REMARK 2 REMARK 2 RESOLUTION. 1.84 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.2 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK, REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.85 REMARK 3 NUMBER OF REFLECTIONS : 44332 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 + TEST SET) : 0.1788 REMARK 3 R VALUE (WORKING SET) : 0.1770 REMARK 3 FREE R VALUE : 0.2139 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.03 REMARK 3 FREE R VALUE TEST SET COUNT : 2228 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 : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.89 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.85 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2705 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2389 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2567 REMARK 3 BIN R VALUE (WORKING SET) : 0.2370 REMARK 3 BIN FREE R VALUE : 0.2731 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 138 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 : 3822 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 40 REMARK 3 SOLVENT ATOMS : 449 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 26.33 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.99 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.0944 REMARK 3 B22 (A**2) : 0.4357 REMARK 3 B33 (A**2) : -1.5300 REMARK 3 B12 (A**2) : 0.0000 REMARK 3 B13 (A**2) : -0.7325 REMARK 3 B23 (A**2) : 0.0000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.243 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.135 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.125 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.131 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.124 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.9526 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9330 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3951 ; 2.00 ; HARMONIC REMARK 3 BOND ANGLES : 5379 ; 2.00 ; HARMONIC REMARK 3 TORSION ANGLES : 1305 ; 2.00 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 83 ; 2.00 ; HARMONIC REMARK 3 GENERAL PLANES : 558 ; 5.00 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3951 ; 20.00 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 537 ; 5.00 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 4704 ; 4.00 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.14 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.75 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.30 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION : (CHAIN C AND RESID 300-327) REMARK 3 ORIGIN FOR THE GROUP (A): 12.6442 32.9806 -5.0870 REMARK 3 T TENSOR REMARK 3 T11: 0.0414 T22: -0.1140 REMARK 3 T33: -0.0849 T12: 0.0077 REMARK 3 T13: 0.0526 T23: -0.0313 REMARK 3 L TENSOR REMARK 3 L11: 1.2272 L22: 1.5426 REMARK 3 L33: 5.4390 L12: 1.3853 REMARK 3 L13: 0.9032 L23: 0.6393 REMARK 3 S TENSOR REMARK 3 S11: -0.1672 S12: 0.0825 S13: -0.0657 REMARK 3 S21: -0.2809 S22: 0.0233 S23: -0.0561 REMARK 3 S31: 0.5362 S32: 0.1068 S33: 0.1439 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION : (CHAIN C AND RESID 328-360) REMARK 3 ORIGIN FOR THE GROUP (A): 7.9093 25.5336 -1.8932 REMARK 3 T TENSOR REMARK 3 T11: 0.0550 T22: 0.0580 REMARK 3 T33: -0.0809 T12: -0.0799 REMARK 3 T13: 0.1293 T23: -0.0382 REMARK 3 L TENSOR REMARK 3 L11: 0.1036 L22: 5.5250 REMARK 3 L33: 4.5497 L12: 1.5874 REMARK 3 L13: 0.8417 L23: -0.9181 REMARK 3 S TENSOR REMARK 3 S11: -0.0226 S12: -0.0010 S13: -0.0875 REMARK 3 S21: -0.0533 S22: 0.0106 S23: -0.0383 REMARK 3 S31: 0.2209 S32: -0.1966 S33: 0.0119 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION : (CHAIN C AND RESID 361-368) REMARK 3 ORIGIN FOR THE GROUP (A): 5.8587 33.8920 -4.5509 REMARK 3 T TENSOR REMARK 3 T11: 0.0504 T22: -0.0445 REMARK 3 T33: -0.0355 T12: 0.0036 REMARK 3 T13: -0.0028 T23: -0.0821 REMARK 3 L TENSOR REMARK 3 L11: -0.2531 L22: 0.0000 REMARK 3 L33: 0.7808 L12: -0.0251 REMARK 3 L13: 1.2198 L23: 0.5365 