REMARK 2 REMARK 2 RESOLUTION. 2.36 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) : 2.36 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.42 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 3 NUMBER OF REFLECTIONS : 39136 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) : 0.187 REMARK 3 R VALUE (WORKING SET) : 0.184 REMARK 3 FREE R VALUE : 0.242 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2091 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.36 REMARK 3 BIN RESOLUTION RANGE LOW : 2.42 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2161 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2010 REMARK 3 BIN FREE R VALUE SET COUNT : 120 REMARK 3 BIN FREE R VALUE : 0.2510 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6698 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 488 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : 41.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.19 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.18000 REMARK 3 B22 (A**2) : 0.06000 REMARK 3 B33 (A**2) : -0.24000 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): 0.371 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.251 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.174 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.513 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946 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): 6893 ; 0.014 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9411 ; 1.501 ; 1.950 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 882 ; 6.491 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 275 ;35.931 ;24.400 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1102 ;14.303 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;16.083 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1048 ; 0.089 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5234 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2902 ; 0.188 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4581 ; 0.297 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 522 ; 0.125 ; 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 ; 0.210 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 33 ; 0.190 ; 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): 4483 ; 0.551 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7110 ; 0.906 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2795 ; 1.416 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2285 ; 2.189 ; 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 : 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 : H 1 H 113 REMARK 3 ORIGIN FOR THE GROUP (A): 28.8700 -10.4960 -47.6860 REMARK 3 T TENSOR REMARK 3 T11: 0.1438 T22: -0.2288 REMARK 3 T33: -0.2615 T12: 0.0260 REMARK 3 T13: 0.1182 T23: 0.0134 REMARK 3 L TENSOR REMARK 3 L11: 2.6886 L22: 5.7158 REMARK 3 L33: 5.9209 L12: -1.3998 REMARK 3 L13: 1.3658 L23: -3.7755 REMARK 3 S TENSOR REMARK 3 S11: -0.0684 S12: 0.0984 S13: -0.0423 REMARK 3 S21: -1.0551 S22: -0.1304 S23: -0.3267 REMARK 3 S31: 1.0128 S32: 0.1317 S33: 0.1988 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 : H 114 H 216 REMARK 3 ORIGIN FOR THE GROUP (A): 19.3600 -12.2430 -12.2100 REMARK 3 T TENSOR REMARK 3 T11: -0.0916 T22: -0.1154 REMARK 3 T33: -0.2271 T12: 0.0009 REMARK 3 T13: -0.0261 T23: 0.0008 REMARK 3 L TENSOR REMARK 3 L11: 0.7524 L22: 2.8026 REMARK 3 L33: 4.3705 L12: -0.4661 REMARK 3 L13: -0.8653 L23: 0.7941 REMARK 3 S TENSOR REMARK 3 S11: 0.0553 S12: -0.0232 S13: -0.0434 REMARK 3 S21: 0.1696 S22: -0.1214 S23: 0.0832 REMARK 3 S31: -0.0256 S32: -0.2494 S33: 0.0660 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 : I 1 I 113 REMARK 3 ORIGIN FOR THE GROUP (A): 68.5030 10.6650 -5.4780 REMARK 3 T TENSOR REMARK 3 T11: 0.1326 T22: -0.0751 REMARK 3 T33: -0.2145 T12: -0.1564 REMARK 3 T13: -0.1055 