REMARK 2 REMARK 2 RESOLUTION. 2.04 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) : 2.04 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.80 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6 REMARK 3 NUMBER OF REFLECTIONS : 40459 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) : 0.218 REMARK 3 R VALUE (WORKING SET) : 0.218 REMARK 3 FREE R VALUE : 0.234 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1981 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) : 2.04 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.09 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.62 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2224 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2291 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2126 REMARK 3 BIN R VALUE (WORKING SET) : 0.2281 REMARK 3 BIN FREE R VALUE : 0.2504 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.41 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 98 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 : 4816 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 65 REMARK 3 SOLVENT ATOMS : 277 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.28 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.84990 REMARK 3 B22 (A**2) : 2.15410 REMARK 3 B33 (A**2) : 0.69590 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 2.25820 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.23 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL 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 : 0.926 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 5032 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 6813 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1734 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 115 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 724 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 5032 ; 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 : 665 ; 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 : 5605 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 0.96 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.31 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.57 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|2 - A|117 } REMARK 3 ORIGIN FOR THE GROUP (A): 26.8770 -15.4051 15.5203 REMARK 3 T TENSOR REMARK 3 T11: -0.0328 T22: -0.0641 REMARK 3 T33: -0.0239 T12: -0.0269 REMARK 3 T13: -0.0162 T23: -0.0129 REMARK 3 L TENSOR REMARK 3 L11: 1.3673 L22: 1.2286 REMARK 3 L33: 1.6562 L12: 0.0364 REMARK 3 L13: 0.4236 L23: 0.2472 REMARK 3 S TENSOR REMARK 3 S11: -0.0225 S12: 0.0648 S13: -0.0425 REMARK 3 S21: 0.1155 S22: 0.0166 S23: 0.0254 REMARK 3 S31: -0.0072 S32: 0.0512 S33: 0.0059 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|133 - A|245 } REMARK 3 ORIGIN FOR THE GROUP (A): 11.0177 -23.7457 3.0979 REMARK 3 T TENSOR REMARK 3 T11: -0.0871 T22: -0.0524 REMARK 3 T33: -0.0271 T12: -0.0111 REMARK 3 T13: -0.0161 T23: -0.0373 REMARK 3 L TENSOR REMARK 3 L11: 2.0433 L22: 2.5416 REMARK 3 L33: 1.3130 L12: 0.3416 REMARK 3 L13: 0.4139 L23: 0.0518 REMARK 3 S TENSOR REMARK 3 S11: -0.0124 S12: 0.2610 S13: -0.1263 REMARK 3 S21: -0.0948 S22: 0.0234 S23: 0.1477 REMARK 3 S31: 0.0025 S32: 0.0648 S33: -0.0110 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { B|2 - B|117 } REMARK 3 ORIGIN FOR THE GROUP (A): 32.7277 1.8337 30.4485 REMARK 3 T TENSOR REMARK 3 T11: 0.0279 T22: -0.0924 REMARK 3 T33: -0.0782 T12: -0.0214 REMARK 3 T13: -0.0175 T23: -0.0434 REMARK 3 L TENSOR REMARK 3 L11: 1.2097 L22: 1.9761 REMARK 3 L33: 2.2426 L12: 0.3906 REMARK 3 L13: 0.4062 L23: -0.1853 REMARK 3 S TENSOR REMARK 3 S11: 0.0123 S12: -0.1183 S13: 0.1404 REMARK 3 S21: 0.0653 S22: 0.0194 S23: 0.0425 REMARK 3 S31: -0.0531 S32: 0.0893 S33: -0.0318 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { