REMARK 2 REMARK 2 RESOLUTION. 2.71 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.9.3 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.17 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 3 NUMBER OF REFLECTIONS : 40983 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) : 0.222 REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 2073 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) : 2.71 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.78 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.63 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2348 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2761 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2214 REMARK 3 BIN R VALUE (WORKING SET) : 0.2734 REMARK 3 BIN FREE R VALUE : 0.3221 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.71 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 134 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 : 8120 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 66 REMARK 3 SOLVENT ATOMS : 343 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 62.45 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.45 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -11.02840 REMARK 3 B22 (A**2) : 12.18050 REMARK 3 B33 (A**2) : -1.15210 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) : 0.44 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.72 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.31 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.67 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.31 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 : 0.908 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.887 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 8354 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 11376 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 2755 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 167 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 1205 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 8354 ; 20.000 ; 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 : 1118 ; 5.000 ; 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 : 8634 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 0.97 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.84 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.50 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: A 282 A 296 REMARK 3 ORIGIN FOR THE GROUP (A): 5.0588 2.2775 -29.4295 REMARK 3 T TENSOR REMARK 3 T11: -0.1124 T22: -0.1099 REMARK 3 T33: 0.0057 T12: 0.0490 REMARK 3 T13: 0.0526 T23: 0.0108 REMARK 3 L TENSOR REMARK 3 L11: 2.2858 L22: 4.5932 REMARK 3 L33: 1.4918 L12: -0.8369 REMARK 3 L13: -0.2459 L23: -1.0169 REMARK 3 S TENSOR REMARK 3 S11: 0.0567 S12: -0.1655 S13: 0.2781 REMARK 3 S21: 0.2063 S22: 0.0064 S23: 0.0957 REMARK 3 S31: -0.2791 S32: -0.0670 S33: -0.0631 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: B 282 B 296 REMARK 3 ORIGIN FOR THE GROUP (A): -31.6127 27.8163 -29.5580 REMARK 3 T TENSOR REMARK 3 T11: 0.0046 T22: -0.1999 REMARK 3 T33: -0.1906 T12: -0.0563 REMARK 3 T13: -0.0071 T23: -0.0053 REMARK 3 L TENSOR REMARK 3 L11: 2.1724 L22: 6.1360 REMARK 3 L33: 3.2820 L12: -0.1721 REMARK 3 L13: -0.6851 L23: -1.6705 REMARK 3 S TENSOR REMARK 3 S11: 0.0155 S12: -0.2280 S13: 0.1088 REMARK 3 S21: 0.5088 S22: -0.0803 S23: -0.1764 REMARK 3 S31: -0.3154 S32: 0.1380 S33: 0.0648 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: H 1 H 124 REMARK 3 ORIGIN FOR THE GROUP (A): 9.1764 -23.6852 -20.3160 REMARK 3 T TENSOR REMARK 3 T11: -0.1261 T22: -0.0507 REMARK 3 T33: -0.0320 T12: -0.0307 REMARK 3 T13: 0.0562 T23: 0.0614 REMARK 3 L TENSOR REMARK 3 L11: 0.8704 L22: 2.9854 REMARK 