REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.J.STAHL,N.R.WATTS,C.RADER,M.A.DIMATTIA,R.G.MAGE, REMARK 1 AUTH 2 I.PALMER,J.D.KAUFMAN,J.M.GRIMES,D.I.STUART, REMARK 1 AUTH 3 A.C.STEVEN,P.T.WINGFIELD REMARK 1 TITL GENERATION AND CHARACTERIZATION OF A CHIMERIC REMARK 1 TITL 2 RABBIT/HUMAN FAB FOR CO-CRYSTALLIZATION OF HIV-1 REMARK 1 TITL 3 REV. REMARK 1 REF J.MOL.BIOL. V. 397 697 2010 REMARK 1 REFN ISSN 0022-2836 REMARK 1 PMID 20138059 REMARK 1 DOI 10.1016/J.JMB.2010.01.061 REMARK 2 REMARK 2 RESOLUTION. 3.17 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) : 3.17 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.78 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 83636 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) : 0.2346 REMARK 3 R VALUE (WORKING SET) : 0.2337 REMARK 3 FREE R VALUE : 0.2500 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.01 REMARK 3 FREE R VALUE TEST SET COUNT : 4187 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) : 3.17 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.25 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5535 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2782 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5261 REMARK 3 BIN R VALUE (WORKING SET) : 0.2777 REMARK 3 BIN FREE R VALUE : 0.2881 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.95 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 274 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 : 22554 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 77.96 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 143.62 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -18.2280 REMARK 3 B22 (A**2) : -15.9372 REMARK 3 B33 (A**2) : 34.1652 REMARK 3 B12 (A**2) : 13.1177 REMARK 3 B13 (A**2) : -6.3827 REMARK 3 B23 (A**2) : -4.1363 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 1.029 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.8909 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.8920 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS (A) : 23112 ; 2.00 ; HARMONIC REMARK 3 BOND ANGLES (DEGREES) : 31500 ; 2.00 ; HARMONIC REMARK 3 TORSION ANGLES (DEGREES) : 7632 ; 2.00 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES (A) : 468 ; 2.00 ; HARMONIC REMARK 3 GENERAL PLANES (A) : 3378 ; 5.00 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 23112 ; 20.00 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS (DEGREES) : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 3102 ; 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 : 25991 ; 4.00 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.32 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.69 REMARK 3 OTHER TORSION ANGLES (DEGREES) :23.05 REMARK 3 REMARK 3 SIMILARITY. REMARK 3 NCS. REMARK 3 NCS REPRESENTATION : RESTRAINT LSSR (-AUTONCS) REMARK 3 TARGET RESTRAINTS. REMARK 3 TARGET REPRESENTATION : NONE REMARK 3 TARGET STRUCTURE : NULL REMARK 3 REMARK 3 TLS DETAILS. REMARK 3 NUMBER OF TLS GROUPS : 18 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION : (CHAIN N) REMARK 3 ORIGIN FOR THE GROUP (A): 32.7648 -0.1976 86.3652 REMARK 3 T TENSOR (A**2) REMARK 3 T11: 0.6743 T22: -0.4283 REMARK 3 T33: -0.5170 T12: 0.0005 REMARK 3 T13: 0.0076 T23: 0.0710 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 5.9158 L22: 6.8328 REMARK 3 L33: 9.6331 L12: 0.0477 REMARK 3 L13: 0.5916 L23: -0.4964 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: 0.0923 S12: -1.2761 S13: 0.7096 REMARK 3 S21: 0.3069 S22: -0.0723 S23: -0.8380 REMARK 3 S31: 0.2295 S32: 1.0624 S33: -0.0199 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION : (CHAIN A) REMARK 3 ORIGIN FOR THE GROUP (A): 34.3512 -26.1913 41.5481 REMARK 3 T TENSOR (A**2) REMARK 3 T11: 0.6931 T22: -0.6855 REMARK 3 T33: -0.2997 