REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 3 NUMBER OF REFLECTIONS : 50562 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) : 0.207 REMARK 3 R VALUE (WORKING SET) : 0.206 REMARK 3 FREE R VALUE : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1636 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) : 3.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.37 REMARK 3 REFLECTION IN BIN (WORKING SET) : 6442 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.17 REMARK 3 BIN R VALUE (WORKING SET) : 0.2810 REMARK 3 BIN FREE R VALUE SET COUNT : 226 REMARK 3 BIN FREE R VALUE : 0.3140 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7920 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 169 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) : 71.72 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 4.23000 REMARK 3 B22 (A**2) : 4.23000 REMARK 3 B33 (A**2) : -6.35000 REMARK 3 B12 (A**2) : 2.12000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.452 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.302 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.217 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.369 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8336 ; 0.006 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11392 ; 1.096 ; 1.968 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1031 ; 5.755 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 350 ;35.728 ;24.171 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1282 ;15.513 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;15.628 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1255 ; 0.073 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6271 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3208 ; 0.192 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5547 ; 0.303 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 208 ; 0.105 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 69 ; 0.183 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.134 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5267 ; 1.849 ; 2.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8330 ; 3.192 ; 5.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3478 ; 1.848 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3062 ; 2.946 ; 5.000 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 5 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 118 REMARK 3 RESIDUE RANGE : L 1 L 108 REMARK 3 RESIDUE RANGE : X 6 X 6 REMARK 3 RESIDUE RANGE : X 8 X 8 REMARK 3 RESIDUE RANGE : X 11 X 11 REMARK 3 ORIGIN FOR THE GROUP (A): 92.8434 -12.4902 -19.1268 REMARK 3 T TENSOR REMARK 3 T11: -0.0401 T22: -0.4501 REMARK 3 T33: -0.3033 T12: -0.0239 REMARK 3 T13: 0.0254 T23: 0.0980 REMARK 3 L TENSOR REMARK 3 L11: 1.0683 L22: 3.2305 REMARK 3 L33: 4.1291 L12: -1.2860 REMARK 3 L13: 0.1045 L23: 0.8119 REMARK 3 S TENSOR REMARK 3 S11: -0.1701 S12: -0.0560 S13: -0.0830 REMARK 3 S21: -0.0565 S22: 0.1504 S23: -0.0250 REMARK 3 S31: 0.5058 S32: 0.1952 S33: 0.0197 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 124 H 217 REMARK 3 RESIDUE RANGE : L 108 L 214 REMARK 3 ORIGIN FOR THE GROUP (A): 112.2239 -33.4437 -0.4987 REMARK 3 T TENSOR REMARK 3 T11: 0.3838 T22: 0.2447 REMARK 3 T33: 0.0274 T12: 0.3858 REMARK 3 T13: 0.0662 T23: -0.0293 REMARK 3 L TENSOR REMARK 3 L11: 2.2984 L22: 3.5275 REMARK 3 L33: 4.7826 L12: -1.5094 REMARK 3 L13: -1.1297 L23: 0.4075 REMARK 3 S TENSOR REMARK 3 S11: -0.0572 S12: -0.6855 S13: 0.1759 REMARK 3 S21: 0.5117 S22: 0.3175 S23: -0.5988 REMARK 3 