HEADER IMMUNE SYSTEM 13-NOV-17 6EYO
TITLE STRUCTURE OF EXTENDED IGE-FC IN COMPLEX WITH TWO ANTI-IGE FABS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMMUNOGLOBULIN HEAVY CONSTANT EPSILON;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: IG EPSILON CHAIN C REGION,IG EPSILON CHAIN C REGION ND;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: FC REGION OF IMMUNOGLOBULIN E;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 8D6 FAB HEAVY CHAIN;
COMPND 9 CHAIN: I, H;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: 8D6 FAB HEAVY CHAIN;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: 8D6 FAB LIGHT CHAIN;
COMPND 14 CHAIN: M, L;
COMPND 15 ENGINEERED: YES;
COMPND 16 OTHER_DETAILS: 8D6 FAB LIGHT CHAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: IGHE;
SOURCE 6 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: MOUSE MYELOMA NS0;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS IMMUNOGLOBULIN E, FAB, ANTIBODY, COMPLEX, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.CHEN,F.RAMADANI,M.O.Y.PANG,R.L.BEAVIL,M.D.HOLDOM,A.N.MITROPOULOU,
AUTHOR 2 A.J.BEAVIL,H.J.GOULD,T.W.CHANG,B.J.SUTTON,J.M.MCDONNELL,A.M.DAVIES
REVDAT 3 17-JAN-24 6EYO 1 HETSYN LINK
REVDAT 2 29-JUL-20 6EYO 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE ATOM
REVDAT 1 15-AUG-18 6EYO 0
JRNL AUTH J.B.CHEN,F.RAMADANI,M.O.Y.PANG,R.L.BEAVIL,M.D.HOLDOM,
JRNL AUTH 2 A.N.MITROPOULOU,A.J.BEAVIL,H.J.GOULD,T.W.CHANG,B.J.SUTTON,
JRNL AUTH 3 J.M.MCDONNELL,A.M.DAVIES
JRNL TITL STRUCTURAL BASIS FOR SELECTIVE INHIBITION OF IMMUNOGLOBULIN
JRNL TITL 2 E-RECEPTOR INTERACTIONS BY AN ANTI-IGE ANTIBODY.
JRNL REF SCI REP V. 8 11548 2018
JRNL REFN ESSN 2045-2322
JRNL PMID 30069035
JRNL DOI 10.1038/S41598-018-29664-4
REMARK 2
REMARK 2 RESOLUTION. 3.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 88.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.250
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 20683
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.250
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.440
REMARK 3 FREE R VALUE TEST SET COUNT : 1125
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 88.9555 - 7.3989 1.00 2605 156 0.2312 0.2764
REMARK 3 2 7.3989 - 5.8731 1.00 2522 143 0.2590 0.3103
REMARK 3 3 5.8731 - 5.1308 1.00 2455 142 0.2335 0.2569
REMARK 3 4 5.1308 - 4.6617 1.00 2447 152 0.2268 0.2491
REMARK 3 5 4.6617 - 4.3276 1.00 2432 140 0.2245 0.2764
REMARK 3 6 4.3276 - 4.0724 1.00 2464 133 0.2605 0.3329
REMARK 3 7 4.0724 - 3.8685 1.00 2413 151 0.2858 0.3349
REMARK 3 8 3.8685 - 3.7001 0.91 2220 108 0.3230 0.3442
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.490
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 10674
REMARK 3 ANGLE : 0.510 14687
REMARK 3 CHIRALITY : 0.040 1748
REMARK 3 PLANARITY : 0.005 1866
REMARK 3 DIHEDRAL : 11.541 6261
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 39
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 231 THROUGH 326 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4946 -60.3328 19.3387
REMARK 3 T TENSOR
REMARK 3 T11: 0.2062 T22: 0.0601
REMARK 3 T33: 0.0698 T12: 0.2824
