REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.SPINELLI,A.DESMYTER,C.T.VERRIPS,H.J.W.DE HAARD, REMARK 1 AUTH 2 S.MOINEAU,C.CAMBILLAU REMARK 1 TITL LACTOCOCCAL BACTERIOPHAGE P2 RECEPTOR-BINDING REMARK 1 TITL 2 PROTEIN STRUCTURE SUGGESTS A COMMON ANCESTOR GENE REMARK 1 TITL 3 WITH BACTERIAL AND MAMMALIAN VIRUSES. REMARK 1 REF NAT.STRUCT.MOL.BIOL. V. 13 85 2006 REMARK 1 REFN ISSN 1545-9993 REMARK 1 PMID 16327804 REMARK 1 DOI 10.1038/NSMB1029 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.9.2 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK; REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.07 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 183300 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.1794 REMARK 3 R VALUE (WORKING SET) : 0.1789 REMARK 3 FREE R VALUE : 0.2078 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.01 REMARK 3 FREE R VALUE TEST SET COUNT : 3689 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.67 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 13522 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2599 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 13268 REMARK 3 BIN R VALUE (WORKING SET) : 0.2593 REMARK 3 BIN FREE R VALUE : 0.2918 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.88 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 254 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 25638 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 2009 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 59.46 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.43 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -17.5803 REMARK 3 B22 (A**2) : -17.5803 REMARK 3 B33 (A**2) : 35.1607 REMARK 3 B12 (A**2) : 0.0000 REMARK 3 B13 (A**2) : 0.0000 REMARK 3 B23 (A**2) : 0.0000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.8463 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.8227 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 26166 ; 2.00 ; HARMONIC REMARK 3 BOND ANGLES : 35533 ; 2.00 ; HARMONIC REMARK 3 TORSION ANGLES : 8918 ; 2.00 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 700 ; 2.00 ; HARMONIC REMARK 3 GENERAL PLANES : 3789 ; 5.00 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 26166 ; 20.00 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 3510 ; 5.00 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 29933 ; 4.00 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.15 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.47 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.89 REMARK 3 REMARK 3 TLS DETAILS. REMARK 3 NUMBER OF TLS GROUPS : 24 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN D AND RESID 2:123) REMARK 3 ORIGIN FOR THE GROUP (A): 15.6482 49.1337 344.0700 REMARK 3 T TENSOR REMARK 3 T11: 0.1115 T22: -0.0791 REMARK 3 T33: -0.0570 T12: -0.1187 REMARK 3 T13: 0.0359 T23: 0.0654 REMARK 3 L TENSOR REMARK 3 L11: 0.6859 L22: 3.0943 REMARK 3 L33: 1.3081 L12: 1.6655 REMARK 3 L13: 1.0275 L23: -1.0386 REMARK 3 S TENSOR REMARK 3 S11: 0.0084 S12: -0.0464 S13: -0.0190 REMARK 3 S21: 0.0233 S22: -0.0441 S23: 0.0185 REMARK 3 S31: 0.0647 S32: 0.0213 S33: 0.0357 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN E AND RESID 2:123) REMARK 