REMARK 2 REMARK 2 RESOLUTION. 3.19 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.19 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.65 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.190 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 3 NUMBER OF REFLECTIONS : 66876 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.201 REMARK 3 R VALUE (WORKING SET) : 0.199 REMARK 3 FREE R VALUE : 0.243 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070 REMARK 3 FREE R VALUE TEST SET COUNT : 3391 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 46.6584 - 6.8703 0.99 6591 356 0.1873 0.2272 REMARK 3 2 6.8703 - 5.4559 1.00 6434 371 0.1713 0.2164 REMARK 3 3 5.4559 - 4.7670 1.00 6431 318 0.1504 0.1808 REMARK 3 4 4.7670 - 4.3315 1.00 6359 347 0.1620 0.2192 REMARK 3 5 4.3315 - 4.0212 1.00 6338 342 0.1881 0.2352 REMARK 3 6 4.0212 - 3.7843 1.00 6325 339 0.2194 0.2785 REMARK 3 7 3.7843 - 3.5948 1.00 6361 316 0.2360 0.2754 REMARK 3 8 3.5948 - 3.4384 1.00 6309 332 0.2646 0.3154 REMARK 3 9 3.4384 - 3.3060 1.00 6307 347 0.2869 0.3248 REMARK 3 10 3.3060 - 3.1920 0.96 6030 323 0.3305 0.3551 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.83 REMARK 3 K_SOL : 0.28 REMARK 3 B_SOL : 43.06 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.540 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.77910 REMARK 3 B22 (A**2) : -2.77910 REMARK 3 B33 (A**2) : 5.55820 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 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.010 20618 REMARK 3 ANGLE : 1.234 28074 REMARK 3 CHIRALITY : 0.079 3097 REMARK 3 PLANARITY : 0.005 3603 REMARK 3 DIHEDRAL : 15.868 7276 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 5 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain A and (resid 3:106a) REMARK 3 SELECTION : chain C and (resid 3:106a) REMARK 3 ATOM PAIRS NUMBER : 800 REMARK 3 RMSD : 0.048 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: chain A and (resid 3:106a) REMARK 3 SELECTION : chain E and (resid 3:106a) REMARK 3 ATOM PAIRS NUMBER : 800 REMARK 3 RMSD : 0.042 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: chain A and (resid 3:106a) REMARK 3 SELECTION : chain G and (resid 3:106a) REMARK 3 ATOM PAIRS NUMBER : 800 REMARK 3 RMSD : 0.047 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: chain A and (resid 3:106a) REMARK 3 SELECTION : chain I and (resid 3:106a) REMARK 3 ATOM PAIRS NUMBER : 800 REMARK 3 RMSD : 0.060 REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: chain A and (resid 3:106a) REMARK 3 SELECTION : chain K and (resid 3:106a) REMARK 3 ATOM PAIRS NUMBER : 800 REMARK 3 RMSD : 0.042 REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain A and (resid 107:153 or resid 159: REMARK 3 165 or resid 171:207) REMARK 3 SELECTION : chain C and (resid 107:153 or resid 159: REMARK 3 165 or resid 171:207) REMARK 3 ATOM PAIRS NUMBER : 686 REMARK 3 RMSD : 0.055 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: chain A and (resid 107:153 or resid 159: REMARK 3 165 or resid 171:207) REMARK 3 SELECTION : chain E and (resid 107:153 or resid 159: REMARK 3 165 or resid 171:207) REMARK 3 ATOM PAIRS NUMBER : 686 REMARK 3 RMSD : 0.051 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: chain A and (resid 107:153 or resid 159: REMARK 3 165 or resid 171:207) REMARK 3 SELECTION : chain G and (resid 107:153 or resid 159: REMARK 3 165 or resid 171:207) REMARK 3 ATOM PAIRS NUMBER : 686 REMARK 3 RMSD : 0.075 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: chain A and (resid 107:153 or resid 159: REMARK 3 165 or resid 171:207) REMARK 3 SELECTION : chain I and (resid 107:153 or resid 159: REMARK 3 165 or resid 171:207) REMARK 3 ATOM PAIRS NUMBER : 686 REMARK 3 RMSD : 0.060 REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: chain A and (resid 107:153 or resid 159: REMARK 3 165 or resid 171:207) REMARK 3 SELECTION : chain K and (resid 107:153 or resid 159: REMARK 3 165 or resid 171:207) REMARK 3 ATOM PAIRS NUMBER : 686 REMARK 3 RMSD : 0.076 REMARK 3 NCS GROUP : 3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain B and (resid 2:97 or resid 100k:113) REMARK 3 SELECTION : chain D and (resid 2:97 or resid 100k:113) REMARK 3 ATOM PAIRS NUMBER : 865 REMARK 3 RMSD : 0.050 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: chain B and (resid 2:97 or resid 100k:113) REMARK 3 SELECTION : chain F and (resid 2:97 or resid 100k:113) REMARK 3 ATOM PAIRS NUMBER : 865 REMARK 3 RMSD : 0.049 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: chain B and (resid 2:97 or resid 100k:113) REMARK 3 SELECTION : chain H and (resid 2:97 or resid 100k:113) REMARK 3 ATOM PAIRS NUMBER : 865 REMARK 3 RMSD : 0.056 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: chain B and (resid 2:97 or resid 100k:113) REMARK 3 SELECTION : chain J and (resid 2:97 or resid 100k:113) REMARK 