3 L33: 4.3906 L12: -1.5562 REMARK 3 L13: 1.1915 L23: -0.6990 REMARK 3 S TENSOR REMARK 3 S11: -0.0221 S12: -0.0945 S13: -0.0694 REMARK 3 S21: 0.0938 S22: -0.0209 S23: 0.0148 REMARK 3 S31: 0.1251 S32: 0.1723 S33: 0.0430 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: H 145 H 223 REMARK 3 ORIGIN FOR THE GROUP (A): 11.7939 -59.1313 -14.9786 REMARK 3 T TENSOR REMARK 3 T11: 0.1795 T22: -0.0998 REMARK 3 T33: -0.1432 T12: 0.1463 REMARK 3 T13: 0.1129 T23: -0.0852 REMARK 3 L TENSOR REMARK 3 L11: 0.0361 L22: 2.5373 REMARK 3 L33: 2.0098 L12: 0.0990 REMARK 3 L13: 1.0995 L23: 0.1600 REMARK 3 S TENSOR REMARK 3 S11: 0.0576 S12: 0.0108 S13: -0.2682 REMARK 3 S21: -0.0150 S22: 0.0628 S23: -0.0132 REMARK 3 S31: 0.2090 S32: 0.1075 S33: -0.1204 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: I 1 I 124 REMARK 3 ORIGIN FOR THE GROUP (A): -28.7744 1.4456 -21.3424 REMARK 3 T TENSOR REMARK 3 T11: -0.1156 T22: -0.1063 REMARK 3 T33: -0.0797 T12: -0.0049 REMARK 3 T13: 0.0207 T23: 0.0594 REMARK 3 L TENSOR REMARK 3 L11: 1.4027 L22: 5.5319 REMARK 3 L33: 4.8646 L12: -1.4248 REMARK 3 L13: 2.6338 L23: -2.6611 REMARK 3 S TENSOR REMARK 3 S11: -0.0214 S12: -0.0611 S13: -0.0449 REMARK 3 S21: 0.0347 S22: -0.0690 S23: -0.2200 REMARK 3 S31: 0.0806 S32: 0.2164 S33: 0.0903 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: I 145 I 223 REMARK 3 ORIGIN FOR THE GROUP (A): -30.2706 -34.7670 -15.2063 REMARK 3 T TENSOR REMARK 3 T11: -0.2228 T22: 0.0690 REMARK 3 T33: -0.0306 T12: 0.0783 REMARK 3 T13: -0.1405 T23: -0.0677 REMARK 3 L TENSOR REMARK 3 L11: 0.8524 L22: 0.8194 REMARK 3 L33: 4.5670 L12: -0.9953 REMARK 3 L13: -0.2494 L23: -0.2988 REMARK 3 S TENSOR REMARK 3 S11: 0.0811 S12: 0.0776 S13: -0.3288 REMARK 3 S21: 0.1175 S22: -0.0620 S23: -0.0710 REMARK 3 S31: 0.0242 S32: 0.2129 S33: -0.0191 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: L 2 L 109 REMARK 3 ORIGIN FOR THE GROUP (A): -4.5658 -31.8409 -36.1760 REMARK 3 T TENSOR REMARK 3 T11: -0.1650 T22: -0.0877 REMARK 3 T33: 0.0696 T12: -0.0266 REMARK 3 T13: -0.0173 T23: -0.0457 REMARK 3 L TENSOR REMARK 3 L11: 0.0000 L22: 6.1898 REMARK 3 L33: 2.3063 L12: 2.8404 REMARK 3 L13: 0.7646 L23: 1.6721 REMARK 3 S TENSOR REMARK 3 S11: -0.0323 S12: 0.2362 S13: -0.1040 REMARK 3 S21: 0.0152 S22: -0.0320 S23: 0.2436 REMARK 3 S31: 0.1042 S32: -0.2538 S33: 0.0643 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: L 110 L 210 REMARK 3 ORIGIN FOR THE GROUP (A): -4.6869 -61.9278 -14.8591 REMARK 3 T TENSOR REMARK 3 T11: 0.2038 T22: -0.1158 REMARK 3 T33: -0.1975 T12: -0.1519 REMARK 3 T13: 0.0899 T23: 0.0946 REMARK 3 L TENSOR REMARK 3 L11: 0.0566 L22: 2.5462 REMARK 3 L33: 2.0144 L12: 0.8445 REMARK 3 L13: -0.3179 L23: -1.3768 REMARK 3 S TENSOR REMARK 3 S11: 0.0421 S12: -0.2076 S13: -0.1740 REMARK 3 S21: 0.0866 S22: -0.0357 S23: 0.0072 REMARK 3 S31: 0.1656 S32: -0.1654 S33: -0.0064 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: M 2 M 109 REMARK 3 ORIGIN FOR THE GROUP (A): -44.1937 -5.3941 -36.3054 REMARK 3 T TENSOR REMARK 3 T11: 0.0383 T22: -0.0631 REMARK 3 T33: -0.0607 T12: 0.0195 REMARK 3 T13: 0.0256 T23: 0.0204 REMARK 3 L TENSOR REMARK 3 L11: 0.3791 L22: 4.3917 REMARK 3 L33: 0.5193 L12: 1.1324 REMARK 3 L13: 0.2437 L23: 0.7060 REMARK 3 S TENSOR REMARK 3 S11: 0.0158 S12: 0.0212 S13: -0.0134 REMARK 3 S21: -0.1720 S22: -0.0610 S23: 0.1908 REMARK 3 S31: 0.0673 S32: -0.0404 S33: 0.0452 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: M 110 M 212 REMARK 3 ORIGIN FOR THE GROUP (A): -46.8293 -35.8289 -14.7458 REMARK 3 T TENSOR REMARK 3 T11: 0.0043 T22: -0.0738 REMARK 3 T33: -0.1118 T12: -0.0850 REMARK 3 T13: -0.0503 T23: 0.0417 REMARK 3 L TENSOR REMARK 3 L11: 0.8686 L22: 2.1769 REMARK 3 L33: 4.1869 L12: -0.8322 REMARK 3 L13: 1.0510 L23: -0.1801 REMARK 3 S TENSOR REMARK 3 S11: 0.0797 S12: -0.2527 S13: -0.1690 REMARK 3 S21: 0.4881 S22: -0.0266 S23: -0.1566 REMARK 3 S31: 0.3165 S32: -0.0604 S33: -0.0531 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3UC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-11. REMARK 100 THE RCSB ID CODE IS RCSB068563. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-SEP-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726 REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111) REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41316 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.710 REMARK 200 RESOLUTION RANGE LOW (A) : 46.175 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 200 DATA REDUNDANCY : 4.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.09000 REMARK 200 FOR THE DATA SET : 11.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.71 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.86 REMARK 200 COMPLETENESS FOR SHELL (%) : 86.4 REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : 0.42900 REMARK 200 R SYM FOR SHELL (I) : 0.42900 REMARK 200 FOR SHELL : 1.800 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: PDB ENTRY 3UAJ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.35 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 292K 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 39.46850 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.79150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.93200 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.79150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.46850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.93200 REMARK 290 SMTRY3 4 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 APPLY THE FOLLOWING TO CHAINS: A, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I, M 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 ASN A 145 REMARK 465 GLY A 146 REMARK 465 ASP A 147 REMARK 465 THR A 148 REMARK 465 HIS A 149 REMARK 465 ALA A 150 REMARK 465 VAL A 151 REMARK 465 GLY A 152 REMARK 465 ASN A 153 REMARK 465 ASP A 154 REMARK 465 THR A 155 REMARK 465 SER A 156 REMARK 465 ASN A 157 REMARK 465 HIS A 158 REMARK 465 MET A 297 REMARK 465 SER A 298 REMARK 465 PRO A 299 REMARK 465 PHE A 300 REMARK 465 GLU A 301 REMARK 465 ASP A 302 REMARK 465 ASP A 303 REMARK 465 ASP A 304 REMARK 465 ASP A 305 REMARK 465 LYS A 306 REMARK 465 ALA A 307 REMARK 465 GLY A 308 REMARK 465 TRP A 309 REMARK 465 SER A 310 REMARK 465 HIS A 311 REMARK 465 PRO A 312 REMARK 465 GLN A 313 REMARK 465 PHE A 314 REMARK 465 GLU A 315 REMARK 465 LYS A 316 REMARK 465 GLY A 317 REMARK 465 GLY A 318 REMARK 465 GLY A 319 REMARK 465 SER A 320 REMARK 465 GLY A 321 REMARK 465 GLY A 322 REMARK 465 GLY A 323 REMARK 465 SER A 324 REMARK 465 GLY A 325 REMARK 465 GLY A 326 REMARK 465 GLY A 327 REMARK 465 SER A 328 REMARK 465 TRP A 329 REMARK 465 SER A 330 REMARK 465 HIS A 331 REMARK 465 PRO A 332 REMARK 465 GLN A 333 REMARK 465 PHE A 334 REMARK 465 GLU A 335 REMARK 465 LYS A 336 REMARK 465 GLY B 146 REMARK 465 ASP B 147 REMARK 465 THR B 148 REMARK 465 HIS B 149 REMARK 465 ALA B 150 REMARK 465 VAL B 151 REMARK 465 GLY B 152 REMARK 465 ASN B 153 REMARK 465 ASP B 154 REMARK 465 MET B 297 REMARK 465 SER B 298 REMARK 465 PRO B 299 REMARK 465 PHE B 300 REMARK 465 GLU B 301 REMARK 465 ASP B 302 REMARK 465 ASP B 303 REMARK 465 ASP B 304 REMARK 465 ASP B 305 REMARK 465 LYS B 306 REMARK 465 ALA B 307 REMARK 465 GLY B 308 REMARK 465 TRP B 309 REMARK 465 SER B 310 REMARK 465 HIS B 311 REMARK 465 PRO B 312 REMARK 465 GLN B 313 REMARK 465 PHE B 314 REMARK 465 GLU B 315 REMARK 465 LYS B 316 REMARK 465 GLY B 317 REMARK 465 GLY B 318 REMARK 465 GLY B 319 REMARK 465 SER B 320 REMARK 465 GLY B 