REMARK 2 REMARK 2 RESOLUTION. 2.50 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9 REMARK 3 NUMBER OF REFLECTIONS : 42711 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) : 0.213 REMARK 3 R VALUE (WORKING SET) : 0.210 REMARK 3 FREE R VALUE : 0.261 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2293 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) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2744 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.40 REMARK 3 BIN R VALUE (WORKING SET) : 0.4020 REMARK 3 BIN FREE R VALUE SET COUNT : 132 REMARK 3 BIN FREE R VALUE : 0.4590 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6485 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 55 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) : 29.51 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.16000 REMARK 3 B22 (A**2) : -1.49000 REMARK 3 B33 (A**2) : 0.17000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 2.28000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.344 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.266 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.197 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.608 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6650 ; 0.029 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 4451 ; 0.005 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9050 ; 2.743 ; 1.954 REMARK 3 BOND ANGLES OTHERS (DEGREES): 10869 ; 1.276 ; 3.003 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 851 ;26.125 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 259 ;33.839 ;24.131 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1056 ;19.927 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;25.465 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1024 ; 0.150 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7417 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1323 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1280 ; 0.222 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4612 ; 0.234 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3177 ; 0.214 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 3876 ; 0.116 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 179 ; 0.180 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.060 ; 0.200 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): 8 ; 0.176 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 20 ; 0.236 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.073 ; 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): 4598 ; 1.060 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1729 ; 0.240 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6886 ; 1.645 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2710 ; 2.763 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2164 ; 4.087 ; 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 2 H 119 REMARK 3 ORIGIN FOR THE GROUP (A): 34.0787 -12.2687 35.4572 REMARK 3 T TENSOR REMARK 3 T11: -0.0432 T22: -0.1391 REMARK 3 T33: -0.1499 T12: 0.0748 REMARK 3 T13: 0.0277 T23: 0.0051 REMARK 3 L TENSOR REMARK 3 L11: 3.6181 L22: 2.6008 REMARK 3 L33: 3.2374 L12: 0.2246 REMARK 3 L13: -0.0934 L23: 0.9354 REMARK 3 S TENSOR REMARK 3 S11: 0.0676 S12: 0.3625 S13: -0.0137 REMARK 3 S21: -0.4846 S22: -0.0351 S23: -0.1982 REMARK 3 S31: -0.1345 S32: -0.1344 S33: -0.0325 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 120 H 219 REMARK 3 ORIGIN FOR THE GROUP (A): 5.4179 3.5560 34.0412 REMARK 3 T TENSOR REMARK 3 T11: -0.0287 T22: 0.3172 REMARK 3 T33: 0.0373 T12: 0.1226 REMARK 3 T13: -0.1622 T23: 0.1879 REMARK 3 L TENSOR REMARK 3 L11: 5.4316 L22: 2.9612 REMARK 3 L33: 4.1849 L12: -2.3635 REMARK 3 L13: -0.2098 L23: 0.9977 REMARK 3 S TENSOR REMARK 3 S11: 0.1496 S12: 0.6084 S13: 0.7141 REMARK 3 S21: -0.3733 S22: 0.0376 S23: 0.1626 REMARK 3 S31: -0.7165 S32: -0.1835 S33: -0.1872 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 : C 2 C 119 REMARK 3 ORIGIN FOR THE GROUP (A): 5.9473 -3.5881 93.8144 REMARK 3 T TENSOR REMARK 3 T11: 0.1648 T22: -0.0059 REMARK 3 T33: 0.1011 T12: -0.0187 REMARK 3 T13: 0.1517 T23: -0.0048 REMARK 3 L TENSOR REMARK 3 L11: 3.7803 L22: 2.6789 REMARK 3 L33: 4.4050 L12: -0.0880 REMARK 3 L13: 0.0554 L23: 0.6351 REMARK 3 S TENSOR REMARK 3 S11: 0.0059 S12: -0.0629 S13: 0.1177 REMARK 3 S21: 0.5097 S22: -0.0213 S23: 0.3286 REMARK 3 S31: -0.1407 S32: -0.4837 S33: 0.0154 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 : C 120 C 219 REMARK 3 ORIGIN FOR THE GROUP (A): -8.6141 -26.5038 76.8205 REMARK 3 T TENSOR REMARK 3 T11: -0.0246 T22: 0.3053 REMARK 3 T33: 0.1928 T12: -0.2577 REMARK 3 T13: 0.0040 T23: 0.1174 REMARK 3 L TENSOR REMARK 3 L11: 4.6977 L22: 6.0474 REMARK 3 L33: 5.9120 L12: -1.4034 REMARK 3 L13: -0.9621 L23: 4.5006 REMARK 3 S TENSOR REMARK 3 S11: 0.0118 S12: -0.5845 S13: -0.5507 REMARK 3 S21: 0.6907 S22: -0.0086 S23: 0.3476 REMARK 3 S31: 1.1919 S32: -0.5457 S33: -0.0032 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): 30.9589 -6.6845 56.9382 REMARK 3 T TENSOR REMARK 3 T11: -0.2681 T22: -0.2716 REMARK 3 T33: -0.2302 T12: -0.0332 REMARK 3 T13: -0.0255 T23: -0.0019 REMARK 3 L TENSOR REMARK 3 L11: 1.8965 L22: 4.0505 REMARK 3 L33: 3.5916 L12: -1.5216 REMARK 3 L13: -1.1680 L23: 0.0070 REMARK 3 S TENSOR REMARK 3 S11: 0.0831 S12: -0.1703 S13: 0.0698 REMARK 3 S21: 0.1188 S22: -0.0551 S23: -0.2349 REMARK 3 S31: 0.0819 S32: 0.0328 S33: -0.0280 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 213 REMARK 3 ORIGIN FOR THE GROUP (A): -3.9687 -2.0863 46.1096 REMARK 3 T TENSOR REMARK 3 T11: -0.2956 T22: 0.2786 REMARK 3 T33: 0.0557 T12: 0.1348 REMARK 3 T13: -0.1251 T23: 0.0505 REMARK 3 L TENSOR REMARK 3 L11: 5.7959 L22: 1.1286 REMARK 3 L33: 4.5507 L12: 0.9999 REMARK 3 L13: 3.2702 L23: 0.9305 REMARK 3 S TENSOR REMARK 3 S11: 0.0926 S12: 0.4820 S13: 0.2358 REMARK 3 S21: -0.0611 S22: -0.1194 S23: 0.4839 REMARK 3 S31: -0.0206 S32: -0.6298 S33: 0.0268 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 : D 1 D 107 REMARK 3 ORIGIN FOR THE GROUP (A): 21.5388 -7.7226 78.2044 REMARK 3 T TENSOR REMARK 3 T11: -0.2017 T22: -0.3100 REMARK 3 T33: -0.2426 T12: -0.0096 REMARK 3 T13: 0.0153 T23: 0.0329 REMARK 3 L TENSOR REMARK 3 L11: 1.8213 L22: 2.9567 REMARK 3 L33: 3.9959 L12: -0.3053 REMARK 3 L13: -1.5045 L23: 0.6493 REMARK 3 S TENSOR REMARK 3 S11: 0.0822 S12: -0.0397 S13: 0.0054 REMARK 3 S21: 0.2252 S22: -0.0248 S23: -0.0580 REMARK 3 S31: -0.0153 S32: -0.0069 S33: -0.0574 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 : D 108 D 213 REMARK 3 ORIGIN FOR THE GROUP (A): -7.1116 -24.0028 60.6362 REMARK 3 T TENSOR REMARK 3 T11: -0.1340 T22: 0.2692 REMARK 3 T33: 0.1213 T12: -0.1970 REMARK 3 T13: -0.1621 T23: -0.0763 REMARK 3 L TENSOR REMARK 3 L11: 8.7679 L22: 1.6722 REMARK 3 L33: 1.8180 L12: 0.5403 REMARK 3 L13: -0.2380 L23: -0.6927 REMARK 3 S TENSOR REMARK 3 S11: 0.2881 S12: 0.5960 S13: -0.4519 REMARK 3 S21: -0.1779 S22: -0.0132 S23: 0.5590 REMARK 3 S31: 0.2516 S32: -0.9165 S33: -0.2749 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: NULL REMARK 4 REMARK 4 3FZU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-09. REMARK 100 THE RCSB ID CODE IS RCSB051244. