REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.S.CHO,K.MASON,K.X.RAMYAR,A.M.STANLEY,S.B.GABELLI, REMARK 1 AUTH 2 D.W.DENNEY JR.,D.J.LEAHY REMARK 1 TITL STRUCTURE OF THE EXTRACELLULAR REGION OF HER2 ALONE AND IN REMARK 1 TITL 2 COMPLEX WITH THE HERCEPTIN FAB REMARK 1 REF NATURE V. 421 756 2003 REMARK 1 REFN ISSN 0028-0836 REMARK 1 PMID 12610629 REMARK 1 DOI 10.1038/NATURE01392 REMARK 1 REFERENCE 2 REMARK 1 AUTH F.F.VAJDOS,C.W.ADAMS,T.N.BREECE,L.G.PRESTA,A.M.DE VOS, REMARK 1 AUTH 2 S.S.SIDHU REMARK 1 TITL COMPREHENSIVE FUNCTIONAL MAPS OF THE ANTIGEN-BINDING SITE OF REMARK 1 TITL 2 AN ANTI-ERBB2 ANTIBODY OBTAINED WITH SHOTGUN SCANNING REMARK 1 TITL 3 MUTAGENESIS REMARK 1 REF J.MOL.BIOL. V. 320 415 2002 REMARK 1 REFN ISSN 0022-2836 REMARK 1 PMID 12079396 REMARK 1 DOI 10.1016/S0022-2836(02)00264-4 REMARK 1 REFERENCE 3 REMARK 1 AUTH D.B.AGUS,R.W.AKITA,W.D.FOX,G.D.LEWIS,B.HIGGINS,P.I.PISACANE, REMARK 1 AUTH 2 J.A.LOFGREN,C.TINDELL,D.P.EVANS,K.MAIESE,H.I.SCHER, REMARK 1 AUTH 3 M.X.SLIWKOWSKI REMARK 1 TITL TARGETING LIGAND-ACTIVATED ERBB2 SIGNALING INHIBITS BREAST REMARK 1 TITL 2 AND PROSTATE TUMOR GROWTH REMARK 1 REF CANCER CELL V. 2 127 2002 REMARK 1 REFN ISSN 1535-6108 REMARK 1 PMID 12204533 REMARK 1 DOI 10.1016/S1535-6108(02)00097-1 REMARK 2 REMARK 2 RESOLUTION. 3.25 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.24 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 52816 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : SHELLS (A): 3.289 - 3.285, REMARK 3 3.370 - 3.366, 3.459 - 3.454, REMARK 3 3.559 - 3.554, 3.670 - 3.664, REMARK 3 3.798 - 3.791, 3.944 - 3.937, REMARK 3 4.117 - 4.107, 4.323 - 4.313, REMARK 3 4.577 - 4.564, 4.904 - 4.886, REMARK 3 5.345 - 5.319, 6.000 - 5.960, REMARK 3 7.157 - 7.073, 10.465 - 10.120 REMARK 3 R VALUE (WORKING + TEST SET) : 0.227 REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.268 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2835 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.25 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.33 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3708 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.3310 REMARK 3 BIN FREE R VALUE SET COUNT : 189 REMARK 3 BIN FREE R VALUE : 0.3970 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 15302 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 179 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : 97.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.59 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.21000 REMARK 3 B22 (A**2) : 2.21000 REMARK 3 B33 (A**2) : -4.43000 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 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.479 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.381 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.571 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15906 ; 0.009 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21684 ; 1.273 ; 1.968 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1987 ; 6.520 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2428 ; 0.083 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12074 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6438 ; 0.208 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 404 ; 0.137 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 33 ; 0.227 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.176 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 9931 ; 1.657 ; 2.