REMARK 3 T13: 0.0547 T23: 0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 0.0723 L22: 0.0462
REMARK 3 L33: -0.0038 L12: -0.0114
REMARK 3 L13: -0.0005 L23: 0.0047
REMARK 3 S TENSOR
REMARK 3 S11: 0.0129 S12: 0.0206 S13: 0.0930
REMARK 3 S21: -0.0307 S22: -0.0062 S23: -0.0049
REMARK 3 S31: -0.0542 S32: -0.0313 S33: -0.0325
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 327 THROUGH 396 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9842 -84.9116 22.2831
REMARK 3 T TENSOR
REMARK 3 T11: 0.2227 T22: 0.3435
REMARK 3 T33: 0.3655 T12: 0.0227
REMARK 3 T13: 0.0623 T23: 0.1380
REMARK 3 L TENSOR
REMARK 3 L11: 0.0463 L22: 0.0559
REMARK 3 L33: 0.0989 L12: 0.0547
REMARK 3 L13: 0.0726 L23: 0.0767
REMARK 3 S TENSOR
REMARK 3 S11: 0.1116 S12: 0.0822 S13: -0.1737
REMARK 3 S21: 0.0160 S22: -0.0108 S23: -0.0680
REMARK 3 S31: -0.1352 S32: -0.0464 S33: 0.0198
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 397 THROUGH 458 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.1810 -91.9895 17.1848
REMARK 3 T TENSOR
REMARK 3 T11: 0.5770 T22: 0.6883
REMARK 3 T33: 0.7010 T12: 0.1513
REMARK 3 T13: -0.0250 T23: 0.1829
REMARK 3 L TENSOR
REMARK 3 L11: 0.0793 L22: 0.0273
REMARK 3 L33: 0.0470 L12: 0.0195
REMARK 3 L13: -0.0421 L23: 0.0166
REMARK 3 S TENSOR
REMARK 3 S11: -0.0292 S12: -0.0856 S13: -0.1008
REMARK 3 S21: -0.4469 S22: -0.0245 S23: 0.2688
REMARK 3 S31: 0.1592 S32: -0.1648 S33: -0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 459 THROUGH 544 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0893-109.0809 20.3943
REMARK 3 T TENSOR
REMARK 3 T11: 0.4341 T22: 0.5898
REMARK 3 T33: 0.4644 T12: 0.0126
REMARK 3 T13: 0.0381 T23: 0.0614
REMARK 3 L TENSOR
REMARK 3 L11: 0.0210 L22: 0.0327
REMARK 3 L33: 0.0260 L12: -0.0202
REMARK 3 L13: -0.0275 L23: 0.0287
REMARK 3 S TENSOR
REMARK 3 S11: -0.0541 S12: -0.2957 S13: -0.0892
REMARK 3 S21: -0.1863 S22: -0.0150 S23: -0.0027
REMARK 3 S31: -0.0087 S32: -0.2038 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 231 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2380 -76.2009 16.2891
REMARK 3 T TENSOR
REMARK 3 T11: -0.0112 T22: 0.2735
REMARK 3 T33: 0.0670 T12: 0.2992
REMARK 3 T13: 0.1189 T23: -0.2293
REMARK 3 L TENSOR
REMARK 3 L11: 0.2847 L22: 0.1039
REMARK 3 L33: 0.1172 L12: -0.1277
REMARK 3 L13: -0.1226 L23: 0.1136
REMARK 3 S TENSOR
REMARK 3 S11: 0.0728 S12: 0.0012 S13: 0.0921
REMARK 3 S21: -0.0218 S22: 0.0843 S23: -0.0740
REMARK 3 S31: -0.0543 S32: 0.1399 S33: 0.4189
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 338 THROUGH 544 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2054-114.9802 9.7936
REMARK 3 T TENSOR
REMARK 3 T11: 0.4007 T22: 0.3269
REMARK 3 T33: 0.6167 T12: 0.1428
REMARK 3 T13: -0.1644 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.1023 L22: 0.0604
REMARK 3 L33: 0.1174 L12: -0.0181
REMARK 3 L13: 0.0345 L23: -0.0742
REMARK 3 S TENSOR
REMARK 3 S11: -0.1091 S12: -0.0896 S13: -0.2279
REMARK 3 S21: 0.2206 S22: 0.2394 S23: -0.0429
REMARK 3 S31: 0.1148 S32: -0.0769 S33: 0.3225
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 2 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7898 -82.4511 -13.0605