T12: 0.0438 REMARK 3 T13: -0.0254 T23: 0.0110 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 1.1549 L22: 2.5817 REMARK 3 L33: 4.8127 L12: 0.4335 REMARK 3 L13: 0.0885 L23: 0.9064 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: -0.0971 S12: -0.0612 S13: 0.0984 REMARK 3 S21: 0.1753 S22: 0.1702 S23: -0.0569 REMARK 3 S31: 0.1907 S32: 0.0117 S33: -0.0731 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION : (CHAIN O) REMARK 3 ORIGIN FOR THE GROUP (A): 48.7523 -23.8246 5.7872 REMARK 3 T TENSOR (A**2) REMARK 3 T11: 0.7217 T22: -0.1062 REMARK 3 T33: -0.5961 T12: -0.1240 REMARK 3 T13: 0.0275 T23: 0.0999 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 14.2382 L22: 12.1767 REMARK 3 L33: 8.4240 L12: 4.8660 REMARK 3 L13: -1.4625 L23: 0.7730 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: -0.0218 S12: 0.9638 S13: 0.4171 REMARK 3 S21: -0.3584 S22: 0.0507 S23: -1.0680 REMARK 3 S31: 0.5722 S32: 1.4061 S33: -0.0289 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION : (CHAIN B) REMARK 3 ORIGIN FOR THE GROUP (A): 38.9756 -42.7079 45.3623 REMARK 3 T TENSOR (A**2) REMARK 3 T11: 0.6796 T22: -0.6821 REMARK 3 T33: -0.3548 T12: 0.0374 REMARK 3 T13: 0.0467 T23: -0.0011 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 0.9188 L22: 3.7436 REMARK 3 L33: 4.5393 L12: 0.3054 REMARK 3 L13: -0.0155 L23: -1.1558 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: -0.2384 S12: -0.0185 S13: -0.0616 REMARK 3 S21: 0.1698 S22: 0.4129 S23: 0.1415 REMARK 3 S31: 0.3271 S32: -0.3610 S33: -0.1745 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION : (CHAIN P) REMARK 3 ORIGIN FOR THE GROUP (A): -22.7754 -31.1074 82.4664 REMARK 3 T TENSOR (A**2) REMARK 3 T11: 0.1182 T22: 0.4739 REMARK 3 T33: -0.5659 T12: -0.3418 REMARK 3 T13: 0.0506 T23: -0.0238 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 6.5463 L22: 7.1662 REMARK 3 L33: 3.5623 L12: 0.9559 REMARK 3 L13: 0.1548 L23: -0.6301 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: 0.0359 S12: -0.3993 S13: 0.3754 REMARK 3 S21: 0.1745 S22: 0.0910 S23: 1.0642 REMARK 3 S31: -0.9036 S32: -0.7306 S33: -0.1269 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION : (CHAIN C) REMARK 3 ORIGIN FOR THE GROUP (A): -6.9363 -26.0630 47.2141 REMARK 3 T TENSOR (A**2) REMARK 3 T11: 0.2952 T22: -0.1769 REMARK 3 T33: -0.3612 T12: -0.2236 REMARK 3 T13: 0.1019 T23: 0.0752 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 2.9992 L22: 4.0363 REMARK 3 L33: 8.1101 L12: 2.0389 REMARK 3 L13: 0.3205 L23: -0.6110 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: -0.0939 S12: 0.3913 S13: 0.2908 REMARK 3 S21: -0.9898 S22: 0.0478 S23: 0.0449 REMARK 3 S31: -0.5451 S32: 0.4544 S33: 0.0461 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION : (CHAIN Q) REMARK 3 ORIGIN FOR THE GROUP (A): -9.1771 -54.3739 88.3200 REMARK 3 T TENSOR (A**2) REMARK 3 T11: -0.1904 T22: 0.4429 REMARK 3 T33: -0.4364 T12: -0.3140 REMARK 3 T13: 0.0222 T23: 0.0522 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 6.6693 L22: 6.5830 REMARK 3 L33: 8.7290 L12: -0.4252 REMARK 3 L13: -0.2545 L23: 1.4593 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: 0.2440 S12: 0.5656 S13: -1.0402 REMARK 3 S21: -1.1412 S22: 0.0096 S23: 0.0502 REMARK 3 S31: 1.0159 S32: 0.2241 S33: -0.2536 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION : (CHAIN D) REMARK 3 ORIGIN FOR THE GROUP (A): -10.2274 -41.7982 40.4657 REMARK 3 T TENSOR (A**2) REMARK 3 T11: 0.6162 T22: -0.2491 REMARK 3 T33: -0.5389 T12: -0.1138 REMARK 3 T13: 0.2961 T23: -0.0058 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 2.4387 L22: 2.7921 REMARK 3 L33: 4.4510 L12: 1.2525 REMARK 3 L13: -0.1946 L23: 1.3713 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: -0.2232 S12: 0.2531 S13: -0.3464 REMARK 3 S21: -1.2514 S22: 0.1920 S23: -0.3362 