REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 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) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.07 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 3 NUMBER OF REFLECTIONS : 53794 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) : 0.179 REMARK 3 R VALUE (WORKING SET) : 0.177 REMARK 3 FREE R VALUE : 0.227 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2815 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3333 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.79 REMARK 3 BIN R VALUE (WORKING SET) : 0.2140 REMARK 3 BIN FREE R VALUE SET COUNT : 194 REMARK 3 BIN FREE R VALUE : 0.2730 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6075 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 45 REMARK 3 SOLVENT ATOMS : 400 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.96 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.75000 REMARK 3 B22 (A**2) : 0.45000 REMARK 3 B33 (A**2) : 0.30000 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 OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.187 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.171 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.119 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.785 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6366 ; 0.025 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8687 ; 1.954 ; 1.963 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 824 ;13.895 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 250 ;34.909 ;25.080 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1039 ;15.985 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;22.459 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 972 ; 0.140 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4785 ; 0.011 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL 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): 4006 ; 0.842 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6481 ; 1.386 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2356 ; 2.489 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2181 ; 3.664 ; 4.500 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 : 9 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 49 REMARK 3 ORIGIN FOR THE GROUP (A): -18.2150 9.8810 -15.9180 REMARK 3 T TENSOR REMARK 3 T11: 0.1512 T22: 0.0786 REMARK 3 T33: 0.1499 T12: -0.0475 REMARK 3 T13: -0.0362 T23: -0.0227 REMARK 3 L TENSOR REMARK 3 L11: 3.1124 L22: 2.9739 REMARK 3 L33: 3.0701 L12: -0.7432 REMARK 3 L13: -0.0090 L23: 0.4447 REMARK 3 S TENSOR REMARK 3 S11: -0.0209 S12: 0.1023 S13: -0.1358 REMARK 3 S21: -0.3866 S22: -0.1073 S23: 0.4028 REMARK 3 S31: 0.0080 S32: -0.3841 S33: 0.1283 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 50 A 306 REMARK 3 ORIGIN FOR THE GROUP (A): -8.4320 22.0700 -2.5910 REMARK 3 T TENSOR REMARK 3 T11: 0.0501 T22: 0.0123 REMARK 3 T33: 0.0325 T12: -0.0160 REMARK 3 T13: 0.0041 T23: 0.0007 REMARK 3 L TENSOR REMARK 3 L11: 0.4297 L22: 2.0054 REMARK 3 L33: 1.9305 L12: -0.1527 REMARK 3 L13: -0.0968 L23: 1.1700 REMARK 3 S TENSOR REMARK 3 S11: -0.0357 S12: 0.0030 S13: -0.0363 REMARK 3 S21: -0.2027 S22: -0.0023 S23: 0.0736 REMARK 3 S31: -0.0810 S32: -0.0302 S33: 0.0380 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 307 A 367 REMARK 3 ORIGIN FOR THE GROUP (A): -2.5510 19.0510 2.2770 REMARK 3 T TENSOR REMARK 3 T11: 0.0205 T22: 0.0303 REMARK 3 T33: 0.0442 T12: -0.0129 REMARK 3 T13: 0.0274 T23: -0.0235 REMARK 3 L TENSOR REMARK 3 L11: 1.2270 L22: 2.2167 REMARK 3 L33: 2.5591 L12: 0.0757 REMARK 3 L13: -0.5012 L23: 0.4304 REMARK 3 S TENSOR REMARK 3 S11: -0.0365 S12: -0.0404 S13: -0.0871 REMARK 3 S21: -0.0861 S22: 0.0286 S23: -0.1664 REMARK 3 S31: 0.0819 S32: 0.1382 S33: 0.0079 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 2 H 22 