3 ORIGIN FOR THE GROUP (A): 34.5701 100.3068 357.4640 REMARK 3 T TENSOR REMARK 3 T11: 0.1309 T22: -0.0668 REMARK 3 T33: -0.0565 T12: -0.1327 REMARK 3 T13: 0.0569 T23: -0.1155 REMARK 3 L TENSOR REMARK 3 L11: -0.6563 L22: 2.0638 REMARK 3 L33: 0.1155 L12: 1.2749 REMARK 3 L13: -1.1803 L23: 1.2205 REMARK 3 S TENSOR REMARK 3 S11: 0.0057 S12: -0.0198 S13: 0.0126 REMARK 3 S21: 0.0159 S22: 0.0068 S23: 0.0054 REMARK 3 S31: -0.0331 S32: -0.0103 S33: -0.0125 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN F AND RESID 2:123) REMARK 3 ORIGIN FOR THE GROUP (A): 67.3767 54.8076 365.4200 REMARK 3 T TENSOR REMARK 3 T11: -0.0031 T22: 0.0831 REMARK 3 T33: -0.0939 T12: -0.0157 REMARK 3 T13: -0.0926 T23: 0.1204 REMARK 3 L TENSOR REMARK 3 L11: 1.8443 L22: -0.6959 REMARK 3 L33: 0.5376 L12: -0.0702 REMARK 3 L13: 1.5332 L23: -0.9103 REMARK 3 S TENSOR REMARK 3 S11: -0.0181 S12: 0.0130 S13: -0.0073 REMARK 3 S21: 0.0125 S22: 0.0154 S23: 0.0037 REMARK 3 S31: 0.0274 S32: 0.0240 S33: 0.0028 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN J AND RESID 2:123) REMARK 3 ORIGIN FOR THE GROUP (A): -55.1721 58.8868 337.4100 REMARK 3 T TENSOR REMARK 3 T11: -0.1138 T22: 0.1191 REMARK 3 T33: 0.0337 T12: 0.0988 REMARK 3 T13: 0.2059 T23: -0.0527 REMARK 3 L TENSOR REMARK 3 L11: 2.7919 L22: -1.3881 REMARK 3 L33: 1.1996 L12: -0.8042 REMARK 3 L13: -0.2137 L23: 0.0928 REMARK 3 S TENSOR REMARK 3 S11: -0.0065 S12: 0.0191 S13: 0.0212 REMARK 3 S21: -0.0195 S22: 0.0134 S23: 0.0514 REMARK 3 S31: -0.0189 S32: -0.0076 S33: -0.0069 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN K AND RESID 2:123) REMARK 3 ORIGIN FOR THE GROUP (A): -6.3939 80.0060 355.1340 REMARK 3 T TENSOR REMARK 3 T11: 0.2184 T22: -0.1400 REMARK 3 T33: -0.0749 T12: 0.0064 REMARK 3 T13: -0.0551 T23: -0.2063 REMARK 3 L TENSOR REMARK 3 L11: -0.2033 L22: 3.8358 REMARK 3 L33: 1.2025 L12: 0.9583 REMARK 3 L13: -0.2910 L23: 1.0306 REMARK 3 S TENSOR REMARK 3 S11: -0.0030 S12: -0.0142 S13: 0.0279 REMARK 3 S21: 0.0105 S22: -0.0032 S23: -0.0217 REMARK 3 S31: -0.0174 S32: 0.0197 S33: 0.0062 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN L AND RESID 2:123) REMARK 3 ORIGIN FOR THE GROUP (A): -19.5139 24.7348 364.7610 REMARK 3 T TENSOR REMARK 3 T11: 0.1786 T22: 0.0491 REMARK 3 T33: -0.2444 T12: -0.0524 REMARK 3 T13: 0.1443 T23: 0.0524 REMARK 3 L TENSOR REMARK 3 L11: -0.4141 L22: 2.8905 REMARK 3 L33: 2.5302 L12: -0.1373 REMARK 3 L13: -0.5259 L23: -1.0585 REMARK 3 S TENSOR REMARK 3 S11: -0.0016 S12: -0.0255 S13: -0.0601 REMARK 3 S21: 0.0234 S22: 0.0050 S23: 0.0142 REMARK 3 S31: 0.0492 S32: 0.0018 S33: -0.0034 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN A AND RESID 2:161) REMARK 3 ORIGIN FOR THE GROUP (A): 74.9004 67.5522 304.0980 REMARK 3 T TENSOR REMARK 3 T11: -0.2737 T22: -0.1077 REMARK 3 T33: 0.2982 T12: 0.1603 REMARK 3 T13: -0.1551 T23: 0.0859 REMARK 3 L TENSOR REMARK 3 L11: 3.0635 L22: 0.5112 REMARK 3 L33: 0.1246 L12: -1.5614 REMARK 3 L13: 1.0168 L23: -0.7479 REMARK 3 S TENSOR REMARK 3 S11: 0.0542 S12: -0.1527 S13: -0.0823 REMARK 3 S21: 0.0696 S22: -0.0891 S23: -0.1093 REMARK 3 S31: 0.1708 S32: 0.1978 S33: 0.0349 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN B AND RESID 2:161) REMARK 3 ORIGIN FOR THE GROUP (A): 