REMARK 2 REMARK 2 RESOLUTION. 2.94 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.3.0017 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) : 2.94 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5 REMARK 3 NUMBER OF REFLECTIONS : 16120 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) : 0.230 REMARK 3 R VALUE (WORKING SET) : 0.227 REMARK 3 FREE R VALUE : 0.281 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 863 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) : 2.94 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.02 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1063 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.95 REMARK 3 BIN R VALUE (WORKING SET) : 0.3800 REMARK 3 BIN FREE R VALUE SET COUNT : 56 REMARK 3 BIN FREE R VALUE : 0.5460 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6320 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 70.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.67 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 4.15000 REMARK 3 B22 (A**2) : -1.05000 REMARK 3 B33 (A**2) : -4.65000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -2.78000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.536 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.457 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 56.081 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.869 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6488 ; 0.006 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 4198 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8874 ; 0.957 ; 1.943 REMARK 3 BOND ANGLES OTHERS (DEGREES): 10324 ; 0.744 ; 3.003 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 834 ; 5.766 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 236 ;31.775 ;24.831 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 990 ;14.298 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;10.274 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1022 ; 0.056 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7206 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1220 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1204 ; 0.178 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4054 ; 0.171 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3030 ; 0.173 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 3563 ; 0.079 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 134 ; 0.129 ; 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): 21 ; 0.125 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 46 ; 0.131 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.133 ; 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): 5336 ; 0.148 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1692 ; 0.021 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6786 ; 0.184 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2800 ; 0.259 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2088 ; 0.395 ; 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 : 2 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 211 4 REMARK 3 1 A 1 A 211 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 L (A): 2619 ; 0.42 ; 0.50 REMARK 3 MEDIUM THERMAL 1 L (A**2): 2619 ; 0.10 ; 2.