REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) 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) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.38 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0 REMARK 3 NUMBER OF REFLECTIONS : 53580 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.215 REMARK 3 FREE R VALUE : 0.262 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950 REMARK 3 FREE R VALUE TEST SET COUNT : 2651 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 47.3870 - 7.7280 0.95 3036 169 0.2180 0.2240 REMARK 3 2 7.7280 - 6.1380 0.98 2963 138 0.2140 0.2730 REMARK 3 3 6.1380 - 5.3630 0.97 2875 138 0.2010 0.2530 REMARK 3 4 5.3630 - 4.8730 0.96 2796 157 0.1720 0.2290 REMARK 3 5 4.8730 - 4.5240 0.94 2729 147 0.1680 0.1980 REMARK 3 6 4.5240 - 4.2580 0.96 2750 160 0.1680 0.2370 REMARK 3 7 4.2580 - 4.0450 0.96 2754 160 0.1880 0.2240 REMARK 3 8 4.0450 - 3.8690 0.96 2756 159 0.2080 0.2540 REMARK 3 9 3.8690 - 3.7200 0.97 2754 145 0.2090 0.2650 REMARK 3 10 3.7200 - 3.5920 0.96 2745 117 0.2110 0.2570 REMARK 3 11 3.5920 - 3.4790 0.96 2777 125 0.2170 0.2680 REMARK 3 12 3.4790 - 3.3800 0.95 2691 146 0.2180 0.2620 REMARK 3 13 3.3800 - 3.2910 0.94 2651 144 0.2380 0.3160 REMARK 3 14 3.2910 - 3.2110 0.92 2619 139 0.2470 0.3020 REMARK 3 15 3.2110 - 3.1380 0.91 2567 132 0.2630 0.3290 REMARK 3 16 3.1380 - 3.0710 0.89 2548 119 0.2550 0.3190 REMARK 3 17 3.0710 - 3.0100 0.86 2450 109 0.2760 0.3450 REMARK 3 18 3.0100 - 2.9530 0.82 2297 140 0.2800 0.3600 REMARK 3 19 2.9530 - 2.9000 0.78 2171 107 0.2830 0.3560 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.28 REMARK 3 B_SOL : 39.25 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 2.240 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.940 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 70.77 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.64 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 4.00300 REMARK 3 B22 (A**2) : 4.00300 REMARK 3 B33 (A**2) : -8.00700 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 : 0.006 12906 REMARK 3 ANGLE : 1.054 17481 REMARK 3 CHIRALITY : 0.065 1909 REMARK 3 PLANARITY : 0.004 2217 REMARK 3 DIHEDRAL : 18.348 4575 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): 57.0530 -5.2288 -10.7684 REMARK 3 T TENSOR REMARK 3 T11: 0.4956 T22: 0.2114 REMARK 3 T33: 0.3657 T12: -0.0427 REMARK 3 T13: -0.0325 T23: -0.0485 REMARK 3 L TENSOR REMARK 3 L11: 1.1147 L22: -0.3733 REMARK 3 L33: 0.5417 L12: 0.6152 REMARK 3 L13: -0.2292 L23: 0.4757 REMARK 3 S TENSOR REMARK 3 S11: 0.1099 S12: -0.0799 S13: 0.0906 REMARK 3 S21: 0.1186 S22: -0.1374 S23: -0.0854 REMARK 3 S31: -0.1056 S32: -0.0040 S33: 0.0309 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): 55.5485 -16.3642 -24.8784 REMARK 3 T TENSOR REMARK 3 T11: 0.4131 T22: 0.2842 REMARK 3 T33: 0.4733 T12: 0.0368 REMARK 3 T13: 0.0408 T23: -0.0463 REMARK 3 L TENSOR REMARK 3 L11: 1.6721 L22: -0.3038 REMARK 3 L33: 0.3267 L12: 1.2903 REMARK 3 L13: -0.1483 L23: 0.0945 REMARK 3 S TENSOR REMARK 3 S11: -0.0018 S12: 0.0722 S13: 0.1473 REMARK 3 S21: -0.0291 S22: -0.1434 S23: -0.0798 REMARK 3 S31: -0.1118 S32: -0.0264 S33: 0.1021 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN C REMARK 3 ORIGIN FOR THE GROUP (A): 74.8702 -8.2292 -65.6981 REMARK 3 T TENSOR REMARK 3 T11: 0.5283 T22: 0.2567 REMARK 3 T33: 0.4206 T12: 0.0766 REMARK 3 T13: -0.0363 T23: 0.0171 REMARK 3 L TENSOR REMARK 3 L11: 0.7247 L22: -0.1746 REMARK 3 L33: 1.0859 L12: -0.7539 REMARK 3 L13: -0.2715 L23: -0.4028 REMARK 3 S TENSOR REMARK 3 S11: 0.1924 S12: 0.1283 S13: 0.1325 REMARK 3 S21: -0.0082 S22: -0.1645 S23: -0.0637 REMARK 3 S31: -0.1873 S32: -0.0396 S33: -0.0147 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN D REMARK 3 ORIGIN FOR THE GROUP (A): 76.3936 -19.4492 -51.6990 REMARK 3 T TENSOR REMARK 3 T11: 0.4667 T22: 0.3751 REMARK 3 T33: 0.5155 T12: 0.0268 REMARK 3 T13: -0.0567 T23: -0.0290 REMARK 3 L TENSOR REMARK 3 L11: 1.2747 L22: -0.0201 REMARK 3 L33: 0.1175 L12: -0.9348 REMARK 3 L13: -0.1802 L23: -0.1880 REMARK 3 S TENSOR REMARK 3 S11: 0.0025 S12: -0.0612 S13: 0.0459 REMARK 3 S21: 0.1646 S22: -0.1107 S23: -0.0388 REMARK 3 S31: -0.0962 S32: 0.0530 S33: 0.0829 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN H REMARK 3 ORIGIN FOR THE GROUP (A): 33.0265 -52.6906 -65.8418 REMARK 3 T TENSOR REMARK 3 T11: 0.3460 T22: 0.5058 REMARK 3 T33: 0.3697 T12: -0.1367 REMARK 3 T13: 0.0752 T23: -0.0686 REMARK 3 L TENSOR REMARK 3 L11: -0.1249 L22: 1.0281 REMARK 3 L33: 0.8651 L12: 0.0918 REMARK 3 L13: 0.6326 L23: 0.1066 REMARK 3 S TENSOR REMARK 3 S11: -0.2039 S12: -0.1257 S13: -0.0389 REMARK 3 S21: -0.3683 S22: 0.3162 S23: 0.0876 REMARK 3 S31: 0.0182 S32: -0.1450 S33: -0.0997 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN L REMARK 3 ORIGIN FOR THE GROUP (A): 41.9560 -45.8305 -51.7943 REMARK 3 T TENSOR REMARK 3 T11: 0.4364 T22: 0.6101 REMARK 3 T33: 0.4657 T12: 0.0506 REMARK 3 T13: 0.0685 T23: -0.1237 REMARK 3 L TENSOR REMARK 3 L11: -0.3542 L22: 1.5728 REMARK 3 L33: 0.1119 L12: 0.2383 REMARK 3 L13: 0.4582 L23: 0.2554 REMARK 3 S TENSOR REMARK 3 S11: -0.1534 S12: -0.2549 S13: 0.0207 REMARK 3 S21: 0.1622 S22: 0.1548 S23: 0.0769 REMARK 3 S31: -0.0074 S32: -0.0569 S33: -0.0114 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN I REMARK 3 ORIGIN FOR THE GROUP (A): 37.9445 -92.5605 -54.8966 REMARK 3 T TENSOR REMARK 3 T11: 0.9006 T22: 0.6058 REMARK 3 T33: 0.9032 T12: -0.1657 REMARK 3 T13: 0.0118 T23: 0.0914 REMARK 3 L TENSOR REMARK 3 L11: 1.1364 L22: 0.2247 REMARK 3 L33: 0.1377 L12: -0.4621 REMARK 3 L13: 0.3736 L23: -0.6192 REMARK 3 S TENSOR REMARK 3 S11: 0.3519 S12: -0.0200 S13: -0.3784 REMARK 3 S21: -0.2723 S22: -0.1156 S23: 0.3447 REMARK 3 S31: 0.7109 S32: -0.0069 S33: -0.2414 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN J REMARK 3 ORIGIN FOR THE GROUP (A): 37.3093 7.0937 -55.6371 REMARK 3 T TENSOR REMARK 3 T11: 0.5958 T22: 0.5629 REMARK 3 T33: 0.5829 T12: 0.3478 REMARK 3 T13: 0.0840 T23: 0.0008 REMARK 3 L TENSOR REMARK 3 L11: -0.0611 L22: 0.3959 REMARK 3 L33: 1.2760 L12: 0.0497 REMARK 3 L13: -0.4143 L23: 0.2089 REMARK 3 S TENSOR REMARK 3 S11: 0.1491 S12: 0.0751 S13: 0.0186 REMARK 3 S21: 