321 REMARK 465 GLY B 322 REMARK 465 GLY B 323 REMARK 465 SER B 324 REMARK 465 GLY B 325 REMARK 465 GLY B 326 REMARK 465 GLY B 327 REMARK 465 SER B 328 REMARK 465 TRP B 329 REMARK 465 SER B 330 REMARK 465 HIS B 331 REMARK 465 PRO B 332 REMARK 465 GLN B 333 REMARK 465 PHE B 334 REMARK 465 GLU B 335 REMARK 465 LYS B 336 REMARK 465 SER H 137 REMARK 465 SER H 138 REMARK 465 LYS H 139 REMARK 465 SER H 140 REMARK 465 THR H 141 REMARK 465 SER H 142 REMARK 465 GLY H 143 REMARK 465 GLY H 144 REMARK 465 LYS H 224 REMARK 465 SER H 225 REMARK 465 CYS H 226 REMARK 465 ASP H 227 REMARK 465 THR H 228 REMARK 465 THR H 229 REMARK 465 SER H 230 REMARK 465 HIS H 231 REMARK 465 HIS H 232 REMARK 465 HIS H 233 REMARK 465 HIS H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 LYS I 139 REMARK 465 SER I 140 REMARK 465 THR I 141 REMARK 465 SER I 142 REMARK 465 GLY I 143 REMARK 465 GLY I 144 REMARK 465 LYS I 224 REMARK 465 SER I 225 REMARK 465 CYS I 226 REMARK 465 ASP I 227 REMARK 465 THR I 228 REMARK 465 THR I 229 REMARK 465 SER I 230 REMARK 465 HIS I 231 REMARK 465 HIS I 232 REMARK 465 HIS I 233 REMARK 465 HIS I 234 REMARK 465 HIS I 235 REMARK 465 HIS I 236 REMARK 465 ALA L 1 REMARK 465 ASN L 211 REMARK 465 ARG L 212 REMARK 465 GLY L 213 REMARK 465 GLU L 214 REMARK 465 CYS L 215 REMARK 465 ALA M 1 REMARK 465 GLY M 213 REMARK 465 GLU M 214 REMARK 465 CYS M 215 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 ARG A 9 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 9 CG CD NE CZ NH1 NH2 REMARK 470 THR B 155 OG1 CG2 REMARK 470 SER B 156 OG REMARK 470 ASN B 157 CG OD1 ND2 REMARK 470 ARG B 167 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 188 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 1 CG CD OE1 OE2 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 ASP A 177 -9.29 78.97 REMARK 500 SER A 189 179.81 61.72 REMARK 500 HIS B 158 -39.02 74.33 REMARK 500 SER B 168 79.65 -118.85 REMARK 500 ASP B 177 -9.46 79.08 REMARK 500 LYS B 295 108.21 -59.24 REMARK 500 SER H 15 -12.36 73.98 REMARK 500 PRO H 41 43.14 -77.03 REMARK 500 THR H 100 -167.13 -123.63 REMARK 500 ASP H 154 74.02 49.89 REMARK 500 SER I 15 -12.36 74.22 REMARK 500 PRO I 41 48.64 -78.22 REMARK 500 THR I 100 -167.26 -123.76 REMARK 500 ASP I 154 85.58 50.81 REMARK 500 SER L 31 -118.85 53.82 REMARK 500 ALA L 52 -35.59 63.35 REMARK 500 PHE L 92 19.75 -143.90 REMARK 500 ASN L 139 86.72 43.47 REMARK 500 ASP L 152 -107.96 73.78 REMARK 500 SER L 157 -72.10 -118.04 REMARK 500 SER M 31 -118.48 53.62 REMARK 500 ALA M 52 -38.76 64.24 REMARK 500 PHE M 92 19.88 -143.79 REMARK 500 ASN M 139 86.98 42.99 REMARK 500 ASN M 153 -4.03 73.23 REMARK 500 SER M 157 -72.15 -118.03 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 A 337 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 338 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 337 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 338 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 237 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 238 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 237 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 216 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 217 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 218 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 219 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 220 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 221 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3UAJ RELATED DB: PDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 PROTEIN FRAGMENT COMPRISES UNP RESIDUES 280-329, A GLY-GLY LINKER, REMARK 999 UNP RESIDUES 414-469, A THR LINKER, UNP RESIDUES 560-577, AND A C- REMARK 999 TERMINAL EXPRESSION TAG.