -139.18
REMARK 500 GLU A 138 93.90 -61.23
REMARK 500 SER A 156 -60.37 -21.40
REMARK 500 GLU A 169 -75.74 -24.60
REMARK 500 ASN A 175 70.30 -115.35
REMARK 500 MET A 184 -141.02 56.92
REMARK 500 ASP A 185 45.93 -94.31
REMARK 500 ASP A 192 58.92 -100.45
REMARK 500 ILE A 195 -62.40 -10.28
REMARK 500 HIS A 221 63.61 63.57
REMARK 500 PRO A 225 -35.17 -36.01
REMARK 500 MET A 230 48.14 39.73
REMARK 500 PRO A 236 -1.17 -48.28
REMARK 500 ASP A 237 -13.75 -143.61
REMARK 500 PRO A 243 95.46 -63.02
REMARK 500 SER A 251 49.97 -73.16
REMARK 500 ILE A 274 133.56 -22.54
REMARK 500 VAL A 276 -1.30 -150.15
REMARK 500 ARG A 284 -17.01 -38.22
REMARK 500 LYS A 287 -35.90 5.76
REMARK 500 PRO A 294 69.51 -60.07
REMARK 500 LEU A 295 101.25 -53.14
REMARK 500 PRO A 345 117.71 -35.24
REMARK 500 ILE A 382 -71.93 -100.51
REMARK 500 TYR A 405 151.95 -40.79
REMARK 500 PRO A 412 -169.15 -65.73
REMARK 500 PRO A 420 -87.05 -58.82
REMARK 500 TRP A 426 -80.95 -71.98
REMARK 500 GLN A 428 104.82 -168.65
REMARK 500 LEU A 429 175.19 -51.13
REMARK 500
REMARK 500 THIS ENTRY HAS 116 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 TBO A 559
DBREF 1UWB A 1 558 UNP P03366 POL_HV1B1 599 1156
DBREF 1UWB B 1 427 UNP P03366 POL_HV1B1 599 1025
SEQADV 1UWB CYS A 181 UNP P03366 TYR 348 ENGINEERED MUTATION
SEQADV 1UWB SER A 280 UNP P03366 CYS 447 ENGINEERED MUTATION
SEQADV 1UWB CYS B 181 UNP P03366 TYR 348 ENGINEERED MUTATION
SEQADV 1UWB SER B 280 UNP P03366 CYS 447 ENGINEERED MUTATION
SEQRES 1 A 558 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 A 558 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 A 558 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 A 558 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 A 558 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 A 558 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 A 558 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 A 558 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS
SEQRES 9 A 558 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 A 558 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 A 558 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 A 558 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 A 558 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 A 558 PRO PHE LYS LYS GLN ASN PRO ASP ILE VAL ILE CYS GLN
SEQRES 15 A 558 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 A 558 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 A 558 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 A 558 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 A 558 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 A 558 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 A 558 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 A 558 ILE LYS VAL ARG GLN LEU SER LYS LEU LEU ARG GLY THR
SEQRES 23 A 558 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 A 558 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 A 558 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 A 558 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 A 558 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 A 558 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 A 558 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 A 558 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 A 558 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 A 558 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 A 558 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU
SEQRES 34 A 558 GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE TYR VAL
