REMARK 2 REMARK 2 RESOLUTION. 3.97 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2) 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) : 3.97 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.45 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.1 REMARK 3 NUMBER OF REFLECTIONS : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.259 REMARK 3 R VALUE (WORKING SET) : 0.256 REMARK 3 FREE R VALUE : 0.317 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 739 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 49.4564 - 6.7892 1.00 3194 166 0.2342 0.3085 REMARK 3 2 6.7892 - 5.3909 0.97 2974 155 0.2472 0.3061 REMARK 3 3 5.3909 - 4.7101 0.94 2853 156 0.2330 0.2964 REMARK 3 4 4.7101 - 4.2797 0.92 2768 131 0.2488 0.3175 REMARK 3 5 4.2797 - 3.9730 0.73 2211 131 0.2941 0.3254 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 : 0.34 REMARK 3 B_SOL : 141.48 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.560 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.740 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) : -13.16220 REMARK 3 B22 (A**2) : 26.54000 REMARK 3 B33 (A**2) : -13.37780 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 : 0.003 10315 REMARK 3 ANGLE : 0.743 14021 REMARK 3 CHIRALITY : 0.048 1570 REMARK 3 PLANARITY : 0.003 1784 REMARK 3 DIHEDRAL : 16.898 3616 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN L AND RESID 1:112 REMARK 3 ORIGIN FOR THE GROUP (A): -2.1475 62.3527 -20.5216 REMARK 3 T TENSOR REMARK 3 T11: 0.6563 T22: 0.9857 REMARK 3 T33: 1.0745 T12: 0.1304 REMARK 3 T13: 0.2082 T23: 0.0722 REMARK 3 L TENSOR REMARK 3 L11: 0.6395 L22: 6.5204 REMARK 3 L33: 2.6134 L12: -1.8733 REMARK 3 L13: 0.1938 L23: 1.1072 REMARK 3 S TENSOR REMARK 3 S11: -0.0673 S12: 0.5088 S13: -0.2187 REMARK 3 S21: -0.5573 S22: -0.1192 S23: 0.0885 REMARK 3 S31: -0.0929 S32: -0.0424 S33: -0.0109 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN L AND RESID 113:213 REMARK 3 ORIGIN FOR THE GROUP (A): -28.8803 61.8743 -6.0555 REMARK 3 T TENSOR REMARK 3 T11: 0.8138 T22: 1.4862 REMARK 3 T33: 1.0402 T12: -0.0774 REMARK 3 T13: 0.1899 T23: -0.0808 REMARK 3 L TENSOR REMARK 3 L11: 2.5776 L22: 2.2033 REMARK 3 L33: 1.3482 L12: 0.1111 REMARK 3 L13: -0.5878 L23: -1.1993 REMARK 3 S TENSOR REMARK 3 S11: -0.2062 S12: 0.9832 S13: 0.1283 REMARK 3 S21: -0.1970 S22: 0.2029 S23: -0.3173 REMARK 3 S31: -0.1524 S32: -0.2732 S33: 0.0367 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN H AND RESID 1:137 REMARK 3 ORIGIN FOR THE GROUP (A): -3.2944 82.7740 -25.4077 REMARK 3 T TENSOR REMARK 3 T11: 0.7845 T22: 0.9841 REMARK 3 T33: 0.8707 T12: -0.0329 REMARK 3 T13: 0.0847 T23: 0.1565 REMARK 3 L TENSOR REMARK 3 L11: 5.5688 L22: 3.0597 REMARK 3 L33: 6.5468 L12: -2.1527 REMARK 3 L13: -2.2008 L23: -2.7524 REMARK 3 S TENSOR REMARK 3 S11: 0.2164 S12: 0.6898 S13: 0.4526 REMARK 3 S21: 0.2398 S22: 0.0606 S23: 0.0069 REMARK 3 S31: -0.6644 S32: 0.5748 S33: -0.2089 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN H AND RESID 138:238 REMARK 3 ORIGIN FOR THE GROUP (A): -29.2359 72.9430 5.8060 REMARK 3 T TENSOR REMARK 3 T11: 1.1624 T22: 1.3716 REMARK 3 T33: 1.0482 T12: 0.3613 REMARK 3 T13: 0.0419 T23: -0.2320 REMARK 3 L TENSOR REMARK 3 L11: 4.3786 L22: 6.4845 REMARK 3 L33: 2.6272 L12: -5.3941 REMARK 3 L13: 1.9571 L23: -2.6287 REMARK 3 S TENSOR REMARK 3 S11: 0.1065 S12: -0.0948 S13: 