3 ATOM PAIRS NUMBER : 865 REMARK 3 RMSD : 0.066 REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: chain B and (resid 2:97 or resid 100k:113) REMARK 3 SELECTION : chain L and (resid 2:97 or resid 100k:113) REMARK 3 ATOM PAIRS NUMBER : 865 REMARK 3 RMSD : 0.050 REMARK 3 NCS GROUP : 4 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain B and (resid 114:126 or resid 135: REMARK 3 213) REMARK 3 SELECTION : chain D and (resid 114:126 or resid 135: REMARK 3 213) REMARK 3 ATOM PAIRS NUMBER : 673 REMARK 3 RMSD : 0.048 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: chain B and (resid 114:126 or resid 135: REMARK 3 213) REMARK 3 SELECTION : chain F and (resid 114:126 or resid 135: REMARK 3 213) REMARK 3 ATOM PAIRS NUMBER : 673 REMARK 3 RMSD : 0.044 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: chain B and (resid 114:126 or resid 135: REMARK 3 213) REMARK 3 SELECTION : chain H and (resid 114:126 or resid 135: REMARK 3 213) REMARK 3 ATOM PAIRS NUMBER : 673 REMARK 3 RMSD : 0.054 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: chain B and (resid 114:126 or resid 135: REMARK 3 213) REMARK 3 SELECTION : chain J and (resid 114:126 or resid 135: REMARK 3 213) REMARK 3 ATOM PAIRS NUMBER : 673 REMARK 3 RMSD : 0.057 REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: chain B and (resid 114:126 or resid 135: REMARK 3 213) REMARK 3 SELECTION : chain L and (resid 114:126 or resid 135: REMARK 3 213) REMARK 3 ATOM PAIRS NUMBER : 673 REMARK 3 RMSD : 0.045 REMARK 3 NCS GROUP : 5 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain B and (resid 98:100j) and backbone REMARK 3 SELECTION : chain D and (resid 98:100j) and backbone REMARK 3 ATOM PAIRS NUMBER : 64 REMARK 3 RMSD : 0.079 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: chain B and (resid 98:100j) and backbone REMARK 3 SELECTION : chain F and (resid 98:100j) and backbone REMARK 3 ATOM PAIRS NUMBER : 64 REMARK 3 RMSD : 0.052 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: chain B and (resid 98:100j) and backbone REMARK 3 SELECTION : chain H and (resid 98:100j) and backbone REMARK 3 ATOM PAIRS NUMBER : 64 REMARK 3 RMSD : 0.087 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: chain B and (resid 98:100j) and backbone REMARK 3 SELECTION : chain J and (resid 98:100j) and backbone REMARK 3 ATOM PAIRS NUMBER : 64 REMARK 3 RMSD : 0.087 REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: chain B and (resid 98:100j) and backbone REMARK 3 SELECTION : chain L and (resid 98:100j) and backbone REMARK 3 ATOM PAIRS NUMBER : 64 REMARK 3 RMSD : 0.066 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3Q6F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-11. REMARK 100 THE RCSB ID CODE IS RCSB063252. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-FEB-10; NULL; NULL; NULL REMARK 200 TEMPERATURE (KELVIN) : 100; NULL; NULL; NULL REMARK 200 PH : 6.8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y; Y; Y REMARK 200 RADIATION SOURCE : APS; NSLS; APS; NSLS REMARK 200 BEAMLINE : 23-ID-B; X6A; 17-ID; X4C REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL; NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL; NULL; NULL REMARK 200 WAVELENGTH OR RANGE (A) : 1.03321; 1.0; 1.0; 1.0 REMARK 200 MONOCHROMATOR : MIRRORS; NULL; NULL; NULL REMARK 200 OPTICS : NULL; NULL; NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD; NULL; NULL; NULL REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE; NULL; REMARK 200 NULL; NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66903 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05 REMARK 200 COMPLETENESS FOR SHELL (%) : 78.3 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; NULL; NULL; NULL 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 (%): 64.90 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 8000, 0.1M HEPES, PH6.8, 0.1M REMARK 280 GLYCINE, AND 8% ETHYLENE GLYCOL, UNDER THE OIL, TEMPERATURE 296K, REMARK 280 EVAPORATION REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 145.93333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 72.96667 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 72.96667 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 145.93333 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6 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: 3880 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20510 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 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: 3740 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20580 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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: 3 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: 3850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20710 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F 