0.2090 S22: 0.0854 S23: 0.0564 REMARK 3 S31: -0.2035 S32: -0.2389 S33: -0.2011 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN K REMARK 3 ORIGIN FOR THE GROUP (A): 94.5506 9.7223 -21.4573 REMARK 3 T TENSOR REMARK 3 T11: 0.6718 T22: 0.5596 REMARK 3 T33: 0.8924 T12: -0.2451 REMARK 3 T13: 0.0593 T23: 0.0359 REMARK 3 L TENSOR REMARK 3 L11: 1.1909 L22: 0.0509 REMARK 3 L33: 0.0548 L12: -0.0473 REMARK 3 L13: 0.4604 L23: 0.2875 REMARK 3 S TENSOR REMARK 3 S11: 0.0967 S12: -0.2770 S13: 0.5107 REMARK 3 S21: -0.0962 S22: 0.0968 S23: 0.0352 REMARK 3 S31: -0.1790 S32: -0.0411 S33: -0.1735 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3IU3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-SEP-09. REMARK 100 THE RCSB ID CODE IS RCSB054865. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JUL-09 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 : SSRF REMARK 200 BEAMLINE : BL17U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796 REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56779 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 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 (%) : 98.0 REMARK 200 DATA REDUNDANCY : 14.800 REMARK 200 R MERGE (I) : 0.16500 REMARK 200 R SYM (I) : 0.16500 REMARK 200 FOR THE DATA SET : 17.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5 REMARK 200 DATA REDUNDANCY IN SHELL : 10.00 REMARK 200 R MERGE FOR SHELL (I) : 0.56100 REMARK 200 R SYM FOR SHELL (I) : 0.56100 REMARK 200 FOR SHELL : 2.000 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 1MIM REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.65 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M KCL, 0.05 M HEPES PH 7.5, AND REMARK 280 45% PENTAERYTHRITOL PROPOXYLATE (5/4 PO/OH), VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2 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 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 REMARK 290 7555 Y,X,-Z+2/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+1/3 REMARK 290 10555 -Y,-X,-Z+1/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+5/6 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 306.06333 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 153.03167 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 229.54750 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 76.51583 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 382.57917 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 306.06333 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 153.03167 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 76.51583 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 229.54750 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 382.57917 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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: 6120 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26430 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6270 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26410 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6240 