S31: 0.0301 S32: 1.1673 S33: -0.2603 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 5 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 197 REMARK 3 RESIDUE RANGE : A 1165 A 1170 REMARK 3 RESIDUE RANGE : X 9 X 9 REMARK 3 RESIDUE RANGE : X 14 X 14 REMARK 3 RESIDUE RANGE : X 16 X 16 REMARK 3 ORIGIN FOR THE GROUP (A): 84.5963 24.1643 -66.1991 REMARK 3 T TENSOR REMARK 3 T11: -0.3030 T22: -0.5359 REMARK 3 T33: -0.4247 T12: -0.0400 REMARK 3 T13: -0.0516 T23: 0.0434 REMARK 3 L TENSOR REMARK 3 L11: 2.8060 L22: 5.0810 REMARK 3 L33: 6.3129 L12: 0.7829 REMARK 3 L13: -0.8795 L23: -1.1327 REMARK 3 S TENSOR REMARK 3 S11: -0.0083 S12: -0.0321 S13: -0.2888 REMARK 3 S21: 0.0689 S22: -0.0092 S23: -0.0725 REMARK 3 S31: 0.7632 S32: -0.2158 S33: 0.0175 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 3 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 198 A 245 REMARK 3 RESIDUE RANGE : A 1237 A 1241 REMARK 3 RESIDUE RANGE : X 3 X 3 REMARK 3 ORIGIN FOR THE GROUP (A): 75.2027 46.5024 -64.0774 REMARK 3 T TENSOR REMARK 3 T11: -0.3684 T22: -0.3640 REMARK 3 T33: -0.3399 T12: 0.0074 REMARK 3 T13: 0.0377 T23: 0.0713 REMARK 3 L TENSOR REMARK 3 L11: 3.6900 L22: 6.3180 REMARK 3 L33: 12.2530 L12: -3.5321 REMARK 3 L13: 2.2368 L23: -1.0253 REMARK 3 S TENSOR REMARK 3 S11: -0.0343 S12: -0.3356 S13: 0.0894 REMARK 3 S21: 0.8054 S22: 0.2165 S23: 0.3374 REMARK 3 S31: -0.3215 S32: -0.7454 S33: -0.1822 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 246 A 266 REMARK 3 ORIGIN FOR THE GROUP (A): 73.1777 58.0450 -46.1135 REMARK 3 T TENSOR REMARK 3 T11: 0.5167 T22: 0.7322 REMARK 3 T33: 0.5216 T12: 0.0282 REMARK 3 T13: -0.0203 T23: 0.1884 REMARK 3 L TENSOR REMARK 3 L11: 2.4303 L22: 40.1094 REMARK 3 L33: 10.8058 L12: -8.1435 REMARK 3 L13: -5.0992 L23: 15.9143 REMARK 3 S TENSOR REMARK 3 S11: 0.6825 S12: -0.8465 S13: 0.4582 REMARK 3 S21: -1.9760 S22: -0.6968 S23: 2.7983 REMARK 3 S31: 0.8395 S32: -1.5073 S33: 0.0144 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 267 A 319 REMARK 3 ORIGIN FOR THE GROUP (A): 84.7907 40.6825 -35.0298 REMARK 3 T TENSOR REMARK 3 T11: 0.4534 T22: 0.0848 REMARK 3 T33: 0.0850 T12: -0.0418 REMARK 3 T13: -0.0852 T23: 0.1350 REMARK 3 L TENSOR REMARK 3 L11: 4.5146 L22: 4.3615 REMARK 3 L33: 9.9103 L12: -2.7926 REMARK 3 L13: 1.9582 L23: -0.4953 REMARK 3 S TENSOR REMARK 3 S11: -0.4183 S12: -1.5003 S13: 0.6203 REMARK 3 S21: 1.1291 S22: 0.1192 S23: -0.6835 REMARK 3 S31: -1.0513 S32: 0.3040 S33: 0.2991 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 6 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 320 A 507 REMARK 3 RESIDUE RANGE : X 1 X 2 REMARK 3 RESIDUE RANGE : X 4 X 4 REMARK 3 RESIDUE RANGE : X 10 X 10 REMARK 3 RESIDUE RANGE : X 12 X 13 REMARK 3 RESIDUE RANGE : X 17 X 17 REMARK 3 ORIGIN FOR THE GROUP (A): 87.2039 14.4516 -32.0225 REMARK 3 T TENSOR REMARK 3 T11: -0.1976 T22: -0.4754 REMARK 3 T33: -0.4118 T12: -0.0609 REMARK 3 T13: -0.0784 T23: 0.0684 REMARK 3 L TENSOR REMARK 3 L11: 4.2013 L22: 5.9125 REMARK 3 L33: 5.1069 L12: 0.6910 REMARK 3 L13: 0.3703 L23: -1.4594 REMARK 3 S TENSOR REMARK 3 S11: -0.1383 S12: 0.1070 S13: 0.0890 REMARK 3 S21: -0.0331 S22: 0.0252 S23: -0.1852 REMARK 3 S31: -0.2178 S32: 0.0586 S33: 0.1131 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 3 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 508 A 620 REMARK 3 RESIDUE RANGE : X 5 X 5 REMARK 3 RESIDUE RANGE : X 7 X 7 REMARK 3 ORIGIN FOR THE GROUP (A): 73.5939 22.1672 10.9814 REMARK 3 T TENSOR REMARK 3 T11: 0.2438 T22: -0.0259 REMARK 3 T33: 0.0163 T12: 0.1771 REMARK 3 T13: 0.1065 T23: 0.1452 REMARK 3 L TENSOR REMARK 3 L11: 1.8962 L22: 2.9378 REMARK 3 L33: 9.9328 L12: 0.6323 REMARK 3 L13: 1.5421 L23: 4.1284 REMARK 3 S TENSOR REMARK 3 S11: -0.0267 S12: -0.3572 S13: 0.3370 REMARK 3 S21: 0.3245 S22: -0.2254 S23: 0.1702 REMARK 3 S31: -0.1575 S32: -0.3940 S33: 0.2521 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3N85 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-10. REMARK 100 THE RCSB ID CODE IS RCSB059500. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-JUL-07; 08-AUG-07 REMARK 200 TEMPERATURE (KELVIN) : 110; 110 REMARK 200 PH : 7.3 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : ALS; ALS REMARK 200 BEAMLINE : 5.0.1; 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : .98; 1.0 REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111); REMARK 200 SAGITALLY FOCUSED SI(111) REMARK 200 OPTICS : NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : AREA DETECTOR; AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210; ADSC QUANTUM REMARK 200 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52459 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2 REMARK 200 DATA REDUNDANCY : 8.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.14700 REMARK 200 FOR THE DATA SET : 13.0000 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; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 1S78 CHAIN A 1FVD CHAINS A,B 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: NACL, NA/K-PHOSPHATE, LI-SULFATE, PH REMARK 280 7.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/2 REMARK 290 6555 X-Y,X,Z+1/2 REMARK 290 7555 Y,X,-Z REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z REMARK 290 10555 -Y,-X,-Z+1/2 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+1/2 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 0.00000 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 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 165.42550 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 165.42550 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 165.42550 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 165.42550 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 165.42550 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 165.42550 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: NONAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 39450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 140040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -784.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, H 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 BIOMT1 2 -0.500000 -0.866025 0.000000 182.22000 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 91.11000 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 157.80715 REMARK 350 BIOMT3 3 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 LEU A 101 REMARK 465 ASN A 102 REMARK 465 ASN A 103 REMARK 465 THR A 104 REMARK 465 THR A 105 REMARK 465 PRO A 106 REMARK 465 VAL A 107 REMARK 465 THR A 108 REMARK 465 GLY A 109 REMARK 465 ALA A 110 REMARK 465 ALA A 248 REMARK 465 LEU A 249 REMARK 465 VAL A 250 REMARK 465 THR A 251 REMARK 465 TYR A 252 REMARK 465 PRO A 621 REMARK 465 ALA A 622 REMARK 465 GLU A 623 REMARK 465 GLN A 624 REMARK 465 GLU L 215 REMARK 465 ILE L 216 REMARK 465 SER L 217 REMARK 465 LYS H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 SER H 136 REMARK 465 SER H 219 REMARK 465 CYS H 220 REMARK 465 ASP H 221 REMARK 465 LYS H 222 REMARK 465 THR H 223 REMARK 465 HIS H 224 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 