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16033 ; 2.717 ; 5.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5975 ; 1.810 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5651 ; 2.830 ; 5.000 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 4 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 1 A 195 1 REMARK 3 1 B 1 B 195 1 REMARK 3 2 A 1001 A 1002 1 REMARK 3 2 B 1001 B 1002 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 1 A (A): 1498 ; 0.03 ; 0.05 REMARK 3 TIGHT THERMAL 1 A (A**2): 1498 ; 0.06 ; 0.50 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 196 A 320 1 REMARK 3 1 B 196 B 320 1 REMARK 3 2 A 1003 A 1004 1 REMARK 3 2 B 1003 B 1004 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 2 A (A): 941 ; 0.03 ; 0.05 REMARK 3 TIGHT THERMAL 2 A (A**2): 941 ; 0.05 ; 0.50 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 321 A 488 1 REMARK 3 1 B 321 B 488 1 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 3 A (A): 1316 ; 0.03 ; 0.05 REMARK 3 TIGHT THERMAL 3 A (A**2): 1316 ; 0.06 ; 0.50 REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 489 A 564 4 REMARK 3 1 B 489 B 564 4 REMARK 3 2 A 1006 A 1006 4 REMARK 3 2 B 1006 B 1006 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 4 A (A): 592 ; 0.29 ; 0.50 REMARK 3 MEDIUM THERMAL 4 A (A**2): 592 ; 0.50 ; 2.00 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 16 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 195 REMARK 3 RESIDUE RANGE : A 1001 A 1002 REMARK 3 ORIGIN FOR THE GROUP (A): 50.8146 64.4207 217.1610 REMARK 3 T TENSOR REMARK 3 T11: 0.3282 T22: 0.3497 REMARK 3 T33: 0.2797 T12: 0.1187 REMARK 3 T13: -0.0903 T23: -0.0079 REMARK 3 L TENSOR REMARK 3 L11: 8.1541 L22: 3.8111 REMARK 3 L33: 4.2918 L12: -0.7112 REMARK 3 L13: -1.2482 L23: -0.4558 REMARK 3 S TENSOR REMARK 3 S11: 0.0164 S12: -0.6025 S13: -0.2231 REMARK 3 S21: 0.2585 S22: -0.1664 S23: -0.0344 REMARK 3 S31: -0.3221 S32: 0.0815 S33: 0.1500 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 196 A 320 REMARK 3 RESIDUE RANGE : A 1003 A 1004 REMARK 3 ORIGIN FOR THE GROUP (A): 60.9738 91.1703 212.4541 REMARK 3 T TENSOR REMARK 3 T11: 0.9610 T22: 0.3340 REMARK 3 T33: 0.5375 T12: 0.0510 REMARK 3 T13: -0.2190 T23: -0.1471 REMARK 3 L TENSOR REMARK 3 L11: 2.9533 L22: 3.5179 REMARK 3 L33: 5.6454 L12: 0.3437 REMARK 3 L13: -1.2479 L23: -0.4711 REMARK 3 S TENSOR REMARK 3 S11: -0.0220 S12: -0.8372 S13: 0.7547 REMARK 3 S21: 0.5839 S22: -0.0193 S23: -0.2326 REMARK 3 S31: -0.9996 S32: 0.7245 S33: 0.0413 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 321 A 488 REMARK 3 ORIGIN FOR THE GROUP (A): 78.4132 64.5571 196.5325 REMARK 3 T TENSOR REMARK 3 T11: 0.1956 T22: 0.3139 REMARK 3 T33: 0.2764 T12: -0.0221 REMARK 3 T13: -0.1179 T23: 0.0380 REMARK 3 L TENSOR REMARK 3 L11: 4.6119 L22: 5.1052 REMARK 3 L33: 4.6820 L12: -0.9412 REMARK 3 L13: -0.1280 L23: -0.8356 REMARK 3 S TENSOR REMARK 3 S11: -0.0068 S12: 0.2070 S13: -0.2034 REMARK 3 S21: -0.0555 S22: -0.0834 