REMARK 2 REMARK 2 RESOLUTION. 3.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168) 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) : 3.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.24 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 13877 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.216 REMARK 3 R VALUE (WORKING SET) : 0.213 REMARK 3 FREE R VALUE : 0.267 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.840 REMARK 3 FREE R VALUE TEST SET COUNT : 671 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 42.2394 - 6.1499 0.99 2725 121 0.1922 0.2423 REMARK 3 2 6.1499 - 4.8837 1.00 2630 155 0.2381 0.2730 REMARK 3 3 4.8837 - 4.2670 1.00 2627 127 0.1955 0.2583 REMARK 3 4 4.2670 - 3.8772 1.00 2612 138 0.2512 0.3384 REMARK 3 5 3.8772 - 3.6000 0.99 2612 130 0.2823 0.3359 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 : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.510 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.410 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) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL 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 : 0.003 6914 REMARK 3 ANGLE : 0.908 9385 REMARK 3 CHIRALITY : 0.060 1112 REMARK 3 PLANARITY : 0.004 1190 REMARK 3 DIHEDRAL : 13.729 2513 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN H AND RESID 1:111 ) OR (CHAIN L AND RESID 1: REMARK 3 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.8979 127.5043 10.9437 REMARK 3 T TENSOR REMARK 3 T11: 1.0506 T22: 0.6092 REMARK 3 T33: 0.6161 T12: 0.0704 REMARK 3 T13: 0.0680 T23: -0.0914 REMARK 3 L TENSOR REMARK 3 L11: 8.6865 L22: 5.8763 REMARK 3 L33: 2.4561 L12: 0.9407 REMARK 3 L13: 1.2051 L23: 0.1160 REMARK 3 S TENSOR REMARK 3 S11: 0.0672 S12: 0.4987 S13: -0.9587 REMARK 3 S21: 0.1769 S22: 0.3322 S23: -0.5828 REMARK 3 S31: 0.8022 S32: 0.0138 S33: -0.3768 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN H AND RESID 112:213 ) OR (CHAIN L AND RESID REMARK 3 114:211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.2047 105.2518 -6.0292 REMARK 3 T TENSOR REMARK 3 T11: 1.9971 T22: 1.3590 REMARK 3 T33: 1.4378 T12: -0.1557 REMARK 3 T13: -0.1107 T23: -0.4665 REMARK 3 L TENSOR REMARK 3 L11: 5.3929 L22: 4.7467 REMARK 3 L33: 2.1190 L12: -1.6282 REMARK 3 L13: 0.0422 L23: -2.4849 REMARK 3 S TENSOR REMARK 3 S11: 0.1925 S12: 1.3722 S13: -1.1346 REMARK 3 S21: -0.8887 S22: -0.0858 S23: -0.3701 REMARK 3 S31: 2.1760 S32: -0.5366 S33: -0.1649 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN F AND RESID 26:73 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.1107 171.8233 37.8653 REMARK 3 T TENSOR REMARK 3 T11: 0.6210 T22: 0.8243 REMARK 3 T33: 0.6749 T12: -0.0962 REMARK 3 T13: 0.2103 T23: 0.1318 REMARK 3 L TENSOR REMARK 3 L11: 1.5242 L22: 4.0759 REMARK 3 L33: 3.5553 L12: 0.2936 REMARK 3 L13: 0.9639 L23: 3.5767 REMARK 3 S TENSOR REMARK 3 S11: 0.1365 S12: -0.3646 S13: 0.0202 REMARK 3 S21: -0.0306 S22: 0.0531 S23: -0.5108 REMARK 3 S31: 0.0523 S32: -0.2529 S33: -0.2426 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN F AND RESID 74:263 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.0100 156.5579 25.5589 REMARK 3 T TENSOR REMARK 3 T11: 0.7603 T22: 0.6710 REMARK 3 T33: 1.0299 T12: 0.2417 REMARK 3 T13: -0.0394 T23: 0.1202 REMARK 3 L TENSOR REMARK 3 L11: 2.4807 L22: 4.5023 REMARK 3 L33: 6.2946 L12: 3.7456 REMARK 3 L13: 1.6123 L23: 4.3837 REMARK 3 S TENSOR REMARK 3 S11: -0.2646 S12: 0.1643 S13: -0.2635 REMARK 3 S21: 0.3529 S22: 0.0219 S23: -0.4071 REMARK 3 