REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH Y.HSIOU,J.DING,K.DAS,A.D.CLARK JUNIOR,S.H.HUGHES, REMARK 1 AUTH 2 E.ARNOLD REMARK 1 TITL STRUCTURE OF UNLIGANDED HIV-1 REVERSE REMARK 1 TITL 2 TRANSCRIPTASE AT 2.7 A RESOLUTION: IMPLICATIONS OF REMARK 1 TITL 3 CONFORMATIONAL CHANGES FOR POLYMERIZATION AND REMARK 1 TITL 4 INHIBITION MECHANISMS REMARK 1 REF STRUCTURE V. 4 853 1996 REMARK 1 REFN ISSN 0969-2126 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.D.CLARK JUNIOR,A.JACOBO-MOLINA,P.CLARK, REMARK 1 AUTH 2 S.H.HUGHES,E.ARNOLD REMARK 1 TITL CRYSTALLIZATION OF HUMAN IMMUNODEFICIENCY VIRUS REMARK 1 TITL 2 TYPE 1 REVERSE TRANSCRIPTASE WITH AND WITHOUT REMARK 1 TITL 3 NUCLEIC ACID SUBSTRATES, INHIBITORS, AND AN REMARK 1 TITL 4 ANTIBODY FAB FRAGMENT REMARK 1 REF METHODS ENZYMOL. V. 262 171 1995 REMARK 1 REFN ISSN 0076-6879 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.DING,K.DAS,C.TANTILLO,W.ZHANG,A.D.CLARK JUNIOR, REMARK 1 AUTH 2 S.JESSEN,X.LU,Y.HSIOU,A.JACOBO-MOLINA,K.ANDRIES, REMARK 1 AUTH 3 R.PAUWELS,H.MOEREELS,L.KOYMANS,P.A.J.JANSSEN, REMARK 1 AUTH 4 R.H.SMITH JUNIOR,M.K.KOEPKE,C.J.MICHEJDA, REMARK 1 AUTH 5 S.H.HUGHES,E.ARNOLD REMARK 1 TITL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN A REMARK 1 TITL 2 COMPLEX WITH THE NON-NUCLEOSIDE INHIBITOR REMARK 1 TITL 3 ALPHA-APA R 95845 AT 2.8 A RESOLUTION REMARK 1 REF STRUCTURE V. 3 365 1995 REMARK 1 REFN ISSN 0969-2126 REMARK 1 REFERENCE 4 REMARK 1 AUTH J.DING,K.DAS,H.MOEREELS,L.KOYMANS,K.ANDRIES, REMARK 1 AUTH 2 P.A.JANSSEN,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 5 REMARK 1 AUTH A.JACOBO-MOLINA,J.DING,R.G.NANNI,A.D.CLARK JUNIOR, REMARK 1 AUTH 2 X.LU,C.TANTILLO,R.L.WILLIAMS,G.KAMER,A.L.FERRIS, REMARK 1 AUTH 3 P.CLARK,A.HIZI,S.H.HUGHES,E.ARNOLD REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN IMMUNODEFICIENCY VIRUS REMARK 1 TITL 2 TYPE 1 REVERSE TRANSCRIPTASE COMPLEXED WITH REMARK 1 TITL 3 DOUBLE-STRANDED DNA AT 3.0 A RESOLUTION SHOWS BENT REMARK 1 TITL 4 DNA REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 90 6320 1993 REMARK 1 REFN ISSN 0027-8424 REMARK 1 REFERENCE 6 REMARK 1 AUTH E.ARNOLD,A.JACOBO-MOLINA,R.G.NANNI,R.L.WILLIAMS, REMARK 1 AUTH 2 X.LU,J.DING,A.D.CLARK JUNIOR,A.ZHANG,A.L.FERRIS, REMARK 1 AUTH 3 P.CLARK,A.HIZI,S.H.HUGHES REMARK 1 TITL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE/DNA REMARK 1 TITL 2 COMPLEX AT 7 A RESOLUTION SHOWING ACTIVE SITE REMARK 1 TITL 3 LOCATIONS REMARK 1 REF NATURE V. 357 85 1992 REMARK 1 REFN ISSN 0028-0836 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 125.