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26430 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, 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 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 B 209 REMARK 465 GLU B 210 REMARK 465 GLU D 210 REMARK 465 GLY L 209 REMARK 465 GLU L 210 REMARK 465 THR I 62 REMARK 465 SER I 63 REMARK 465 SER I 64 REMARK 465 ALA I 65 REMARK 465 THR I 66 REMARK 465 ARG I 67 REMARK 465 ASN I 68 REMARK 465 THR I 69 REMARK 465 THR I 70 REMARK 465 LYS I 71 REMARK 465 GLN I 72 REMARK 465 VAL I 73 REMARK 465 THR I 74 REMARK 465 PRO I 75 REMARK 465 GLN I 76 REMARK 465 PRO I 77 REMARK 465 GLU I 78 REMARK 465 GLU I 79 REMARK 465 GLN I 80 REMARK 465 LYS I 81 REMARK 465 GLU I 82 REMARK 465 ARG I 83 REMARK 465 LYS I 84 REMARK 465 THR I 85 REMARK 465 THR I 86 REMARK 465 GLU I 87 REMARK 465 MET I 88 REMARK 465 GLN I 89 REMARK 465 SER I 90 REMARK 465 PRO I 91 REMARK 465 MET I 92 REMARK 465 GLN I 93 REMARK 465 PRO I 94 REMARK 465 VAL I 95 REMARK 465 ASP I 96 REMARK 465 GLN I 97 REMARK 465 ALA I 98 REMARK 465 SER I 99 REMARK 465 LEU I 100 REMARK 465 PRO I 159 REMARK 465 GLN I 160 REMARK 465 LEU I 161 REMARK 465 ILE I 162 REMARK 465 CYS I 163 REMARK 465 THR I 164 REMARK 465 GLY I 165 REMARK 465 GLU I 166 REMARK 465 MET I 167 REMARK 465 GLU I 168 REMARK 465 THR I 169 REMARK 465 SER I 170 REMARK 465 GLN I 171 REMARK 465 PHE I 172 REMARK 465 PRO I 173 REMARK 465 GLY I 174 REMARK 465 GLU I 175 REMARK 465 GLU I 176 REMARK 465 LYS I 177 REMARK 465 PRO I 178 REMARK 465 GLN I 179 REMARK 465 ALA I 180 REMARK 465 SER I 181 REMARK 465 PRO I 182 REMARK 465 GLU I 183 REMARK 465 GLY I 184 REMARK 465 ARG I 185 REMARK 465 PRO I 186 REMARK 465 GLU I 187 REMARK 465 SER I 188 REMARK 465 GLU I 189 REMARK 465 THR I 190 REMARK 465 SER I 191 REMARK 465 CYS I 192 REMARK 465 LEU I 193 REMARK 465 VAL I 194 REMARK 465 THR I 195 REMARK 465 THR I 196 REMARK 465 THR I 197 REMARK 465 ASP I 198 REMARK 465 PHE I 199 REMARK 465 GLN I 200 REMARK 465 ILE I 201 REMARK 465 GLN I 202 REMARK 465 THR I 203 REMARK 465 GLU I 204 REMARK 465 MET I 205 REMARK 465 ALA I 206 REMARK 465 ALA I 207 REMARK 465 THR I 208 REMARK 465 MET I 209 REMARK 465 GLU I 210 REMARK 465 THR I 211 REMARK 465 SER I 212 REMARK 465 ILE I 213 REMARK 465 PHE I 214 REMARK 465 THR I 215 REMARK 465 THR I 216 REMARK 465 GLU I 217 REMARK 465 HIS I 218 REMARK 465 HIS I 219 REMARK 465 HIS I 220 REMARK 465 HIS I 221 REMARK 465 HIS I 222 REMARK 465 HIS I 223 REMARK 465 PHE J 34 REMARK 465 ARG J 35 REMARK 465 ARG J 36 REMARK 465 SER J 64 REMARK 465 ALA J 65 REMARK 465 THR J 66 REMARK 465 ARG J 67 REMARK 465 ASN J 68 REMARK 465 THR J 69 REMARK 465 THR J 70 REMARK 465 LYS J 71 REMARK 465 GLN J 72 REMARK 465 VAL J 73 REMARK 465 THR J 74 REMARK 465 PRO J 75 REMARK 465 GLN J 76 REMARK 465 PRO J 77 REMARK 465 GLU J 78 REMARK 465 GLU J 79 REMARK 465 GLN J 80 REMARK 465 LYS J 81 REMARK 465 GLU J 82 REMARK 465 ARG J 83 REMARK 465 LYS J 84 REMARK 465 THR J 85 REMARK 465 THR J 86 REMARK 465 GLU J 87 REMARK 465 MET J 88 REMARK 465 GLN J 89 REMARK 465 SER J 90 REMARK 465 PRO J 