REMARK 3 S TENSOR REMARK 3 S11: -0.0027 S12: 0.0776 S13: -0.0013 REMARK 3 S21: -0.0090 S22: -0.0139 S23: 0.1492 REMARK 3 S31: 0.0157 S32: -0.0903 S33: 0.0166 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION : (CHAIN C AND RESID 369-391) REMARK 3 ORIGIN FOR THE GROUP (A): 21.3107 28.2101 -4.6125 REMARK 3 T TENSOR REMARK 3 T11: -0.0242 T22: -0.0207 REMARK 3 T33: 0.0853 T12: 0.1364 REMARK 3 T13: 0.1891 T23: 0.0035 REMARK 3 L TENSOR REMARK 3 L11: 0.7414 L22: 1.6539 REMARK 3 L33: -0.5820 L12: -1.5288 REMARK 3 L13: -2.8618 L23: -0.0973 REMARK 3 S TENSOR REMARK 3 S11: 0.0062 S12: 0.0005 S13: -0.1617 REMARK 3 S21: -0.0255 S22: -0.1119 S23: -0.1607 REMARK 3 S31: 0.0780 S32: 0.2500 S33: 0.1057 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION : (CHAIN H AND RESID 1-27) REMARK 3 ORIGIN FOR THE GROUP (A): 10.8916 62.3867 8.5541 REMARK 3 T TENSOR REMARK 3 T11: 0.0253 T22: -0.0870 REMARK 3 T33: -0.0617 T12: -0.0383 REMARK 3 T13: -0.0631 T23: 0.0307 REMARK 3 L TENSOR REMARK 3 L11: 0.6606 L22: 1.5537 REMARK 3 L33: 0.7415 L12: -1.7074 REMARK 3 L13: -0.1122 L23: 0.0427 REMARK 3 S TENSOR REMARK 3 S11: -0.0142 S12: -0.0108 S13: 0.1721 REMARK 3 S21: -0.1305 S22: -0.0103 S23: -0.1414 REMARK 3 S31: -0.2232 S32: 0.0791 S33: 0.0245 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION : (CHAIN H AND RESID 28-119) REMARK 3 ORIGIN FOR THE GROUP (A): 9.5549 53.6168 7.4187 REMARK 3 T TENSOR REMARK 3 T11: -0.0688 T22: -0.1277 REMARK 3 T33: -0.1324 T12: -0.0379 REMARK 3 T13: -0.0276 T23: 0.0261 REMARK 3 L TENSOR REMARK 3 L11: 0.7165 L22: 1.2317 REMARK 3 L33: 1.8350 L12: -0.3645 REMARK 3 L13: 0.1731 L23: 0.3078 REMARK 3 S TENSOR REMARK 3 S11: -0.0574 S12: 0.0109 S13: -0.0237 REMARK 3 S21: -0.1847 S22: -0.0047 S23: 0.0122 REMARK 3 S31: -0.2150 S32: 0.0461 S33: 0.0621 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION : (CHAIN H AND RESID 120-194) REMARK 3 ORIGIN FOR THE GROUP (A): -7.1607 74.2762 29.6975 REMARK 3 T TENSOR REMARK 3 T11: -0.1129 T22: -0.0349 REMARK 3 T33: -0.0395 T12: 0.0267 REMARK 3 T13: -0.0258 T23: -0.0621 REMARK 3 L TENSOR REMARK 3 L11: 1.5799 L22: 3.3445 REMARK 3 L33: 6.7334 L12: -1.0876 REMARK 3 L13: -1.2384 L23: 1.0733 REMARK 3 S TENSOR REMARK 3 S11: 0.1535 S12: -0.1031 S13: 0.2508 REMARK 3 S21: 0.0677 S22: 0.2649 S23: -0.1371 REMARK 3 S31: 0.0899 S32: 0.3415 S33: -0.4185 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION : (CHAIN H AND RESID 195-217) REMARK 3 ORIGIN FOR THE GROUP (A): -5.1415 82.3902 29.0230 REMARK 3 T TENSOR REMARK 3 T11: -0.0476 T22: -0.0117 REMARK 3 T33: 0.0182 T12: -0.0484 REMARK 3 T13: 0.0257 T23: -0.0673 REMARK 3 L TENSOR REMARK 3 L11: 3.3506 L22: 3.9052 REMARK 3 L33: 0.6543 L12: -0.2437 REMARK 3 L13: -0.7435 L23: -1.3316 REMARK 3 S TENSOR REMARK 3 S11: -0.0802 S12: 0.1034 S13: 0.3976 REMARK 3 S21: 0.0528 S22: 0.1682 S23: 0.0711 REMARK 3 S31: -0.2381 S32: 0.1374 S33: -0.0880 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION : (CHAIN L AND RESID 1-44) REMARK 3 ORIGIN FOR THE GROUP (A): 6.1309 41.9177 25.2238 REMARK 3 T TENSOR REMARK 3 T11: 0.0227 T22: -0.0170 REMARK 3 T33: -0.0118 T12: -0.0052 REMARK 3 T13: -0.0179 T23: 0.0078 REMARK 3 L TENSOR REMARK 3 L11: 0.6896 L22: 1.3036 REMARK 3 L33: 3.0481 L12: -0.0825 REMARK 3 L13: -0.1465 L23: 0.2447 REMARK 3 S TENSOR REMARK 3 S11: -0.0967 S12: -0.0316 S13: -0.0518 REMARK 3 S21: 0.1279 S22: -0.0428 S23: -0.0376 REMARK 3 S31: 0.0890 S32: -0.1424 S33: 0.1395 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION : (CHAIN L AND RESID 45-104) REMARK 3 ORIGIN FOR THE GROUP (A): 11.8760 43.1653 25.5206 REMARK 3 T TENSOR REMARK 3 T11: -0.0172 T22: -0.0741 REMARK 3 T33: -0.0613 T12: -0.0257 REMARK 3 T13: -0.0277 T23: 0.0193 REMARK 3 L TENSOR REMARK 3 L11: 0.8248 L22: 1.3690 REMARK 3 L33: 4.2422 L12: 0.1313 REMARK 3 L13: -0.4837 L23: -0.1363 REMARK 3 S TENSOR REMARK 3 S11: -0.0202 S12: -0.1361 S13: -0.0771 REMARK 3 S21: 0.1864 S22: -0.0562 S23: -0.1375 REMARK 3 S31: -0.0551 S32: 0.2098 S33: 0.0764 