REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.843 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 74.1 REMARK 3 NUMBER OF REFLECTIONS : 49518 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) : 0.274 REMARK 3 FREE R VALUE : 0.316 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1053 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 : 11206 REMARK 3 NUCLEIC ACID ATOMS : 933 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL 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) : 0.012 REMARK 3 BOND ANGLES (DEGREES) : 1.72 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 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: NULL REMARK 4 REMARK 4 1HYS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-01. REMARK 100 THE RCSB ID CODE IS RCSB012694. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-MAR-96 REMARK 200 TEMPERATURE (KELVIN) : 115 REMARK 200 PH : 5.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X25 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0909 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL 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 : 56482 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 82.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.15000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.2000 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) : 3.13 REMARK 200 COMPLETENESS FOR SHELL (%) : 65.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.35600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: 2HMI REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, CACODYLATE, PH REMARK 280 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K 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 145.87333 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 72.93667 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 72.93667 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 145.87333 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 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 73 CG CD CE NZ REMARK 470 GLU A 302 CG CD OE1 OE2 REMARK 470 ARG A 356 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 358 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 394 CG CD OE1 NE2 REMARK 470 LYS A 424 CG CD CE NZ REMARK 470 GLU A 449 CG CD OE1 OE2 REMARK 470 GLU A 514 CG CD OE1 OE2 REMARK 470 GLN A 524 CG CD OE1 NE2 REMARK 470 LEU B 92 CG CD1 CD2 REMARK 470 LEU B 246 CG CD1 CD2 REMARK 470 GLU B 305 CG CD OE1 OE2 REMARK 470 GLU B 312 CG CD OE1 OE2 REMARK 470 MET B 357 CG SD CE REMARK 470 ARG B 358 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 GLU A 6 CG CD OE1 OE2 REMARK 480 LYS A 22 CG CD CE NZ REMARK 480 TRP A 24 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 