B|134 - B|243 } REMARK 3 ORIGIN FOR THE GROUP (A): 29.2023 10.0418 50.1665 REMARK 3 T TENSOR REMARK 3 T11: -0.0153 T22: -0.0561 REMARK 3 T33: -0.1081 T12: -0.0247 REMARK 3 T13: 0.0377 T23: -0.0821 REMARK 3 L TENSOR REMARK 3 L11: 1.1168 L22: 3.8790 REMARK 3 L33: 2.2102 L12: -0.1051 REMARK 3 L13: 0.2873 L23: 0.8825 REMARK 3 S TENSOR REMARK 3 S11: 0.0049 S12: -0.2198 S13: 0.1188 REMARK 3 S21: 0.2263 S22: -0.0243 S23: 0.2341 REMARK 3 S31: -0.0037 S32: -0.0883 S33: 0.0193 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { C|299 - C|314 C|317 - C|361 C|365 - C|397 } REMARK 3 ORIGIN FOR THE GROUP (A): 13.5752 1.4405 -6.6341 REMARK 3 T TENSOR REMARK 3 T11: -0.0692 T22: -0.0912 REMARK 3 T33: -0.0234 T12: -0.0177 REMARK 3 T13: -0.0207 T23: 0.0137 REMARK 3 L TENSOR REMARK 3 L11: 2.5477 L22: 2.7087 REMARK 3 L33: 2.0667 L12: -0.9164 REMARK 3 L13: 0.2109 L23: -0.7387 REMARK 3 S TENSOR REMARK 3 S11: -0.0681 S12: 0.1885 S13: 0.2177 REMARK 3 S21: -0.1059 S22: -0.0474 S23: -0.1068 REMARK 3 S31: 0.0862 S32: -0.0507 S33: 0.1155 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: { D|300 - D|314 D|319 - D|341 D|350 - D|359 D|365 - REMARK 3 D|382 D|386 - D|393} REMARK 3 ORIGIN FOR THE GROUP (A): 37.6507 -14.4292 54.8571 REMARK 3 T TENSOR REMARK 3 T11: 0.2823 T22: -0.2672 REMARK 3 T33: -0.2658 T12: 0.0560 REMARK 3 T13: 0.0070 T23: 0.0002 REMARK 3 L TENSOR REMARK 3 L11: 2.2227 L22: 5.1542 REMARK 3 L33: 3.7792 L12: -2.0642 REMARK 3 L13: 0.2674 L23: -3.5263 REMARK 3 S TENSOR REMARK 3 S11: -0.1048 S12: -0.1979 S13: -0.0207 REMARK 3 S21: 0.1353 S22: 0.0285 S23: -0.0839 REMARK 3 S31: 0.2372 S32: -0.0853 S33: 0.0763 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3UZE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-12. REMARK 100 THE RCSB ID CODE IS RCSB069400. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-JUN-08 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 : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0721 REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111) REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40602 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.037 REMARK 200 RESOLUTION RANGE LOW (A) : 42.857 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.08400 REMARK 200 FOR THE DATA SET : 10.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15 REMARK 200 COMPLETENESS FOR SHELL (%) : 76.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.50 REMARK 200 R MERGE FOR SHELL (I) : 0.44400 REMARK 200 R SYM FOR SHELL (I) : 0.44400 REMARK 200 FOR SHELL : 1.700 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: 1UZG, 3UZQ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38.66 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 0.1M HEPES, PH 7.5, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K 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 37.33500 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 GLU A 1 REMARK 465 GLY A 118 REMARK 465 GLY A 119 REMARK 465 GLY A 120 REMARK 465 GLY A 121 REMARK 465 SER A 122 REMARK 465 GLY A 123 REMARK 465 GLY A 124 REMARK 465 GLY A 125 REMARK 465 GLY A 126 REMARK 465 SER A 127 REMARK 465 GLY A 128 REMARK 465 GLY A 129 REMARK 465 GLY A 130 REMARK 465 GLY A 131 REMARK 465 SER A 132 REMARK 465 LEU A 246 REMARK 465 GLU A 247 REMARK 465 HIS A 248 REMARK 465 HIS A 249 REMARK 465 HIS A 250 REMARK 465 HIS A 251 REMARK 465 HIS A 252 REMARK 465 HIS A 253 REMARK 465 GLU B 1 REMARK 465 GLY B 118 REMARK 465 GLY B 119 REMARK 465 GLY B 120 REMARK 465 GLY B 121 REMARK 465 SER B 122 REMARK 465 GLY B 123 REMARK 465 GLY B 124 REMARK 465 GLY B 125 REMARK 465 GLY B 126 REMARK 465 SER B 127 REMARK 465 GLY B 128 REMARK 465 GLY B 129 REMARK 465 GLY B 130 REMARK 465 GLY B 131 REMARK 465 SER B 132 REMARK 465 GLU B 133 REMARK 465 ARG B 244 REMARK 465 