REMARK 3 S31: -0.1853 S32: 1.1761 S33: 0.0312 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION : (CHAIN R) REMARK 3 ORIGIN FOR THE GROUP (A): 17.9219 -64.7313 168.9562 REMARK 3 T TENSOR (A**2) REMARK 3 T11: 0.0442 T22: 0.4472 REMARK 3 T33: -0.5798 T12: -0.3863 REMARK 3 T13: 0.1827 T23: 0.0177 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 7.8333 L22: 16.3961 REMARK 3 L33: 4.3412 L12: 2.4522 REMARK 3 L13: 1.5646 L23: -0.9268 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: -0.0691 S12: -0.6668 S13: -1.3161 REMARK 3 S21: 0.7780 S22: 0.2751 S23: 0.6277 REMARK 3 S31: 1.0809 S32: 0.5975 S33: -0.2060 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION : (CHAIN E) REMARK 3 ORIGIN FOR THE GROUP (A): 16.4529 -49.6849 133.1572 REMARK 3 T TENSOR (A**2) REMARK 3 T11: -0.4466 T22: 0.4807 REMARK 3 T33: -0.3014 T12: -0.4505 REMARK 3 T13: 0.0255 T23: -0.1802 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 2.6170 L22: 0.6789 REMARK 3 L33: 3.8526 L12: 0.0690 REMARK 3 L13: 0.3440 L23: 0.3118 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: 0.1509 S12: 0.2620 S13: -0.0989 REMARK 3 S21: 0.0776 S22: -0.1778 S23: 0.0786 REMARK 3 S31: 0.1708 S32: -0.0146 S33: 0.0269 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION : (CHAIN F) REMARK 3 ORIGIN FOR THE GROUP (A): 33.5699 -49.9481 129.3281 REMARK 3 T TENSOR (A**2) REMARK 3 T11: -0.4649 T22: 0.4783 REMARK 3 T33: -0.3246 T12: -0.4030 REMARK 3 T13: -0.0375 T23: -0.0272 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 3.5175 L22: 1.1049 REMARK 3 L33: 3.9181 L12: 0.4651 REMARK 3 L13: -1.3598 L23: 0.0115 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: 0.2370 S12: 0.4574 S13: 0.2728 REMARK 3 S21: 0.0084 S22: -0.0999 S23: 0.0220 REMARK 3 S31: -0.4211 S32: 0.3786 S33: -0.1371 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION : (CHAIN G) REMARK 3 ORIGIN FOR THE GROUP (A): 5.7662 -9.5231 127.4520 REMARK 3 T TENSOR (A**2) REMARK 3 T11: -0.1563 T22: 0.2142 REMARK 3 T33: -0.5132 T12: -0.4711 REMARK 3 T13: 0.0645 T23: 0.0849 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 1.7006 L22: 4.0970 REMARK 3 L33: 8.8325 L12: 0.9929 REMARK 3 L13: -0.0105 L23: 0.1837 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: 0.1489 S12: -0.8230 S13: -0.0558 REMARK 3 S21: 0.3519 S22: -0.2723 S23: 0.3899 REMARK 3 S31: 0.9019 S32: -0.8837 S33: 0.1234 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION : (CHAIN H) REMARK 3 ORIGIN FOR THE GROUP (A): 27.6102 -3.4121 47.9094 REMARK 3 T TENSOR (A**2) REMARK 3 T11: 0.6550 T22: -0.6391 REMARK 3 T33: -0.0377 T12: 0.1282 REMARK 3 T13: -0.0745 T23: -0.0015 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 1.1612 L22: 2.2103 REMARK 3 L33: 7.6799 L12: -0.2836 REMARK 3 L13: -0.5324 L23: 0.1019 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: 0.0578 S12: -0.0454 S13: -0.1226 REMARK 3 S21: -0.5412 S22: 0.0109 S23: -0.2733 REMARK 3 S31: 0.0410 S32: 0.0201 S33: -0.0687 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION : (CHAIN I) REMARK 3 ORIGIN FOR THE GROUP (A): 20.1250 -2.3292 134.2170 REMARK 3 T TENSOR (A**2) REMARK 3 T11: -0.0560 T22: 0.3917 REMARK 3 T33: -0.5573 T12: -0.4130 REMARK 3 T13: -0.0680 T23: 0.1523 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 1.0253 L22: 2.3260 REMARK 3 L33: 3.3845 L12: -0.0452 REMARK 3 L13: 0.5421 L23: -0.9674 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: 0.3336 S12: -0.9351 S13: -0.1049 REMARK 3 S21: 0.1532 S22: -0.3452 S23: -0.3048 REMARK 3 S31: 1.1475 S32: 0.0271 S33: 0.0116 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION : (CHAIN J) REMARK 3 ORIGIN FOR THE GROUP (A): -7.3501 -48.7364 126.7643 REMARK 3 T TENSOR (A**2) REMARK 3 T11: -0.5834 T22: 0.4240 REMARK 3 T33: -0.0539 T12: -0.1805 REMARK 3 T13: 0.0087 T23: -0.1759 