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION : (CHAIN L AND RESID 105-155) REMARK 3 ORIGIN FOR THE GROUP (A): -15.9565 65.2906 35.8484 REMARK 3 T TENSOR REMARK 3 T11: -0.0473 T22: -0.0668 REMARK 3 T33: -0.0662 T12: 0.0164 REMARK 3 T13: -0.0651 T23: -0.0022 REMARK 3 L TENSOR REMARK 3 L11: 2.5315 L22: 2.1064 REMARK 3 L33: 2.4465 L12: -1.7164 REMARK 3 L13: 1.1033 L23: -0.7890 REMARK 3 S TENSOR REMARK 3 S11: 0.1478 S12: -0.0067 S13: -0.1190 REMARK 3 S21: 0.0179 S22: 0.0657 S23: 0.2245 REMARK 3 S31: 0.2987 S32: -0.1120 S33: -0.2136 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION : (CHAIN L AND RESID 156-212) REMARK 3 ORIGIN FOR THE GROUP (A): -18.7332 65.8560 35.1020 REMARK 3 T TENSOR REMARK 3 T11: -0.0202 T22: 0.0268 REMARK 3 T33: -0.0088 T12: 0.0140 REMARK 3 T13: -0.0514 T23: 0.0153 REMARK 3 L TENSOR REMARK 3 L11: 1.7945 L22: 0.9861 REMARK 3 L33: 1.8528 L12: -0.8164 REMARK 3 L13: 0.8420 L23: -0.2394 REMARK 3 S TENSOR REMARK 3 S11: 0.1759 S12: -0.1219 S13: -0.1475 REMARK 3 S21: 0.0128 S22: 0.0285 S23: 0.1578 REMARK 3 S31: 0.3622 S32: -0.2908 S33: -0.2043 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4ALA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAR-12. REMARK 100 THE PDBE ID CODE IS EBI-51526. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I04 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.975 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44605 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.84 REMARK 200 RESOLUTION RANGE LOW (A) : 38.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 200 DATA REDUNDANCY : 7.3 REMARK 200 R MERGE (I) : 0.11 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.00 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.3 REMARK 200 R MERGE FOR SHELL (I) : 0.98 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.00 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M DI-HYDROGEN REMARK 280 PHOSPHATE REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 63.02000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 5300 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28340 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.3 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H, L 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 LYS C 295 REMARK 465 GLY C 296 REMARK 465 MET C 297 REMARK 465 SER C 298 REMARK 465 TYR C 299 REMARK 465 GLU C 340 REMARK 465 ASP C 341 REMARK 465 GLY C 342 REMARK 465 GLN C 343 REMARK 465 GLY C 344 REMARK 465 LYS C 345 REMARK 465 ALA C 346 REMARK 465 HIS C 347 REMARK 465 ASN C 348 REMARK 465 GLY C 349 REMARK 465 GLU C 375 REMARK 465 SER C 376 REMARK 465 GLY C 383 REMARK 465 ASP C 384 REMARK 465 TYR C 392 REMARK 465 ARG C 393 REMARK 465 LYS C 394 REMARK 465 GLY C 395 REMARK 465 CYS H 132 REMARK 465 GLY H 133 REMARK 465 ASP H 134 REMARK 465 THR H 135 REMARK 465 THR H 136 REMARK 465 GLY H 137 REMARK 465 SER H 164 REMARK 465 SER H 165 REMARK 465 SER H 166 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ILE C 382 CG1 CG2 CD1 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH L 2187 O HOH L 2188 2.17 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 ASN C 304 -164.06 -100.70 REMARK 500 ALA H 103 -155.04 68.36 REMARK 500 ASP H 105 -67.56 -103.54 REMARK 500 GLN H 175 76.13 -159.73 REMARK 500 ARG L 30 -115.27 54.17 REMARK 500 ALA L 51 -38.05 65.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 VAL H 167 22.5 L L OUTSIDE RANGE 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 GOL H1218 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H1219 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L1214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L1215 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4AL8 RELATED DB: PDB REMARK 900 STRUCTURE OF DENGUE VIRUS DIII IN COMPLEX WITH FAB REMARK 900 2H12 REMARK 900 RELATED ID: 4AM0 RELATED DB: PDB REMARK 900 STRUCTURE OF DENGUE VIRUS STRAIN 4 DIII IN COMPLEX REMARK 900 WITH FAB 2H12