PRO B 245 REMARK 465 LEU B 246 REMARK 465 GLU B 247 REMARK 465 HIS B 248 REMARK 465 HIS B 249 REMARK 465 HIS B 250 REMARK 465 HIS B 251 REMARK 465 HIS B 252 REMARK 465 HIS B 253 REMARK 465 LYS C 295 REMARK 465 GLY C 296 REMARK 465 MET C 297 REMARK 465 SER C 298 REMARK 465 THR C 315 REMARK 465 GLN C 316 REMARK 465 GLU C 362 REMARK 465 GLU C 363 REMARK 465 PRO C 364 REMARK 465 GLU C 398 REMARK 465 ASP C 399 REMARK 465 ASP C 400 REMARK 465 ASP C 401 REMARK 465 ASP C 402 REMARK 465 LYS C 403 REMARK 465 ALA C 404 REMARK 465 GLY C 405 REMARK 465 TRP C 406 REMARK 465 SER C 407 REMARK 465 HIS C 408 REMARK 465 PRO C 409 REMARK 465 GLN C 410 REMARK 465 PHE C 411 REMARK 465 GLU C 412 REMARK 465 LYS C 413 REMARK 465 GLY C 414 REMARK 465 GLY C 415 REMARK 465 GLY C 416 REMARK 465 SER C 417 REMARK 465 GLY C 418 REMARK 465 GLY C 419 REMARK 465 GLY C 420 REMARK 465 SER C 421 REMARK 465 GLY C 422 REMARK 465 GLY C 423 REMARK 465 GLY C 424 REMARK 465 SER C 425 REMARK 465 TRP C 426 REMARK 465 SER C 427 REMARK 465 HIS C 428 REMARK 465 PRO C 429 REMARK 465 GLN C 430 REMARK 465 PHE C 431 REMARK 465 GLU C 432 REMARK 465 LYS C 433 REMARK 465 LYS D 295 REMARK 465 GLY D 296 REMARK 465 MET D 297 REMARK 465 SER D 298 REMARK 465 TYR D 299 REMARK 465 THR D 315 REMARK 465 GLN D 316 REMARK 465 HIS D 317 REMARK 465 GLY D 318 REMARK 465 GLY D 342 REMARK 465 GLN D 343 REMARK 465 GLY D 344 REMARK 465 LYS D 345 REMARK 465 ALA D 346 REMARK 465 HIS D 347 REMARK 465 ASN D 348 REMARK 465 GLY D 349 REMARK 465 LYS D 360 REMARK 465 LYS D 361 REMARK 465 GLU D 362 REMARK 465 GLU D 363 REMARK 465 PRO D 364 REMARK 465 GLY D 383 REMARK 465 ASP D 384 REMARK 465 LYS D 385 REMARK 465 LYS D 394 REMARK 465 GLY D 395 REMARK 465 PRO D 396 REMARK 465 PHE D 397 REMARK 465 GLU D 398 REMARK 465 ASP D 399 REMARK 465 ASP D 400 REMARK 465 ASP D 401 REMARK 465 ASP D 402 REMARK 465 LYS D 403 REMARK 465 ALA D 404 REMARK 465 GLY D 405 REMARK 465 TRP D 406 REMARK 465 SER D 407 REMARK 465 HIS D 408 REMARK 465 PRO D 409 REMARK 465 GLN D 410 REMARK 465 PHE D 411 REMARK 465 GLU D 412 REMARK 465 LYS D 413 REMARK 465 GLY D 414 REMARK 465 GLY D 415 REMARK 465 GLY D 416 REMARK 465 SER D 417 REMARK 465 GLY D 418 REMARK 465 GLY D 419 REMARK 465 GLY D 420 REMARK 465 SER D 421 REMARK 465 GLY D 422 REMARK 465 GLY D 423 REMARK 465 GLY D 424 REMARK 465 SER D 425 REMARK 465 TRP D 426 REMARK 465 SER D 427 REMARK 465 HIS D 428 REMARK 465 PRO D 429 REMARK 465 GLN D 430 REMARK 465 PHE D 431 REMARK 465 GLU D 432 REMARK 465 LYS D 433 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 LYS A 68 -52.60 -120.24 REMARK 500 SER A 86 66.58 31.13 REMARK 500 TRP A 101 -57.90 -128.33 REMARK 500 ALA A 187 -39.99 62.20 REMARK 500 ARG A 204 -102.66 57.46 REMARK 500 LYS B 68 -51.52 -138.68 REMARK 500 SER B 86 66.35 29.64 REMARK 500 TRP B 101 -57.15 -124.60 REMARK 500 ALA B 187 -41.92 64.01 REMARK 500 ARG B 204 -93.77 57.26 REMARK 500 ARG C 350 114.93 -168.62 REMARK 500 ALA C 386 134.46 -33.06 REMARK 500 ASP D 330 28.05 -79.46 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH B 328 DISTANCE = 5.36 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 254 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 255 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 256 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 257 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 258 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 254 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 255 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 256 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 257 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 258 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3UYP RELATED DB: PDB REMARK 900 RELATED ID: 3UZQ RELATED DB: PDB REMARK 900 RELATED ID: 3UZV RELATED DB: PDB