REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650) 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) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.17 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 89.1 REMARK 3 NUMBER OF REFLECTIONS : 57680 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.220 REMARK 3 R VALUE (WORKING SET) : 0.219 REMARK 3 FREE R VALUE : 0.240 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110 REMARK 3 FREE R VALUE TEST SET COUNT : 2948 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 40.1726 - 8.5252 0.81 2535 155 0.2225 0.2325 REMARK 3 2 8.5252 - 6.7772 0.85 2534 152 0.1982 0.2146 REMARK 3 3 6.7772 - 5.9236 0.86 2596 111 0.2324 0.2544 REMARK 3 4 5.9236 - 5.3834 0.87 2567 127 0.2204 0.2403 REMARK 3 5 5.3834 - 4.9983 0.87 2552 150 0.1818 0.1954 REMARK 3 6 4.9983 - 4.7041 0.88 2574 143 0.1758 0.1920 REMARK 3 7 4.7041 - 4.4688 0.88 2601 117 0.1759 0.1892 REMARK 3 8 4.4688 - 4.2745 0.89 2610 127 0.1842 0.2305 REMARK 3 9 4.2745 - 4.1101 0.89 2600 150 0.2066 0.2051 REMARK 3 10 4.1101 - 3.9684 0.90 2598 142 0.2054 0.2173 REMARK 3 11 3.9684 - 3.8445 0.90 2626 133 0.2152 0.2709 REMARK 3 12 3.8445 - 3.7347 0.90 2637 151 0.2272 0.2197 REMARK 3 13 3.7347 - 3.6364 0.91 2612 142 0.2274 0.2866 REMARK 3 14 3.6364 - 3.5477 0.91 2595 155 0.2321 0.2362 REMARK 3 15 3.5477 - 3.4671 0.91 2690 144 0.2459 0.2738 REMARK 3 16 3.4671 - 3.3934 0.91 2599 143 0.2579 0.3029 REMARK 3 17 3.3934 - 3.3255 0.92 2631 160 0.2726 0.3239 REMARK 3 18 3.3255 - 3.2628 0.92 2669 139 0.2890 0.3039 REMARK 3 19 3.2628 - 3.2046 0.92 2642 123 0.2925 0.3343 REMARK 3 20 3.2046 - 3.1503 0.92 2703 149 0.3073 0.3671 REMARK 3 21 3.1503 - 3.0990 0.89 2561 135 0.3257 0.3322 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 : 0.29 REMARK 3 B_SOL : 28.98 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.280 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 75.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -5.18780 REMARK 3 B22 (A**2) : 7.67380 REMARK 3 B33 (A**2) : -2.48600 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 : 0.008 14661 REMARK 3 ANGLE : 0.944 19984 REMARK 3 CHIRALITY : 0.054 2268 REMARK 3 PLANARITY : 0.002 2482 REMARK 3 DIHEDRAL : 9.644 5005 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (chain A and resid 5:507) REMARK 3 ORIGIN FOR THE GROUP (A): -71.6828 33.6011 10.2436 REMARK 3 T TENSOR REMARK 3 T11: 0.2658 T22: 0.3637 REMARK 3 T33: 0.3207 T12: 0.0365 REMARK 3 T13: -0.0003 T23: -0.0360 REMARK 3 L TENSOR REMARK 3 L11: 1.1433 L22: 1.5122 REMARK 3 L33: 1.3871 L12: 0.1462 REMARK 3 L13: 0.2516 L23: 0.1434 REMARK 3 S TENSOR REMARK 3 S11: 0.0106 S12: -0.2396 S13: -0.0584 REMARK 3 S21: 0.1929 S22: -0.0752 S23: 0.2630 REMARK 3 S31: -0.0847 S32: -0.2934 S33: -0.0020 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (chain B and resid 6:507) REMARK 3 ORIGIN FOR THE GROUP (A): -74.7841 28.7768 -38.3005 REMARK 3 T TENSOR REMARK 3 T11: 0.4827 T22: 0.5799 REMARK 3 T33: 0.5257 T12: 0.1426 REMARK 3 T13: -0.0458 T23: -0.1413 REMARK 3 L TENSOR REMARK 3 L11: 2.1456 L22: 1.1886 REMARK 3 L33: 2.2009 L12: -0.0972 REMARK 3 L13: -0.5395 L23: 0.1233 REMARK 3 S TENSOR REMARK 3 S11: 0.0301 S12: 0.5059 S13: 0.2418 REMARK 3 S21: -0.3448 S22: -0.1018 S23: 0.2379 REMARK 3 S31: -0.2748 S32: -0.5768 S33: -0.0053 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (chain H and resid 20:142) REMARK 3 ORIGIN FOR THE GROUP (A): -29.8297 12.9909 -43.0863 REMARK 3 T TENSOR REMARK 3 T11: 0.6034 T22: 0.5727 