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 2.7913 L22: 1.4138 REMARK 3 L33: 6.2442 L12: -0.1094 REMARK 3 L13: 0.4221 L23: -0.7929 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: 0.0978 S12: -0.4454 S13: -0.1519 REMARK 3 S21: 0.0456 S22: 0.0617 S23: -0.1846 REMARK 3 S31: -0.0520 S32: 0.1863 S33: -0.1595 REMARK 3 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION : (CHAIN K) REMARK 3 ORIGIN FOR THE GROUP (A): -24.4142 -49.9280 130.5796 REMARK 3 T TENSOR (A**2) REMARK 3 T11: -0.6004 T22: 0.6317 REMARK 3 T33: -0.1904 T12: -0.1612 REMARK 3 T13: -0.0225 T23: -0.1309 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 2.8194 L22: 0.3792 REMARK 3 L33: 7.0259 L12: -0.2679 REMARK 3 L13: -0.9662 L23: -0.2091 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: 0.1020 S12: -0.6844 S13: 0.1184 REMARK 3 S21: 0.1093 S22: 0.0764 S23: -0.0998 REMARK 3 S31: -0.4447 S32: -0.0552 S33: -0.1784 REMARK 3 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION : (CHAIN L) REMARK 3 ORIGIN FOR THE GROUP (A): 24.5190 13.4005 44.1190 REMARK 3 T TENSOR (A**2) REMARK 3 T11: 0.6391 T22: -0.6180 REMARK 3 T33: -0.1685 T12: 0.1562 REMARK 3 T13: -0.0620 T23: -0.0191 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 1.0308 L22: 3.0835 REMARK 3 L33: 6.0442 L12: -0.9758 REMARK 3 L13: -0.1269 L23: -0.5393 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: 0.1412 S12: 0.0951 S13: -0.0580 REMARK 3 S21: -0.5954 S22: 0.0495 S23: 0.0828 REMARK 3 S31: -0.4143 S32: -0.5462 S33: -0.1906 REMARK 3 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION : (CHAIN M) REMARK 3 ORIGIN FOR THE GROUP (A): 6.7245 7.1551 92.1848 REMARK 3 T TENSOR (A**2) REMARK 3 T11: 0.6226 T22: 0.0139 REMARK 3 T33: -0.5771 T12: -0.1685 REMARK 3 T13: -0.0132 T23: 0.0003 REMARK 3 L TENSOR (DEG**2) REMARK 3 L11: 6.8838 L22: 8.2266 REMARK 3 L33: 3.4397 L12: -0.6838 REMARK 3 L13: 0.2386 L23: -0.3917 REMARK 3 S TENSOR (A DEG) REMARK 3 S11: 0.2629 S12: 0.2120 S13: 0.7679 REMARK 3 S21: -0.5329 S22: -0.0895 S23: 0.5459 REMARK 3 S31: -0.3599 S32: -1.1952 S33: -0.1735 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP. REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY REMARK 4 REMARK 4 2X7L COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAR-10. REMARK 100 THE PDBE ID CODE IS EBI-43071. 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 : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I02 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97 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 : HKL2000 REMARK 200 DATA SCALING SOFTWARE : HKL2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83664 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.20 REMARK 200 RESOLUTION RANGE LOW (A) : 48.80 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 3.4 REMARK 200 R MERGE (I) : 0.12 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.90 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.4 REMARK 200 R MERGE FOR SHELL (I) : 1.00 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.10 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 ENTRIES 1JPS, 2QR0, 2R8S, 3BDY, 1TZH, 1ZA3, 2R0K, REMARK 200 2V7N, 3DVG, 1B2W, 1BEY, 1TZI, 2FJF, 2QQN, 1B4J, 2FGW, 2FJH, REMARK 200 3D85 REMARK 200 REMARK 200 REMARK: 18 DIFFERENT MODELS USED IN PHASER AS AN ENSEMBLE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 69.83 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.11 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 12% POLYETHYLENE GLYCOL (PEG) REMARK 280 6000, 100 MM DI-AMMONIUM PHOSPHATE (DAP), AND 100 MM REMARK 280 TRIS/HCL (PH 8.5) REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 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: 3860 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.4 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F 