S23: 0.0157 REMARK 3 S31: -0.3053 S32: 0.1755 S33: 0.0902 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 489 A 564 REMARK 3 RESIDUE RANGE : A 1006 A 1006 REMARK 3 ORIGIN FOR THE GROUP (A): 107.8938 74.4499 199.1873 REMARK 3 T TENSOR REMARK 3 T11: 1.3333 T22: 1.7001 REMARK 3 T33: 1.3954 T12: -0.7924 REMARK 3 T13: 0.0967 T23: 0.0570 REMARK 3 L TENSOR REMARK 3 L11: 26.6254 L22: 9.7618 REMARK 3 L33: 15.1993 L12: 11.2059 REMARK 3 L13: -9.9308 L23: -4.8181 REMARK 3 S TENSOR REMARK 3 S11: 0.9530 S12: -0.7793 S13: 3.3216 REMARK 3 S21: -0.3028 S22: 0.0129 S23: -0.6317 REMARK 3 S31: -3.4595 S32: 3.6272 S33: -0.9659 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 1 B 195 REMARK 3 RESIDUE RANGE : B 1001 B 1002 REMARK 3 ORIGIN FOR THE GROUP (A): 21.2489 60.2082 207.0842 REMARK 3 T TENSOR REMARK 3 T11: 0.2078 T22: 0.5371 REMARK 3 T33: 0.4653 T12: 0.3115 REMARK 3 T13: 0.0085 T23: -0.1678 REMARK 3 L TENSOR REMARK 3 L11: 4.9365 L22: 4.6783 REMARK 3 L33: 6.6367 L12: 0.2706 REMARK 3 L13: 2.3988 L23: 0.5274 REMARK 3 S TENSOR REMARK 3 S11: -0.2511 S12: -0.3848 S13: 0.4705 REMARK 3 S21: -0.0098 S22: -0.1548 S23: 0.3979 REMARK 3 S31: -0.6068 S32: -0.7756 S33: 0.4059 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 196 B 320 REMARK 3 RESIDUE RANGE : B 1003 B 1005 REMARK 3 ORIGIN FOR THE GROUP (A): 10.1019 34.5373 214.5874 REMARK 3 T TENSOR REMARK 3 T11: 0.2026 T22: 0.8984 REMARK 3 T33: 0.5368 T12: 0.1224 REMARK 3 T13: 0.1648 T23: 0.0845 REMARK 3 L TENSOR REMARK 3 L11: 3.0653 L22: 3.8276 REMARK 3 L33: 2.7017 L12: 0.1090 REMARK 3 L13: -0.3779 L23: -0.6258 REMARK 3 S TENSOR REMARK 3 S11: -0.0160 S12: -0.5385 S13: -0.0493 REMARK 3 S21: 0.2442 S22: -0.1130 S23: 1.0809 REMARK 3 S31: -0.1483 S32: -1.1409 S33: 0.1290 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 321 B 488 REMARK 3 ORIGIN FOR THE GROUP (A): 11.9376 41.1730 179.7694 REMARK 3 T TENSOR REMARK 3 T11: 0.1241 T22: 0.3717 REMARK 3 T33: 0.3708 T12: 0.1050 REMARK 3 T13: -0.0274 T23: -0.0228 REMARK 3 L TENSOR REMARK 3 L11: 3.7897 L22: 6.1533 REMARK 3 L33: 5.6096 L12: -0.6603 REMARK 3 L13: 1.0769 L23: 0.0291 REMARK 3 S TENSOR REMARK 3 S11: -0.0143 S12: -0.0663 S13: 0.0290 REMARK 3 S21: -0.2414 S22: -0.0084 S23: -0.0043 REMARK 3 S31: -0.2120 S32: -0.0867 S33: 0.0227 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 489 B 577 REMARK 3 RESIDUE RANGE : B 1007 B 1008 REMARK 3 ORIGIN FOR THE GROUP (A): -14.3634 23.6989 169.1663 REMARK 3 T TENSOR REMARK 3 T11: 0.7103 T22: 0.8833 REMARK 3 T33: 1.2723 T12: 0.4000 REMARK 3 T13: -0.0820 T23: 0.1138 REMARK 3 L TENSOR REMARK 3 L11: 13.0057 L22: 20.3978 REMARK 3 L33: 3.6376 L12: 13.1292 REMARK 3 L13: 3.8171 L23: 6.9274 REMARK 3 S TENSOR REMARK 3 S11: -0.1521 S12: -0.4122 S13: -2.3614 REMARK 3 S21: -0.2759 S22: 0.1274 S23: -0.7275 REMARK 3 S31: 0.7782 S32: -0.1044 S33: 0.0247 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 1 C 109 REMARK 3 ORIGIN FOR THE GROUP (A): 59.2854 104.7732 177.6731 REMARK 3 T TENSOR REMARK 3 T11: 0.9770 T22: 0.0973 REMARK 3 T33: 0.5391 T12: -0.0297 REMARK 3 T13: -0.0938 T23: 0.0641 REMARK 3 L TENSOR REMARK 3 L11: 3.2120 L22: 2.1977 REMARK 3 L33: 8.9553 L12: -0.6991 REMARK 3 L13: 1.1422 L23: -0.8387 REMARK 3 S TENSOR REMARK 3 S11: 0.1391 