REMARK 3 T TENSOR
REMARK 3 T11: 0.2154 T22: 0.5471
REMARK 3 T33: 0.2492 T12: -0.2155
REMARK 3 T13: 0.0521 T23: -0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 0.0022 L22: 0.0005
REMARK 3 L33: 0.0008 L12: 0.0012
REMARK 3 L13: -0.0001 L23: -0.0012
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: -0.0850 S13: 0.0363
REMARK 3 S21: 0.0102 S22: -0.0518 S23: -0.1177
REMARK 3 S31: -0.0320 S32: 0.1267 S33: -0.0862
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 41 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2347 -91.0356 -11.4042
REMARK 3 T TENSOR
REMARK 3 T11: 0.1486 T22: 0.4374
REMARK 3 T33: 0.3077 T12: 0.1528
REMARK 3 T13: -0.0867 T23: -0.2868
REMARK 3 L TENSOR
REMARK 3 L11: 0.0100 L22: 0.0051
REMARK 3 L33: 0.0057 L12: 0.0088
REMARK 3 L13: 0.0067 L23: 0.0053
REMARK 3 S TENSOR
REMARK 3 S11: -0.0018 S12: 0.0206 S13: -0.0143
REMARK 3 S21: -0.0171 S22: 0.0133 S23: -0.0036
REMARK 3 S31: 0.0120 S32: 0.0324 S33: -0.0645
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 61 THROUGH 151 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4018 -78.3586 -19.4836
REMARK 3 T TENSOR
REMARK 3 T11: 0.1414 T22: 0.4425
REMARK 3 T33: 0.2238 T12: -0.0655
REMARK 3 T13: 0.0859 T23: -0.0741
REMARK 3 L TENSOR
REMARK 3 L11: 0.2255 L22: 0.4609
REMARK 3 L33: 0.3174 L12: 0.0637
REMARK 3 L13: -0.2017 L23: -0.1636
REMARK 3 S TENSOR
REMARK 3 S11: -0.1182 S12: -0.0069 S13: -0.1467
REMARK 3 S21: 0.0692 S22: -0.1239 S23: -0.0671
REMARK 3 S31: 0.0322 S32: 0.0580 S33: -0.4093
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 152 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5446 -59.8278 -27.2393
REMARK 3 T TENSOR
REMARK 3 T11: 1.2841 T22: 0.5435
REMARK 3 T33: 0.9633 T12: -0.1432
REMARK 3 T13: 0.0154 T23: -0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 0.0143 L22: 0.0143
REMARK 3 L33: 0.0134 L12: 0.0065
REMARK 3 L13: 0.0029 L23: -0.0116
REMARK 3 S TENSOR
REMARK 3 S11: -0.2192 S12: -0.0584 S13: 0.1711
REMARK 3 S21: -0.0476 S22: -0.0897 S23: -0.1098
REMARK 3 S31: -0.1259 S32: 0.1283 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 2 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1496 -83.1296 56.1100
REMARK 3 T TENSOR
REMARK 3 T11: 0.5499 T22: 0.3759
REMARK 3 T33: 0.3977 T12: -0.2566
REMARK 3 T13: -0.0204 T23: -0.1668
REMARK 3 L TENSOR
REMARK 3 L11: 0.0008 L22: 0.0199
REMARK 3 L33: 0.0044 L12: 0.0030
REMARK 3 L13: 0.0018 L23: 0.0090
REMARK 3 S TENSOR
REMARK 3 S11: -0.0335 S12: 0.0252 S13: 0.0209
REMARK 3 S21: -0.0541 S22: 0.0288 S23: -0.0018
REMARK 3 S31: -0.0480 S32: 0.0296 S33: -0.0091
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 17 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9893 -83.5334 42.6327
REMARK 3 T TENSOR
REMARK 3 T11: 0.3489 T22: 0.3349
REMARK 3 T33: 0.0918 T12: -0.0466
REMARK 3 T13: -0.0219 T23: -0.0560
REMARK 3 L TENSOR
REMARK 3 L11: 0.0904 L22: 0.0092
REMARK 3 L33: 0.0195 L12: 0.0173
REMARK 3 L13: 0.0393 L23: 0.0031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0716 S12: -0.0549 S13: 0.0237
REMARK 3 S21: 0.0476 S22: 0.1092 S23: -0.0344
REMARK 3 S31: -0.0118 S32: -0.0469 S33: 0.0277