63.7727 89.4044 301.7510 REMARK 3 T TENSOR REMARK 3 T11: -0.3070 T22: -0.0266 REMARK 3 T33: 0.2892 T12: 0.0499 REMARK 3 T13: -0.1523 T23: 0.0298 REMARK 3 L TENSOR REMARK 3 L11: 1.3848 L22: 0.7227 REMARK 3 L33: 0.4486 L12: 0.0651 REMARK 3 L13: 0.1398 L23: -0.2433 REMARK 3 S TENSOR REMARK 3 S11: 0.0558 S12: -0.2533 S13: -0.0294 REMARK 3 S21: 0.1275 S22: -0.1009 S23: -0.1748 REMARK 3 S31: -0.0364 S32: 0.2400 S33: 0.0452 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN C AND RESID 2:161) REMARK 3 ORIGIN FOR THE GROUP (A): 52.8947 68.9088 293.1420 REMARK 3 T TENSOR REMARK 3 T11: -0.2400 T22: -0.1292 REMARK 3 T33: 0.3010 T12: 0.1659 REMARK 3 T13: -0.0334 T23: 0.0874 REMARK 3 L TENSOR REMARK 3 L11: 1.6400 L22: 1.1767 REMARK 3 L33: 0.2558 L12: 0.1065 REMARK 3 L13: 0.5914 L23: -0.1280 REMARK 3 S TENSOR REMARK 3 S11: 0.0545 S12: -0.0844 S13: -0.1362 REMARK 3 S21: 0.0052 S22: -0.1308 S23: -0.1129 REMARK 3 S31: 0.2952 S32: 0.1323 S33: 0.0763 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN G AND RESID 2:161) REMARK 3 ORIGIN FOR THE GROUP (A): 1.3673 25.0297 304.9670 REMARK 3 T TENSOR REMARK 3 T11: -0.0793 T22: -0.2511 REMARK 3 T33: 0.2932 T12: -0.0265 REMARK 3 T13: -0.0123 T23: -0.0221 REMARK 3 L TENSOR REMARK 3 L11: 0.2860 L22: 1.1746 REMARK 3 L33: 1.2825 L12: 0.3130 REMARK 3 L13: 0.0873 L23: -0.5223 REMARK 3 S TENSOR REMARK 3 S11: 0.0314 S12: -0.1354 S13: -0.0124 REMARK 3 S21: 0.1658 S22: -0.0375 S23: -0.1386 REMARK 3 S31: 0.1959 S32: -0.1157 S33: 0.0061 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: (CHAIN H AND RESID 2:161) REMARK 3 ORIGIN FOR THE GROUP (A): 11.4396 47.2100 303.0390 REMARK 3 T TENSOR REMARK 3 T11: -0.0745 T22: -0.2580 REMARK 3 T33: 0.2920 T12: -0.0108 REMARK 3 T13: -0.0413 T23: -0.0441 REMARK 3 L TENSOR REMARK 3 L11: 0.4700 L22: 1.0524 REMARK 3 L33: 1.0211 L12: 0.2489 REMARK 3 L13: 0.1175 L23: 0.4448 REMARK 3 S TENSOR REMARK 3 S11: 0.0102 S12: -0.1562 S13: 0.0936 REMARK 3 S21: 0.2027 S22: 0.0032 S23: -0.1431 REMARK 3 S31: -0.1897 S32: 0.0525 S33: -0.0134 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: (CHAIN I AND RESID 2:161) REMARK 3 ORIGIN FOR THE GROUP (A): -10.7226 42.7348 292.9080 REMARK 3 T TENSOR REMARK 3 T11: -0.1603 T22: -0.1878 REMARK 3 T33: 0.2882 T12: 0.0272 REMARK 3 T13: 0.0450 T23: -0.0677 REMARK 3 L TENSOR REMARK 3 L11: 0.9166 L22: 0.4511 REMARK 3 L33: 1.3749 L12: -0.2200 REMARK 3 L13: 0.2208 L23: -0.2351 REMARK 3 S TENSOR REMARK 3 S11: 0.0878 S12: -0.0577 S13: 0.0106 REMARK 3 S21: 0.1560 S22: -0.0919 S23: 0.0933 REMARK 3 S31: -0.0923 S32: -0.4136 S33: 0.0041 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: (CHAIN A AND RESID 162:267) REMARK 3 ORIGIN FOR THE GROUP (A): 49.9809 79.7531 346.8580 REMARK 3 T TENSOR REMARK 3 T11: 0.0220 T22: 0.0751 REMARK 3 T33: -0.1255 T12: -0.2056 REMARK 3 T13: -0.1997 T23: 0.0602 REMARK 3 L TENSOR REMARK 3 L11: 2.8082 L22: 0.4123 REMARK 3 L33: 0.7055 L12: 1.1677 REMARK 3 L13: 2.2972 L23: 1.3423 REMARK 3 S TENSOR REMARK 3 S11: 0.0280 S12: -0.0454 S13: 0.0438 REMARK 3 S21: 0.0057 S22: -0.0253 S23: 0.0013 REMARK 3 S31: -0.0046 S32: 0.0203 S33: -0.0027 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: (CHAIN B AND RESID 162:267) REMARK 3 ORIGIN FOR THE GROUP (A): 32.9988 69.9866 