91 REMARK 465 MET J 92 REMARK 465 GLN J 93 REMARK 465 PRO J 94 REMARK 465 VAL J 95 REMARK 465 ASP J 96 REMARK 465 GLN J 97 REMARK 465 ALA J 98 REMARK 465 SER J 99 REMARK 465 LEU J 100 REMARK 465 PRO J 101 REMARK 465 GLY J 102 REMARK 465 PRO J 159 REMARK 465 GLN J 160 REMARK 465 LEU J 161 REMARK 465 ILE J 162 REMARK 465 CYS J 163 REMARK 465 THR J 164 REMARK 465 GLY J 165 REMARK 465 GLU J 166 REMARK 465 MET J 167 REMARK 465 GLU J 168 REMARK 465 THR J 169 REMARK 465 SER J 170 REMARK 465 GLN J 171 REMARK 465 PHE J 172 REMARK 465 PRO J 173 REMARK 465 GLY J 174 REMARK 465 GLU J 175 REMARK 465 GLU J 176 REMARK 465 LYS J 177 REMARK 465 PRO J 178 REMARK 465 GLN J 179 REMARK 465 ALA J 180 REMARK 465 SER J 181 REMARK 465 PRO J 182 REMARK 465 GLU J 183 REMARK 465 GLY J 184 REMARK 465 ARG J 185 REMARK 465 PRO J 186 REMARK 465 GLU J 187 REMARK 465 SER J 188 REMARK 465 GLU J 189 REMARK 465 THR J 190 REMARK 465 SER J 191 REMARK 465 CYS J 192 REMARK 465 LEU J 193 REMARK 465 VAL J 194 REMARK 465 THR J 195 REMARK 465 THR J 196 REMARK 465 THR J 197 REMARK 465 ASP J 198 REMARK 465 PHE J 199 REMARK 465 GLN J 200 REMARK 465 ILE J 201 REMARK 465 GLN J 202 REMARK 465 THR J 203 REMARK 465 GLU J 204 REMARK 465 MET J 205 REMARK 465 ALA J 206 REMARK 465 ALA J 207 REMARK 465 THR J 208 REMARK 465 MET J 209 REMARK 465 GLU J 210 REMARK 465 THR J 211 REMARK 465 SER J 212 REMARK 465 ILE J 213 REMARK 465 PHE J 214 REMARK 465 THR J 215 REMARK 465 THR J 216 REMARK 465 GLU J 217 REMARK 465 HIS J 218 REMARK 465 HIS J 219 REMARK 465 HIS J 220 REMARK 465 HIS J 221 REMARK 465 HIS J 222 REMARK 465 HIS J 223 REMARK 465 LYS K 31 REMARK 465 ARG K 32 REMARK 465 GLY K 33 REMARK 465 PHE K 34 REMARK 465 ARG K 35 REMARK 465 SER K 64 REMARK 465 ALA K 65 REMARK 465 THR K 66 REMARK 465 ARG K 67 REMARK 465 ASN K 68 REMARK 465 THR K 69 REMARK 465 THR K 70 REMARK 465 LYS K 71 REMARK 465 GLN K 72 REMARK 465 VAL K 73 REMARK 465 THR K 74 REMARK 465 PRO K 75 REMARK 465 GLN K 76 REMARK 465 PRO K 77 REMARK 465 GLU K 78 REMARK 465 GLU K 79 REMARK 465 GLN K 80 REMARK 465 LYS K 81 REMARK 465 GLU K 82 REMARK 465 ARG K 83 REMARK 465 LYS K 84 REMARK 465 THR K 85 REMARK 465 THR K 86 REMARK 465 GLU K 87 REMARK 465 MET K 88 REMARK 465 GLN K 89 REMARK 465 SER K 90 REMARK 465 PRO K 91 REMARK 465 MET K 92 REMARK 465 GLN K 93 REMARK 465 PRO K 94 REMARK 465 VAL K 95 REMARK 465 ASP K 96 REMARK 465 GLN K 97 REMARK 465 ALA K 98 REMARK 465 SER K 99 REMARK 465 LEU K 100 REMARK 465 THR K 157 REMARK 465 GLN K 158 REMARK 465 PRO K 159 REMARK 465 GLN K 160 REMARK 465 LEU K 161 REMARK 465 ILE K 162 REMARK 465 CYS K 163 REMARK 465 THR K 164 REMARK 465 GLY K 165 REMARK 465 GLU K 166 REMARK 465 MET K 167 REMARK 465 GLU K 168 REMARK 465 THR K 169 REMARK 465 SER K 170 REMARK 465 GLN K 171 REMARK 465 PHE K 172 REMARK 465 PRO K 173 REMARK 465 GLY K 174 REMARK 465 GLU K 175 REMARK 465 GLU K 176 REMARK 465 LYS K 177 REMARK 465 PRO K 178 REMARK 465 GLN K 179 REMARK 465 ALA K 180 REMARK 465 SER K 181 REMARK 465 PRO K 182 REMARK 465 GLU K 183 REMARK 465 GLY K 184 REMARK 465 ARG K 185 REMARK 465 PRO K 186 REMARK 