0.6638 REMARK 3 S21: 0.6010 S22: -0.1274 S23: 0.0329 REMARK 3 S31: 0.4111 S32: 0.7403 S33: -0.0627 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN B AND RESID 1:112 REMARK 3 ORIGIN FOR THE GROUP (A): -14.9947 17.4923 10.1392 REMARK 3 T TENSOR REMARK 3 T11: 0.9114 T22: 1.0430 REMARK 3 T33: 1.4871 T12: 0.0979 REMARK 3 T13: -0.1065 T23: 0.1838 REMARK 3 L TENSOR REMARK 3 L11: 1.5212 L22: 5.8650 REMARK 3 L33: 0.8952 L12: 0.8351 REMARK 3 L13: -1.1970 L23: -1.1164 REMARK 3 S TENSOR REMARK 3 S11: 0.7501 S12: 0.1734 S13: -0.4045 REMARK 3 S21: 0.0409 S22: -0.3201 S23: -0.5708 REMARK 3 S31: 0.0010 S32: -0.0753 S33: -0.1735 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN B AND RESID 113:213 REMARK 3 ORIGIN FOR THE GROUP (A): -44.2567 15.2818 -0.8495 REMARK 3 T TENSOR REMARK 3 T11: 0.7844 T22: 0.9993 REMARK 3 T33: 0.8620 T12: 0.1980 REMARK 3 T13: 0.0240 T23: -0.0307 REMARK 3 L TENSOR REMARK 3 L11: 2.6555 L22: 4.6554 REMARK 3 L33: 1.7792 L12: -0.2277 REMARK 3 L13: 1.4343 L23: -2.2939 REMARK 3 S TENSOR REMARK 3 S11: -0.0973 S12: 0.0055 S13: 0.2158 REMARK 3 S21: 0.3464 S22: -0.2891 S23: 0.0115 REMARK 3 S31: -0.1597 S32: 0.7448 S33: 0.6342 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN A AND RESID 1:137 REMARK 3 ORIGIN FOR THE GROUP (A): -14.7062 38.3906 8.3446 REMARK 3 T TENSOR REMARK 3 T11: 0.5226 T22: 0.6218 REMARK 3 T33: 0.8201 T12: -0.0795 REMARK 3 T13: 0.1354 T23: 0.1948 REMARK 3 L TENSOR REMARK 3 L11: 5.3021 L22: 6.5854 REMARK 3 L33: 2.1318 L12: -0.8122 REMARK 3 L13: 1.9591 L23: 0.0122 REMARK 3 S TENSOR REMARK 3 S11: 0.0731 S12: -0.2338 S13: -0.3120 REMARK 3 S21: 0.3288 S22: 0.2426 S23: -0.2441 REMARK 3 S31: -0.5072 S32: 0.5363 S33: -0.3757 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN A AND RESID 138:238 REMARK 3 ORIGIN FOR THE GROUP (A): -53.9794 23.6738 9.2785 REMARK 3 T TENSOR REMARK 3 T11: 0.7935 T22: 0.9325 REMARK 3 T33: 0.8364 T12: 0.4002 REMARK 3 T13: -0.0010 T23: -0.1328 REMARK 3 L TENSOR REMARK 3 L11: 3.6130 L22: 4.1798 REMARK 3 L33: 7.0924 L12: -1.5217 REMARK 3 L13: 0.6478 L23: -3.9830 REMARK 3 S TENSOR REMARK 3 S11: -0.6001 S12: -0.6987 S13: -0.1137 REMARK 3 S21: -0.0581 S22: -0.0395 S23: 0.4652 REMARK 3 S31: 1.0443 S32: 0.6082 S33: 0.3246 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN D AND RESID 1:112 REMARK 3 ORIGIN FOR THE GROUP (A): -24.0279 18.2761 -35.5590 REMARK 3 T TENSOR REMARK 3 T11: 2.1587 T22: 1.5594 REMARK 3 T33: 1.6684 T12: 0.4620 REMARK 3 T13: 0.8181 T23: 0.1659 REMARK 3 L TENSOR REMARK 3 L11: 2.5085 L22: 0.4346 REMARK 3 L33: 0.7080 L12: -0.2915 REMARK 3 L13: -0.5205 L23: 0.5687 REMARK 3 S TENSOR REMARK 3 S11: -0.0679 S12: 0.2356 S13: -0.6448 REMARK 3 S21: -0.3809 S22: 0.3869 S23: -0.2051 REMARK 3 S31: 0.1855 S32: 0.0628 S33: 0.3452 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN D AND RESID 113:213 REMARK 3 ORIGIN FOR THE GROUP (A): -27.2189 48.8217 -36.8513 REMARK 3 T TENSOR REMARK 3 T11: 3.0229 T22: 1.6526 REMARK 3 T33: 1.1280 T12: 0.7815 REMARK 3 T13: 0.3600 T23: 0.3735 REMARK 3 L TENSOR REMARK 3 L11: 2.4615 L22: 1.8763 REMARK 3 L33: 0.0451 L12: 1.7580 REMARK 3 L13: -0.2992 L23: -0.0993 REMARK 3 S TENSOR REMARK 3 S11: -0.8669 S12: 0.5611 S13: 0.5475 REMARK 3 S21: -1.5103 S22: -1.1831 S23: -0.8191 REMARK 3 S31: -0.6401 S32: -0.9310 S33: 1.3607 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN C AND RESID 