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 74.8 REMARK 3 NUMBER OF REFLECTIONS : 63413 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) : 0.271 REMARK 3 FREE R VALUE : 0.352 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 3203 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006 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) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 40.90 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3266 REMARK 3 BIN R VALUE (WORKING SET) : 0.3920 REMARK 3 BIN FREE R VALUE : 0.4350 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.60 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 194 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.031 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10894 REMARK 3 NUCLEIC ACID ATOMS : 753 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 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) : 0.47 REMARK 3 ESD FROM SIGMAA (A) : 0.88 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) : 0.57 REMARK 3 ESD FROM C-V SIGMAA (A) : 1.24 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.012 REMARK 3 BOND ANGLES (DEGREES) : 0.90 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.90 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.73 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) : 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 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 : RNA-DNA.PARAM REMARK 3 PARAMETER FILE 3 : ADD_PROLINE.PRO REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : RNA-DNA.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 2HMI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 1992 REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 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) : NULL 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 : 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 : 4.300 REMARK 200 R MERGE (I) : 0.13000 REMARK 200 R SYM (I) : NULL REMARK 200 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 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: INTENSITY-INTEGRATION SOFTWARE USED WAS A MODIFIED REMARK 200 VERSION OF THE PURDUE OSCILLATION FILM PROCESSING PACKAGE AND REMARK 200 DENZO REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 75.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 1 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -Y,-X,-Z+1/3 REMARK 290 5555 -X+Y,Y,-Z+2/3 REMARK 290 6555 X,X-Y,-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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 147.33333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 73.66667 REMARK 290 SMTRY1 4 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 73.66667 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 147.33333 REMARK 290 SMTRY1 6 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 400 REMARK 400 COMPOUND REMARK 400 REMARK 400 HIV-1 RT IS COMPOSED OF TWO SUBUNITS OF 66 KDA AND 51 KDA, REMARK 400 DESIGNATED AS P66 (CHAIN A) AND P51 (CHAIN B), REMARK 