S31: 0.6831 S32: 0.6872 S33: 0.3347 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN F AND RESID 264:318 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.6164 167.6820 42.3761 REMARK 3 T TENSOR REMARK 3 T11: 0.8397 T22: 0.9310 REMARK 3 T33: 0.6204 T12: -0.0604 REMARK 3 T13: 0.0762 T23: 0.2303 REMARK 3 L TENSOR REMARK 3 L11: 2.8897 L22: 7.9304 REMARK 3 L33: 3.8452 L12: -0.1516 REMARK 3 L13: 1.6135 L23: 3.2205 REMARK 3 S TENSOR REMARK 3 S11: 0.4091 S12: -0.5478 S13: -0.2944 REMARK 3 S21: 1.1057 S22: -0.3575 S23: 0.6307 REMARK 3 S31: 1.1094 S32: -0.8502 S33: 0.1558 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN F AND RESID 319:363 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.5106 194.2468 50.1069 REMARK 3 T TENSOR REMARK 3 T11: 0.6634 T22: 0.9057 REMARK 3 T33: 1.0044 T12: 0.1382 REMARK 3 T13: -0.0684 T23: -0.1286 REMARK 3 L TENSOR REMARK 3 L11: 7.2804 L22: 2.1291 REMARK 3 L33: 7.0279 L12: 7.4154 REMARK 3 L13: -1.1842 L23: -2.2674 REMARK 3 S TENSOR REMARK 3 S11: 0.2220 S12: -0.3464 S13: 0.5607 REMARK 3 S21: -0.6350 S22: -0.1943 S23: 1.7419 REMARK 3 S31: -0.1763 S32: 0.4406 S33: 0.1005 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN F AND RESID 364:443 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.4504 198.6866 50.3108 REMARK 3 T TENSOR REMARK 3 T11: 1.0139 T22: 0.9065 REMARK 3 T33: 0.6144 T12: 0.1131 REMARK 3 T13: -0.0287 T23: -0.2562 REMARK 3 L TENSOR REMARK 3 L11: 3.7512 L22: 4.2173 REMARK 3 L33: 0.2550 L12: -0.4022 REMARK 3 L13: -0.5331 L23: -1.1300 REMARK 3 S TENSOR REMARK 3 S11: -0.0023 S12: -0.5413 S13: 0.5028 REMARK 3 S21: 0.0047 S22: 0.1046 S23: -0.1025 REMARK 3 S31: -0.3606 S32: 0.3096 S33: -0.1886 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN F AND RESID 444:477 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.8771 202.3134 48.0421 REMARK 3 T TENSOR REMARK 3 T11: 0.6814 T22: 0.7918 REMARK 3 T33: 0.7075 T12: -0.0022 REMARK 3 T13: 0.2497 T23: -0.0899 REMARK 3 L TENSOR REMARK 3 L11: 3.4189 L22: 9.2165 REMARK 3 L33: 2.0917 L12: -2.9393 REMARK 3 L13: 1.3594 L23: -1.8292 REMARK 3 S TENSOR REMARK 3 S11: -0.4918 S12: -0.6807 S13: -0.2403 REMARK 3 S21: 0.5588 S22: -0.2933 S23: 0.4703 REMARK 3 S31: 0.2518 S32: 0.0727 S33: 0.9278 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN F AND RESID 478:513 ) REMARK 3 ORIGIN FOR THE GROUP (A): 47.2175 207.5473 59.7095 REMARK 3 T TENSOR REMARK 3 T11: 1.2462 T22: 1.3743 REMARK 3 T33: 1.7858 T12: -0.3997 REMARK 3 T13: 0.1176 T23: -0.0721 REMARK 3 L TENSOR REMARK 3 L11: 6.9197 L22: 8.4794 REMARK 3 L33: 8.8338 L12: -0.1482 REMARK 3 L13: 2.8303 L23: 1.8172 REMARK 3 S TENSOR REMARK 3 S11: -1.3687 S12: 1.0569 S13: 0.2955 REMARK 3 S21: 0.0291 S22: 0.6001 S23: -1.0579 REMARK 3 S31: -0.1472 S32: 1.8039 S33: 0.6614 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 4JHW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-13. REMARK 100 THE RCSB ID CODE IS RCSB078066. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-DEC-12 REMARK 200 TEMPERATURE (KELVIN) : 200 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 : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : SI 111. ROSENBAUM-ROCK DOUBLE- REMARK 200 CRYSTAL MONOCHROMATOR REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13898 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 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) : 3.