REMARK 3 T33: 0.4783 T12: -0.0408 REMARK 3 T13: 0.0483 T23: -0.1875 REMARK 3 L TENSOR REMARK 3 L11: 1.9361 L22: 1.7911 REMARK 3 L33: 1.6597 L12: -0.8019 REMARK 3 L13: -1.2598 L23: 0.9916 REMARK 3 S TENSOR REMARK 3 S11: 0.0660 S12: -0.2947 S13: 0.2212 REMARK 3 S21: 0.1385 S22: 0.0576 S23: 0.0738 REMARK 3 S31: 0.0544 S32: 0.2716 S33: 0.0002 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (chain H and resid 143:238) REMARK 3 ORIGIN FOR THE GROUP (A): -4.7363 0.5465 -54.3015 REMARK 3 T TENSOR REMARK 3 T11: 0.6110 T22: 0.7529 REMARK 3 T33: 0.8104 T12: 0.0310 REMARK 3 T13: 0.0505 T23: -0.1828 REMARK 3 L TENSOR REMARK 3 L11: 1.0980 L22: 0.7148 REMARK 3 L33: 0.2342 L12: -0.5386 REMARK 3 L13: 0.3654 L23: 0.1123 REMARK 3 S TENSOR REMARK 3 S11: -0.1717 S12: -0.5269 S13: 0.0683 REMARK 3 S21: 0.2085 S22: 0.2250 S23: -0.3755 REMARK 3 S31: -0.0146 S32: 0.2881 S33: 0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (chain I and resid 20:142) REMARK 3 ORIGIN FOR THE GROUP (A): -40.5278 -2.2802 15.2034 REMARK 3 T TENSOR REMARK 3 T11: 0.7631 T22: 0.5843 REMARK 3 T33: 0.5501 T12: -0.0163 REMARK 3 T13: -0.1541 T23: 0.0407 REMARK 3 L TENSOR REMARK 3 L11: 1.3995 L22: 1.3259 REMARK 3 L33: 1.8321 L12: -0.7121 REMARK 3 L13: 1.1857 L23: -1.1571 REMARK 3 S TENSOR REMARK 3 S11: 0.3203 S12: 0.2750 S13: -0.2452 REMARK 3 S21: -0.3729 S22: -0.1764 S23: 0.1885 REMARK 3 S31: 0.3094 S32: 0.1513 S33: 0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (chain I and resid 143:238) REMARK 3 ORIGIN FOR THE GROUP (A): -19.1702 -20.3690 26.4751 REMARK 3 T TENSOR REMARK 3 T11: 0.9155 T22: 0.7586 REMARK 3 T33: 0.8367 T12: 0.2143 REMARK 3 T13: -0.1381 T23: -0.0261 REMARK 3 L TENSOR REMARK 3 L11: 0.4448 L22: 0.5903 REMARK 3 L33: 0.2275 L12: -0.2704 REMARK 3 L13: -0.1099 L23: 0.3707 REMARK 3 S TENSOR REMARK 3 S11: 0.4245 S12: 0.2977 S13: -0.3847 REMARK 3 S21: -0.4499 S22: -0.2519 S23: 0.0086 REMARK 3 S31: 0.2716 S32: 0.1810 S33: 0.0001 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (chain L and resid 21:131) REMARK 3 ORIGIN FOR THE GROUP (A): -34.3317 -3.2742 -51.7768 REMARK 3 T TENSOR REMARK 3 T11: 0.6070 T22: 0.5020 REMARK 3 T33: 0.5285 T12: -0.0574 REMARK 3 T13: 0.1040 T23: -0.1163 REMARK 3 L TENSOR REMARK 3 L11: 1.2415 L22: 2.3126 REMARK 3 L33: 1.2335 L12: 0.0223 REMARK 3 L13: -0.0569 L23: 0.3592 REMARK 3 S TENSOR REMARK 3 S11: -0.2490 S12: 0.0149 S13: -0.2927 REMARK 3 S21: 0.1124 S22: -0.0705 S23: 0.1302 REMARK 3 S31: 0.1523 S32: 0.1214 S33: -0.0000 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (chain L and resid 132:235) REMARK 3 ORIGIN FOR THE GROUP (A): -5.4670 -15.5739 -47.4483 REMARK 3 T TENSOR REMARK 3 T11: 0.8938 T22: 0.9580 REMARK 3 T33: 1.0436 T12: 0.2998 REMARK 3 T13: 0.1063 T23: 0.2372 REMARK 3 L TENSOR REMARK 3 L11: 0.7803 L22: 0.9445 REMARK 3 L33: 1.1012 L12: 0.2766 REMARK 3 L13: -0.5725 L23: 0.5751 REMARK 3 S TENSOR REMARK 3 S11: -0.5259 S12: -1.4340 S13: -1.2380 REMARK 3 S21: 0.5554 S22: 0.5196 S23: -0.4026 REMARK 3 S31: 0.2532 S32: 0.2136 S33: 0.0004 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (chain M and resid 21:131) REMARK 3 ORIGIN FOR THE GROUP (A): -26.6977 8.2957 22.9785 REMARK 3 T TENSOR REMARK 3 T11: 0.5246 T22: 0.4945 REMARK 3 T33: 0.4991 T12: -0.0099 REMARK 3 T13: -0.0614 T23: 0.1346 REMARK 3 L TENSOR REMARK 3 L11: 1.5127 L22: 1.1159 REMARK 3 L33: 1.1133 L12: -0.0676 REMARK 3 L13: -0.2108 L23: 0.2520 REMARK 3 S TENSOR REMARK 3 S11: -0.0400 S12: 0.3123 S13: 0.2355 REMARK 3 S21: 0.0359 S22: -0.0950 