REMARK 3 ORIGIN FOR THE GROUP (A): 29.3480 30.0410 -16.4390 REMARK 3 T TENSOR REMARK 3 T11: 0.3320 T22: 0.2031 REMARK 3 T33: 0.3388 T12: 0.0177 REMARK 3 T13: 0.2261 T23: -0.0159 REMARK 3 L TENSOR REMARK 3 L11: 4.0649 L22: 1.4036 REMARK 3 L33: 4.7833 L12: 1.5132 REMARK 3 L13: -2.5421 L23: -1.3054 REMARK 3 S TENSOR REMARK 3 S11: -0.0815 S12: -0.6327 S13: -0.0861 REMARK 3 S21: -0.0227 S22: 0.0180 S23: -0.2595 REMARK 3 S31: 0.2329 S32: 0.4278 S33: 0.0635 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 : H 23 H 114 REMARK 3 ORIGIN FOR THE GROUP (A): 18.2190 29.9330 -17.3680 REMARK 3 T TENSOR REMARK 3 T11: 0.2922 T22: 0.0534 REMARK 3 T33: 0.1666 T12: -0.0501 REMARK 3 T13: 0.1944 T23: -0.0416 REMARK 3 L TENSOR REMARK 3 L11: 2.8885 L22: 0.6136 REMARK 3 L33: 1.2110 L12: 0.5796 REMARK 3 L13: -1.5469 L23: -0.2218 REMARK 3 S TENSOR REMARK 3 S11: -0.1197 S12: 0.0037 S13: -0.0654 REMARK 3 S21: -0.2602 S22: 0.0640 S23: -0.2769 REMARK 3 S31: 0.2027 S32: 0.0770 S33: 0.0558 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 : H 115 H 202 REMARK 3 ORIGIN FOR THE GROUP (A): 40.8810 56.2170 -12.9790 REMARK 3 T TENSOR REMARK 3 T11: 0.1143 T22: 0.1048 REMARK 3 T33: 0.1228 T12: 0.0242 REMARK 3 T13: 0.0638 T23: 0.0438 REMARK 3 L TENSOR REMARK 3 L11: 1.9044 L22: 3.6462 REMARK 3 L33: 2.1828 L12: -0.1450 REMARK 3 L13: -0.3184 L23: 1.7094 REMARK 3 S TENSOR REMARK 3 S11: -0.2320 S12: -0.1603 S13: -0.0931 REMARK 3 S21: -0.0546 S22: 0.0132 S23: -0.2342 REMARK 3 S31: 0.0016 S32: 0.1356 S33: 0.2188 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 203 H 216 REMARK 3 ORIGIN FOR THE GROUP (A): 49.3780 55.1120 -9.5250 REMARK 3 T TENSOR REMARK 3 T11: 0.3320 T22: 0.4175 REMARK 3 T33: 0.3928 T12: 0.2201 REMARK 3 T13: 0.0530 T23: 0.0391 REMARK 3 L TENSOR REMARK 3 L11: 4.5066 L22: 45.8545 REMARK 3 L33: 3.9574 L12: 11.2374 REMARK 3 L13: 3.8446 L23: 9.3358 REMARK 3 S TENSOR REMARK 3 S11: -0.3914 S12: 0.1226 S13: -0.4547 REMARK 3 S21: 0.5637 S22: 0.6068 S23: -2.3690 REMARK 3 S31: -0.0350 S32: 0.5883 S33: -0.2154 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 1 L 106 REMARK 3 ORIGIN FOR THE GROUP (A): 7.5290 47.6990 -17.9170 REMARK 3 T TENSOR REMARK 3 T11: 0.1464 T22: 0.0859 REMARK 3 T33: 0.0659 T12: -0.0831 REMARK 3 T13: 0.0095 T23: -0.0124 REMARK 3 L TENSOR REMARK 3 L11: 1.4979 L22: 5.6061 REMARK 3 L33: 0.8303 L12: 0.6061 REMARK 3 L13: -0.7027 L23: -0.4188 REMARK 3 S TENSOR REMARK 3 S11: -0.1846 S12: 0.1741 S13: 0.1389 REMARK 3 S21: -0.6378 S22: 0.1339 S23: 0.1323 REMARK 3 S31: 0.0966 S32: -0.1141 S33: 0.0508 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 107 L 214 REMARK 3 ORIGIN FOR THE GROUP (A): 37.9840 66.2110 -23.9110 REMARK 3 T TENSOR REMARK 3 T11: 0.0931 T22: 0.0517 REMARK 3 T33: 0.0466 T12: -0.0141 REMARK 3 T13: 0.0177 T23: 0.0084 REMARK 3 L TENSOR REMARK 3 L11: 3.6749 L22: 1.4732 REMARK 3 L33: 1.4631 L12: -0.4022 REMARK 3 L13: -1.2713 L23: 0.0723 REMARK 3 S TENSOR REMARK 3 S11: -0.0713 S12: -0.0021 S13: -0.0614 REMARK 3 S21: -0.0509 S22: -0.0337 S23: -0.2221 REMARK 3 S31: 0.0442 S32: 0.1718 S33: 0.1051 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3PGF COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-10. REMARK 100 THE RCSB ID CODE IS RCSB062345. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-JUN-10 REMARK 200 TEMPERATURE (KELVIN) : 200 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 21-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.07817 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL REMARK 200 DATA SCALING SOFTWARE : HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74893 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 85.2 REMARK 200 DATA REDUNDANCY : 4.500 REMARK 200 R MERGE (I) : 0.06000 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) : 1.83 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86 