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: 3860 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18630 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.4 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 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: 3880 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18600 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.8 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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: 4 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: 3830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.2 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K 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: 5 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: 3860 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18590 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.8 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: 6 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: 3830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18630 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.6 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: 7 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: M 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: 8 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: N 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: 9 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: O 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: 10 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: P 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: 11 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q 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: 12 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 A 222 REMARK 465 THR A 223 REMARK 465 ARG A 224 REMARK 465 GLY A 225 REMARK 465 HIS A 226 REMARK 465 HIS A 227 REMARK 465 HIS A 228 REMARK 465 HIS A 229 REMARK 465 HIS A 230 REMARK 465 HIS A 231 REMARK 465 LYS C 222 REMARK 465 THR C 223 REMARK 465 ARG C 224 REMARK 465 GLY C 225 REMARK 465 HIS C 226 REMARK 465 HIS C 227 REMARK 465 HIS C 228 REMARK 465 HIS C 229 REMARK 465 HIS C 230 REMARK 465 HIS C 231 REMARK 465 LYS E 222 REMARK 465 THR E 223 REMARK 465 ARG E 224 REMARK 465 GLY E 225 REMARK 465 HIS E 226 REMARK 465 HIS E 227 REMARK 465 HIS E 228 REMARK 465 HIS E 229 REMARK 465 HIS E 230 REMARK 465 HIS E 231 REMARK 465 LYS G 222 REMARK 465 THR G 223 REMARK 465 ARG G 224 REMARK 465 GLY G 225 REMARK 465 HIS G 226 REMARK 465 HIS G 227 REMARK 465 HIS G 228 REMARK 465 HIS G 229 REMARK 465 HIS G 230 REMARK 465 HIS G 231 REMARK 465 LYS H 222 REMARK 465 THR H 223 REMARK 465 ARG H 224 REMARK 465 GLY H 225 REMARK 465 HIS H 226 REMARK 465 HIS H 227 REMARK 465 HIS H 228 REMARK 465 HIS H 229 REMARK 465 HIS H 230 REMARK 465 HIS H 231 REMARK 465 LYS J 222 REMARK 465 THR J 223 REMARK 465 ARG J 224 REMARK 465 GLY J 225 REMARK 465 HIS J 226 REMARK 465 HIS J 227 REMARK 465 HIS J 228 REMARK 465 HIS J 229 REMARK 465 HIS J 230 REMARK 465 HIS J 231 REMARK 465 ALA M 2 REMARK 465 GLY M 3 REMARK 465 ARG M 4 REMARK 465 SER M 5 REMARK 465 GLY M 6 REMARK 465 ASP M 7 REMARK 465 SER M 8 REMARK 465 ARG M 66 REMARK 465 SER M 67 REMARK 465 ALA M 68 REMARK 465 GLU M 69 REMARK 465 PRO M 70 REMARK 465 VAL M 71 REMARK 465 PRO M 72 REMARK 465 LEU M 73 REMARK 465 GLN M 74 REMARK 465 LEU M 75 REMARK 465 PRO M 76 REMARK 465 PRO M 77 REMARK 465 LEU M 78 REMARK 465 GLU M 79 REMARK 465 ARG M 80 REMARK 465 LEU M 81 REMARK 465 THR M 82 REMARK 465 LEU M 83 REMARK 465 ASP M 84 REMARK 465 CYS M 85 REMARK 465 ASN M 86 REMARK 465 GLU M 87 REMARK 465 ASP M 88 REMARK 465 CYS M 89 REMARK 465 GLY M 90 REMARK 465 THR M 91 REMARK 465 SER M 92 REMARK 465 