S23: -0.1799 REMARK 3 S31: 0.2413 S32: 0.1805 S33: 0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (chain M and resid 132:235) REMARK 3 ORIGIN FOR THE GROUP (A): -4.7465 -14.1278 18.6850 REMARK 3 T TENSOR REMARK 3 T11: 0.9272 T22: 1.0767 REMARK 3 T33: 0.7565 T12: 0.3494 REMARK 3 T13: 0.1883 T23: 0.0791 REMARK 3 L TENSOR REMARK 3 L11: 0.6978 L22: 1.0801 REMARK 3 L33: 1.2517 L12: 0.3974 REMARK 3 L13: 0.3336 L23: -0.7756 REMARK 3 S TENSOR REMARK 3 S11: 0.2924 S12: 0.9151 S13: -0.0528 REMARK 3 S21: -0.8868 S22: -0.1527 S23: -0.7627 REMARK 3 S31: 0.3725 S32: 0.5373 S33: 0.0012 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 3 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain A and (resseq 6:129 or resseq 135: REMARK 3 308 or resseq 310:471 or resseq 480:507 ) REMARK 3 SELECTION : chain B and (resseq 6:129 or resseq 135: REMARK 3 308 or resseq 310:471 or resseq 480:507 ) REMARK 3 ATOM PAIRS NUMBER : 3762 REMARK 3 RMSD : 0.008 REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain L and (resseq 21:215 ) REMARK 3 SELECTION : chain M and (resseq 21:215 ) REMARK 3 ATOM PAIRS NUMBER : 1515 REMARK 3 RMSD : 0.007 REMARK 3 NCS GROUP : 3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain H and (resseq 20:135 or resseq 143: REMARK 3 154 or resseq 162:219 ) REMARK 3 SELECTION : chain I and (resseq 20:135 or resseq 143: REMARK 3 154 or resseq 162:219 ) REMARK 3 ATOM PAIRS NUMBER : 1419 REMARK 3 RMSD : 0.009 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3TT1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-11. REMARK 100 THE RCSB ID CODE IS RCSB067882. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL 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 : APS REMARK 200 BEAMLINE : 24-ID-E REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(220) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57718 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.099 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 (%) : 89.1 REMARK 200 DATA REDUNDANCY : 7.200 REMARK 200 R MERGE (I) : 0.10600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21 REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0 REMARK 200 DATA REDUNDANCY IN SHELL : 4.10 REMARK 200 R MERGE FOR SHELL (I) : 0.56100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.920 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 3F3A REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 70.49 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.17 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 40 MM TRIS-HCL, 23-26% PEG550 MME, 50- REMARK 280 100 MM SODIUM CHLORIDE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 298.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 51.42950 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 105.04050 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 81.38050 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 105.04050 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.42950 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 81.38050 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, M, I 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 APPLY THE FOLLOWING TO CHAINS: B, 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 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 MET A 1 REMARK 465 GLU A 2 REMARK 465 VAL A 3 REMARK 465 LYS A 4 REMARK 465 PRO A 130 REMARK 465 PRO A 131 REMARK 465 PRO A 132 REMARK 465 ASN A 133 REMARK 465 ALA A 134 REMARK 465 