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: 4 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: 3860 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20470 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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: 5 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: 3850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J 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: 6 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: 3780 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20560 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, 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 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 A 1 REMARK 465 LYS B 129 REMARK 465 SER B 130 REMARK 465 THR B 131 REMARK 465 SER B 132 REMARK 465 GLY B 133 REMARK 465 SER C 1 REMARK 465 LYS D 129 REMARK 465 SER D 130 REMARK 465 THR D 131 REMARK 465 SER D 132 REMARK 465 GLY D 133 REMARK 465 SER E 1 REMARK 465 LYS F 129 REMARK 465 SER F 130 REMARK 465 THR F 131 REMARK 465 SER F 132 REMARK 465 GLY F 133 REMARK 465 SER G 1 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 SER I 1 REMARK 465 LYS J 129 REMARK 465 SER J 130 REMARK 465 THR J 131 REMARK 465 SER K 1 REMARK 465 SER L 128 REMARK 465 LYS L 129 REMARK 465 SER L 130 REMARK 465 THR L 131 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OE1 GLN C 126 OG SER L 115 2.09 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 ARG A 189 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 ARG A 189 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 ARG C 189 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 ARG C 189 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES REMARK 500 ARG E 189 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 ARG E 189 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES REMARK 500 PRO G 154 C - N - CA ANGL. DEV. = 9.0 DEGREES REMARK 500 ARG G 189 CD - NE - CZ ANGL. DEV. = 10.6 DEGREES REMARK 500 ARG G 189 NE - CZ - NH1 ANGL. DEV. = -7.4 DEGREES REMARK 500 ARG G 189 NE - CZ - NH2 ANGL. DEV. = 7.2 DEGREES REMARK 500 ARG I 189 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG I 189 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 ARG K 189 CD - NE - CZ ANGL. DEV. = 10.6 DEGREES REMARK 500 ARG K 189 NE - CZ - NH1 ANGL. DEV. = -7.3 DEGREES REMARK 500 ARG K 189 NE - CZ - NH2 ANGL. DEV. = 7.4 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 PRO A 40 128.28 -36.91 REMARK 500 ASP A 51 -74.11 80.20 REMARK 500 ASN A 66 103.15 -161.83 REMARK 500 ALA A 84 -168.14 -172.40 REMARK 500 ASP A 151 -46.83 71.30 REMARK 500 PRO A 164 154.68 -48.70 REMARK 500 GLN A 167 -165.38 -120.22 REMARK 500 SER A 168 33.86 -73.43 REMARK 500 ASN A 169 30.31 -169.12 REMARK 500 ASN A 170 -6.47 53.32 REMARK 500 THR A 209 89.67 -68.70 REMARK 500 GLU A 210 -148.95 153.78 REMARK 500 ASN B 10 -155.37 -164.12 REMARK 500 ALA B 88 -172.68 -177.36 REMARK 500 SER B 99 -157.64 -127.78 REMARK 500 ASP B 100 131.15 175.10 REMARK 500 ASP B 100B 107.39 -162.60 REMARK 500 TYR B 100L 158.23 178.64 REMARK 500 ASP B 144 74.71 44.01 REMARK 500 PHE B 146 139.94 178.11 REMARK 500 PRO B 185 108.16 -39.61 REMARK 500 THR B 191 -73.53 -108.56 REMARK 500 LYS B 214 -163.05 -64.92 REMARK 500 LYS C 17 -169.34 -71.79 REMARK 500 PRO C 40 127.08 -37.88 REMARK 500 ASP C 51 -72.62 81.07 REMARK 500 ASN C 66 102.51 -164.45 REMARK 500 ALA C 84 -168.89 -170.09 REMARK 500 ASP C 151 -47.53 69.99 REMARK 500 PRO C 164 155.32 -47.69 REMARK 500 ASN C 170 1.96 57.43 REMARK 500 THR C 209 56.53 -58.93 REMARK 500 GLU C 210 147.74 66.35 REMARK 500 ASN D 10 -153.45 -160.45 REMARK 500 ALA D 88 -173.34 -175.58 REMARK 500 SER D 99 -159.68 -127.60 REMARK 500 ASP D 100 134.17 176.24 REMARK 500 ASP D 100B 102.42 -160.43 REMARK 500 TYS D 100C -49.29 -20.22 REMARK 500 ASP D 144 74.87 44.87 REMARK 500 PHE D 146 139.46 175.45 REMARK 500 PRO D 185 105.08 -39.57 REMARK 500 THR D 191 -73.23 -108.54 REMARK 500 LYS D 214 179.84 142.83 REMARK 500 PRO E 40 127.25 -37.18 REMARK 500 ASP E 51 -70.77 79.46 REMARK 500 ASN E 66 103.63 -162.43 REMARK 500 ALA E 84 -169.00 -170.92 REMARK 500 LEU E 106A 85.30 -68.11 REMARK 500 ASP E 151 -47.46 70.38 REMARK 500 REMARK 500 THIS ENTRY HAS 129 RAMACHANDRAN OUTLIERS. 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 ALA G 157 GLY G 158 -149.89 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 TYS B 100C 22.4 L L OUTSIDE RANGE REMARK 500 TYS F 100C 18.4 L L OUTSIDE RANGE REMARK 500 TYS J 100C 24.9 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 PEG G 212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG I 212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG E 212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG K 212 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3Q6G RELATED DB: PDB