GLY M 93 REMARK 465 THR M 94 REMARK 465 GLN M 95 REMARK 465 GLY M 96 REMARK 465 VAL M 97 REMARK 465 GLY M 98 REMARK 465 SER M 99 REMARK 465 PRO M 100 REMARK 465 GLN M 101 REMARK 465 ILE M 102 REMARK 465 LEU M 103 REMARK 465 VAL M 104 REMARK 465 GLU M 105 REMARK 465 SER M 106 REMARK 465 PRO M 107 REMARK 465 THR M 108 REMARK 465 VAL M 109 REMARK 465 LEU M 110 REMARK 465 GLU M 111 REMARK 465 SER M 112 REMARK 465 GLY M 113 REMARK 465 ALA M 114 REMARK 465 LYS M 115 REMARK 465 GLU M 116 REMARK 465 ALA N 2 REMARK 465 GLY N 3 REMARK 465 ARG N 4 REMARK 465 SER N 5 REMARK 465 GLY N 6 REMARK 465 ASP N 7 REMARK 465 SER N 8 REMARK 465 ARG N 66 REMARK 465 SER N 67 REMARK 465 ALA N 68 REMARK 465 GLU N 69 REMARK 465 PRO N 70 REMARK 465 VAL N 71 REMARK 465 PRO N 72 REMARK 465 LEU N 73 REMARK 465 GLN N 74 REMARK 465 LEU N 75 REMARK 465 PRO N 76 REMARK 465 PRO N 77 REMARK 465 LEU N 78 REMARK 465 GLU N 79 REMARK 465 ARG N 80 REMARK 465 LEU N 81 REMARK 465 THR N 82 REMARK 465 LEU N 83 REMARK 465 ASP N 84 REMARK 465 CYS N 85 REMARK 465 ASN N 86 REMARK 465 GLU N 87 REMARK 465 ASP N 88 REMARK 465 CYS N 89 REMARK 465 GLY N 90 REMARK 465 THR N 91 REMARK 465 SER N 92 REMARK 465 GLY N 93 REMARK 465 THR N 94 REMARK 465 GLN N 95 REMARK 465 GLY N 96 REMARK 465 VAL N 97 REMARK 465 GLY N 98 REMARK 465 SER N 99 REMARK 465 PRO N 100 REMARK 465 GLN N 101 REMARK 465 ILE N 102 REMARK 465 LEU N 103 REMARK 465 VAL N 104 REMARK 465 GLU N 105 REMARK 465 SER N 106 REMARK 465 PRO N 107 REMARK 465 THR N 108 REMARK 465 VAL N 109 REMARK 465 LEU N 110 REMARK 465 GLU N 111 REMARK 465 SER N 112 REMARK 465 GLY N 113 REMARK 465 ALA N 114 REMARK 465 LYS N 115 REMARK 465 GLU N 116 REMARK 465 ALA O 2 REMARK 465 GLY O 3 REMARK 465 ARG O 4 REMARK 465 SER O 5 REMARK 465 GLY O 6 REMARK 465 ASP O 7 REMARK 465 SER O 8 REMARK 465 ARG O 66 REMARK 465 SER O 67 REMARK 465 ALA O 68 REMARK 465 GLU O 69 REMARK 465 PRO O 70 REMARK 465 VAL O 71 REMARK 465 PRO O 72 REMARK 465 LEU O 73 REMARK 465 GLN O 74 REMARK 465 LEU O 75 REMARK 465 PRO O 76 REMARK 465 PRO O 77 REMARK 465 LEU O 78 REMARK 465 GLU O 79 REMARK 465 ARG O 80 REMARK 465 LEU O 81 REMARK 465 THR O 82 REMARK 465 LEU O 83 REMARK 465 ASP O 84 REMARK 465 CYS O 85 REMARK 465 ASN O 86 REMARK 465 GLU O 87 REMARK 465 ASP O 88 REMARK 465 CYS O 89 REMARK 465 GLY O 90 REMARK 465 THR O 91 REMARK 465 SER O 92 REMARK 465 GLY O 93 REMARK 465 THR O 94 REMARK 465 GLN O 95 REMARK 465 GLY O 96 REMARK 465 VAL O 97 REMARK 465 GLY O 98 REMARK 465 SER O 99 REMARK 465 PRO O 100 REMARK 465 GLN O 101 REMARK 465 ILE O 102 REMARK 465 LEU O 103 REMARK 465 VAL O 104 REMARK 465 GLU O 105 REMARK 465 SER O 106 REMARK 465 PRO O 107 REMARK 465 THR O 108 REMARK 465 VAL O 109 REMARK 465 LEU O 110 REMARK 465 GLU O 111 REMARK 465 SER O 112 REMARK 465 GLY O 113 REMARK 465 ALA O 114 REMARK 465 LYS O 115 REMARK 465 GLU O 116 REMARK 465 ALA P 2 REMARK 465 GLY P 3 REMARK 465 ARG P 4 REMARK 465 SER P 5 REMARK 465 GLY P 6 REMARK 465 ASP P 7 REMARK 465 SER P 8 REMARK 465 ARG P 66 REMARK 465 SER P 67 REMARK 465 ALA P 68 REMARK 465 GLU P 69 REMARK 465 PRO P 70 REMARK 465 VAL P 71 REMARK 465 PRO P 72 REMARK 465 LEU P 73 REMARK 465 GLN P 74 REMARK 465 LEU P 75 REMARK 465 PRO P 76 REMARK 465 PRO P 77 REMARK 465 LEU P 78 REMARK 465 GLU P 79 REMARK 465 ARG P 80 REMARK 465 LEU P 81 REMARK 465 THR P 82 REMARK 465 LEU P 83 REMARK 465 ASP P 84 REMARK 465 CYS P 85 REMARK 465 ASN P 86 REMARK 465 GLU P 87 REMARK 465 ASP P 88 REMARK 465 CYS P 89 REMARK 465 GLY P 90 REMARK 465 THR P 91 REMARK 465 SER P 92 REMARK 465 GLY P 93 REMARK 465 THR P 94 REMARK 465 GLN P 95 REMARK 465 GLY P 96 REMARK 465 VAL P 97 REMARK 465 GLY P 98 REMARK 465 SER P 99 REMARK 465 PRO P 100 REMARK 465 GLN P 101 REMARK 465 ILE P 102 REMARK 465 LEU P 103 REMARK 465 VAL P 104 REMARK 465 GLU P 105 REMARK 465 SER