400 RESPECTIVELY. IN THIS STRUCTURE, 558 AMINO ACID RESIDUES REMARK 400 WERE TRACED FOR THE P66 SUBUNIT AND 430 AMINO ACID RESIDUES REMARK 400 WERE LOCATED IN THE P51 SUBUNIT. REMARK 400 REMARK 400 THE POLYMERASE DOMAINS OF BOTH P66 AND P51 ARE COMPRISED REMARK 400 OF FOUR SUBDOMAINS, NAMED FINGERS, PALM, THUMB, AND REMARK 400 CONNECTION. THE BOUNDARIES OF INDIVIDUAL SUBDOMAINS ARE REMARK 400 AS FOLLOWING: REMARK 400 FINGERS: 1 - 84 AND 120 - 150 REMARK 400 PALM: 85 - 119 AND 151 - 243 REMARK 400 THUMB: 244 - 322 REMARK 400 CONNECTION: 323 - 437 IN P66 AND 327 - 430 IN P51. 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 LYS A 13 CG CD CE NZ REMARK 470 GLU A 28 CG CD OE1 OE2 REMARK 470 GLU A 29 CG CD OE1 OE2 REMARK 470 LYS A 30 CG CD CE NZ REMARK 470 LYS A 32 CG CD CE NZ REMARK 470 GLU A 36 CG CD OE1 OE2 REMARK 470 GLU A 40 CG CD OE1 OE2 REMARK 470 LYS A 43 CG CD CE NZ REMARK 470 GLU A 44 CG CD OE1 OE2 REMARK 470 PHE A 61 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 64 CG CD CE NZ REMARK 470 LYS A 65 CG CD CE NZ REMARK 470 LYS A 66 CG CD CE NZ REMARK 470 ASP A 67 CG OD1 OD2 REMARK 470 SER A 68 OG REMARK 470 THR A 69 OG1 CG2 REMARK 470 LYS A 70 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 LYS A 73 CG CD CE NZ REMARK 470 LEU A 74 CG CD1 CD2 REMARK 470 ARG A 78 CG CD NE CZ NH1 NH2 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 GLU A 194 CG CD OE1 OE2 REMARK 470 ARG A 199 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 203 CG CD OE1 OE2 REMARK 470 ARG A 211 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 222 CG CD OE1 NE2 REMARK 470 LYS A 223 CG CD CE NZ REMARK 470 LYS A 238 CG CD CE NZ REMARK 470 GLN A 242 CG CD OE1 NE2 REMARK 470 ILE A 244 CG1 CG2 CD1 REMARK 470 VAL A 245 CG1 CG2 REMARK 470 LEU A 246 CG CD1 CD2 REMARK 470 PRO A 247 CG CD REMARK 470 GLU A 248 CG CD OE1 OE2 REMARK 470 LYS A 249 CG CD CE NZ REMARK 470 ASP A 250 CG OD1 OD2 REMARK 470 SER A 251 OG REMARK 470 TRP A 252 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 252 CZ3 CH2 REMARK 470 THR A 253 OG1 CG2 REMARK 470 LYS A 275 CG CD CE NZ REMARK 470 GLN A 278 CG CD OE1 NE2 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 PRO A 294 CG CD REMARK 470 LEU A 295 CG CD1 CD2 REMARK 470 THR A 296 OG1 CG2 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 LEU A 303 CG CD1 CD2 REMARK 470 GLU A 305 CG CD OE1 OE2 REMARK 470 ASN A 306 CG OD1 ND2 REMARK 470 ARG A 307 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 308 CG CD OE1 OE2 REMARK 470 ILE A 309 CG1 CG2 CD1 REMARK 470 LEU A 310 CG CD1 CD2 REMARK 470 LYS A 311 CG CD CE NZ REMARK 470 GLU A 312 CG CD OE1 OE2 REMARK 470 LYS A 331 CG CD CE NZ REMARK 470 ARG A 448 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 449 CG CD OE1 OE2 REMARK 470 GLN A 524 CG CD OE1 NE2 REMARK 470 LYS A 530 CG CD CE