REMARK 2 REMARK 2 RESOLUTION. 1.80 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) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.78 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 3 NUMBER OF REFLECTIONS : 72513 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) : 0.173 REMARK 3 R VALUE (WORKING SET) : 0.172 REMARK 3 FREE R VALUE : 0.204 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 3774 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) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85 REMARK 3 REFLECTION IN BIN (WORKING SET) : 5211 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.50 REMARK 3 BIN R VALUE (WORKING SET) : 0.2010 REMARK 3 BIN FREE R VALUE SET COUNT : 271 REMARK 3 BIN FREE R VALUE : 0.2690 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6441 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 18 REMARK 3 SOLVENT ATOMS : 442 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : 21.64 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.28 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.33000 REMARK 3 B22 (A**2) : -0.28000 REMARK 3 B33 (A**2) : -0.01000 REMARK 3 B12 (A**2) : -0.58000 REMARK 3 B13 (A**2) : -0.80000 REMARK 3 B23 (A**2) : 0.80000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.128 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.118 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.002 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6922 ; 0.009 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9525 ; 1.470 ; 1.950 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 917 ; 6.676 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 234 ;33.570 ;24.145 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1046 ;13.785 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;16.941 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1092 ; 0.099 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5238 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2865 ; 0.200 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4718 ; 0.304 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 433 ; 0.122 ; 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): 77 ; 0.194 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.144 ; 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): 4561 ; 0.758 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7320 ; 1.223 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2745 ; 1.941 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2203 ; 2.953 ; 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 : 10 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): 20.5038 -4.6512 53.4750 REMARK 3 T TENSOR REMARK 3 T11: -0.2256 T22: -0.1782 REMARK 3 T33: -0.1581 T12: 0.0232 REMARK 3 T13: 0.0122 T23: -0.0022 REMARK 3 L TENSOR REMARK 3 L11: 4.0694 L22: 2.2443 REMARK 3 L33: 0.8707 L12: 0.0730 REMARK 3 L13: 0.8384 L23: -0.0473 REMARK 3 S TENSOR REMARK 3 S11: -0.0390 S12: -0.0790 S13: 0.0017 REMARK 3 S21: -0.0154 S22: 0.0110 S23: 0.0373 REMARK 3 S31: 0.0099 S32: -0.0679 S33: 0.0280 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 210 REMARK 3 ORIGIN FOR THE GROUP (A): 25.9234 26.7813 50.4630 REMARK 3 T TENSOR REMARK 3 T11: -0.1132 T22: -0.1651 REMARK 3 T33: -0.1354 T12: 0.0215 REMARK 3 T13: 0.0001 T23: -0.0046 REMARK 3 L TENSOR REMARK 3 L11: 1.6005 L22: 5.5299 REMARK 3 L33: 0.5237 L12: -1.9319 REMARK 3 L13: -0.0719 L23: 0.0273 REMARK 3 S TENSOR REMARK 3 S11: 0.0146 S12: 0.0306 S13: -0.0683 REMARK 3 S21: 0.0739 S22: -0.0467 S23: 0.0772 REMARK 3 S31: -0.0640 S32: -0.0498 S33: 0.0321 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): 9.4994 -1.4190 34.7773 REMARK 3 T TENSOR REMARK 3 T11: -0.1579 T22: -0.1369 REMARK 3 T33: -0.1364 T12: 0.0053 REMARK 3 T13: -0.0086 T23: -0.0314 REMARK 3 L TENSOR REMARK 3 L11: 2.1274 L22: 3.5276 REMARK 3 L33: 2.6453 L12: 0.0518 REMARK 3 L13: 0.0522 L23: -1.5224 REMARK 3 S TENSOR REMARK 3 S11: 0.0336 S12: 0.1544 S13: -0.0251 REMARK 3 S21: -0.2373 S22: 0.0469 S23: 0.0144 REMARK 3 S31: 0.1139 S32: -0.0843 S33: -0.0805 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 213 REMARK 3 ORIGIN FOR THE GROUP (A): 29.8968 27.6487 34.5934 REMARK 3 T TENSOR REMARK 3 T11: -0.1171 T22: -0.1841 REMARK 3 T33: -0.1154 T12: 0.0260 REMARK 3 T13: -0.0264 T23: -0.0078 REMARK 3 L TENSOR REMARK 3 L11: 4.4521 L22: 3.2364 REMARK 3 L33: 4.7819 L12: 0.1010 REMARK 3 L13: 1.7363 L23: 0.1442 REMARK 3 S TENSOR REMARK 3 S11: -0.1767 S12: -0.1233 S13: 0.1653 REMARK 3 S21: 0.0553 S22: 0.1219 S23: -0.1820 REMARK 3 S31: -0.1591 S32: 0.2219 S33: 0.0548 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 : P 1 P 8 REMARK 3 ORIGIN FOR THE GROUP (A): 6.3803 -16.4859 46.6509 REMARK 3 T TENSOR REMARK 3 T11: 0.0391 T22: -0.0562 REMARK 3 T33: 0.0580 T12: -0.0267 REMARK 3 T13: -0.0171 T23: 0.0015 REMARK 3 L TENSOR REMARK 3 L11: 2.9270 L22: 7.2931 REMARK 3 L33: 34.3760 L12: -0.4770 REMARK 3 L13: 7.0439 L23: 10.0650 REMARK 3 S TENSOR REMARK 3 S11: 0.0231 S12: -0.6640 S13: -0.4568 REMARK 3 S21: 0.6109 S22: 0.0468 S23: 0.0662 REMARK 3 S31: 2.0749 S32: -0.4325 S33: -0.0699 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 : M 2 M 108 REMARK 3 ORIGIN FOR THE GROUP (A): 29.3034 -13.0679 73.5812 REMARK 3 T TENSOR REMARK 3 T11: -0.1171 T22: -0.1561 REMARK 3 T33: -0.1549 T12: -0.0018 REMARK 3 T13: 0.0080 T23: -0.0048 REMARK 3 L TENSOR REMARK 3 L11: 1.8840 L22: 2.6861 REMARK 3 L33: 3.7045 L12: 1.1269 REMARK 3 L13: 0.7929 L23: 0.2463 REMARK 3 S TENSOR REMARK 3 S11: 0.0728 S12: -0.1950 S13: 0.0553 REMARK 3 S21: 0.2729 S22: -0.1774 S23: -0.0078 REMARK 3 S31: -0.2652 S32: 0.0580 S33: 0.1046 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 109 M 208 REMARK 3 ORIGIN FOR THE GROUP (A): 12.5687 -41.9027 84.7948 REMARK 3 T TENSOR REMARK 3 T11: -0.0321 T22: 0.1416 REMARK 3 T33: -0.0079 T12: -0.0134 REMARK 3 T13: -0.0300 T23: 0.1000 REMARK 3 L TENSOR REMARK 3 L11: 1.7591 L22: 4.3330 REMARK 3 L33: 13.1814 L12: 1.9274 REMARK 3 L13: -3.8629 L23: -5.4436 REMARK 3 S TENSOR REMARK 3 S11: -0.0549 S12: 0.1425 S13: 0.1952 REMARK 3 S21: -0.3490 S22: 0.6377 S23: 0.5282 REMARK 3 S31: -0.0385 S32: -1.4967 S33: -0.5828 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 : I 1 I 113 REMARK 3 ORIGIN FOR THE GROUP (A): 39.6390 -18.1950 92.4950 REMARK 3 T TENSOR REMARK 3 T11: -0.0246 T22: -0.0332 REMARK 3 T33: -0.0955 T12: -0.0588 REMARK 3 T13: -0.0485 T23: 0.0210 REMARK 3 L TENSOR REMARK 3 L11: 2.2114 L22: 2.8861 REMARK 3 L33: 5.0171 L12: 1.3457 REMARK 3 L13: -0.5824 L23: -0.6235 REMARK 3 S TENSOR REMARK 3 S11: 0.0690 S12: -0.2145 S13: -0.0381 REMARK 3 S21: 0.2527 S22: -0.1169 S23: -0.0751 REMARK 3 S31: -0.1044 S32: 0.2645 S33: 0.0479 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 : I 114 I 212 REMARK 3 ORIGIN FOR THE GROUP (A): 24.5410 -48.1193 93.8664 REMARK 3 T TENSOR REMARK 3 T11: -0.1239 T22: -0.0532 REMARK 3 T33: -0.1102 T12: -0.0221 REMARK 3 T13: 0.0428 T23: 0.0262 REMARK 3 L TENSOR REMARK 3 L11: 2.2801 L22: 5.8036 REMARK 3 L33: 7.3169 L12: 1.2829 REMARK 3 L13: 1.7224 L23: -0.0285 REMARK 3 S TENSOR REMARK 3 S11: -0.0740 S12: 0.2796 S13: -0.0937 REMARK 3 