480 TRP A 24 CZ3 CH2 REMARK 480 LYS A 30 CG CD CE NZ REMARK 480 LYS A 32 CG CD CE NZ REMARK 480 LYS A 43 CG CD CE NZ REMARK 480 GLU A 44 CG CD OE1 OE2 REMARK 480 SER A 68 OG REMARK 480 TRP A 71 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 480 TRP A 71 CZ3 CH2 REMARK 480 LYS A 104 CG CD CE NZ REMARK 480 ASN A 137 CG OD1 ND2 REMARK 480 GLU A 138 CG CD OE1 OE2 REMARK 480 GLN A 161 CG CD OE1 NE2 REMARK 480 ASP A 177 CG OD1 OD2 REMARK 480 ASP A 192 CG OD1 OD2 REMARK 480 GLN A 197 CG CD OE1 NE2 REMARK 480 GLN A 207 CG CD OE1 NE2 REMARK 480 ARG A 211 CG CD NE CZ NH1 NH2 REMARK 480 LYS A 219 CG CD CE NZ REMARK 480 LYS A 223 CG CD CE NZ REMARK 480 GLU A 224 CG CD OE1 OE2 REMARK 480 GLU A 233 CG CD OE1 OE2 REMARK 480 HIS A 235 CG ND1 CD2 CE1 NE2 REMARK 480 LYS A 238 CG CD CE NZ REMARK 480 VAL A 245 CG1 CG2 REMARK 480 GLU A 248 CG CD OE1 OE2 REMARK 480 LYS A 249 CG CD CE NZ REMARK 480 TRP A 252 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 480 TRP A 252 CZ3 CH2 REMARK 480 VAL A 254 CG1 CG2 REMARK 480 ILE A 257 CG1 CG2 CD1 REMARK 480 GLN A 269 CG CD OE1 NE2 REMARK 480 VAL A 276 CG1 CG2 REMARK 480 GLN A 278 CG CD OE1 NE2 REMARK 480 ARG A 284 CG CD NE CZ NH1 NH2 REMARK 480 THR A 286 OG1 CG2 REMARK 480 LYS A 287 CG CD CE NZ REMARK 480 THR A 290 OG1 CG2 REMARK 480 LEU A 295 CG CD1 CD2 REMARK 480 THR A 296 OG1 CG2 REMARK 480 GLU A 297 CG CD OE1 OE2 REMARK 480 GLU A 298 CG CD OE1 OE2 REMARK 480 LEU A 301 CG CD1 CD2 REMARK 480 GLU A 305 CG CD OE1 OE2 REMARK 480 GLU A 308 CG CD OE1 OE2 REMARK 480 GLU A 312 CG CD OE1 OE2 REMARK 480 ILE A 326 CG1 CG2 CD1 REMARK 480 TYR A 342 CG CD1 CD2 CE1 CE2 CZ OH REMARK 480 PHE A 346 CG CD1 CD2 CE1 CE2 CZ REMARK 480 GLU A 396 CG CD OE1 OE2 REMARK 480 GLU A 399 CG CD OE1 OE2 REMARK 480 GLU A 404 CG CD OE1 OE2 REMARK 480 TRP A 406 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 480 TRP A 406 CZ3 CH2 REMARK 480 GLU A 430 CG CD OE1 OE2 REMARK 480 LYS A 451 CG CD CE NZ REMARK 480 LEU A 452 CG CD1 CD2 REMARK 480 ASN A 471 CG OD1 ND2 REMARK 480 GLN A 487 CG CD OE1 NE2 REMARK 480 LYS A 528 CG CD CE NZ REMARK 480 GLU A 546 CG CD OE1 OE2 REMARK 480 ASP A 549 CG OD1 OD2 REMARK 480 LYS A 550 CG CD CE NZ REMARK 480 LYS B 11 CG CD CE NZ REMARK 480 LYS B 13 CG CD CE NZ REMARK 480 GLU B 29 CG CD OE1 OE2 REMARK 480 LYS B 32 CG CD CE NZ REMARK 480 SER B 68 OG REMARK 480 THR B 69 OG1 CG2 REMARK 480 LYS B 70 CG CD CE NZ REMARK 480 TRP B 88 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 480 TRP B 88 CZ3 CH2 REMARK 480 GLU B 89 CG CD OE1 OE2 REMARK 480 GLN B 91 CG CD OE1 NE2 REMARK 480 LEU B 214 CG CD1 CD2 REMARK 480 LYS B 249 CG CD CE NZ REMARK 480 ARG B 277 CG CD NE CZ NH1 NH2 REMARK 480 SER B 280 OG REMARK 480 THR B 290 OG1 CG2 REMARK 