ARG A 508 REMARK 465 ASN A 509 REMARK 465 HIS A 510 REMARK 465 GLU A 511 REMARK 465 SER A 512 REMARK 465 ALA A 513 REMARK 465 GLY A 514 REMARK 465 THR A 515 REMARK 465 LEU A 516 REMARK 465 VAL A 517 REMARK 465 PRO A 518 REMARK 465 ARG A 519 REMARK 465 MET B 1 REMARK 465 GLU B 2 REMARK 465 VAL B 3 REMARK 465 LYS B 4 REMARK 465 PRO B 130 REMARK 465 PRO B 131 REMARK 465 PRO B 132 REMARK 465 ASN B 133 REMARK 465 ALA B 134 REMARK 465 ARG B 508 REMARK 465 ASN B 509 REMARK 465 HIS B 510 REMARK 465 GLU B 511 REMARK 465 SER B 512 REMARK 465 ALA B 513 REMARK 465 GLY B 514 REMARK 465 THR B 515 REMARK 465 LEU B 516 REMARK 465 VAL B 517 REMARK 465 PRO B 518 REMARK 465 ARG B 519 REMARK 465 ASN L 216 REMARK 465 GLU L 217 REMARK 465 CYS L 218 REMARK 465 CYS H 136 REMARK 465 GLY H 137 REMARK 465 ASP H 138 REMARK 465 THR H 139 REMARK 465 THR H 140 REMARK 465 GLY H 141 REMARK 465 SER H 142 REMARK 465 ASN M 216 REMARK 465 GLU M 217 REMARK 465 CYS M 218 REMARK 465 CYS I 136 REMARK 465 GLY I 137 REMARK 465 ASP I 138 REMARK 465 THR I 139 REMARK 465 THR I 140 REMARK 465 GLY I 141 REMARK 465 SER I 142 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 VAL A 54 CG1 CG2 REMARK 470 ARG A 88 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 91 CG CD CE NZ REMARK 470 LYS A 121 CG CD CE NZ REMARK 470 LEU A 126 CG CD1 CD2 REMARK 470 VAL A 127 CG1 CG2 REMARK 470 GLU A 129 CG CD OE1 OE2 REMARK 470 ARG A 142 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 146 CG CD OE1 OE2 REMARK 470 ASP A 158 CG OD1 OD2 REMARK 470 GLU A 159 CG CD OE1 OE2 REMARK 470 ASP A 234 CG OD1 OD2 REMARK 470 GLU A 236 CG CD OE1 OE2 REMARK 470 LYS A 237 CG CD CE NZ REMARK 470 LYS A 239 CG CD CE NZ REMARK 470 VAL A 308 CG1 CG2 REMARK 470 VAL A 312 CG1 CG2 REMARK 470 LYS A 316 CG CD CE NZ REMARK 470 ILE A 421 CG1 CG2 CD1 REMARK 470 TYR A 450 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL A 465 CG1 CG2 REMARK 470 VAL A 466 CG1 CG2 REMARK 470 ARG A 469 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 470 CG CD OE1 OE2 REMARK 470 TYR A 471 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 474 CG CD CE NZ REMARK 470 GLU A 478 CG CD OE1 OE2 REMARK 470 LEU A 493 CG CD1 CD2 REMARK 470 GLU A 505 CG CD OE1 OE2 REMARK 470 ARG A 506 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 507 CG CD NE CZ NH1 NH2 REMARK 470 VAL B 54 CG1 CG2 REMARK 470 ARG B 88 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 91 CG CD CE NZ REMARK 470 LYS B 121 CG CD CE NZ REMARK 470 LEU B 126 CG CD1 CD2 REMARK 470 VAL B 127 CG1 CG2 REMARK 470 GLU B 129 CG CD OE1 OE2 REMARK 470 ARG B 142 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 146 CG CD OE1 OE2 REMARK 470 ASP B 158 CG OD1 OD2 REMARK 470 GLU B 159 CG CD OE1 OE2 REMARK 470 ASP B 234 CG OD1 OD2 REMARK 470 GLU B 236 CG CD OE1 OE2 REMARK 470 LYS B 237 CG CD CE NZ REMARK 470 LYS B 239 CG CD CE NZ REMARK 470 VAL B 308 CG1 CG2 REMARK 470 VAL B 312 CG1 CG2 REMARK 470 LYS B 316 CG CD CE NZ REMARK 470 ILE B 421 CG1 CG2 CD1 REMARK 470 TYR B 450 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL B 465 CG1 CG2 REMARK 470 VAL B 466 CG1 CG2 REMARK 470 ARG B 469 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 470 CG CD OE1 OE2 REMARK 470 TYR B 471 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS B 474 CG CD CE NZ REMARK 470 GLU B 478 CG CD OE1 OE2 REMARK 470 LEU B 493 CG CD1 CD2 REMARK 470 GLU B 505 CG CD OE1 OE2 REMARK 470 ARG B 506 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 507 