465 GLU K 187 REMARK 465 SER K 188 REMARK 465 GLU K 189 REMARK 465 THR K 190 REMARK 465 SER K 191 REMARK 465 CYS K 192 REMARK 465 LEU K 193 REMARK 465 VAL K 194 REMARK 465 THR K 195 REMARK 465 THR K 196 REMARK 465 THR K 197 REMARK 465 ASP K 198 REMARK 465 PHE K 199 REMARK 465 GLN K 200 REMARK 465 ILE K 201 REMARK 465 GLN K 202 REMARK 465 THR K 203 REMARK 465 GLU K 204 REMARK 465 MET K 205 REMARK 465 ALA K 206 REMARK 465 ALA K 207 REMARK 465 THR K 208 REMARK 465 MET K 209 REMARK 465 GLU K 210 REMARK 465 THR K 211 REMARK 465 SER K 212 REMARK 465 ILE K 213 REMARK 465 PHE K 214 REMARK 465 THR K 215 REMARK 465 THR K 216 REMARK 465 GLU K 217 REMARK 465 HIS K 218 REMARK 465 HIS K 219 REMARK 465 HIS K 220 REMARK 465 HIS K 221 REMARK 465 HIS K 222 REMARK 465 HIS K 223 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 O3 NAG J 300 O5 NAG J 301 2.03 REMARK 500 ND2 ASN J 49 O5 NAG J 300 2.19 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 GLN A 41 -164.87 -70.28 REMARK 500 SER A 83 66.12 34.88 REMARK 500 SER A 132 10.62 94.35 REMARK 500 ASP A 146 61.10 65.52 REMARK 500 THR A 162 -53.39 -135.97 REMARK 500 ASN A 206 8.75 57.77 REMARK 500 TRP B 46 -59.16 -135.26 REMARK 500 THR B 50 -55.48 73.77 REMARK 500 ASN B 135 74.69 46.19 REMARK 500 LYS B 187 -56.34 -122.89 REMARK 500 ASP C 146 61.88 64.76 REMARK 500 PRO C 149 -155.33 -92.43 REMARK 500 THR C 162 -53.45 -135.84 REMARK 500 TRP D 46 -59.68 -129.81 REMARK 500 THR D 50 -51.69 74.48 REMARK 500 SER D 66 145.67 -171.92 REMARK 500 ASN D 135 73.76 50.34 REMARK 500 ASN D 149 -17.79 85.60 REMARK 500 SER H 54 61.42 -41.25 REMARK 500 SER H 83 70.36 30.04 REMARK 500 SER H 89 104.35 -54.90 REMARK 500 THR H 118 106.80 -52.47 REMARK 500 LYS H 131 -15.95 -179.20 REMARK 500 ASP H 146 68.40 60.68 REMARK 500 PRO H 149 -155.49 -90.04 REMARK 500 SER H 158 14.39 51.88 REMARK 500 THR H 193 -70.37 -87.08 REMARK 500 TRP L 46 -51.57 -136.44 REMARK 500 ASP L 49 52.32 39.71 REMARK 500 THR L 50 -53.26 65.85 REMARK 500 ALA L 82 93.05 -61.86 REMARK 500 ASN L 135 75.22 52.67 REMARK 500 LYS L 166 -60.34 -95.91 REMARK 500 PRO I 11 -38.07 -31.98 REMARK 500 THR I 47 -158.26 -153.14 REMARK 500 ASN I 49 -166.93 -74.60 REMARK 500 ASP I 56 -74.14 -84.22 REMARK 500 TRP I 110 -41.20 -144.77 REMARK 500 GLU I 111 68.43 153.70 REMARK 500 GLU I 116 5.75 50.17 REMARK 500 ARG I 117 174.34 58.44 REMARK 500 GLN I 133 72.35 54.77 REMARK 500 ALA I 137 58.13 -103.78 REMARK 500 PRO J 11 108.77 -29.32 REMARK 500 LYS J 38 112.83 58.01 REMARK 500 ASN J 49 -172.08 -61.74 REMARK 500 SER J 51 79.89 53.53 REMARK 500 HIS J 52 87.76 158.97 REMARK 500 CYS J 104 -169.72 -124.52 REMARK 500 GLU J 111 -75.48 -38.91 REMARK 500 REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS. 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 NAG I 300 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA I 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 300 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA J 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 300 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA K 302