S12: 0.3801 S13: 0.6882 REMARK 3 S21: -0.0834 S22: -0.1490 S23: 0.1628 REMARK 3 S31: -1.0709 S32: 0.3813 S33: 0.0099 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 1 D 113 REMARK 3 ORIGIN FOR THE GROUP (A): 48.1018 100.3724 196.5645 REMARK 3 T TENSOR REMARK 3 T11: 0.9705 T22: 0.1703 REMARK 3 T33: 0.5214 T12: 0.0894 REMARK 3 T13: -0.0523 T23: -0.0800 REMARK 3 L TENSOR REMARK 3 L11: 8.1035 L22: 4.1635 REMARK 3 L33: 2.8854 L12: -3.1748 REMARK 3 L13: 1.2233 L23: -1.3046 REMARK 3 S TENSOR REMARK 3 S11: -0.0027 S12: -0.4567 S13: 0.5441 REMARK 3 S21: 0.1669 S22: 0.1452 S23: 0.4931 REMARK 3 S31: -0.5833 S32: -0.3368 S33: -0.1425 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : E 1 E 109 REMARK 3 ORIGIN FOR THE GROUP (A): 28.5404 3.1198 205.1855 REMARK 3 T TENSOR REMARK 3 T11: 0.4836 T22: 0.3909 REMARK 3 T33: 0.4820 T12: -0.0457 REMARK 3 T13: -0.0135 T23: 0.1657 REMARK 3 L TENSOR REMARK 3 L11: 5.1573 L22: 4.6116 REMARK 3 L33: 6.0494 L12: -2.9620 REMARK 3 L13: -1.1690 L23: 0.4103 REMARK 3 S TENSOR REMARK 3 S11: 0.3404 S12: -0.4462 S13: -0.6168 REMARK 3 S21: -0.1250 S22: -0.2058 S23: 0.2537 REMARK 3 S31: 1.0039 S32: 0.0846 S33: -0.1346 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : F 1 F 113 REMARK 3 ORIGIN FOR THE GROUP (A): 27.5213 20.7101 219.0470 REMARK 3 T TENSOR REMARK 3 T11: 0.1520 T22: 0.7943 REMARK 3 T33: 0.3885 T12: -0.0746 REMARK 3 T13: 0.1136 T23: 0.0758 REMARK 3 L TENSOR REMARK 3 L11: 5.6269 L22: 3.7517 REMARK 3 L33: 3.7920 L12: -2.5780 REMARK 3 L13: 2.2461 L23: -0.5989 REMARK 3 S TENSOR REMARK 3 S11: -0.0471 S12: -1.0246 S13: 0.0294 REMARK 3 S21: 0.2129 S22: 0.2125 S23: -0.2772 REMARK 3 S31: -0.0092 S32: 0.0290 S33: -0.1654 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 110 C 214 REMARK 3 ORIGIN FOR THE GROUP (A): 25.8744 112.5158 163.9545 REMARK 3 T TENSOR REMARK 3 T11: 1.3987 T22: 2.7895 REMARK 3 T33: 1.9763 T12: 0.9150 REMARK 3 T13: 0.4767 T23: -0.5554 REMARK 3 L TENSOR REMARK 3 L11: 30.7116 L22: 15.2478 REMARK 3 L33: 15.6594 L12: -4.7048 REMARK 3 L13: -8.8241 L23: 0.9795 REMARK 3 S TENSOR REMARK 3 S11: 2.3845 S12: 5.1090 S13: 1.6169 REMARK 3 S21: 1.8285 S22: -2.8033 S23: 3.5391 REMARK 3 S31: -1.8008 S32: -5.8563 S33: 0.4188 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 114 D 216 REMARK 3 ORIGIN FOR THE GROUP (A): 23.3762 98.9991 171.5865 REMARK 3 T TENSOR REMARK 3 T11: 1.9025 T22: 1.6820 REMARK 3 T33: 2.0294 T12: -0.0547 REMARK 3 T13: 0.3142 T23: -0.7016 REMARK 3 L TENSOR REMARK 3 L11: 3.6061 L22: 14.3447 REMARK 3 L33: 13.5098 L12: -4.5102 REMARK 3 L13: -0.0943 L23: 7.2635 REMARK 3 S TENSOR REMARK 3 S11: 0.5384 S12: 2.3612 S13: -1.6467 REMARK 3 S21: -0.8897 S22: -2.3754 S23: 1.8933 REMARK 3 S31: 1.8244 S32: -2.4838 S33: 1.8370 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : E 110 E 214 REMARK 3 ORIGIN FOR THE GROUP (A): 56.9009 -7.5915 224.4427 REMARK 3 T TENSOR REMARK 3 T11: 0.5182 T22: 1.4923 REMARK 3 T33: 1.0088 T12: 0.2288 REMARK 3 T13: -0.0916 T23: 0.4339 REMARK 3 L TENSOR REMARK 3 L11: 6.9041 L22: 6.7464 REMARK 3 L33: 13.4581 L12: -2.9560 REMARK 3 L13: 5.0969 L23: -0.7392 REMARK 3 S TENSOR REMARK 3 S11: 0.7320 S12: -0.8789 S13: -0.4093 REMARK 3 S21: 0.2284 S22: -0.4218 S23: -1.0813 REMARK 3 S31: 1.1113 