GLU A 485 CD GLU A 485 OE2 0.082 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 ASP A 8 75.63 -152.47 REMARK 500 LYS A 10 -124.18 48.47 REMARK 500 LEU A 74 37.84 -98.65 REMARK 500 TYR A 141 -9.56 77.96 REMARK 500 LYS A 178 -82.99 -28.54 REMARK 500 ARG A 195 -53.74 -127.49 REMARK 500 CYS A 202 109.95 41.89 REMARK 500 GLU A 216 -23.84 -37.07 REMARK 500 ALA A 220 -22.74 66.48 REMARK 500 HIS A 235 -65.92 -121.44 REMARK 500 PRO A 261 -167.96 -60.60 REMARK 500 ASN A 262 99.47 65.46 REMARK 500 GLU A 264 -121.99 21.97 REMARK 500 PRO A 294 -179.58 -65.91 REMARK 500 GLN A 298 -136.99 -95.00 REMARK 500 GLU A 299 93.80 -176.20 REMARK 500 GLU A 326 -128.92 50.21 REMARK 500 ASN A 416 14.78 54.68 REMARK 500 ALA A 418 -35.77 -138.76 REMARK 500 ARG A 465 -66.18 -108.77 REMARK 500 ARG A 495 20.00 56.29 REMARK 500 GLN A 511 -101.38 -113.95 REMARK 500 LEU A 528 -92.81 -43.00 REMARK 500 HIS A 567 -114.77 -127.41 REMARK 500 PRO A 571 118.18 -28.90 REMARK 500 SER A 587 -7.85 72.44 REMARK 500 PRO A 605 -135.85 -85.16 REMARK 500 CYS A 608 176.11 62.21 REMARK 500 THR A 609 -68.28 69.50 REMARK 500 HIS A 610 75.29 -103.71 REMARK 500 CYS A 612 130.46 70.73 REMARK 500 VAL A 613 124.20 -173.24 REMARK 500 ASP A 614 -92.61 43.99 REMARK 500 LEU A 615 44.75 -107.28 REMARK 500 ASP A 616 137.95 63.14 REMARK 500 SER L 30 -144.73 57.52 REMARK 500 ALA L 51 -51.18 67.33 REMARK 500 SER L 127 -25.30 -151.01 REMARK 500 ASN L 138 82.71 60.25 REMARK 500 ARG L 211 109.78 -45.32 REMARK 500 SER H 97 -75.72 57.55 REMARK 500 SER H 98 59.32 -171.27 REMARK 500 SER H 126 -164.94 -115.78 REMARK 500 ASP H 148 75.24 62.75 REMARK 500 PRO H 217 92.25 -62.62 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 CL A 625 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 626 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 627 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 628 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 629 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 630 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 225 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 631 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 218 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 632 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 633 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 219 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 634 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 635 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 636 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 638 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1165 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1166 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1167 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 1170 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1237 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1238 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1239 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1N8Z RELATED DB: PDB REMARK 900 HER2 ECD WITH HERCEPTIN FAB REMARK 900 RELATED ID: 1S78 RELATED DB: PDB REMARK 900 HER2 ECD WITH PERTUZUMAB FAB REMARK 900 RELATED ID: 1IVO RELATED DB: PDB REMARK 900 EGFR ECD WITH EGF REMARK 900 RELATED ID: 1MOX RELATED DB: PDB REMARK 900 EGFR ECD WITH TGF-ALPHA REMARK 900 RELATED ID: 3I2T RELATED DB: PDB REMARK 900 DROSOPHILA EGFR ECD REMARK 900 RELATED ID: 1ZA3 RELATED DB: PDB REMARK 900 TYROSINE/SERINE BINARY FAB COMPLEXED WITH DEATH RECEPTOR 5