REMARK 2 REMARK 2 RESOLUTION. 2.18 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) : 2.18 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.27 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 91.9 REMARK 3 NUMBER OF REFLECTIONS : 37589 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) : 0.204 REMARK 3 R VALUE (WORKING SET) : 0.201 REMARK 3 FREE R VALUE : 0.256 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1994 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) : 2.18 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.24 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2392 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.58 REMARK 3 BIN R VALUE (WORKING SET) : 0.2600 REMARK 3 BIN FREE R VALUE SET COUNT : 127 REMARK 3 BIN FREE R VALUE : 0.3220 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6538 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 38 REMARK 3 SOLVENT ATOMS : 162 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.44 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.03000 REMARK 3 B22 (A**2) : 0.14000 REMARK 3 B33 (A**2) : -0.17000 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): 0.366 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.248 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.184 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.166 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6746 ; 0.014 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 4472 ; 0.008 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9192 ; 1.527 ; 1.961 REMARK 3 BOND ANGLES OTHERS (DEGREES): 10948 ; 0.867 ; 3.004 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 854 ; 6.840 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 256 ;37.324 ;24.766 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1068 ;16.063 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;16.337 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1032 ; 0.085 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7476 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1282 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1063 ; 0.192 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4314 ; 0.204 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3153 ; 0.182 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 3779 ; 0.092 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 249 ; 0.141 ; 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): 16 ; 0.240 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 36 ; 0.222 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.283 ; 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): 5381 ; 1.461 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1736 ; 0.157 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6932 ; 1.249 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2971 ; 2.694 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2260 ; 3.486 ; 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 : 4 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : L A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 L 1 L 107 6 REMARK 3 1 A 1 A 107 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 LOOSE POSITIONAL 1 A (A): 1469 ; 0.24 ; 5.00 REMARK 3 LOOSE THERMAL 1 H (A**2): 1469 ; 1.00 ; 10.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : L A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 L 108 L 211 6 REMARK 3 1 A 108 A 211 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 LOOSE POSITIONAL 2 A (A): 1359 ; 0.35 ; 5.00 REMARK 3 LOOSE THERMAL 2 B (A**2): 1359 ; 1.05 ; 10.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : H B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 H 1 H 113 6 REMARK 3 1 B 1 B 113 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 LOOSE POSITIONAL 3 A (A): 1538 ; 0.18 ; 5.00 REMARK 3 LOOSE THERMAL 3 H (A**2): 1538 ; 0.82 ; 10.