480 GLU B 291 CG CD OE1 OE2 REMARK 480 VAL B 292 CG1 CG2 REMARK 480 GLU B 297 CG CD OE1 OE2 REMARK 480 TYR B 318 CG CD1 CD2 CE1 CE2 CZ OH REMARK 480 LYS B 323 CG CD CE NZ REMARK 480 THR D 142 OG1 CG2 REMARK 480 ASN D 143 CG OD1 ND2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 U E 854 C5 U E 854 C6 0.063 REMARK 500 ARG B 211 CZ ARG B 211 NH1 0.297 REMARK 500 REMARK 500 REMARK: NULL 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 U E 854 O4' - C4' - C3' ANGL. DEV. = -6.2 DEGREES REMARK 500 U E 854 N1 - C1' - C2' ANGL. DEV. = 11.3 DEGREES REMARK 500 A E 860 O3' - P - O5' ANGL. DEV. = -12.2 DEGREES REMARK 500 U E 864 O3' - P - O5' ANGL. DEV. = 12.0 DEGREES REMARK 500 DA F 888 O3' - P - O5' ANGL. DEV. = 12.0 DEGREES REMARK 500 DA F 892 N9 - C1' - C2' ANGL. DEV. = 14.1 DEGREES REMARK 500 ARG A 72 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES REMARK 500 PRO A 421 N - CA - C ANGL. DEV. = -16.0 DEGREES REMARK 500 ARG B 211 CD - NE - CZ ANGL. DEV. = 9.8 DEGREES REMARK 500 ARG B 211 NH1 - CZ - NH2 ANGL. DEV. = -16.6 DEGREES REMARK 500 ARG B 211 NE - CZ - NH1 ANGL. DEV. = -14.2 DEGREES REMARK 500 ARG B 211 NE - CZ - NH2 ANGL. DEV. = 17.1 DEGREES REMARK 500 MET B 230 CG - SD - CE ANGL. DEV. = 9.6 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 MET A 16 -142.29 -146.72 REMARK 500 ASP A 17 -174.20 -176.85 REMARK 500 GLU A 44 28.14 -79.38 REMARK 500 PRO A 52 64.20 -64.26 REMARK 500 GLU A 53 -13.53 -154.59 REMARK 500 ILE A 63 100.85 -179.11 REMARK 500 SER A 68 -11.25 -49.73 REMARK 500 THR A 69 -75.15 -102.98 REMARK 500 LYS A 70 70.58 -102.46 REMARK 500 GLN A 85 144.67 -28.85 REMARK 500 VAL A 90 86.04 47.57 REMARK 500 ALA A 114 -71.94 -54.77 REMARK 500 ASP A 121 103.44 -45.55 REMARK 500 ARG A 125 -40.61 -25.38 REMARK 500 LYS A 126 15.07 -58.87 REMARK 500 ALA A 129 98.59 -56.43 REMARK 500 VAL A 148 -162.80 -105.95 REMARK 500 ALA A 158 -75.94 -76.78 REMARK 500 SER A 162 -35.58 -38.67 REMARK 500 ASN A 175 58.81 -173.82 REMARK 500 PRO A 176 2.86 -44.57 REMARK 500 MET A 184 -100.49 60.78 REMARK 500 ASP A 192 4.12 -69.34 REMARK 500 PRO A 217 -167.50 -79.52 REMARK 500 LEU A 228 53.91 -63.32 REMARK 500 PRO A 236 -38.34 -37.09 REMARK 500 ASP A 237 24.59 -144.33 REMARK 500 VAL A 241 79.44 -156.86 REMARK 500 PRO A 243 81.24 -64.87 REMARK 500 VAL A 245 93.96 -19.88 REMARK 500 GLU A 248 -90.73 -30.14 REMARK 500 ASP A 250 3.86 -52.44 REMARK 500 SER A 251 13.95 -64.95 REMARK 500 VAL A 276 -7.91 -142.97 REMARK 500 ARG A 277 -37.52 -39.27 REMARK 500 ARG A 284 -69.28 -29.24 REMARK 500 LYS A 287 0.21 -155.57 REMARK 500 THR A 290 3.50 92.69 REMARK 500 LEU A 295 119.61 -14.77 REMARK 500 SER A 322 -58.20 -167.40 REMARK 500 GLN A 332 -1.10 -150.84 REMARK 500 PRO A 345 -89.93 -13.07 REMARK 