1:137 REMARK 3 ORIGIN FOR THE GROUP (A): -45.6184 18.4651 -31.8152 REMARK 3 T TENSOR REMARK 3 T11: 2.2058 T22: 1.3763 REMARK 3 T33: 1.2463 T12: 0.5256 REMARK 3 T13: 0.1733 T23: 0.0709 REMARK 3 L TENSOR REMARK 3 L11: 4.2362 L22: 3.4890 REMARK 3 L33: 3.6545 L12: -1.3081 REMARK 3 L13: -1.0186 L23: -2.9956 REMARK 3 S TENSOR REMARK 3 S11: 0.5593 S12: 0.0842 S13: 0.0078 REMARK 3 S21: -1.0270 S22: 0.0006 S23: 0.3993 REMARK 3 S31: 0.1093 S32: -1.0005 S33: -0.2327 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN C AND RESID 138:238 REMARK 3 ORIGIN FOR THE GROUP (A): -37.7372 52.6925 -48.6991 REMARK 3 T TENSOR REMARK 3 T11: 2.7174 T22: 1.0371 REMARK 3 T33: 0.6672 T12: 0.4409 REMARK 3 T13: 0.0886 T23: 0.0167 REMARK 3 L TENSOR REMARK 3 L11: 5.4248 L22: 1.0681 REMARK 3 L33: 3.9192 L12: 0.2221 REMARK 3 L13: 1.2826 L23: 1.5171 REMARK 3 S TENSOR REMARK 3 S11: -2.2571 S12: -0.2599 S13: 0.5605 REMARK 3 S21: -0.7732 S22: 1.0365 S23: -0.5724 REMARK 3 S31: 1.2105 S32: 1.8895 S33: 1.2937 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 3MME COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-10. REMARK 100 THE RCSB ID CODE IS RCSB058726. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-OCT-09 REMARK 200 TEMPERATURE (KELVIN) : 100.00 REMARK 200 PH : 4.5 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) : 1.00 REMARK 200 MONOCHROMATOR : NULL 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 : 5511 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.970 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 (%) : 93.3 REMARK 200 DATA REDUNDANCY : 5.200 REMARK 200 R MERGE (I) : 0.23700 REMARK 200 R SYM (I) : 0.20200 REMARK 200 FOR THE DATA SET : 6.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.14 REMARK 200 COMPLETENESS FOR SHELL (%) : 82.5 REMARK 200 DATA REDUNDANCY IN SHELL : 2.60 REMARK 200 R MERGE FOR SHELL (I) : 0.55600 REMARK 200 R SYM FOR SHELL (I) : 0.51500 REMARK 200 FOR SHELL : 1.500 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 3LRS CHAIN AB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.54 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.96M AMMONIUM SULFATE, 0.2 M NACL, REMARK 280 0.1M ACETATE PH 4.5 WITH 3% 1,6 DIAMINOHEXANE, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 293.00K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z REMARK 290 7555 -X+1/2,Y+1/2,-Z REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 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 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 95.98050 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 115.40200 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 95.98050 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 115.40200 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 95.98050 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 115.40200 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 95.98050 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 115.40200 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20710 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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: 3420 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20840 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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: 