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-FEB-08 REMARK 200 TEMPERATURE (KELVIN) : 100 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 : 31-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : DIAMOND(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42711 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9 REMARK 200 DATA REDUNDANCY : 4.200 REMARK 200 R MERGE (I) : 0.08900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 31.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.54 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 38% PEG 400, 200 MM SODIUM CHLORIDE, REMARK 280 100 MM TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 121.52550 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.96900 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 121.52550 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.96900 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: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3280 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19520 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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: 3090 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19450 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, C 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 CYS L 214 REMARK 465 THR H 136 REMARK 465 SER H 137 REMARK 465 SER H 220 REMARK 465 CYS H 221 REMARK 465 ASP H 222 REMARK 465 LYS H 223 REMARK 465 LYS C 134 REMARK 465 SER C 135 REMARK 465 THR C 136 REMARK 465 SER C 137 REMARK 465 GLY C 138 REMARK 465 SER C 220 REMARK 465 CYS C 221 REMARK 465 ASP C 222 REMARK 465 LYS C 223 REMARK 465 CYS D 214 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 GLU H 1 CG CD OE1 OE2 REMARK 470 LYS H 134 CG CD CE NZ REMARK 470 GLU C 1 CG CD OE1 OE2 REMARK 470 ASP D 122 CG OD1 OD2 REMARK 470 GLU D 123 CG CD OE1 OE2 REMARK 470 LYS D 126 CG CD CE NZ REMARK 470 ASP D 151 CG OD1 OD2 REMARK 470 LYS D 190 CG CD CE NZ 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 PRO C 218 C - N - CA ANGL. DEV. = 9.6 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 ARG L 30 -120.33 54.88 REMARK 500 VAL L 50 38.13 36.04 REMARK 500 ALA L 51 -17.18 94.52 REMARK 500 SER L 52 -1.16 -172.22 REMARK 500 PRO L 120 157.73 -46.58 REMARK 500 LYS L 126 -13.05 -45.51 REMARK 500 ASN L 138 67.03 36.32 REMARK 500 LYS L 183 -55.47 -23.02 REMARK 500 ALA L 184 -75.58 -37.94 REMARK 500 SER H 132 -125.24 -176.10 REMARK 500 SER H 133 34.56 -78.17 REMARK 500 LYS H 134 44.04 -88.93 REMARK 500 ASP H 149 70.39 66.66 REMARK 500 SER H 191 -71.18 -44.87 REMARK 500 THR H 196 -70.83 127.25 REMARK 500 PRO H 218 165.84 -48.19 REMARK 500 PHE C 29 -163.92 -115.67 REMARK 500 ASN C 79 49.40 34.85 REMARK 500 LEU C 88 166.86 -49.55 REMARK 500 PRO C 131 -177.28 -56.17 REMARK 500 SER C 132 -135.27 143.60 REMARK 500 ASP C 149 60.49 74.68 REMARK 500 PRO C 218 131.88 -28.72 REMARK 500 ARG D 30 -120.15 55.38 REMARK 500 VAL D 50 47.83 38.66 REMARK 500 ALA D 51 -17.14 67.12 REMARK 500 SER D 52 -7.50 -146.73 REMARK 500 ASP D 122 -71.76 -174.18 REMARK 500 GLU D 123 -165.65 76.33 REMARK 500 GLN D 124 -78.04 9.23 REMARK 500 LEU D 125 -54.43 -20.02 REMARK 500 LYS D 126 29.83 -62.95 REMARK 500 SER D 127 3.72 -151.34 REMARK 500 ASP D 151 87.07 46.07 REMARK 500 ASN D 152 43.53 -8.37 REMARK 500 SER D 159 141.50 -172.65 REMARK 500 LYS D 190 -72.50 -85.24 REMARK 500 HIS D 198 144.22 -171.83 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 TYR H 97 CYS H 98 147.39 REMARK 500 GLY H 138 GLY H 139 -144.69 REMARK 500 ASP D 151 ASN D 152 -146.91 REMARK 500 REMARK 500 REMARK: NULL