338.6520 REMARK 3 T TENSOR REMARK 3 T11: 0.0258 T22: 0.0292 REMARK 3 T33: -0.0409 T12: -0.1335 REMARK 3 T13: -0.0865 T23: 0.0294 REMARK 3 L TENSOR REMARK 3 L11: 2.1683 L22: 0.0154 REMARK 3 L33: 1.4328 L12: 0.6255 REMARK 3 L13: -0.0239 L23: -0.5095 REMARK 3 S TENSOR REMARK 3 S11: 0.0524 S12: -0.0590 S13: 0.0292 REMARK 3 S21: 0.0659 S22: -0.0923 S23: 0.0233 REMARK 3 S31: 0.0046 S32: 0.0267 S33: 0.0399 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: (CHAIN C AND RESID 162:267) REMARK 3 ORIGIN FOR THE GROUP (A): 50.0122 58.6230 344.3220 REMARK 3 T TENSOR REMARK 3 T11: -0.0796 T22: 0.1809 REMARK 3 T33: -0.0684 T12: -0.0093 REMARK 3 T13: -0.0563 T23: 0.1407 REMARK 3 L TENSOR REMARK 3 L11: 3.3404 L22: -1.8167 REMARK 3 L33: 1.6085 L12: -0.8915 REMARK 3 L13: 2.4736 L23: -1.6841 REMARK 3 S TENSOR REMARK 3 S11: 0.0135 S12: -0.0175 S13: 0.0150 REMARK 3 S21: 0.0341 S22: -0.0383 S23: -0.0119 REMARK 3 S31: 0.0440 S32: 0.0161 S33: 0.0248 REMARK 3 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: (CHAIN G AND RESID 162:267) REMARK 3 ORIGIN FOR THE GROUP (A): -10.0565 54.0318 345.7920 REMARK 3 T TENSOR REMARK 3 T11: 0.1459 T22: -0.0343 REMARK 3 T33: -0.1019 T12: -0.0166 REMARK 3 T13: 0.1050 T23: -0.1133 REMARK 3 L TENSOR REMARK 3 L11: 0.5699 L22: 2.1728 REMARK 3 L33: 1.8063 L12: -0.2501 REMARK 3 L13: -0.2280 L23: 1.7542 REMARK 3 S TENSOR REMARK 3 S11: -0.0003 S12: -0.1079 S13: 0.0131 REMARK 3 S21: 0.0677 S22: -0.0055 S23: -0.0262 REMARK 3 S31: -0.0641 S32: -0.0004 S33: 0.0058 REMARK 3 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: (CHAIN H AND RESID 162:267) REMARK 3 ORIGIN FOR THE GROUP (A): -27.4705 59.6617 335.2320 REMARK 3 T TENSOR REMARK 3 T11: 0.0097 T22: 0.0222 REMARK 3 T33: -0.0143 T12: 0.2257 REMARK 3 T13: 0.1938 T23: -0.0624 REMARK 3 L TENSOR REMARK 3 L11: 1.9183 L22: 1.8102 REMARK 3 L33: 0.2615 L12: -0.9385 REMARK 3 L13: -1.4836 L23: 0.3788 REMARK 3 S TENSOR REMARK 3 S11: 0.0188 S12: -0.0224 S13: 0.0361 REMARK 3 S21: -0.0028 S22: 0.0169 S23: 0.0214 REMARK 3 S31: -0.0443 S32: -0.0861 S33: -0.0357 REMARK 3 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: (CHAIN I AND RESID 162:267) REMARK 3 ORIGIN FOR THE GROUP (A): -25.3625 39.7802 342.2800 REMARK 3 T TENSOR REMARK 3 T11: -0.0373 T22: 0.1291 REMARK 3 T33: -0.0512 T12: -0.0037 REMARK 3 T13: 0.2020 T23: -0.0558 REMARK 3 L TENSOR REMARK 3 L11: 0.4357 L22: 0.9111 REMARK 3 L33: 1.6970 L12: 0.7969 REMARK 3 L13: -0.8393 L23: -0.3164 REMARK 3 S TENSOR REMARK 3 S11: 0.0269 S12: -0.0769 S13: -0.0137 REMARK 3 S21: 0.0333 S22: -0.0113 S23: -0.0021 REMARK 3 S31: 0.0279 S32: -0.1325 S33: -0.0156 REMARK 3 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: (CHAIN P AND RESID 1:135) REMARK 3 ORIGIN FOR THE GROUP (A): 16.5699 92.7617 302.2880 REMARK 3 T TENSOR REMARK 3 T11: -0.1213 T22: -0.2165 REMARK 3 T33: 0.2940 T12: 0.0420 REMARK 3 T13: -0.0124 T23: 0.0126 REMARK 3 L TENSOR REMARK 3 L11: 1.2206 L22: 0.8321 REMARK 3 L33: 0.5419 L12: 0.7291 REMARK 3 L13: 0.1717 L23: 0.1176 REMARK 3 S TENSOR REMARK 3 S11: -0.0052 S12: -0.0488 S13: -0.0256 REMARK 3 S21: 0.2048 S22: -0.0558 S23: -0.1088 REMARK 3 S31: -0.0006 S32: -0.0101 S33: 0.0610 REMARK 3 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: (CHAIN P AND RESID 