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: 3360 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19810 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 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 THR H 131 REMARK 465 SER H 132 REMARK 465 LYS H 214 REMARK 465 GLN L 1 REMARK 465 SER L 2 REMARK 465 GLU L 210 REMARK 465 CYS L 211 REMARK 465 SER L 212 REMARK 465 THR A 131 REMARK 465 SER A 132 REMARK 465 LYS A 214 REMARK 465 GLN B 1 REMARK 465 SER B 2 REMARK 465 GLU B 210 REMARK 465 CYS B 211 REMARK 465 SER B 212 REMARK 465 ILE C 99A REMARK 465 TRP C 99B REMARK 465 HIS C 99C REMARK 465 ASP C 99D REMARK 465 ASP C 99E REMARK 465 VAL C 99F REMARK 465 LYS C 99G REMARK 465 TYR C 99H REMARK 465 TYR C 99I REMARK 465 ASP C 99J REMARK 465 PHE C 99K REMARK 465 ASN C 99L REMARK 465 ASP C 99M REMARK 465 GLY C 99N REMARK 465 THR C 131 REMARK 465 SER C 132 REMARK 465 GLN D 1 REMARK 465 SER D 2 REMARK 465 GLU D 210 REMARK 465 CYS D 211 REMARK 465 SER D 212 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 ND2 ASN D 23 O5 NAG D 570 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 SER H 25 149.44 173.73 REMARK 500 HIS H 30 8.51 -69.59 REMARK 500 ASP H 100C -110.11 76.99 REMARK 500 TYR H 100H -164.80 -111.81 REMARK 500 ASN H 100K -9.41 84.32 REMARK 500 HIS H 100R 53.79 87.68 REMARK 500 TYR H 100S 120.99 -179.62 REMARK 500 ASP H 144 55.54 79.87 REMARK 500 PHE H 146 134.01 -173.57 REMARK 500 SER H 156 37.02 73.34 REMARK 500 HIS H 200 74.21 -107.47 REMARK 500 ASP L 27A -90.83 -152.64 REMARK 500 ASP L 30 52.25 -102.93 REMARK 500 PRO L 39 133.31 -37.11 REMARK 500 PRO L 43 155.15 -42.67 REMARK 500 VAL L 50 -60.20 86.20 REMARK 500 SER L 58 150.63 -43.47 REMARK 500 PRO L 141 172.60 -58.65 REMARK 500 ASP L 151 -99.90 69.98 REMARK 500 SER A 82A 148.34 -170.82 REMARK 500 ALA A 88 -179.41 -177.26 REMARK 500 ASP A 100C -115.14 60.59 REMARK 500 ASP A 100L 5.30 81.71 REMARK 500 HIS A 100R 38.95 91.05 REMARK 500 LEU A 124 78.24 -105.89 REMARK 500 ASP A 144 63.87 63.09 REMARK 500 PHE A 146 129.66 -178.26 REMARK 500 HIS A 200 76.80 -113.48 REMARK 500 ASP B 27A -96.96 -139.28 REMARK 500 ASP B 30 52.25 -111.25 REMARK 500 VAL B 50 -50.61 86.30 REMARK 500 SER B 58 151.63 -43.65 REMARK 500 ASP B 138 38.64 71.22 REMARK 500 ASP B 151 -90.94 61.58 REMARK 500 SER C 25 147.39 -172.53 REMARK 500 SER C 82A 140.70 -179.83 REMARK 500 TYR C 100S 144.85 -174.38 REMARK 500 ALA C 114 -54.07 -124.32 REMARK 500 THR C 116 146.44 -38.99 REMARK 500 ASP C 144 62.64 64.67 REMARK 500 PHE C 146 133.03 170.30 REMARK 500 THR C 160 -37.51 -139.99 REMARK 500 ASP D 27A -93.63 -147.27 REMARK 500 ASP D 30 51.69 -114.96 REMARK 500 PRO D 43 170.62 -54.01 REMARK 500 VAL D 50 -57.45 80.97 REMARK 500 PRO D 109 -177.00 -53.85 REMARK 500 ASP D 151 -104.09 62.94 REMARK 500 ASN D 170 -1.48 67.69 REMARK 500 PRO D 208 -74.29 -61.57 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 L 570 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG L 571 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA L 572 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 570 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 570 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 571 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3LRS RELATED DB: PDB REMARK 900 STRUCTURE OF PG16, AN ANTIBODY WITH BROAD AND POTENT REMARK 900 NEUTRALIZATION OF HIV-1