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 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 228 4 REMARK 3 1 B 1 B 228 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 H (A): 2640 ; 0.47 ; 0.50 REMARK 3 MEDIUM THERMAL 2 H (A**2): 2640 ; 0.09 ; 2.00 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 108 REMARK 3 ORIGIN FOR THE GROUP (A): -7.5799 -1.4292 -5.1741 REMARK 3 T TENSOR REMARK 3 T11: -0.1805 T22: -0.0318 REMARK 3 T33: -0.0650 T12: -0.1556 REMARK 3 T13: -0.0035 T23: -0.0165 REMARK 3 L TENSOR REMARK 3 L11: 4.3963 L22: 7.3807 REMARK 3 L33: 8.5970 L12: -0.9784 REMARK 3 L13: 3.0515 L23: -3.9916 REMARK 3 S TENSOR REMARK 3 S11: -0.0077 S12: 0.0947 S13: 0.2770 REMARK 3 S21: -0.5121 S22: 0.2006 S23: 0.7823 REMARK 3 S31: 0.2407 S32: -0.5352 S33: -0.1929 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 109 L 211 REMARK 3 ORIGIN FOR THE GROUP (A): 2.0486 7.2333 27.7858 REMARK 3 T TENSOR REMARK 3 T11: -0.3499 T22: -0.0211 REMARK 3 T33: -0.0543 T12: -0.1204 REMARK 3 T13: 0.0804 T23: 0.0750 REMARK 3 L TENSOR REMARK 3 L11: 2.4374 L22: 11.7941 REMARK 3 L33: 10.4015 L12: 2.3334 REMARK 3 L13: 2.3185 L23: 7.6219 REMARK 3 S TENSOR REMARK 3 S11: 0.1212 S12: -0.3440 S13: 0.1846 REMARK 3 S21: 0.3072 S22: -0.3745 S23: 0.9051 REMARK 3 S31: -0.0268 S32: -0.8007 S33: 0.2533 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): -0.8866 19.3738 -8.6858 REMARK 3 T TENSOR REMARK 3 T11: -0.0162 T22: -0.0866 REMARK 3 T33: -0.0437 T12: -0.0189 REMARK 3 T13: -0.1099 T23: 0.0854 REMARK 3 L TENSOR REMARK 3 L11: 3.1806 L22: 5.8033 REMARK 3 L33: 6.8508 L12: 1.4593 REMARK 3 L13: 1.0887 L23: 1.6768 REMARK 3 S TENSOR REMARK 3 S11: -0.4756 S12: 0.2410 S13: 0.3263 REMARK 3 S21: -0.3869 S22: 0.2442 S23: 0.4483 REMARK 3 S31: -1.0088 S32: -0.1327 S33: 0.2314 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 228 REMARK 3 ORIGIN FOR THE GROUP (A): 17.0068 12.9292 24.4130 REMARK 3 T TENSOR REMARK 3 T11: -0.1965 T22: -0.0897 REMARK 3 T33: -0.0824 T12: -0.1986 REMARK 3 T13: 0.0747 T23: -0.0575 REMARK 3 L TENSOR REMARK 3 L11: 2.1562 L22: 9.3566 REMARK 3 L33: 8.1228 L12: -0.4538 REMARK 3 L13: 1.4860 L23: 0.0272 REMARK 3 S TENSOR REMARK 3 S11: 0.1230 S12: -0.2305 S13: -0.3482 REMARK 3 S21: 0.1233 S22: -0.2125 S23: -0.4958 REMARK 3 S31: 0.3604 S32: 0.2962 S33: 0.0895 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 108 REMARK 3 ORIGIN FOR THE GROUP (A): 17.9138 -18.6505 -27.4788 REMARK 3 T TENSOR REMARK 3 T11: -0.0500 T22: -0.2598 REMARK 3 T33: -0.0404 T12: 0.0412 REMARK 3 T13: -0.0812 T23: 0.0054 REMARK 3 L TENSOR REMARK 3 L11: 3.6807 L22: 6.3238 REMARK 3 L33: 11.3008 L12: 3.0177 REMARK 3 L13: -1.8509 L23: -2.1094 REMARK 3 S TENSOR REMARK 3 S11: 0.0575 S12: -0.2336 S13: 0.3395 REMARK 3 S21: 0.8723 S22: -0.1479 S23: 0.2522 REMARK 3 S31: -0.6169 S32: 0.1284 S33: 0.0904 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 109 A 211 REMARK 3 ORIGIN FOR THE GROUP (A): -1.7947 -20.9638 -57.3275 REMARK 3 T TENSOR REMARK 3 T11: -0.1034 T22: 0.1327 REMARK 3 T33: -0.0569 T12: 0.0222 REMARK 3 T13: 0.0259 T23: -0.0278 REMARK 3 L TENSOR REMARK 3 L11: 7.6895 L22: 3.4166 REMARK 3 L33: 5.9611 L12: 2.7639 REMARK 3 L13: 2.8880 L23: 2.8781 REMARK 3 S TENSOR REMARK 3 S11: -0.1316 S12: -0.1641 S13: 0.4559 REMARK 3 S21: -0.0503 S22: -0.2819 S23: 0.3584 REMARK 3 S31: -0.7956 S32: -1.0599 S33: 0.4135 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): 5.3410 -35.8577 -21.7836 REMARK 3 T TENSOR REMARK 3 T11: 0.0483 T22: -0.0500 REMARK 3 T33: -0.0543 T12: -0.0505 REMARK 3 T13: 0.1311 T23: 0.0208 REMARK 3 L TENSOR REMARK 3 L11: 3.2463 L22: 2.7988 REMARK 3 L33: 8.7017 L12: 1.1728 REMARK 3 L13: 1.1219 L23: -2.2443 REMARK 3 S TENSOR REMARK 3 S11: -0.0035 S12: -0.0761 S13: -0.1274 REMARK 3 S21: 0.1614 S22: 0.1966 S23: 0.3450 REMARK 3 S31: 0.3601 S32: -1.0761 S33: -0.1931 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 228 REMARK 3 ORIGIN FOR THE GROUP (A): -0.0123 -36.9630 -59.3793 REMARK 3 T TENSOR REMARK 3 T11: 0.0143 T22: -0.1246 REMARK 3 T33: -0.0278 T12: -0.0631 REMARK 3 T13: -0.0360 T23: -0.0189 REMARK 3 L TENSOR REMARK 3 L11: 5.0976 L22: 2.0836 REMARK 3 L33: 8.2524 L12: 1.1156 REMARK 3 L13: -0.3189 L23: 0.4529 REMARK 3 S TENSOR REMARK 3 S11: 0.3046 S12: -0.1799 S13: -0.2862 REMARK 3 S21: -0.0189 S22: -0.4048 S23: 0.0782 REMARK 3 S31: 0.3710 S32: -0.5552 S33: 0.1002 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. CNS WAS ALSO USED FOR THE REFINEMENT. REMARK 4 REMARK 4 3MJ8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-10. REMARK 100 THE RCSB ID CODE IS RCSB058612. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-JUL-06 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 4.60 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946 REMARK 200 MONOCHROMATOR : SIDE SCATTERING BENT CUBE- ROOT REMARK 200 I-BEAM SINGLE CRYSTAL, ASYMMETRIC REMARK 200 CUT 4.965 DEGS REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING), REMARK 200 SINGLE CRYSTAL SI(111) BENT REMARK 200 MONOCHROMATOR (HORIZONTAL REMARK 200 FOCUSING) REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17012 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.940 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3 REMARK 200 DATA REDUNDANCY : 2.300 REMARK 200 R MERGE (I) : 0.10500 REMARK 200 R SYM (I) : 0.10500 REMARK 200 FOR THE DATA SET : 7.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.94 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.54100 REMARK 200 R SYM FOR SHELL (I) : 0.54100 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: HL4E10 LIGHT CHAIN SEQUENCE THREADED ONTO 1W72, REMARK 200 HL4E10 HEAVY CHAIN SEQUENCE THREADED ONTO 2ARJ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.96 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10-12.5 % PEG 4000, 0.1 M NA- ACETATE, REMARK 280 0.2 M (NH4)2SO4, PH 4.60, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 295K 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 74.38400 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19960 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3410 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19800 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 SER L 212 REMARK 465 ALA L 213 REMARK 465 CYS L 214 REMARK 465 SER L 215 REMARK 465 ASP H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 THR H 132 REMARK 465 SER H 133 REMARK 465 THR H 134 REMARK 465 THR H 135 REMARK 465 ASP H 229 REMARK 465 GLY H 230 REMARK 465 SER H 231 REMARK 465 GLY H 232 REMARK 465 CYS H 233 REMARK 465 SER A 212 REMARK 465 ALA A 213 REMARK 465 CYS A 214 REMARK 465 SER A 215 REMARK 465 ASP B 129 REMARK 465 SER B 130 REMARK 465 THR B 131 REMARK 465 THR B 132 REMARK 465 SER B 133 REMARK 465 THR B 134 REMARK 465 THR B 135 REMARK 465 ASP B 229 REMARK 465 GLY B 230 REMARK 465 SER B 231 REMARK 465 GLY B 232 REMARK 465 CYS B 233 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 13 125.54 -171.14 REMARK 500 ALA L 40 124.39 -31.49 REMARK 500 ASP L 51 -61.06 66.51 REMARK 500 ASN L 52 56.19 -145.17 REMARK 500 ALA L 84 174.99 177.77 REMARK 500 THR L 94 -48.88 -29.47 REMARK 500 SER L 95A 100.69 -48.87 REMARK 500 PRO L 154 122.65 -35.06 REMARK 500 ASP L 170 -74.54 57.04 REMARK 500 PRO H 14 8.71 -61.28 REMARK 500 ARG H 66 32.23 -157.42 REMARK 500 SER H 82B 73.77 60.82 REMARK 500 TYR H 97 -118.75 54.51 REMARK 500 ASP A 51 -54.96 69.92 REMARK 500 ASN A 52 52.91 -150.10 REMARK 500 PRO A 154 105.43 -45.83 REMARK 500 ASP A 170 -122.60 59.25 REMARK 500 LEU A 209 109.04 -169.78 REMARK 500 PRO B 14 48.88 -63.37 REMARK 500 SER B 15 -45.88 -153.68 REMARK 500 PRO B 41 113.06 -37.78 REMARK 500 ARG B 66 22.35 -161.15 REMARK 500 TYR B 97 -133.95 57.48 REMARK 500 ALA B 127 -149.57 -80.47 REMARK 500 ASN B 162 52.42 37.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3MJ6 RELATED DB: PDB REMARK 900 RELATED ID: 3MJ7 RELATED DB: PDB REMARK 900 RELATED ID: 3MJ9 RELATED DB: PDB