136:298) REMARK 3 ORIGIN FOR THE GROUP (A): 13.9329 64.1891 280.1990 REMARK 3 T TENSOR REMARK 3 T11: -0.1243 T22: -0.2521 REMARK 3 T33: 0.2937 T12: 0.0329 REMARK 3 T13: -0.0114 T23: 0.0040 REMARK 3 L TENSOR REMARK 3 L11: 0.4713 L22: 1.9370 REMARK 3 L33: 0.1851 L12: 0.4803 REMARK 3 L13: -0.0756 L23: -0.4121 REMARK 3 S TENSOR REMARK 3 S11: -0.0336 S12: 0.0581 S13: -0.0036 REMARK 3 S21: -0.0658 S22: 0.0167 S23: 0.0321 REMARK 3 S31: 0.0620 S32: -0.0413 S33: 0.0169 REMARK 3 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: (CHAIN Q AND RESID 1:135) REMARK 3 ORIGIN FOR THE GROUP (A): 29.4919 119.1671 302.1870 REMARK 3 T TENSOR REMARK 3 T11: -0.1542 T22: -0.1615 REMARK 3 T33: 0.2514 T12: -0.0142 REMARK 3 T13: -0.0505 T23: -0.0093 REMARK 3 L TENSOR REMARK 3 L11: -0.1491 L22: 2.9908 REMARK 3 L33: 0.5471 L12: 0.0668 REMARK 3 L13: -0.0375 L23: 0.5102 REMARK 3 S TENSOR REMARK 3 S11: -0.0935 S12: -0.0498 S13: 0.0286 REMARK 3 S21: 0.2018 S22: 0.0073 S23: -0.1206 REMARK 3 S31: -0.0029 S32: 0.1148 S33: 0.0862 REMARK 3 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: (CHAIN Q AND RESID 136:298) REMARK 3 ORIGIN FOR THE GROUP (A): 51.4648 101.3219 279.3190 REMARK 3 T TENSOR REMARK 3 T11: -0.3016 T22: -0.1008 REMARK 3 T33: 0.2971 T12: 0.0295 REMARK 3 T13: -0.0518 T23: 0.0014 REMARK 3 L TENSOR REMARK 3 L11: 1.3638 L22: 1.0781 REMARK 3 L33: 0.6568 L12: -0.0966 REMARK 3 L13: 0.0646 L23: -0.3905 REMARK 3 S TENSOR REMARK 3 S11: -0.0421 S12: 0.0346 S13: -0.0683 REMARK 3 S21: -0.0675 S22: 0.0114 S23: 0.0180 REMARK 3 S31: -0.0500 S32: 0.2869 S33: 0.0307 REMARK 3 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: (CHAIN R AND RESID 1:213) REMARK 3 ORIGIN FOR THE GROUP (A): 25.4239 109.6835 254.7610 REMARK 3 T TENSOR REMARK 3 T11: -0.2365 T22: -0.1906 REMARK 3 T33: 0.3014 T12: 0.0158 REMARK 3 T13: 0.0222 T23: -0.0137 REMARK 3 L TENSOR REMARK 3 L11: 0.8506 L22: 1.1740 REMARK 3 L33: 1.0153 L12: 0.1059 REMARK 3 L13: 0.3264 L23: -0.5027 REMARK 3 S TENSOR REMARK 3 S11: 0.0368 S12: 0.0552 S13: -0.0205 REMARK 3 S21: 0.0184 S22: -0.0650 S23: -0.1804 REMARK 3 S31: 0.0459 S32: 0.1758 S33: 0.0282 REMARK 3 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: (CHAIN R AND RESID 214:375) REMARK 3 ORIGIN FOR THE GROUP (A): 6.1450 94.0541 251.4720 REMARK 3 T TENSOR REMARK 3 T11: -0.1735 T22: -0.2418 REMARK 3 T33: 0.3010 T12: 0.0117 REMARK 3 T13: 0.0137 T23: -0.0110 REMARK 3 L TENSOR REMARK 3 L11: 0.7618 L22: 0.5640 REMARK 3 L33: 1.5021 L12: 0.1252 REMARK 3 L13: 0.3936 L23: 0.1466 REMARK 3 S TENSOR REMARK 3 S11: 0.0192 S12: -0.0168 S13: -0.0676 REMARK 3 S21: -0.0140 S22: -0.0073 S23: -0.0460 REMARK 3 S31: 0.1141 S32: -0.0195 S33: -0.0119 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE BIOLOGICAL UNIT, THE BASEPLATE REMARK 3 SHOULD BE RECONSTITUTED USING THE 3-FOLD CRYSTALLOGRAPHIC REMARK 3 SYMMETRY REMARK 4 REMARK 4 2WZP COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-DEC-09. REMARK 100 THE PDBE ID CODE IS EBI-41906. 