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.73 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3 REMARK 200 DATA REDUNDANCY IN SHELL : 5.20 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: PHASER REMARK 200 STARTING MODEL: 3RRR AND 4JHA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (W/V) PEG 400, 3.75% (W/V) PEG REMARK 280 3350, 0.1 M HEPES PH 7.5, AND 1% (V/V) 1,2-BUTANEDIOL, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3 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 5555 Z,X,Y REMARK 290 6555 Z+1/2,-X+1/2,-Y REMARK 290 7555 -Z+1/2,-X,Y+1/2 REMARK 290 8555 -Z,X+1/2,-Y+1/2 REMARK 290 9555 Y,Z,X REMARK 290 10555 -Y,Z+1/2,-X+1/2 REMARK 290 11555 Y+1/2,-Z+1/2,-X REMARK 290 12555 -Y+1/2,-Z,X+1/2 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 76.14300 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.14300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.14300 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.14300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 76.14300 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 76.14300 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 76.14300 REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 76.14300 REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 76.14300 REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 76.14300 REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 76.14300 REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 76.14300 REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 76.14300 REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 76.14300 REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 76.14300 REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 76.14300 REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 76.14300 REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 76.14300 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: NONAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 29540 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 104890 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -170.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, 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 350 BIOMT1 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 152.28600 REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 -152.28600 REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 -152.28600 REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 152.28600 REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 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 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 GLN F 125 REMARK 465 SER F 126 REMARK 465 THR F 127 REMARK 465 PRO F 128 REMARK 465 ALA F 129 REMARK 465 THR F 130 REMARK 465 ASN F 131 REMARK 465 ASN F 132 REMARK 465 ARG F 133 REMARK 465 ALA F 134 REMARK 465 ARG F 135 REMARK 465 ARG F 136 REMARK 465 SER F 514 REMARK 465 ALA F 515 REMARK 465 ILE F 516 REMARK 465 GLY F 517 REMARK 465 GLY F 518 REMARK 465 TYR F 519 REMARK 465 ILE F 520 REMARK 465 PRO F 521 REMARK 465 GLU F 522 REMARK 465 ALA F 523 REMARK 465 PRO F 524 REMARK 465 ARG F 525 REMARK 465 ASP F 526 REMARK 465 GLY F 527 REMARK 465 GLN F 528 REMARK 465 ALA F 529 REMARK 465 TYR F 530 REMARK 465 VAL F 531 REMARK 465 ARG F 532 REMARK 465 LYS F 533 REMARK 465 ASP F 534 REMARK 465 GLY F 535 REMARK 465 GLU F 536 REMARK 465 TRP F 537 REMARK 465 VAL F 538 REMARK 465 LEU F 539 REMARK 465 LEU F 540 REMARK 465 SER F 541 REMARK 465 THR F 542 REMARK 465 PHE F 543 REMARK 465 LEU F 544 REMARK 465 GLY F 545 REMARK 465 GLY F 546 REMARK 465 LEU F 547 REMARK 