P 106 REMARK 465 PRO P 107 REMARK 465 THR P 108 REMARK 465 VAL P 109 REMARK 465 LEU P 110 REMARK 465 GLU P 111 REMARK 465 SER P 112 REMARK 465 GLY P 113 REMARK 465 ALA P 114 REMARK 465 LYS P 115 REMARK 465 GLU P 116 REMARK 465 ALA Q 2 REMARK 465 GLY Q 3 REMARK 465 ARG Q 4 REMARK 465 SER Q 5 REMARK 465 GLY Q 6 REMARK 465 ASP Q 7 REMARK 465 SER Q 8 REMARK 465 ARG Q 66 REMARK 465 SER Q 67 REMARK 465 ALA Q 68 REMARK 465 GLU Q 69 REMARK 465 PRO Q 70 REMARK 465 VAL Q 71 REMARK 465 PRO Q 72 REMARK 465 LEU Q 73 REMARK 465 GLN Q 74 REMARK 465 LEU Q 75 REMARK 465 PRO Q 76 REMARK 465 PRO Q 77 REMARK 465 LEU Q 78 REMARK 465 GLU Q 79 REMARK 465 ARG Q 80 REMARK 465 LEU Q 81 REMARK 465 THR Q 82 REMARK 465 LEU Q 83 REMARK 465 ASP Q 84 REMARK 465 CYS Q 85 REMARK 465 ASN Q 86 REMARK 465 GLU Q 87 REMARK 465 ASP Q 88 REMARK 465 CYS Q 89 REMARK 465 GLY Q 90 REMARK 465 THR Q 91 REMARK 465 SER Q 92 REMARK 465 GLY Q 93 REMARK 465 THR Q 94 REMARK 465 GLN Q 95 REMARK 465 GLY Q 96 REMARK 465 VAL Q 97 REMARK 465 GLY Q 98 REMARK 465 SER Q 99 REMARK 465 PRO Q 100 REMARK 465 GLN Q 101 REMARK 465 ILE Q 102 REMARK 465 LEU Q 103 REMARK 465 VAL Q 104 REMARK 465 GLU Q 105 REMARK 465 SER Q 106 REMARK 465 PRO Q 107 REMARK 465 THR Q 108 REMARK 465 VAL Q 109 REMARK 465 LEU Q 110 REMARK 465 GLU Q 111 REMARK 465 SER Q 112 REMARK 465 GLY Q 113 REMARK 465 ALA Q 114 REMARK 465 LYS Q 115 REMARK 465 GLU Q 116 REMARK 465 ALA R 2 REMARK 465 GLY R 3 REMARK 465 ARG R 4 REMARK 465 SER R 5 REMARK 465 GLY R 6 REMARK 465 ASP R 7 REMARK 465 SER R 8 REMARK 465 ARG R 66 REMARK 465 SER R 67 REMARK 465 ALA R 68 REMARK 465 GLU R 69 REMARK 465 PRO R 70 REMARK 465 VAL R 71 REMARK 465 PRO R 72 REMARK 465 LEU R 73 REMARK 465 GLN R 74 REMARK 465 LEU R 75 REMARK 465 PRO R 76 REMARK 465 PRO R 77 REMARK 465 LEU R 78 REMARK 465 GLU R 79 REMARK 465 ARG R 80 REMARK 465 LEU R 81 REMARK 465 THR R 82 REMARK 465 LEU R 83 REMARK 465 ASP R 84 REMARK 465 CYS R 85 REMARK 465 ASN R 86 REMARK 465 GLU R 87 REMARK 465 ASP R 88 REMARK 465 CYS R 89 REMARK 465 GLY R 90 REMARK 465 THR R 91 REMARK 465 SER R 92 REMARK 465 GLY R 93 REMARK 465 THR R 94 REMARK 465 GLN R 95 REMARK 465 GLY R 96 REMARK 465 VAL R 97 REMARK 465 GLY R 98 REMARK 465 SER R 99 REMARK 465 PRO R 100 REMARK 465 GLN R 101 REMARK 465 ILE R 102 REMARK 465 LEU R 103 REMARK 465 VAL R 104 REMARK 465 GLU R 105 REMARK 465 SER R 106 REMARK 465 PRO R 107 REMARK 465 THR R 108 REMARK 465 VAL R 109 REMARK 465 LEU R 110 REMARK 465 GLU R 111 REMARK 465 SER R 112 REMARK 465 GLY R 113 REMARK 465 ALA R 114 REMARK 465 LYS R 115 REMARK 465 GLU R 116 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 ASP A 221 CA C O CB CG OD1 OD2 REMARK 470 ARG B 98 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 221 CA C O CB CG OD1 OD2 REMARK 470 ARG D 98 CG CD NE CZ NH1 NH2 REMARK 470 ASP E 221 CA C O CB CG OD1 OD2 REMARK 470 ARG F 98 CG CD NE CZ NH1 NH2 REMARK 470 ASP G 221 CA C O CB CG OD1 OD2 REMARK 470 ASP H 221 CA C O CB CG OD1 OD2 REMARK 470 ARG I 98 CG CD NE CZ NH1 NH2 REMARK 470 ASP J 221 CA C O CB CG OD1 OD2 REMARK 470 ARG K 98 CG CD NE CZ NH1 NH2 REMARK 470 ARG L 98 CG CD NE CZ NH1 NH2 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 A 30 -77.31 -56.88 REMARK 500 SER A 55 -153.92 -105.68 REMARK 500 THR A 76 -159.42 -154.32 REMARK 500 ALA A 129 100.52 -54.97 REMARK 500 PRO A 130 -100.59 -78.46 REMARK 500 SER A 131 -115.12 65.70 REMARK 500 SER A 134 23.56 -140.63 REMARK 500 ASP A 148 90.64 46.79 REMARK 500 PRO A 153 -158.24 -101.24 REMARK 500 SER A 183 108.67 -160.76 REMARK 500 SER A 192 31.61 -86.81 REMARK 500 PRO A 206 17.53 -66.92 REMARK 500 ASN A 208 -19.61 79.45 REMARK 500 LYS A 210 43.76 -140.70 REMARK 500 PRO A 217 83.86 -65.26 REMARK 500 LYS A 218 -139.23 51.00 REMARK 500 SER A 219 -63.58 -148.86 REMARK 500 SER B 28 -81.69 -37.73 REMARK 