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 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9708 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 184640 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.60 REMARK 200 RESOLUTION RANGE LOW (A) : 48.70 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 5.0 REMARK 200 R MERGE (I) : 0.13 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.10 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 5 REMARK 200 R MERGE FOR SHELL (I) : 0.48 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.60 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 1ZRU REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 68.2 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 4 MG/ML OF COMPLEX, 25% PEG REMARK 280 2000 MME, 0.1 M NA-HEPES PH 7.5. REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 X+2/3,Y+1/3,Z+1/3 REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3 REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3 REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3 REMARK 290 13555 X+1/3,Y+2/3,Z+2/3 REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3 REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3 REMARK 290 18555 -X+1/3,-X+Y+2/3,-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 0.00000 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 0.00000 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 0.00000 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 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 101.44050 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 58.56670 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 253.50667 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 101.44050 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 58.56670 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 253.50667 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 101.44050 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 58.56670 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 253.50667 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 101.44050 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 58.56670 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 253.50667 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 101.44050 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 58.56670 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 253.50667 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 101.44050 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 58.56670 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 253.50667 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 117.13340 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 507.01333 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 117.13340 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 507.01333 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 117.13340 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 507.01333 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 117.13340 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 507.01333 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 117.13340 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 507.01333 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 117.13340 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 507.01333 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: 45-MERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 