465 VAL F 548 REMARK 465 PRO F 549 REMARK 465 ARG F 550 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 OG SER F 46 OG1 THR F 311 2.13 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 LEU H 124 77.66 -108.73 REMARK 500 SER H 130 68.32 -108.81 REMARK 500 ASP H 144 63.31 64.21 REMARK 500 VAL L 30 -114.20 54.70 REMARK 500 ALA L 51 -38.18 71.99 REMARK 500 SER L 52 -4.76 -140.07 REMARK 500 SER L 77 89.26 -150.46 REMARK 500 ASN L 138 76.52 56.07 REMARK 500 ASP L 151 -105.65 55.42 REMARK 500 THR F 50 -105.46 56.48 REMARK 500 LEU F 138 179.11 60.17 REMARK 500 GLU F 161 -117.59 36.16 REMARK 500 SER F 182 -68.13 52.18 REMARK 500 GLN F 202 -37.67 -149.05 REMARK 500 LYS F 209 -71.09 -32.87 REMARK 500 GLN F 210 -81.03 -52.89 REMARK 500 SER F 211 -53.70 -144.56 REMARK 500 CYS F 212 -10.17 -173.67 REMARK 500 SER F 213 88.14 -69.97 REMARK 500 ASN F 216 92.07 -162.03 REMARK 500 PRO F 265 67.70 -63.22 REMARK 500 SER F 290 -94.56 -88.85 REMARK 500 ILE F 292 35.31 -140.91 REMARK 500 GLU F 294 -147.45 54.90 REMARK 500 GLU F 295 64.44 -115.85 REMARK 500 SER F 330 13.33 57.43 REMARK 500 THR F 357 47.99 -88.81 REMARK 500 GLN F 361 65.12 -112.29 REMARK 500 SER F 362 -73.59 61.42 REMARK 500 ASN F 363 -73.98 -67.95 REMARK 500 THR F 369 42.21 -73.50 REMARK 500 ASN F 371 33.29 -98.65 REMARK 500 GLU F 378 36.42 -90.63 REMARK 500 ASP F 385 90.59 -162.19 REMARK 500 LYS F 399 -8.03 -146.64 REMARK 500 LEU F 481 -40.77 70.13 REMARK 500 ASP F 489 19.01 -145.00 REMARK 500 PHE F 505 -78.82 -54.43 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4JHA RELATED DB: PDB REMARK 900 'CRYSTAL STRUCTURE OF RSV-NEUTRALIZING HUMAN ANTIBODY D25' REMARK 999 REMARK 999 SEQUENCE REMARK 999 AUTHOR STATES THAT THE ORF FOR THE CRYSTALLIZED RSV F PROTEIN IS: REMARK 999 MELLILKANAITTILTAVTFCFASGQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENK REMARK 999 CNGTDAKVKLIKQELDKYKNAVTELQLLMQSTPATNNRARRELPRFMNYTLNNAKKTNVTLSKKRKR REMARK 999 RFLGFLLGVGSAIASGVAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQ REMARK 999 LLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITND REMARK 999 QKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEGSNICLTR REMARK 999 TDRGWYCDNAGSVSFFPQAETCKVQSNRVFCDTMNSLTLPSEVNLCNVDIFNPKYDCKIMTSKTDVS REMARK 999 SSVITSLGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKQEGKSLYVK REMARK 999 GEPIINFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELLSAIGGYIPEAPRDGQAYVRKDGEW REMARK 999 VLLSTFLGGLVPRGSHHHHHHSAWSHPQFEK. THE N-TERMINAL, C-TERMINAL, AND 27 REMARK 999 INTERVENING RESIDUES ARE NOT PRESENT IN THE MATURE PROTEIN DUE REMARK 999 EITHER TO CELLULAR PROTEASES OR THROMBIN TREATMENT. THE SEQUENCE OF REMARK 999 THE MATURE PROTEIN THAT WAS CRYSTALLIZED IS: REMARK 999 QNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKNAVTE REMARK 999 LQLLMQSTPATNNRARRFLGFLLGVGSAIASGVAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVS REMARK 999 VLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLT REMARK 999 NSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSP REMARK 999 LCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPQAETCKVQSNRVFCDTMNSLTLPSEVNLCNVDIF REMARK 999 NPKYDCKIMTSKTDVSSSVITSLGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGVDTVSVGN REMARK 999 TLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELLSAIGGYIP REMARK 999 EAPRDGQAYVRKDGEWVLLSTFLGGLVPR. THE CRYSTALLIZED PROTEIN IS A REMARK 999 VARIANT OF UNP P03420 (FUS_HRSVA) SEQUENCE CONTAINING THREE AMINO REMARK 999 ACID SUBSTITUTIONS (P102A, I379V, AND M447V).