S32: 0.9680 S33: -0.3102 REMARK 3 REMARK 3 TLS GROUP : 16 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : F 114 F 216 REMARK 3 ORIGIN FOR THE GROUP (A): 62.3013 7.1213 222.5789 REMARK 3 T TENSOR REMARK 3 T11: 0.1358 T22: 1.5819 REMARK 3 T33: 1.5376 T12: -0.0264 REMARK 3 T13: 0.0579 T23: 0.2546 REMARK 3 L TENSOR REMARK 3 L11: 13.8110 L22: 7.6742 REMARK 3 L33: 11.8616 L12: -3.8288 REMARK 3 L13: -2.2234 L23: 1.5717 REMARK 3 S TENSOR REMARK 3 S11: 0.3416 S12: -0.6068 S13: 1.8502 REMARK 3 S21: 0.3369 S22: -0.3212 S23: -2.7345 REMARK 3 S31: -0.1137 S32: 1.3929 S33: -0.0204 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1S78 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-04. REMARK 100 THE RCSB ID CODE IS RCSB021454. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-NOV-01 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.1 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 : SINGLE CRYSTAL SI(220) REMARK 200 MONOCHROMATOR, CYLINDRICALLY BENT REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56351 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.250 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 8.200 REMARK 200 R MERGE (I) : 0.11600 REMARK 200 R SYM (I) : 0.11600 REMARK 200 FOR THE DATA SET : 19.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 8.30 REMARK 200 R MERGE FOR SHELL (I) : 0.69100 REMARK 200 R SYM FOR SHELL (I) : 0.69100 REMARK 200 FOR SHELL : 3.300 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: RAT ERBB2 EXTRACELLULAR DOMAIN (PDB CODE 1N8Y) AND REMARK 200 UNCOMPLEXED PERTUZUMAB FAB (PDB CODE 1L7I) REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 69.01 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM FORMATE, PH 6.5, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+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 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 178.43650 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 69.70600 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 69.70600 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 267.65475 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 69.70600 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 69.70600 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 89.21825 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 69.70600 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 69.70600 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 267.65475 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 69.70600 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 69.70600 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 89.21825 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 178.43650 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7480 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 45800 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7810 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 46650 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 ASN A 102 REMARK 465 ASN A 103 REMARK 465 THR A 104 REMARK 465 THR A 105 REMARK 465 PRO A 106 REMARK 465 VAL A 107 REMARK 465 THR A 108 REMARK 465 GLY A 109 REMARK 465 ALA A 110 REMARK 465 CYS A 565 REMARK 465 ALA