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : H B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 H 114 H 227 6 REMARK 3 1 B 114 B 227 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 LOOSE POSITIONAL 4 A (A): 1128 ; 0.23 ; 5.00 REMARK 3 LOOSE THERMAL 4 B (A**2): 1128 ; 0.93 ; 10.00 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 : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 1 L 107 REMARK 3 ORIGIN FOR THE GROUP (A): -32.2295 -7.5074 37.0396 REMARK 3 T TENSOR REMARK 3 T11: -0.2892 T22: -0.1995 REMARK 3 T33: -0.2313 T12: 0.0021 REMARK 3 T13: 0.0056 T23: 0.0047 REMARK 3 L TENSOR REMARK 3 L11: 1.4933 L22: 3.3984 REMARK 3 L33: 1.7625 L12: -0.7076 REMARK 3 L13: -0.0798 L23: 1.0071 REMARK 3 S TENSOR REMARK 3 S11: 0.0119 S12: -0.0569 S13: -0.0336 REMARK 3 S21: 0.0765 S22: -0.0968 S23: 0.0320 REMARK 3 S31: 0.0354 S32: 0.0309 S33: 0.0849 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 : L 108 L 211 REMARK 3 ORIGIN FOR THE GROUP (A): -17.1385 -26.6042 8.1054 REMARK 3 T TENSOR REMARK 3 T11: -0.2084 T22: -0.1645 REMARK 3 T33: -0.1585 T12: 0.0352 REMARK 3 T13: 0.0174 T23: -0.0249 REMARK 3 L TENSOR REMARK 3 L11: 2.1187 L22: 2.2174 REMARK 3 L33: 8.1600 L12: -0.6320 REMARK 3 L13: -0.1854 L23: -0.5169 REMARK 3 S TENSOR REMARK 3 S11: 0.2054 S12: 0.3054 S13: -0.0327 REMARK 3 S21: -0.4174 S22: -0.0681 S23: -0.2058 REMARK 3 S31: 0.0772 S32: 0.7530 S33: -0.1374 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 : H 1 H 113 REMARK 3 ORIGIN FOR THE GROUP (A): -39.7625 4.5364 20.7608 REMARK 3 T TENSOR REMARK 3 T11: -0.2384 T22: -0.2819 REMARK 3 T33: -0.2137 T12: -0.0096 REMARK 3 T13: -0.0341 T23: -0.0219 REMARK 3 L TENSOR REMARK 3 L11: 2.4849 L22: 1.2986 REMARK 3 L33: 3.8656 L12: -0.4828 REMARK 3 L13: -2.0563 L23: -0.1285 REMARK 3 S TENSOR REMARK 3 S11: 0.0068 S12: 0.0053 S13: 0.1376 REMARK 3 S21: -0.1851 S22: 0.0306 S23: 0.1136 REMARK 3 S31: -0.0505 S32: 0.0797 S33: -0.0373 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 114 H 221 REMARK 3 ORIGIN FOR THE GROUP (A): -31.8509 -19.5780 3.8921 REMARK 3 T TENSOR REMARK 3 T11: -0.1323 T22: -0.1470 REMARK 3 T33: -0.1736 T12: 0.0360 REMARK 3 T13: -0.0797 T23: -0.0420 REMARK 3 L TENSOR REMARK 3 L11: 2.6963 L22: 7.3183 REMARK 3 L33: 2.3017 L12: 1.0244 REMARK 3 L13: -1.2285 L23: -1.2503 REMARK 3 S TENSOR REMARK 3 S11: -0.0468 S12: 0.0515 S13: -0.3195 REMARK 3 S21: -0.3383 S22: 0.0463 S23: 0.5248 REMARK 3 S31: 0.1621 S32: -0.1259 S33: 0.0005 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 1 A 107 REMARK 3 ORIGIN FOR THE GROUP (A): -9.1401 11.3503 37.0343 REMARK 3 T TENSOR REMARK 3 T11: -0.2314 T22: -0.2175 REMARK 3 T33: -0.2360 T12: 0.0023 REMARK 3 T13: 0.0033 T23: -0.0137 REMARK 3 L TENSOR REMARK 3 L11: 2.0781 L22: 3.5050 REMARK 3 L33: 2.6792 L12: -0.8691 REMARK 3 L13: -0.7274 L23: -0.1135 REMARK 3 S TENSOR REMARK 3 S11: 0.1200 S12: 0.0488 S13: 0.1475 REMARK 3 S21: -0.0420 S22: -0.1204 S23: -0.0764 REMARK 3 S31: -0.2622 S32: -0.1950 S33: 0.0004 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 108 A 211 REMARK 3 ORIGIN FOR THE GROUP (A): -24.0228 29.7568 7.6378 REMARK 3 T TENSOR REMARK 3 T11: -0.1942 T22: -0.1274 REMARK 3 T33: -0.1045 T12: 0.0037 REMARK 3 T13: -0.0149 T23: 0.0438 REMARK 3 L TENSOR REMARK 3 L11: 1.7755 L22: 1.7932 REMARK 3 L33: 8.7897 L12: -0.1238 REMARK 3 L13: -0.6835 L23: 0.5922 REMARK 3 S TENSOR REMARK 3 S11: 0.0331 S12: 0.2814 S13: 0.1458 REMARK 3 S21: -0.2802 S22: -0.0111 S23: 0.2033 REMARK 3 S31: 0.0387 S32: -0.6221 S33: -0.0220 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 : B 1 B 113 REMARK 3 ORIGIN FOR THE GROUP (A): -1.4248 -0.8467 20.9329 REMARK 3 T TENSOR REMARK 3 T11: -0.2158 T22: -0.2513 REMARK 3 T33: -0.2163 T12: -0.0213 REMARK 3 T13: 0.0589 T23: 0.0170 REMARK 3 L TENSOR REMARK 3 L11: 2.1480 L22: 1.3373 REMARK 3 L33: 3.7719 L12: -0.2640 REMARK 3 L13: 1.8261 L23: 0.2880 REMARK 3 S TENSOR REMARK 3 S11: -0.0007 S12: 0.0810 S13: -0.0647 REMARK 3 S21: -0.1291 S22: 0.0071 S23: -0.1550 REMARK 3 S31: 0.0723 S32: -0.0750 S33: -0.0063 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 : B 114 B 221 REMARK 3 ORIGIN FOR THE GROUP (A): -9.0207 23.1954 3.8464 REMARK 3 T TENSOR REMARK 3 T11: -0.1200 T22: -0.1120 REMARK 3 T33: -0.1822 T12: 0.0260 REMARK 3 T13: 0.0616 T23: 0.0564 REMARK 3 L TENSOR REMARK 3 L11: 2.5533 L22: 8.1162 REMARK 3 L33: 1.3282 L12: 1.9087 REMARK 3 L13: 0.8607 L23: 0.7050 REMARK 3 S TENSOR REMARK 3 S11: -0.0342 S12: -0.0691 S13: 0.2570 REMARK 3 S21: -0.2635 S22: -0.0670 S23: -0.4920 REMARK 3 S31: -0.0087 S32: 0.1680 S33: 0.1012 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3FO2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-DEC-08. REMARK 100 THE RCSB ID CODE IS RCSB050828. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-OCT-06 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED REMARK 200 SI(111) REMARK 200 OPTICS : ADJUSTABLE FOCUSING MIRRORS IN K REMARK 200 -B GEOMETRY REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39309 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.180 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.8 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.09300 REMARK 200 FOR THE DATA SET : 15.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.20 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.61300 REMARK 200 FOR SHELL : 2.200 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 2GJZ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.62 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.1M TRIS-HCL, PH 8.5, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K 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 41.55800 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.82150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.11000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.82150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.55800 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.11000 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3350 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19400 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.8 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, B, H, A 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3340 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19450 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.4 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, B, 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 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 GLY L 217 REMARK 465 GLU L 218 REMARK 465 CYS L 219 REMARK 465 SER H 135 REMARK 465 SER H 136 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 LYS H 222 REMARK 465 SER H 223 REMARK 465 CYS H 224 REMARK 465 ASP H 225 REMARK 465 LYS H 226 REMARK 465 THR H 227 REMARK 465 HIS H 228 REMARK 465 THR H 229 REMARK 465 GLY A 217 REMARK 465 GLU A 218 REMARK 465 CYS A 219 REMARK 465 SER B 135 REMARK 465 SER B 136 REMARK 465 LYS B 137 REMARK 465 SER B 138 REMARK 465 THR B 139 REMARK 465 SER B 140 REMARK 465 GLY B 141 REMARK 465 LYS B 222 REMARK 465 SER B 223 REMARK 465 CYS B 224 REMARK 465 ASP B 225 REMARK 465 LYS B 226 REMARK 465 THR B 227 REMARK 465 HIS B 228 REMARK 465 THR B 229 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 CYS A 199 CB CYS A 199 SG -0.105 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 VAL L 56 -51.16 72.75 REMARK 500 ASP L 156 48.66 39.68 REMARK 500 SER H 15 -20.02 74.80 REMARK 500 ASP H 88 -33.29 -39.75 REMARK 500 TYR H 102 -69.34 -106.41 REMARK 500 VAL A 56 -55.19 75.57 REMARK 500 ARG A 82 84.09 84.80 REMARK 500 ASN A 143 66.92 62.08 REMARK 500 SER B 15 -19.01 81.08 REMARK 500 TYR B 102 -64.54 -109.25 REMARK 500 ASP B 152 62.45 64.45 REMARK 500 THR B 168 -42.48 -134.02 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 BZH H 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BZH A 401 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3FO0 RELATED DB: PDB REMARK 900 HAPTEN COMPLEX OF CATALYTIC ELIMINATION ANTIBODY 13G5 (WILD REMARK 900 -TYPE) REMARK 900 RELATED ID: 3FO1 RELATED DB: PDB REMARK 900 HAPTEN COMPLEX OF CATALYTIC ELIMINATION ANTIBODY 13G5 REMARK 900 (GLU(L39)ALA MUTANT) REMARK 900 RELATED ID: 2GJZ RELATED DB: PDB REMARK 900 CATALYTIC ELIMINATION ANTIBODY 13G5 FROM A CRYSTAL IN SPACE REMARK 900 GROUP P2(1) REMARK 900 RELATED ID: 2GK0 RELATED DB: PDB REMARK 900 CATALYTIC ELIMINATION ANTIBODY 13G5 FROM A TWINNED CRYSTAL REMARK 900 IN SPACE GROUP C2 REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCES OF THE FAB COMPLEXES ARE NOT REMARK 999 AVAILABLE IN ANY SEQUENCE DATABASES.