REMARK 200 COMPLETENESS FOR SHELL (%) : 39.7 REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : 0.51600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL 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 ENTRIES 1ANF AND 2R8S REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.15 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG 3400, 8% TACSIMATE, PH 6.0, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.78500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.78500 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 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 31.93500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 114.23000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 31.93500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 114.23000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 67.78500 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 31.93500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 114.23000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 67.78500 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 31.93500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 114.23000 REMARK 290 SMTRY3 8 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7730 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 32660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL 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 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 MET A -30 REMARK 465 LYS A -29 REMARK 465 HIS A -28 REMARK 465 HIS A -27 REMARK 465 HIS A -26 REMARK 465 HIS A -25 REMARK 465 HIS A -24 REMARK 465 HIS A -23 REMARK 465 HIS A -22 REMARK 465 HIS A -21 REMARK 465 HIS A -20 REMARK 465 HIS A -19 REMARK 465 SER A -18 REMARK 465 SER A -17 REMARK 465 ASP A -16 REMARK 465 TYR A -15 REMARK 465 LYS A -14 REMARK 465 ASP A -13 REMARK 465 ASP A -12 REMARK 465 ASP A -11 REMARK 465 ASP A -10 REMARK 465 LYS A -9 REMARK 465 GLY A -8 REMARK 465 GLU A -7 REMARK 465 ASN A -6 REMARK 465 LEU A -5 REMARK 465 TYR A -4 REMARK 465 PHE A -3 REMARK 465 GLN A -2 REMARK 465 GLY A -1 REMARK 465 SER A 0 REMARK 465 GLY A 166 REMARK 465 TYR A 167 REMARK 465 ALA A 168 REMARK 465 PHE A 169 REMARK 465 LYS A 170 REMARK 465 TYR A 171 REMARK 465 GLU A 172 REMARK 465 ASN A 173 REMARK 465 GLY A 174 REMARK 465 GLU H -2 REMARK 465 ILE H -1 REMARK 465 SER H 0 REMARK 465 GLU H 1 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 THR H 221 REMARK 465 SER L 0 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 ARG A 98 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ASP A 314 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES REMARK 500 LEU H 178 CA - CB - CG ANGL. DEV. = 13.8 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 ASP A 209 -167.44 -126.26 REMARK 500 LYS A 239 -5.88 67.23 REMARK 500 PRO H 41 119.69 -37.50 REMARK 500 ALA H 88 156.24 177.42 REMARK 500 ASP H 144 62.84 65.41 REMARK 500 SER L 31 13.23 -50.69 REMARK 500 ALA L 51 -37.93 70.88 REMARK 500 LYS L 126 -20.26 -38.51 REMARK 500 ASN L 138 65.40 62.49 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 PHE H 146 PRO H 147 -30.77 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 ASP A 30 19.5 L L OUTSIDE RANGE REMARK 500 VAL H 48 23.7 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 GLC A 371 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 372 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 368 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 369 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 222 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 215 REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SAB HEAVY AND LIGHT CHAINS CONTAIN BOTH A VARIABLE DOMAIN REMARK 999 REPRESENTED BY THE SEQUENCE SELF REFERENCE AND A CONSTANT DOMAIN REMARK 999 THAT REFERENCES THE UNIPROT DATABASE