NZ REMARK 470 LYS A 540 CG CD CE NZ REMARK 470 GLU A 546 CG CD OE1 OE2 REMARK 470 GLN A 547 CG CD OE1 NE2 REMARK 470 LYS A 550 CG CD CE NZ 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 VAL B 90 CG1 CG2 REMARK 470 GLN B 91 CG CD OE1 NE2 REMARK 470 LYS B 173 CG CD CE NZ REMARK 470 THR B 240 OG1 CG2 REMARK 470 VAL B 241 CG1 CG2 REMARK 470 GLN B 242 CG CD OE1 NE2 REMARK 470 PRO B 243 CG CD REMARK 470 ILE B 244 CG1 CG2 CD1 REMARK 470 VAL B 245 CG1 CG2 REMARK 470 LEU B 246 CG CD1 CD2 REMARK 470 PRO B 247 CG CD REMARK 470 GLU B 248 CG CD OE1 OE2 REMARK 470 LYS B 249 CG CD CE NZ REMARK 470 ASP B 250 CG OD1 OD2 REMARK 470 SER B 251 OG REMARK 470 TRP B 252 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 252 CZ3 CH2 REMARK 470 SER B 268 OG REMARK 470 LYS B 275 CG CD CE NZ REMARK 470 VAL B 276 CG1 CG2 REMARK 470 ARG B 277 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 278 CG CD OE1 NE2 REMARK 470 LYS B 281 CG CD CE NZ REMARK 470 LEU B 282 CG CD1 CD2 REMARK 470 ARG B 284 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 291 CG CD OE1 OE2 REMARK 470 VAL B 292 CG1 CG2 REMARK 470 ILE B 293 CG1 CG2 CD1 REMARK 470 GLU B 297 CG CD OE1 OE2 REMARK 470 GLU B 298 CG CD OE1 OE2 REMARK 470 GLU B 300 CG CD OE1 OE2 REMARK 470 GLU B 305 CG CD OE1 OE2 REMARK 470 GLU B 308 CG CD OE1 OE2 REMARK 470 ILE B 309 CG1 CG2 CD1 REMARK 470 LEU B 310 CG CD1 CD2 REMARK 470 LYS B 311 CG CD CE NZ REMARK 470 GLU B 312 CG CD OE1 OE2 REMARK 470 PRO B 313 CG CD REMARK 470 VAL B 314 CG1 CG2 REMARK 470 HIS B 315 CG ND1 CD2 CE1 NE2 REMARK 470 LYS B 424 CG CD CE NZ REMARK 470 GLN B 428 CG CD OE1 NE2 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 243 N - CA - CB ANGL. DEV. = 7.3 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 94.90 -52.96 REMARK 500 GLU A 44 -70.19 -74.12 REMARK 500 GLU A 53 -14.76 -141.73 REMARK 500 ILE A 63 77.67 -176.58 REMARK 500 LYS A 64 44.94 -79.71 REMARK 500 LYS A 73 50.94 -166.54 REMARK 500 ASP A 76 74.62 -100.61 REMARK 500 PHE A 77 14.74 -61.50 REMARK 500 LYS A 82 5.44 -61.68 REMARK 500 ARG A 83 -34.90 -132.05 REMARK 500 GLN A 85 168.63 -40.70 REMARK 500 PHE A 87 -153.71 -128.90 REMARK 500 GLU A 89 -17.00 -39.78 REMARK 500 ASP A 121 107.90 -45.80 REMARK 500 LYS A 126 -18.47 -48.07 REMARK 500 ALA A 129 136.30 -28.80 REMARK 500 PRO A 133 144.70 -37.56 REMARK 500 ASN A 136 -28.32 -27.73 REMARK 500 VAL A 148 -167.35 -118.53 REMARK 500 PRO A 157 -74.70 -39.47 REMARK 500 ASN A 175 72.21 -164.73 REMARK 500 MET A 184 -106.86 54.27 REMARK 500 SER A 191 133.55 -175.06 REMARK 500 ASP A 192 79.97 -69.45 REMARK 500 ILE A 195 -38.74 -38.24 REMARK 500 THR A 215 -167.70 -59.51 REMARK 500 THR A 216 70.25 -160.07 REMARK 500 PRO A 217 152.95 -41.96 REMARK 500 ASP A 218 1.16 -68.94 REMARK 500 LYS A 223 109.07 -48.39 REMARK 500 ASP A 237 6.05 -159.80 REMARK 500 VAL A 