45-MERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 188190 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 372360 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -900.5 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, G, H, I, P, Q, K, REMARK 350 AND CHAINS: J, L, E, F, D, R 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 -0.500000 0.866025 0.000000 -101.44050 REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 175.70010 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 -0.866025 0.000000 101.44050 REMARK 350 BIOMT2 3 0.866025 -0.500000 0.000000 175.70010 REMARK 350 BIOMT3 3 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 GLN D 1 REMARK 465 GLN E 1 REMARK 465 GLN F 1 REMARK 465 GLN J 1 REMARK 465 GLN K 1 REMARK 465 GLN L 1 REMARK 465 MET P -27 REMARK 465 SER P -26 REMARK 465 TYR P -25 REMARK 465 TYR P -24 REMARK 465 HIS P -23 REMARK 465 HIS P -22 REMARK 465 HIS P -21 REMARK 465 HIS P -20 REMARK 465 HIS P -19 REMARK 465 HIS P -18 REMARK 465 LEU P -17 REMARK 465 GLU P -16 REMARK 465 SER P -15 REMARK 465 THR P -14 REMARK 465 SER P -13 REMARK 465 LEU P -12 REMARK 465 TYR P -11 REMARK 465 LYS P -10 REMARK 465 LYS P -9 REMARK 465 ALA P -8 REMARK 465 GLY P -7 REMARK 465 LEU P -6 REMARK 465 GLU P -5 REMARK 465 ASN P -4 REMARK 465 LEU P -3 REMARK 465 TYR P -2 REMARK 465 PHE P -1 REMARK 465 GLN P 0 REMARK 465 MET Q -27 REMARK 465 SER Q -26 REMARK 465 TYR Q -25 REMARK 465 TYR Q -24 REMARK 465 HIS Q -23 REMARK 465 HIS Q -22 REMARK 465 HIS Q -21 REMARK 465 HIS Q -20 REMARK 465 HIS Q -19 REMARK 465 HIS Q -18 REMARK 465 LEU Q -17 REMARK 465 GLU Q -16 REMARK 465 SER Q -15 REMARK 465 THR Q -14 REMARK 465 SER Q -13 REMARK 465 LEU Q -12 REMARK 465 TYR Q -11 REMARK 465 LYS Q -10 REMARK 465 LYS Q -9 REMARK 465 ALA Q -8 REMARK 465 GLY Q -7 REMARK 465 LEU Q -6 REMARK 465 GLU Q -5 REMARK 465 ASN Q -4 REMARK 465 LEU Q -3 REMARK 465 TYR Q -2 REMARK 465 PHE Q -1 REMARK 465 GLN Q 0 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 TRP A 267 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3 REMARK 470 TRP A 267 CH2 REMARK 470 TRP B 267 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3 REMARK 470 TRP B 267 CH2 REMARK 470 TRP C 267 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3 REMARK 470 TRP C 267 CH2 REMARK 470 ARG E 38 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 43 CG CD CE NZ REMARK 470 ARG E 72 CG CD NE CZ NH1 NH2 REMARK 470 TYR F 80 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TRP G 267 CH2 REMARK 470 TRP G 267 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3 REMARK 470 TRP H 267 CH2 REMARK 470 TRP H 267 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3 REMARK 470 TRP I 267 CH2 REMARK 470 TRP I 267 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3 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 PHE A 6 -58.64 -125.25 REMARK 500 ALA A 50 -135.41 52.21 REMARK 500 LEU A 51 58.49 -91.80 REMARK 500 ASN A 57 88.18 -159.71 REMARK 500 SER A 129 -163.99 -108.38 REMARK 500 ASP A 146 -81.16 -100.65 REMARK 500 ASP A 184 -57.27 -130.26 REMARK 500 PHE B 6 -58.96 -123.40 REMARK 500 SER B 13 17.43 56.74 REMARK 500 ASP B 34 -169.57 -106.84 REMARK 500 ALA B 50 -135.38 49.89 REMARK 500 LEU