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 10 CG CD OE1 OE2 REMARK 470 ARG H 13 CG CD NE CZ NH1 NH2 REMARK 470 SER H 211 OG REMARK 470 LYS H 213 CG CD CE NZ REMARK 470 GLU I 10 CG CD OE1 OE2 REMARK 470 ARG I 13 CG CD NE CZ NH1 NH2 REMARK 470 SER I 211 OG REMARK 470 LYS I 213 CG CD CE NZ 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 A 54 -45.57 -132.10 REMARK 500 ARG A 86 85.37 -67.57 REMARK 500 PRO A 160 47.66 -87.28 REMARK 500 GLU A 290 -63.62 -94.59 REMARK 500 SER A 298 -75.97 -57.27 REMARK 500 ASN A 310 -18.00 78.26 REMARK 500 ILE A 325 -61.75 -124.43 REMARK 500 THR A 409 -71.97 -120.25 REMARK 500 VAL B 54 -45.56 -132.35 REMARK 500 ARG B 86 85.56 -67.80 REMARK 500 PRO B 160 47.34 -87.23 REMARK 500 GLU B 290 -63.48 -94.42 REMARK 500 SER B 298 -76.14 -57.10 REMARK 500 ASN B 310 -19.65 82.60 REMARK 500 ILE B 325 -61.77 -124.36 REMARK 500 THR B 409 -72.07 -120.56 REMARK 500 TYR L 31 114.07 -163.53 REMARK 500 ALA L 55 -43.56 74.68 REMARK 500 LYS L 173 -60.88 -103.41 REMARK 500 GLU L 191 33.81 -84.60 REMARK 500 ALA H 92 -175.66 -171.74 REMARK 500 PRO H 134 172.40 -56.78 REMARK 500 PHE H 154 137.58 -172.63 REMARK 500 TRP H 162 -102.07 -90.46 REMARK 500 LEU H 167 64.62 64.29 REMARK 500 SER H 210 -96.89 -125.10 REMARK 500 TYR M 31 113.98 -163.77 REMARK 500 ALA M 55 -43.36 74.65 REMARK 500 LYS M 173 -60.97 -103.06 REMARK 500 GLU M 191 33.93 -84.71 REMARK 500 ALA I 92 -175.72 -171.49 REMARK 500 PRO I 134 172.53 -56.99 REMARK 500 PHE I 154 137.87 -173.24 REMARK 500 TRP I 162 -101.69 -91.78 REMARK 500 LEU I 167 64.98 64.38 REMARK 500 SER I 210 -96.92 -124.97 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 SOG A 521 REMARK 610 SOG A 522 REMARK 610 SOG B 521 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 602 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA B 351 O REMARK 620 2 VAL B 23 O 113.6 REMARK 620 3 THR B 354 OG1 92.8 143.6 REMARK 620 4 SER B 355 OG 99.6 87.2 113.8 REMARK 620 5 GLY B 20 O 163.8 82.3 71.5 83.9 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 602 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA A 351 O REMARK 620 2 VAL A 23 O 112.8 REMARK 620 3 THR A 354 OG1 92.7 143.0 REMARK 620 4 SER A 355 OG 100.1 87.7 114.8 REMARK 620 5 GLY A 20 O 163.9 82.6 71.4 84.9 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 601 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR A 254 O REMARK 620 2 THR A 254 OG1 80.1 REMARK 620 3 ALA A 22 O 80.2 159.3 REMARK 620 4 ASN A 286 OD1 100.2 92.4 85.0 REMARK 620 5 ASN A 27 OD1 167.6 96.6 104.0 91.9 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 601 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR B 254 O REMARK 620 2 ALA B 22 O 80.3 REMARK 620 3 THR B 254 OG1 79.9 158.7 REMARK 620 4 ASN B 27 OD1 169.0 105.0 95.9 REMARK 620 5 ASN B 286 OD1 98.8 84.6 90.8 91.4 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SOG A 520 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SOG A 521 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SOG A 522 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SOG B 520 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SOG B 521 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2A65 RELATED DB: PDB REMARK 900 RELATED ID: 3TT3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF LEUT IN THE INWARD-OPEN CONFORMATION REMARK 900 IN COMPLEX WITH FAB REMARK 900 RELATED ID: 3TU0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF T355V, S354A, K288A LEUT MUTANT IN REMARK 900 COMPLEX WITH ALANINE AND SODIUM