500 LEU A 349 -84.92 -97.85 REMARK 500 HIS A 361 58.89 -112.27 REMARK 500 LEU A 368 -70.24 -83.44 REMARK 500 PRO A 392 33.23 -75.19 REMARK 500 TRP A 401 -70.09 -58.75 REMARK 500 TRP A 410 -177.19 -170.76 REMARK 500 PRO A 412 -163.53 -71.15 REMARK 500 GLU A 413 99.82 -39.69 REMARK 500 ASN A 418 52.87 -149.06 REMARK 500 LEU A 422 132.84 -24.17 REMARK 500 TRP A 426 -85.16 -63.33 REMARK 500 THR A 439 50.98 -97.22 REMARK 500 PHE A 440 91.64 -40.51 REMARK 500 VAL A 466 149.49 -173.52 REMARK 500 GLN A 487 -71.48 -71.10 REMARK 500 ASP A 488 75.40 -69.13 REMARK 500 SER A 489 151.18 172.90 REMARK 500 HIS A 539 52.00 -102.76 REMARK 500 LYS A 540 -30.31 -130.46 REMARK 500 LEU A 551 -70.69 -71.47 REMARK 500 ILE B 2 -58.52 -154.14 REMARK 500 PRO B 4 10.74 -69.01 REMARK 500 LYS B 20 57.82 -145.65 REMARK 500 GLU B 28 -72.09 -35.38 REMARK 500 GLU B 36 -74.59 -50.33 REMARK 500 GLU B 53 -18.40 -39.94 REMARK 500 LYS B 66 63.12 -69.38 REMARK 500 SER B 68 9.25 -56.88 REMARK 500 THR B 69 -94.98 -91.28 REMARK 500 TRP B 71 -167.97 -72.68 REMARK 500 PHE B 77 21.99 -74.83 REMARK 500 GLU B 79 -73.86 -68.19 REMARK 500 GLN B 85 -178.35 -66.59 REMARK 500 GLN B 91 -85.44 -94.49 REMARK 500 PRO B 95 175.87 -59.59 REMARK 500 ASP B 110 69.22 -65.90 REMARK 500 VAL B 111 48.67 -73.41 REMARK 500 ASP B 113 -11.77 -41.78 REMARK 500 SER B 117 0.22 -65.01 REMARK 500 ARG B 125 -18.25 -43.75 REMARK 500 PRO B 133 -160.04 -74.79 REMARK 500 SER B 134 128.94 -175.00 REMARK 500 GLU B 138 -98.00 -56.39 REMARK 500 LYS B 154 -16.30 -38.49 REMARK 500 ASN B 175 49.68 -156.98 REMARK 500 MET B 184 -125.34 64.08 REMARK 500 ARG B 199 -17.41 -49.09 REMARK 500 ARG B 206 14.08 -69.23 REMARK 500 ARG B 211 -4.85 -57.22 REMARK 500 LEU B 214 48.79 23.17 REMARK 500 GLU B 224 -90.03 -111.49 REMARK 500 PRO B 225 -110.54 -8.83 REMARK 500 PHE B 227 79.62 -32.29 REMARK 500 THR B 240 -155.45 -99.62 REMARK 500 VAL B 241 -142.59 -135.05 REMARK 500 GLN B 242 37.24 -158.18 REMARK 500 VAL B 245 -73.41 -23.81 REMARK 500 LEU B 246 106.58 -30.71 REMARK 500 GLU B 248 105.10 -163.55 REMARK 500 TRP B 252 99.96 -59.56 REMARK 500 PRO B 272 -100.66 -57.45 REMARK 500 VAL B 276 59.71 -117.71 REMARK 500 LEU B 283 46.66 -103.52 REMARK 500 THR B 286 36.84 -67.41 REMARK 500 LEU B 289 -88.17 -48.97 REMARK 500 THR B 290 -8.70 -41.89 REMARK 500 GLU B 291 -50.34 -130.74 REMARK 500 THR B 296 108.71 -8.35 REMARK 500 PRO B 313 88.26 -64.48 REMARK 500 VAL B 314 135.60 -36.86 REMARK 500 TYR B 318 139.18 178.66 REMARK 500 SER B 322 -74.68 -56.63 REMARK 500 ASP B 324 -163.68 -68.68 REMARK 500 LYS B 331 91.66 -67.37 REMARK 500 GLN B 332 76.77 -101.74 REMARK 500 GLN B 343 -77.78 -110.04 REMARK 500 PRO B 345 158.20 -40.08 REMARK 500 LYS B 347 48.51 -148.81 REMARK 500 LYS B 350 132.50 -179.55 REMARK 500 ASN B 363 115.54 -171.02 REMARK 500 PRO B 392 70.07 -61.15 REMARK 500 THR B 397 -76.14 -69.99 REMARK 500 TRP B 398 -24.48 -37.91 REMARK 500 TYR B 405 33.41 -141.65 REMARK 500 PRO B 420 -179.21 -50.88 REMARK 500 VAL B 423 21.83 -65.68 REMARK 500 ASP C 17 170.35 -49.27 REMARK 500 SER C 30 50.85 35.50 REMARK 500 SER C 31 18.63 59.60 REMARK 500 TYR C 50 20.41 84.99 REMARK 500 SER C 52 -30.96 -164.18 REMARK 500 SER C 65 140.59 179.89 REMARK 500 SER C 67 114.87 -170.72 REMARK 500 SER C 76 -83.23 -53.57 REMARK 500 ASP C 82 -9.16 -47.94 REMARK 500 SER C 92 -75.04 -77.28 REMARK 500 PRO C 95 79.91 -58.31 REMARK 500 ALA C 111 115.29 -160.27 REMARK 500 THR C 126 26.72 -69.21 REMARK 500 SER C 127 14.94 -156.64 REMARK 500 ASN C 138 103.75 30.24 REMARK 500 TYR C 140 -160.85 -71.39 REMARK 500 PRO C 141 112.52 5.84 REMARK 500 ASP C 143 97.00 -46.63 REMARK 500 ASP C 151 88.18 2.29 REMARK 500 SER C 153 -1.03 61.22 REMARK 500 ALA C 156 121.50 -30.56 REMARK 500 LYS C 169 -93.98 -64.91 REMARK 500 SER C 171 -0.12 77.12 REMARK 500 ASN C 190 -64.56 -96.34 REMARK 500 SER C 203 105.99 -56.82 REMARK 500 ALA C 211 69.04 -179.81 REMARK 500 LEU D 29 20.22 -78.28 REMARK 500 SER D 32 -81.21 -13.58 REMARK 500 ILE D 34 -175.46 -58.78 REMARK 500 SER D 43 87.95 -12.32 REMARK 500 ASP D 57 -3.16 70.72 REMARK 500 SER D 72 172.57 174.41 REMARK 500 THR D 86 71.60 41.88 REMARK 500 THR D 89 -75.03 -37.27 REMARK 500 ALA D 90 -39.60 -33.77 REMARK 500 ALA D 93 -175.12 -175.47 REMARK 500 TRP D 113 -151.30 -97.36 REMARK 500 GLN D 115 99.41 -62.18 REMARK 500 SER D 122 139.65 -173.43 REMARK 500 ALA D 124 145.87 -31.84 REMARK 500 SER D 138 19.35 -60.00 REMARK 500 CYS D 150 95.68 -163.92 REMARK 500 PHE D 156 -64.41 -98.92 REMARK 500 PRO D 157 96.97 -51.24 REMARK 500 ASN D 165 65.81 72.40 REMARK 500 SER D 166 19.60 53.00 REMARK 500 SER D 170 -52.29 -120.96 REMARK 500 SER D 195 -37.11 -37.86 REMARK 500 SER D 213 45.45 75.76 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 TYR B 146 0.12 SIDE_CHAIN REMARK 500 TYR B 183 0.08 SIDE_CHAIN REMARK 500 TYR B 188 0.06 SIDE_CHAIN REMARK 500 ARG B 211 0.11 SIDE_CHAIN REMARK 500 TYR B 342 0.07 SIDE_CHAIN REMARK 500 TYR D 95 0.07 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2HMI RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX REMARK 900 WITH DNA:DNA REMARK 900 RELATED ID: 1RTD RELATED DB: PDB REMARK 900 STRUCTURE OF A COVALENTLY TRAPPED CATALYTIC COMPLEX OF HIV- REMARK 900 1 REVERSE TRANSCRIPTASE: IMPLICATIONS FOR DRUG RESISTANCE REMARK 900 RELATED ID: 1DLO RELATED DB: PDB REMARK 900 STRUCTURE OF UNLIGANDED HIV-1 REVERSE TRANSCRIPTASE AT 2.7 REMARK 900 A RESOLUTION: IMPLICATIONS OF CONFORMATIONAL CHANGES FOR REMARK 900 POLYMERIZATION AND INHIBITION MECHANISMS