241 71.49 -151.30 REMARK 500 PRO A 243 44.94 -68.80 REMARK 500 ILE A 244 46.48 -92.19 REMARK 500 SER A 251 26.39 -57.98 REMARK 500 PRO A 272 -175.96 -44.39 REMARK 500 LYS A 287 -42.01 -132.70 REMARK 500 ALA A 288 95.54 -66.13 REMARK 500 THR A 290 -67.13 -170.23 REMARK 500 GLU A 291 175.69 -53.89 REMARK 500 LEU A 295 -18.07 -44.34 REMARK 500 GLU A 302 -72.78 -69.08 REMARK 500 GLN A 332 -85.20 -107.05 REMARK 500 GLN A 334 67.51 -66.59 REMARK 500 PRO A 345 -90.00 4.63 REMARK 500 LYS A 347 87.31 -68.73 REMARK 500 LEU A 349 -77.83 -96.25 REMARK 500 ALA A 355 67.13 -162.05 REMARK 500 VAL A 381 -62.85 -100.09 REMARK 500 TYR A 405 100.14 -48.99 REMARK 500 PRO A 412 -178.46 -65.72 REMARK 500 GLU A 413 108.43 -49.68 REMARK 500 THR A 419 -71.13 -167.29 REMARK 500 PRO A 421 86.43 -51.24 REMARK 500 LEU A 422 115.17 -39.10 REMARK 500 TRP A 426 -87.85 -75.88 REMARK 500 ALA A 445 157.51 175.70 REMARK 500 TYR A 457 -179.20 -171.93 REMARK 500 ASN A 471 17.62 83.99 REMARK 500 ASN A 494 78.63 -109.85 REMARK 500 GLN A 509 47.93 78.54 REMARK 500 SER A 513 148.63 -179.18 REMARK 500 SER B 3 152.11 -43.77 REMARK 500 LYS B 20 43.90 -152.04 REMARK 500 LEU B 34 -16.97 -49.32 REMARK 500 VAL B 35 -74.03 -88.91 REMARK 500 ASN B 57 144.89 -172.45 REMARK 500 THR B 69 -96.97 -62.76 REMARK 500 LYS B 70 -166.73 -170.18 REMARK 500 ASP B 76 102.85 -57.54 REMARK 500 GLU B 79 -70.42 -61.50 REMARK 500 LEU B 80 -36.53 -39.04 REMARK 500 GLN B 85 174.78 -56.32 REMARK 500 ASN B 136 7.48 54.55 REMARK 500 PRO B 140 -157.58 -75.66 REMARK 500 LYS B 154 -36.93 -34.38 REMARK 500 GLN B 161 -67.20 -28.05 REMARK 500 ASN B 175 76.82 -119.50 REMARK 500 MET B 184 -93.70 52.85 REMARK 500 LEU B 214 46.20 25.48 REMARK 500 GLU B 224 -81.84 -99.08 REMARK 500 PRO B 225 -107.08 -11.39 REMARK 500 PHE B 227 71.12 -58.05 REMARK 500 THR B 240 102.21 -34.92 REMARK 500 PRO B 243 41.85 174.06 REMARK 500 LYS B 249 -170.06 -172.25 REMARK 500 ASP B 250 -95.42 -109.89 REMARK 500 LYS B 263 -73.89 -54.89 REMARK 500 LEU B 283 76.18 -119.20 REMARK 500 THR B 286 48.06 -70.93 REMARK 500 THR B 290 -101.13 -84.76 REMARK 500 GLU B 291 -33.17 -38.59 REMARK 500 PRO B 294 67.31 -67.17 REMARK 500 LEU B 310 40.25 -87.09 REMARK 500 PRO B 313 131.76 -34.46 REMARK 500 PRO B 321 2.26 -55.36 REMARK 500 PHE B 346 -2.80 69.25 REMARK 500 ALA B 355 -147.19 -80.02 REMARK 500 ALA B 360 -1.06 -53.69 REMARK 500 ASN B 363 111.98 -166.58 REMARK 500 ILE B 382 -99.73 -94.31 REMARK 500 GLU B 399 1.50 -65.75 REMARK 500 TRP B 401 -19.45 -148.37 REMARK 500 GLU B 404 20.34 -68.49 REMARK 500 TYR B 405 -23.66 -148.58 REMARK 500 GLN B 407 -18.11 -147.67 REMARK 500 LYS B 424 6.81 -69.71 REMARK 500 LEU B 425 0.26 -69.38 REMARK 500 TRP B 426 -2.17 81.95 REMARK 500 LEU B 429 105.09 -25.64 REMARK 500 THR C 7 -74.07 -42.48 REMARK 500 GLN C 27 140.76 -172.41 REMARK 500 ASP C 