A 566 REMARK 465 HIS A 567 REMARK 465 TYR A 568 REMARK 465 LYS A 569 REMARK 465 ASP A 570 REMARK 465 PRO A 571 REMARK 465 PRO A 572 REMARK 465 PHE A 573 REMARK 465 CYS A 574 REMARK 465 VAL A 575 REMARK 465 ALA A 576 REMARK 465 ARG A 577 REMARK 465 CYS A 578 REMARK 465 PRO A 579 REMARK 465 SER A 580 REMARK 465 GLY A 581 REMARK 465 VAL A 582 REMARK 465 LYS A 583 REMARK 465 PRO A 584 REMARK 465 ASP A 585 REMARK 465 LEU A 586 REMARK 465 SER A 587 REMARK 465 TYR A 588 REMARK 465 MET A 589 REMARK 465 PRO A 590 REMARK 465 ILE A 591 REMARK 465 TRP A 592 REMARK 465 LYS A 593 REMARK 465 PHE A 594 REMARK 465 PRO A 595 REMARK 465 ASP A 596 REMARK 465 GLU A 597 REMARK 465 GLU A 598 REMARK 465 GLY A 599 REMARK 465 ALA A 600 REMARK 465 CYS A 601 REMARK 465 GLN A 602 REMARK 465 PRO A 603 REMARK 465 CYS A 604 REMARK 465 PRO A 605 REMARK 465 ILE A 606 REMARK 465 ASN A 607 REMARK 465 CYS A 608 REMARK 465 THR A 609 REMARK 465 HIS A 610 REMARK 465 SER A 611 REMARK 465 CYS A 612 REMARK 465 VAL A 613 REMARK 465 ASP A 614 REMARK 465 LEU A 615 REMARK 465 ASP A 616 REMARK 465 ASP A 617 REMARK 465 LYS A 618 REMARK 465 GLY A 619 REMARK 465 CYS A 620 REMARK 465 PRO A 621 REMARK 465 ALA A 622 REMARK 465 GLU A 623 REMARK 465 GLN A 624 REMARK 465 ASN B 102 REMARK 465 ASN B 103 REMARK 465 THR B 104 REMARK 465 THR B 105 REMARK 465 PRO B 106 REMARK 465 VAL B 107 REMARK 465 THR B 108 REMARK 465 GLY B 109 REMARK 465 ALA B 110 REMARK 465 CYS B 578 REMARK 465 PRO B 579 REMARK 465 SER B 580 REMARK 465 GLY B 581 REMARK 465 VAL B 582 REMARK 465 LYS B 583 REMARK 465 PRO B 584 REMARK 465 ASP B 585 REMARK 465 LEU B 586 REMARK 465 SER B 587 REMARK 465 TYR B 588 REMARK 465 MET B 589 REMARK 465 PRO B 590 REMARK 465 ILE B 591 REMARK 465 TRP B 592 REMARK 465 LYS B 593 REMARK 465 PHE B 594 REMARK 465 PRO B 595 REMARK 465 ASP B 596 REMARK 465 GLU B 597 REMARK 465 GLU B 598 REMARK 465 GLY B 599 REMARK 465 ALA B 600 REMARK 465 CYS B 601 REMARK 465 GLN B 602 REMARK 465 PRO B 603 REMARK 465 CYS B 604 REMARK 465 PRO B 605 REMARK 465 ILE B 606 REMARK 465 ASN B 607 REMARK 465 CYS B 608 REMARK 465 THR B 609 REMARK 465 HIS B 610 REMARK 465 SER B 611 REMARK 465 CYS B 612 REMARK 465 VAL B 613 REMARK 465 ASP B 614 REMARK 465 LEU B 615 REMARK 465 ASP B 616 REMARK 465 ASP B 617 REMARK 465 LYS B 618 REMARK 465 GLY B 619 REMARK 465 CYS B 620 REMARK 465 PRO B 621 REMARK 465 ALA B 622 REMARK 465 GLU B 623 REMARK 465 GLN B 624 REMARK 465 ASP D 217 REMARK 465 LYS D 218 REMARK 465 THR D 219 REMARK 465 HIS D 220 REMARK 465 ASP F 217 REMARK 465 LYS F 218 REMARK 465 THR F 219 REMARK 465 HIS F 220 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 OD1 ASN F 95 O SER F 99 2.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 212 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 ARG A 318 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES REMARK 500 ARG A 318 NE - CZ - NH2 ANGL. DEV. = 4.7 DEGREES REMARK 500 ASP B 96 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 ASP B 212 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES REMARK 500 ARG B 318 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG B 318 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 ASP D 35 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES REMARK 500 ASP D 50 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES REMARK 500 GLY D 97 N - CA - C ANGL. DEV. = -19.6 DEGREES REMARK 500 ASP E 185 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 ASP F 31 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 GLY F 97 N - CA - C ANGL. DEV. = -20.6 DEGREES 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 LYS A 10 -138.72 53.42 REMARK 500 ALA A 47 118.54 -28.38 REMARK 500 GLN A 53 5.72 -68.14 REMARK 500 LEU A 74 39.22 -92.66 REMARK 500 ASP A 88 15.55 58.30 REMARK 500 ASN A 89 -30.11 -138.60 REMARK 500 ASP A 96 51.38 36.14 REMARK 500 PRO A 100 61.02 -67.87 REMARK 500 LEU A 120 57.05 -98.17 REMARK 500 LEU A 123 96.18 -62.91 REMARK 500 SER A 180 -9.56 -59.79 REMARK 500 THR A 194 -14.63 -143.38 REMARK 500 ALA A 219 -37.18 -132.79 REMARK 500 HIS A 235 -77.07 -114.66 REMARK 500 THR A 254 -15.79 85.75 REMARK 500 PRO A 278 170.12 -59.74 REMARK 500 GLU A 303 3.18 -66.01 REMARK 500 ASP A 304 -78.10 -95.87 REMARK 500 SER A 313 -78.57 -59.92 REMARK 500 LYS A 314 169.68 -49.83 REMARK 500 GLU A 326 -128.77 44.88 REMARK 500 PRO A 363 -83.04 -55.90 REMARK 500 ALA A 364 -78.38 9.01 REMARK 500 ASN A 366 80.46 -13.64 REMARK 500 LEU A 400 33.39 -95.72 REMARK 500 GLN A 404 -48.85 -3.41 REMARK 500 ASN A 416 15.85 54.54 REMARK 500 ASP A 461 -39.03 -30.19 REMARK 500 ARG A 495 13.22 55.02 REMARK 500 GLN A 511 -98.29 -103.18 REMARK 500 ARG A 523 67.60 -106.26 REMARK 500 GLN A 526 59.72 -143.37 REMARK 500 LEU A 528 -73.36 -75.82 REMARK 500 PRO A 543 -14.93 -49.39 REMARK 500 GLU A 544 41.81 -108.91 REMARK 500 LYS B 10 -138.09 53.88 REMARK 500 ALA B 47 116.66 -31.82 REMARK 500 GLN B 53 6.56 -64.15 REMARK 500 LEU B 74 41.52 -91.78 REMARK 500 ASP B 88 14.27 58.39 REMARK 500 ASN B 89 -31.56 -138.25 REMARK 500 ASP B 96 51.91 37.82 REMARK 500 PRO B 100 60.12 -68.69 REMARK 500 LEU B 120 58.20 -98.38 REMARK 500 LEU B 123 93.92 -64.28 REMARK 500 SER B 180 -8.62 -59.78 REMARK 500 THR B 194 -13.13 -145.40 REMARK 500 CYS B 202 127.24 -39.41 REMARK 500 ALA B 219 -33.94 -134.89 REMARK 500 HIS B 235 -77.98 -115.57 REMARK 500 REMARK 500 THIS ENTRY HAS 117 RAMACHANDRAN OUTLIERS. 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 A 1001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1004 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1006 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1004 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 1005 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1006 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1007 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1008 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1N8Y RELATED DB: PDB REMARK 900 ERBB2 FROM RAT, UNCOMPLEXED REMARK 900 RELATED ID: 1N8Z RELATED DB: PDB REMARK 900 ERBB2 FROM HUMAN, COMPLEXED WITH HERCEPTIN (TRASTUZUMAB) FAB REMARK 900 RELATED ID: 1L7I RELATED DB: PDB REMARK 900 PERTUZUMAB (2C4) FAB, UNCOMPLEXED REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCES OF THE CHAINS C,E AND D,F REMARK 999 WERE NOT DEPOSITED INTO ANY SEQUENCE DATABASE. REMARK 999 RESIDUES C110-C214 AND D113-D216 LIE IN A REGION REMARK 999 OF VERY POOR ELECTRON DENSITY AND HAVE NOT REMARK 999 BEEN WELL REFINED.