S21: -0.3035 S22: -0.0448 S23: -0.1810 REMARK 3 S31: 0.2377 S32: 0.2016 S33: 0.1188 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : Q 1 Q 8 REMARK 3 ORIGIN FOR THE GROUP (A): 44.2829 -3.0484 81.0185 REMARK 3 T TENSOR REMARK 3 T11: 0.1634 T22: 0.1113 REMARK 3 T33: 0.0042 T12: -0.1695 REMARK 3 T13: -0.0250 T23: 0.0823 REMARK 3 L TENSOR REMARK 3 L11: 31.5804 L22: 21.9623 REMARK 3 L33: 10.0810 L12: -19.3718 REMARK 3 L13: 17.8138 L23: -10.3539 REMARK 3 S TENSOR REMARK 3 S11: 0.0212 S12: 1.1050 S13: 1.3423 REMARK 3 S21: -0.9109 S22: -0.8699 S23: -1.0527 REMARK 3 S31: -0.6960 S32: 0.8787 S33: 0.8488 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 2ZPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JUL-08. REMARK 100 THE RCSB ID CODE IS RCSB028264. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-DEC-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL44XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : DIP-6040 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76301 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 46.780 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 200 DATA REDUNDANCY : 2.500 REMARK 200 R MERGE (I) : 0.04200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3 REMARK 200 DATA REDUNDANCY IN SHELL : 2.50 REMARK 200 R MERGE FOR SHELL (I) : 0.23400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 1NC4 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.61 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20-23% (WT/VOL) PEG 3000, 0.1M SODIUM REMARK 280 ACETATE (PH4.5), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18440 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, P 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4860 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, I, Q 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 H 127 REMARK 465 SER H 128 REMARK 465 ALA H 129 REMARK 465 ALA H 130 REMARK 465 GLN H 131 REMARK 465 THR H 132 REMARK 465 ASN H 133 REMARK 465 SER H 134 REMARK 465 PCA M 1 REMARK 465 ARG M 209 REMARK 465 ALA M 210 REMARK 465 GLY I 127 REMARK 465 SER I 128 REMARK 465 ALA I 129 REMARK 465 ALA I 130 REMARK 465 GLN I 131 REMARK 465 THR I 132 REMARK 465 ASN I 133 REMARK 465 ARG I 213 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG P 2 CG CD NE CZ NH1 NH2 REMARK 470 LYS M 150 CG CD CE NZ REMARK 470 VAL M 151 CG1 CG2 REMARK 470 ASP M 152 CG OD1 OD2 REMARK 470 THR M 154 OG1 CG2 REMARK 470 PRO M 155 CG CD REMARK 470 VAL M 156 CG1 CG2 REMARK 470 THR M 157 OG1 CG2 REMARK 470 GLN M 158 CG CD OE1 NE2 REMARK 470 GLU M 187 CG CD OE1 OE2 REMARK 470 ARG M 188 CG CD NE CZ NH1 NH2 REMARK 470 HIS M 189 CG ND1 CD2 CE1 NE2 REMARK 470 SER M 190 OG REMARK 470 SER M 191 OG REMARK 470 ARG Q 2 CG CD NE CZ NH1 NH2 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 HIS L 42 44.95 32.72 REMARK 500 THR L 51 -53.69 78.85 REMARK 500 ASN L 52 17.35 -141.70 REMARK 500 SER L 190 -61.27 -106.83 REMARK 500 ASP H 173 10.28 53.76 REMARK 500 TYR M 32 52.49 39.57 REMARK 500 THR M 51 -49.87 74.74 REMARK 500 ASN M 52 12.02 -142.14 REMARK 500 TYR M 92 75.93 -110.36 REMARK 500 SER M 93 -45.05 69.42 REMARK 500 ASN M 94 8.43 -152.31 REMARK 500 SER M 190 -81.10 -99.66 REMARK 500 ASP I 173 -0.81 70.72 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 H 173 22.3 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 GOL I 214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL M 211 REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCE OF ENTITY 1 (AB447555) AND 2 (AB447554) HAVE BEEN REMARK 999 DEPOSITED TO DDBJ.