28 109.83 -30.78 REMARK 500 THR C 51 17.14 50.76 REMARK 500 SER C 52 -48.43 -153.79 REMARK 500 ALA C 61 -28.45 -36.24 REMARK 500 SER C 76 -81.30 -51.31 REMARK 500 PRO C 80 -19.19 -43.05 REMARK 500 ALA C 84 -155.50 -153.10 REMARK 500 TYR C 91 49.73 -151.63 REMARK 500 SER C 92 -76.14 -93.33 REMARK 500 PRO C 95 86.21 -63.78 REMARK 500 ASP C 110 156.84 -36.25 REMARK 500 LEU C 125 -38.97 -38.76 REMARK 500 ASN C 138 99.10 42.43 REMARK 500 ASP C 143 88.73 -38.18 REMARK 500 ASP C 151 107.69 -31.65 REMARK 500 ALA C 156 126.45 -32.42 REMARK 500 SER C 168 16.53 -58.08 REMARK 500 ALA C 189 -174.21 -63.92 REMARK 500 ASN C 190 -75.25 -127.65 REMARK 500 LYS C 199 19.26 -58.42 REMARK 500 THR C 200 -77.49 -55.00 REMARK 500 SER C 201 37.70 -156.65 REMARK 500 ALA C 211 87.48 179.48 REMARK 500 ASN C 212 47.05 -81.80 REMARK 500 SER D 15 -18.78 83.65 REMARK 500 PHE D 27 -151.84 -104.96 REMARK 500 LEU D 29 32.14 -82.58 REMARK 500 SER D 32 -47.15 -18.22 REMARK 500 SER D 43 106.36 -58.59 REMARK 500 LEU D 50 -67.30 -92.64 REMARK 500 ASP D 57 -4.55 77.24 REMARK 500 LYS D 66 -34.36 -33.05 REMARK 500 LYS D 73 103.30 -171.44 REMARK 500 THR D 86 76.19 45.28 REMARK 500 THR D 89 -74.22 -18.39 REMARK 500 ILE D 102 80.06 -68.24 REMARK 500 VAL D 105 -25.11 -38.92 REMARK 500 SER D 108 91.58 -160.51 REMARK 500 TRP D 113 -146.12 -115.12 REMARK 500 GLN D 115 122.62 -39.24 REMARK 500 LEU D 134 70.88 -106.00 REMARK 500 SER D 138 -56.47 -18.30 REMARK 500 THR D 142 -67.44 -103.92 REMARK 500 PHE D 156 -60.79 -102.52 REMARK 500 GLU D 158 -38.08 -29.56 REMARK 500 SER D 170 -31.04 -161.91 REMARK 500 LEU D 180 76.84 -63.23 REMARK 500 ASP D 183 -1.22 70.67 REMARK 500 SER D 195 -98.40 15.00 REMARK 500 SER D 196 -52.84 -22.70 REMARK 500 THR D 197 -79.66 -43.58 REMARK 500 SER D 200 -71.05 -86.32 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 DA E 801 0.07 SIDE_CHAIN REMARK 500 TYR A 188 0.06 SIDE_CHAIN REMARK 500 TYR B 188 0.07 SIDE_CHAIN REMARK 500 TYR C 87 0.08 SIDE_CHAIN REMARK 500 TYR C 91 0.07 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 REMARK 999 THE BOUND DOUBLE-STRANDED DNA IS A 19-MER/18-MER TEMPLATE- REMARK 999 PRIMER. BOTH THE TEMPLATE STRAND AND THE PRIMER STRAND ARE REMARK 999 REMARK 999 NUMBERED IN THE 5'-3' DIRECTION. THE FIRST NUCLEOTIDE AT REMARK 999 REMARK 999 REMARK 999 THE 5'-TERMINUS OF THE TEMPLATE STRAND (ADE) FORMS A REMARK 999 REMARK 999 ONE-BASE OVERHANG. THE DNA OLIGOMERS WERE NOT REMARK 999 REMARK 999 PHOSPHORYLATED AT THE 5'-TERMINUS, SO E801 AND F821 DO NOT REMARK 999 REMARK 999 HAVE PHOSPHORUS ATOM POSITIONS. REMARK 999 REMARK 999 THE FOLLOWING REGIONS ARE HIGHLY DISORDERED WITH VERY POOR REMARK 999 ELECTRON DENSITY; THE BACKBONE TRACE IN THESE REGIONS IS REMARK 999 TENTATIVE. REMARK 999 P66: 64-74, 136-138, 242-253, 286-293, AND 554-558. REMARK 999 P51: 242-252.