B 51 56.92 -91.25 REMARK 500 ASN B 57 89.12 -158.86 REMARK 500 SER B 129 -162.94 -106.27 REMARK 500 ASP B 146 -82.26 -98.18 REMARK 500 ASN B 182 17.44 58.98 REMARK 500 ASP B 184 -57.52 -130.78 REMARK 500 SER C 13 17.43 57.38 REMARK 500 ALA C 50 -136.41 52.22 REMARK 500 LEU C 51 58.34 -92.01 REMARK 500 ASN C 57 88.95 -158.51 REMARK 500 SER C 129 -161.93 -103.02 REMARK 500 ASP C 146 -79.57 -96.49 REMARK 500 ASN C 172 19.91 59.21 REMARK 500 ASP C 184 -56.60 -128.58 REMARK 500 SER D 74 -121.06 57.78 REMARK 500 ALA E 14 25.76 46.41 REMARK 500 LYS E 43 -159.15 -139.69 REMARK 500 LEU F 86 96.30 -62.81 REMARK 500 PHE G 6 -59.34 -125.22 REMARK 500 SER G 13 10.42 58.97 REMARK 500 ALA G 50 -135.74 52.37 REMARK 500 LEU G 51 57.25 -92.44 REMARK 500 ASN G 57 87.99 -158.63 REMARK 500 SER G 129 -162.59 -101.88 REMARK 500 ASP G 146 -81.95 -99.73 REMARK 500 ASP G 184 -55.26 -129.62 REMARK 500 PHE H 6 -60.07 -125.18 REMARK 500 PHE H 16 59.01 -116.58 REMARK 500 ALA H 50 -136.40 51.30 REMARK 500 LEU H 51 57.84 -91.00 REMARK 500 ASN H 57 88.46 -159.85 REMARK 500 ASP H 146 -83.18 -104.10 REMARK 500 ASP H 184 -58.31 -134.16 REMARK 500 PHE I 6 -60.75 -124.60 REMARK 500 SER I 13 15.76 58.01 REMARK 500 ALA I 50 -137.81 53.81 REMARK 500 LEU I 51 58.27 -91.40 REMARK 500 ASN I 57 87.91 -158.75 REMARK 500 SER I 129 -164.04 -100.75 REMARK 500 REMARK 500 THIS ENTRY HAS 79 RAMACHANDRAN OUTLIERS. 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 VAL A 18 23.4 L L OUTSIDE RANGE REMARK 500 VAL B 18 23.5 L L OUTSIDE RANGE REMARK 500 VAL C 18 23.1 L L OUTSIDE RANGE REMARK 500 VAL D 2 24.8 L L OUTSIDE RANGE REMARK 500 VAL E 48 24.8 L L OUTSIDE RANGE REMARK 500 LYS E 76 25.0 L L OUTSIDE RANGE REMARK 500 GLU F 89 23.4 L L OUTSIDE RANGE REMARK 500 VAL G 18 22.9 L L OUTSIDE RANGE REMARK 500 THR G 93 24.6 L L OUTSIDE RANGE REMARK 500 VAL H 18 23.9 L L OUTSIDE RANGE REMARK 500 THR H 93 25.0 L L OUTSIDE RANGE REMARK 500 VAL I 18 22.7 L L OUTSIDE RANGE REMARK 500 THR I 93 24.8 L L OUTSIDE RANGE REMARK 500 VAL K 121 24.9 L L OUTSIDE RANGE REMARK 500 LEU L 86 24.7 L L OUTSIDE RANGE REMARK 500 VAL P 21 23.9 L L OUTSIDE RANGE REMARK 500 TYR P 118 24.1 L L OUTSIDE RANGE REMARK 500 TYR Q 118 23.7 L L OUTSIDE RANGE REMARK 500 ILE Q 196 23.9 L L OUTSIDE RANGE REMARK 500 LYS R 85 23.7 L L OUTSIDE RANGE REMARK 500 VAL R 121 23.3 L L OUTSIDE RANGE REMARK 500 VAL R 175 21.8 L L OUTSIDE RANGE REMARK 500 THR R 219 24.3 L L OUTSIDE RANGE REMARK 500 ASN R 335 24.1 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 700 REMARK 700 SHEET REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, REMARK 700 TWO SHEETS ARE DEFINED. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1ZRU RELATED DB: PDB REMARK 900 STRUCTURE OF THE LACTOPHAGE P2 RECEPTOR REMARK 900 BINDING PROTEIN INCOMPLEX WITH GLYCEROL REMARK 900 RELATED ID: 2BSD RELATED DB: PDB REMARK 900 STRUCTURE OF LACTOCOCCAL BACTERIOPHAGE P2 REMARK 900 RECEPTOR BINDING PROTEIN REMARK 900 RELATED ID: 2BSE RELATED DB: PDB REMARK 900 STRUCTURE OF LACTOCOCCAL BACTERIOPHAGE P2 REMARK 900 RECEPTOR BINDING PROTEIN IN COMPLEX WITH A REMARK 900 LLAMA VHH DOMAIN REMARK 999 REMARK 999 SEQUENCE REMARK 999 CHAINS P AND Q: PHAGE P2 SEQUENCE IS DEPOSITED IN GENBANK, REMARK 999 NR GQ253898