T23: 0.0399 REMARK 3 L TENSOR REMARK 3 L11: 2.3607 L22: 3.9212 REMARK 3 L33: 5.2977 L12: 1.2975 REMARK 3 L13: -1.5668 L23: -2.6570 REMARK 3 S TENSOR REMARK 3 S11: 0.1343 S12: -0.1923 S13: -0.0326 REMARK 3 S21: 0.6482 S22: -0.4167 S23: -0.2373 REMARK 3 S31: -0.8318 S32: 0.6082 S33: 0.2825 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 : I 114 I 216 REMARK 3 ORIGIN FOR THE GROUP (A): 59.8130 11.1270 -40.8860 REMARK 3 T TENSOR REMARK 3 T11: 0.0265 T22: -0.1097 REMARK 3 T33: -0.2022 T12: 0.0111 REMARK 3 T13: 0.0272 T23: 0.0312 REMARK 3 L TENSOR REMARK 3 L11: 1.0933 L22: 2.2373 REMARK 3 L33: 3.9552 L12: 0.1204 REMARK 3 L13: 0.5339 L23: 0.7531 REMARK 3 S TENSOR REMARK 3 S11: -0.0771 S12: -0.0095 S13: -0.0305 REMARK 3 S21: -0.0176 S22: 0.0655 S23: -0.0144 REMARK 3 S31: -0.1834 S32: -0.1017 S33: 0.0116 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 : L 1 L 107 REMARK 3 ORIGIN FOR THE GROUP (A): 23.0220 12.4150 -41.6100 REMARK 3 T TENSOR REMARK 3 T11: 0.0662 T22: -0.1935 REMARK 3 T33: -0.2618 T12: 0.0709 REMARK 3 T13: -0.0312 T23: -0.0049 REMARK 3 L TENSOR REMARK 3 L11: 2.4148 L22: 5.5651 REMARK 3 L33: 4.9400 L12: -1.0730 REMARK 3 L13: -0.0772 L23: -1.9500 REMARK 3 S TENSOR REMARK 3 S11: -0.2467 S12: -0.1064 S13: 0.1954 REMARK 3 S21: 0.4038 S22: 0.2834 S23: -0.1454 REMARK 3 S31: -0.7853 S32: -0.3981 S33: -0.0367 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 : L 108 L 214 REMARK 3 ORIGIN FOR THE GROUP (A): 29.1000 -0.0080 -7.3480 REMARK 3 T TENSOR REMARK 3 T11: -0.0173 T22: -0.1272 REMARK 3 T33: -0.2473 T12: -0.0559 REMARK 3 T13: -0.0286 T23: -0.0115 REMARK 3 L TENSOR REMARK 3 L11: 2.3351 L22: 3.7044 REMARK 3 L33: 4.9701 L12: -2.1024 REMARK 3 L13: 1.2591 L23: -1.9333 REMARK 3 S TENSOR REMARK 3 S11: 0.0304 S12: 0.0217 S13: 0.0494 REMARK 3 S21: 0.2391 S22: -0.0501 S23: -0.1487 REMARK 3 S31: -0.5228 S32: 0.2580 S33: 0.0196 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 : M 1 M 107 REMARK 3 ORIGIN FOR THE GROUP (A): 60.9870 -12.1110 -10.5930 REMARK 3 T TENSOR REMARK 3 T11: 0.0380 T22: -0.0980 REMARK 3 T33: -0.1753 T12: -0.0037 REMARK 3 T13: 0.0386 T23: 0.0417 REMARK 3 L TENSOR REMARK 3 L11: 1.1878 L22: 2.8679 REMARK 3 L33: 3.2528 L12: 0.6755 REMARK 3 L13: 0.5032 L23: -0.1816 REMARK 3 S TENSOR REMARK 3 S11: -0.1067 S12: -0.0528 S13: -0.0926 REMARK 3 S21: -0.0288 S22: -0.0461 S23: -0.1258 REMARK 3 S31: 0.2432 S32: -0.0623 S33: 0.1528 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 : M 108 M 214 REMARK 3 ORIGIN FOR THE GROUP (A): 69.2760 -1.7860 -44.9260 REMARK 3 T TENSOR REMARK 3 T11: -0.0024 T22: -0.1143 REMARK 3 T33: -0.1813 T12: 0.0649 REMARK 3 T13: 0.0351 T23: -0.0033 REMARK 3 L TENSOR REMARK 3 L11: 3.1752 L22: 3.4179 REMARK 3 L33: 6.1679 L12: 2.1523 REMARK 3 L13: -2.9985 L23: -2.1737 REMARK 3 S TENSOR REMARK 3 S11: -0.1242 S12: -0.1186 S13: -0.1757 REMARK 3 S21: -0.1294 S22: 0.0274 S23: -0.2784 REMARK 3 S31: 0.4089 S32: 0.4461 S33: 0.0968 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 : 1.40 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 REMARK 3 RIDING POSITIONS. MOLECULE A (CHAINS H AND L) AND A REMARK 3 CRYSTALLOGRAPHIC SYMMETRY MATE OF MOLECULE B (CHAINS I AND M) REMARK 3 ARE RELATED BY TRANSLATIONAL PSEUDO-SYMMETRY. MOLECULE A IS REMARK 3 TRANSFORMED ONTO MOLECULE B_SYM BY ROTATION OF 4.4 DEGREES REMARK 3 ABOUT AN AXIS WITH DIRECTION COSINES (-0.6574, 0.3326, 0. REMARK 3 6762) FOLLOWED BY TRANSLATION OF (0.7249, 46.9819, 53.2092) REMARK 3 ANGSTROM UNITS. REMARK 4 REMARK 4 2VXU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUL-08. REMARK 100 THE PDBE ID CODE IS EBI-36816. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-MAR-03 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 : APS REMARK 200 BEAMLINE : 17-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00 REMARK 200 MONOCHROMATOR : SI 111 REMARK 200 OPTICS : MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41229 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.33 REMARK 200 RESOLUTION RANGE LOW (A) : 17.50 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0 REMARK 200 DATA REDUNDANCY : 5.2 REMARK 200 R MERGE (I) : 0.05 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 18.90 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39 REMARK 200 COMPLETENESS FOR SHELL (%) : 25.2 REMARK 200 DATA REDUNDANCY IN SHELL : 2.4 REMARK 200 R MERGE FOR SHELL (I) : 0.24 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.90 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 1FNS REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.3 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: FAB (13 MG/ML, 2 MICROLITERS REMARK 280 [UL]) WAS MIXED WITH 2 UL OF RESERVOIR (10% REMARK 280 POLYETHYLENEGLYCOL (PEG) 6000, 100 MM HEPES, PH 7.5, 5% 2, REMARK 280 4-METHYLPENTANEDIOL) AND SUSPENDED OVER THE RESERVOIR AT REMARK 280 277 K. ROD-LIKE CRYSTALS APPEARED WITHIN ONE DAY. 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 39.53050 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.82250 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.24500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.82250 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.53050 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.24500 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 4000 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.1 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 3950 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24950 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.4 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ASP H 31 CG ASP H 31 OD1 0.206 REMARK 500 ASN H 54 CA ASN H 54 C 0.190 REMARK 500 ASN H 54 CB ASN H 54 CG 0.193 REMARK 500 ASN H 54 CG ASN H 54 ND2 -0.175 REMARK 500 GLY H 55 N GLY H 55 CA 0.120 REMARK 500 ASP H 72 CB ASP H 72 CG 0.192 REMARK 500 ASP H 72 CG ASP H 72 OD1 0.150 REMARK 500 ASP H 72 CG ASP H 72 OD2 0.153 REMARK 500 SER H 74 CB SER H 74 OG 0.157 REMARK 500 SER H 74 C SER H 74 O -0.119 REMARK 500 GLN H 73 C SER H 74 N 0.149 REMARK 500 SER H 74 C SER H 75 N 0.301 REMARK 500 SER L 14 CA SER L 14 CB 0.160 REMARK 500 LYS L 107 CB LYS L 107 CG 0.179 REMARK 500 LYS L 107 CD LYS L 107 CE 0.253 REMARK 500 REMARK 500 REMARK: NULL 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 ASP H 31 CB - CG - OD1 ANGL. DEV. = 11.9 DEGREES REMARK 500 ASP H 72 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES REMARK 500 ASP H 72 CB - CG - OD2 ANGL. DEV. = -11.3 DEGREES REMARK 500 LEU M 104 CA - CB - CG ANGL. DEV. = 14.6 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 SER H 28 95.55 -69.77 REMARK 500 HIS H 41 0.80 57.18 REMARK 500 LYS H 43 -57.17 -130.30 REMARK 500 ALA H 88 -179.29 177.18 REMARK 500 ASP H 173 -6.23 74.07 REMARK 500 HIS I 41 19.20 50.06 REMARK 500 LYS I 43 -65.08 -146.95 REMARK 500 ASN I 54 -13.42 -149.60 REMARK 500 GLN I 171 75.37 -102.29 REMARK 500 SER I 172 72.99 59.08 REMARK 500 ASP I 173 -14.86 76.40 REMARK 500 THR L 51 -44.71 73.42 REMARK 500 VAL L 84 -155.00 -136.24 REMARK 500 THR M 51 -48.31 73.50 REMARK 500 SER M 77 94.63 -161.97 REMARK 500 VAL M 84 -158.00 -134.89 REMARK 500 ASN M 190 -60.32 -108.43 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 LYS H 43 25.0 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 700 REMARK 700 SHEET REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, REMARK 700 TWO SHEETS ARE DEFINED. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2VXT RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN IL-18 COMPLEXED REMARK 900 TO MURINE REFERENCE ANTIBODY 125-2H FAB REMARK 900 RELATED ID: 2VXV RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN IGG ABT-325 FAB REMARK 900 FRAGMENT