500 ILE B 29 99.57 53.64 REMARK 500 SER B 30 -100.71 -77.39 REMARK 500 TRP B 32 39.16 -64.17 REMARK 500 PRO B 44 152.39 -47.91 REMARK 500 ASP B 50 47.81 39.75 REMARK 500 ALA B 51 -24.43 56.45 REMARK 500 SER B 76 -110.72 -74.81 REMARK 500 ASP B 82 -11.38 -46.78 REMARK 500 ALA B 94 36.21 -68.37 REMARK 500 ALA B 95 -153.05 50.42 REMARK 500 ARG B 98 -151.86 59.02 REMARK 500 THR B 105 97.44 -162.09 REMARK 500 SER B 130 -45.02 -167.90 REMARK 500 ASN B 141 90.83 34.44 REMARK 500 SER B 159 -78.87 -131.25 REMARK 500 SER B 174 26.07 28.51 REMARK 500 SER B 177 129.81 -170.81 REMARK 500 PRO B 207 84.23 -53.04 REMARK 500 ARG B 214 107.07 -56.10 REMARK 500 SER C 30 -76.78 -57.41 REMARK 500 SER C 55 -153.94 -107.49 REMARK 500 THR C 76 -159.55 -155.33 REMARK 500 ALA C 129 101.41 -55.77 REMARK 500 PRO C 130 -100.38 -78.78 REMARK 500 SER C 131 -114.79 64.67 REMARK 500 SER C 134 22.98 -140.53 REMARK 500 ASP C 148 90.65 46.51 REMARK 500 PRO C 153 -158.35 -102.81 REMARK 500 SER C 192 31.95 -87.66 REMARK 500 PRO C 206 17.21 -66.81 REMARK 500 ASN C 208 -16.74 75.32 REMARK 500 LYS C 210 44.85 -141.25 REMARK 500 REMARK 500 THIS ENTRY HAS 228 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 ARG A 53 24.1 L L OUTSIDE RANGE REMARK 500 VAL A 77 24.9 L L OUTSIDE RANGE REMARK 500 VAL A 125 24.9 L L OUTSIDE RANGE REMARK 500 THR A 135 24.2 L L OUTSIDE RANGE REMARK 500 THR B 18 24.2 L L OUTSIDE RANGE REMARK 500 ALA B 51 25.0 L L OUTSIDE RANGE REMARK 500 LEU B 54 23.3 L L OUTSIDE RANGE REMARK 500 VAL B 78 23.5 L L OUTSIDE RANGE REMARK 500 THR B 85 24.5 L L OUTSIDE RANGE REMARK 500 VAL B 136 24.3 L L OUTSIDE RANGE REMARK 500 ASN B 141 25.0 L L OUTSIDE RANGE REMARK 500 SER B 174 23.7 L L OUTSIDE RANGE REMARK 500 ARG C 53 24.1 L L OUTSIDE RANGE REMARK 500 VAL C 77 24.8 L L OUTSIDE RANGE REMARK 500 THR C 135 24.4 L L OUTSIDE RANGE REMARK 500 THR D 18 24.9 L L OUTSIDE RANGE REMARK 500 ALA D 51 24.8 L L OUTSIDE RANGE REMARK 500 LEU D 54 22.9 L L OUTSIDE RANGE REMARK 500 VAL D 78 23.1 L L OUTSIDE RANGE REMARK 500 VAL D 136 24.9 L L OUTSIDE RANGE REMARK 500 ASN D 141 25.0 L L OUTSIDE RANGE REMARK 500 SER D 174 23.8 L L OUTSIDE RANGE REMARK 500 ARG E 53 24.1 L L OUTSIDE RANGE REMARK 500 VAL E 77 24.8 L L OUTSIDE RANGE REMARK 500 THR E 135 24.2 L L OUTSIDE RANGE REMARK 500 THR F 18 24.1 L L OUTSIDE RANGE REMARK 500 ALA F 51 24.7 L L OUTSIDE RANGE REMARK 500 LEU F 54 23.1 L L OUTSIDE RANGE REMARK 500 VAL F 78 23.5 L L OUTSIDE RANGE REMARK 500 THR F 85 24.5 L L OUTSIDE RANGE REMARK 500 VAL F 136 24.6 L L OUTSIDE RANGE REMARK 500 ASN F 141 24.4 L L OUTSIDE RANGE REMARK 500 SER F 174 24.0 L L OUTSIDE RANGE REMARK 500 ARG G 53 24.2 L L OUTSIDE RANGE REMARK 500 VAL G 77 24.9 L L OUTSIDE RANGE REMARK 500 THR G 135 24.3 L L OUTSIDE RANGE REMARK 500 ARG H 53 24.3 L L OUTSIDE RANGE REMARK 500 VAL H 77 24.9 L L OUTSIDE RANGE REMARK 500 THR H 135 24.1 L L OUTSIDE RANGE REMARK 500 ALA I 51 24.7 L L OUTSIDE RANGE REMARK 500 LEU I 54 22.9 L L OUTSIDE RANGE REMARK 500 VAL I 78 23.1 L L OUTSIDE RANGE REMARK 500 VAL I 136 24.7 L L OUTSIDE RANGE REMARK 500 SER I 174 23.8 L L OUTSIDE RANGE REMARK 500 ARG J 53 23.9 L L OUTSIDE RANGE REMARK 500 THR J 135 24.3 L L OUTSIDE RANGE REMARK 500 THR K 18 24.7 L L OUTSIDE RANGE REMARK 500 ALA K 51 24.1 L L OUTSIDE RANGE REMARK 500 LEU K 54 23.0 L L OUTSIDE RANGE REMARK 500 VAL K 78 23.0 L L OUTSIDE RANGE REMARK 500 REMARK 500 THIS ENTRY HAS 59 CHIRALITY DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 THE C-TERMINAL DOMAIN OF REV IS DISORDERED IN THE CRYSTAL REMARK 999 STRUCTURE. N-TERMINAL MET HAS BEEN CLEAVED OFF IN E. COLI REMARK 999 REMARK 999 SEQUENCE REMARK 999 AUTHOR PROVIDED GENBANK ACCESSION NUMBERS: REMARK 999 CHAINS A,C,E,G,H,J GU223202 REMARK 999 CHAINS B,D,F,I,K,L GU223201 REMARK 999 CHAINS M,N,O,P,Q,R AAL29461