SEQRES 35 A 558 ASP GLY ALA ALA ASN ARG GLU THR LYS LEU GLY LYS ALA
SEQRES 36 A 558 GLY TYR VAL THR ASN LYS GLY ARG GLN LYS VAL VAL PRO
SEQRES 37 A 558 LEU THR ASN THR THR ASN GLN LYS THR GLU LEU GLN ALA
SEQRES 38 A 558 ILE TYR LEU ALA LEU GLN ASP SER GLY LEU GLU VAL ASN
SEQRES 39 A 558 ILE VAL THR ASP SER GLN TYR ALA LEU GLY ILE ILE GLN
SEQRES 40 A 558 ALA GLN PRO ASP LYS SER GLU SER GLU LEU VAL ASN GLN
SEQRES 41 A 558 ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS VAL TYR LEU
SEQRES 42 A 558 ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY GLY ASN GLU
SEQRES 43 A 558 GLN VAL ASP LYS LEU VAL SER ALA GLY ILE ARG LYS
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 LYS 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 CYS 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 SER 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 TBO A 559 21
HETNAM TBO 5-CHLORO-8-METHYL-7-(3-METHYL-BUT-2-ENYL)-6,7,8,9-
HETNAM 2 TBO TETRAHYDRO-2H-2,7,9A-TRIAZA-BENZO[CD]AZULENE-1-THIONE
HETSYN TBO TBO 8; TIBO R86183
FORMUL 3 TBO C16 H20 CL N3 S
HELIX 1 AA GLU A 28 GLU A 44 1 17
HELIX 2 AB ARG A 78 ARG A 83 1 6
HELIX 3 AC ALA A 114 SER A 117 1 4
HELIX 4 AD GLU A 122 TYR A 127 1 6
HELIX 5 AE LYS A 154 GLN A 174 1 21
HELIX 6 AF ILE A 195 TRP A 212 1 18
HELIX 7 AH VAL A 254 GLN A 269 1 16
HELIX 8 AI ARG A 277 LEU A 283 1 7
HELIX 9 AJ GLU A 297 LYS A 311 1 15
HELIX 10 AK ASP A 364 TRP A 383 1 20
HELIX 11 AL LYS A 395 GLU A 404 1 10
HELIX 12 A' ASN A 474 ASP A 488 1 15
HELIX 13 B' GLN A 500 ALA A 508 1 9
HELIX 14 D' GLU A 516 LYS A 527 1 12
HELIX 15 E' GLY A 544 ALA A 554 1 11
HELIX 16 BA GLU B 28 GLU B 44 1 17
HELIX 17 BB ARG B 78 VAL B 90 1 13
HELIX 18 BC GLY B 112 SER B 117 1 6
HELIX 19 BD GLU B 122 THR B 128 1 7
HELIX 20 BE LYS B 154 GLN B 174 1 21
HELIX 21 BF ILE B 195 TRP B 212 1 18
HELIX 22 BH VAL B 254 ILE B 270 1 17
HELIX 23 BI ARG B 277 LEU B 283 1 7
HELIX 24 BJ GLU B 297 LYS B 311 1 15
HELIX 25 BK ASP B 364 TRP B 383 1 20
HELIX 26 BL LYS B 395 TYR B 405 1 11
SHEET 1 S1 3 ILE A 47 ILE A 50 0
SHEET 2 S1 3 ILE A 142 TYR A 146 -1
SHEET 3 S1 3 THR A 128 ILE A 132 -1
SHEET 1 S2 2 ASN A 57 LYS A 64 0
SHEET 2 S2 2 ARG A 72 PHE A 77 -1
SHEET 1 S3 3 SER A 105 VAL A 111 0
SHEET 2 S3 3 ASP A 186 SER A 191 -1
SHEET 3 S3 3 ILE A 178 TYR A 183 -1
SHEET 1 S4 4 PHE A 227 TRP A 229 0
SHEET 2 S4 4 TYR A 232 HIS A 235 -1
SHEET 3 S4 4 LYS A 238 VAL A 241 -1
SHEET 4 S4 4 VAL A 314 ASP A 320 -1
SHEET 1 S5 5 LYS A 347 ARG A 356 0
SHEET 2 S5 5 GLN A 336 TYR A 342 -1
SHEET 3 S5 5 LEU A 325 GLN A 332 -1
SHEET 4 S5 5 PRO A 387 LEU A 391 1
SHEET 5 S5 5 GLU A 413 THR A 419 1
SHEET 1 S6 5 GLY A 462 THR A 470 0
SHEET 2 S6 5 LEU A 452 THR A 459 -1
SHEET 3 S6 5 GLU A 438 ASN A 447 -1
SHEET 4 S6 5 GLU A 492 THR A 497 1
SHEET 5 S6 5 LYS A 530 VAL A 536 1
SHEET 1 S7 3 ILE B 47 GLY B 51 0
SHEET 2 S7 3 ILE B 142 TYR B 146 -1
SHEET 3 S7 3 ALA B 129 ILE B 132 -1
SHEET 1 S8 2 TYR B 56 LYS B 64 0
SHEET 2 S8 2 TRP B 71 ASP B 76 -1
SHEET 1 S9 3 SER B 105 ASP B 110 0
SHEET 2 S9 3 ASP B 186 SER B 191 -1
SHEET 3 S9 3 ILE B 178 TYR B 183 -1
SHEET 1 S10 5 LYS B 347 ARG B 356 0
SHEET 2 S10 5 GLN B 336 TYR B 342 -1
SHEET 3 S10 5 LEU B 325 LYS B 331 -1
SHEET 4 S10 5 PRO B 387 LEU B 391 1
SHEET 5 S10 5 GLU B 413 VAL B 417 1
SITE 1 AC1 6 LEU A 100 LYS A 101 LYS A 103 TYR A 188
SITE 2 AC1 6 TRP A 229 TYR A 318
CRYST1 225.700 69.200 104.900 90.00 106.60 90.00 C 1 2 1 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 0.004431 0.000000 0.001321 0.00000
SCALE2 0.000000 0.014451 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009947 0.00000
(ATOM LINES ARE NOT SHOWN.)
END