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 40 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3965 -95.3234 48.9959
REMARK 3 T TENSOR
REMARK 3 T11: 0.0379 T22: 0.0936
REMARK 3 T33: 0.2341 T12: -0.0287
REMARK 3 T13: 0.0415 T23: 0.0797
REMARK 3 L TENSOR
REMARK 3 L11: 0.0077 L22: 0.0030
REMARK 3 L33: 0.0225 L12: 0.0027
REMARK 3 L13: 0.0101 L23: 0.0007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0263 S12: -0.0045 S13: 0.0205
REMARK 3 S21: 0.0010 S22: 0.0306 S23: 0.0038
REMARK 3 S31: -0.0213 S32: -0.0451 S33: 0.1150
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 52 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0959 -83.9326 43.7668
REMARK 3 T TENSOR
REMARK 3 T11: 0.2627 T22: 0.1867
REMARK 3 T33: 0.3778 T12: 0.0123
REMARK 3 T13: -0.0352 T23: -0.1639
REMARK 3 L TENSOR
REMARK 3 L11: 0.2019 L22: 0.1546
REMARK 3 L33: 0.2339 L12: 0.0580
REMARK 3 L13: 0.1885 L23: -0.0360
REMARK 3 S TENSOR
REMARK 3 S11: 0.1522 S12: -0.0281 S13: -0.0431
REMARK 3 S21: 0.0684 S22: -0.0433 S23: 0.0631
REMARK 3 S31: -0.0008 S32: -0.0201 S33: 0.0824
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 78 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.4730 -86.0625 56.0724
REMARK 3 T TENSOR
REMARK 3 T11: 0.5885 T22: 0.6545
REMARK 3 T33: 0.4936 T12: 0.0462
REMARK 3 T13: -0.0162 T23: 0.1248
REMARK 3 L TENSOR
REMARK 3 L11: -0.0010 L22: 0.0015
REMARK 3 L33: 0.0021 L12: -0.0007
REMARK 3 L13: 0.0000 L23: -0.0033
REMARK 3 S TENSOR
REMARK 3 S11: 0.0164 S12: -0.0210 S13: 0.0614
REMARK 3 S21: -0.0482 S22: -0.0035 S23: -0.0310
REMARK 3 S31: -0.0243 S32: -0.0048 S33: 0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 93 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6963 -90.2162 38.9764
REMARK 3 T TENSOR
REMARK 3 T11: 0.4070 T22: 0.3588
REMARK 3 T33: 0.3976 T12: 0.0185
REMARK 3 T13: 0.0104 T23: 0.1290
REMARK 3 L TENSOR
REMARK 3 L11: 0.0061 L22: 0.0090
REMARK 3 L33: 0.0076 L12: 0.0058
REMARK 3 L13: 0.0022 L23: -0.0036
REMARK 3 S TENSOR
REMARK 3 S11: 0.0226 S12: -0.0079 S13: 0.1815
REMARK 3 S21: 0.0843 S22: -0.0404 S23: -0.0980
REMARK 3 S31: 0.0005 S32: 0.0876 S33: 0.0001
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 110 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2300 -85.7539 64.2743
REMARK 3 T TENSOR
REMARK 3 T11: 0.8607 T22: 0.6114
REMARK 3 T33: 0.6140 T12: -0.1157
REMARK 3 T13: 0.0520 T23: 0.0712
REMARK 3 L TENSOR
REMARK 3 L11: 0.0006 L22: 0.0029
REMARK 3 L33: 0.0021 L12: 0.0022
REMARK 3 L13: -0.0023 L23: -0.0010
REMARK 3 S TENSOR
REMARK 3 S11: -0.0307 S12: -0.0561 S13: 0.0354
REMARK 3 S21: 0.0220 S22: 0.0143 S23: -0.0300
REMARK 3 S31: 0.0013 S32: -0.0532 S33: 0.0000
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 126 THROUGH 151 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9227 -90.2826 72.1335
REMARK 3 T TENSOR
REMARK 3 T11: 0.8349 T22: 0.6814
REMARK 3 T33: 1.1018 T12: -0.2069
REMARK 3 T13: -0.2071 T23: -0.2436
REMARK 3 L TENSOR
REMARK 3 L11: 0.0032 L22: 0.0031
REMARK 3 L33: 0.0078 L12: 0.0004
REMARK 3 L13: 0.0010 L23: 0.0057
REMARK 3 S TENSOR
REMARK 3 S11: -0.0655 S12: -0.0264 S13: 0.0688
REMARK 3 S21: 0.0492 S22: -0.1594 S23: 0.0447
REMARK 3 S31: -0.0454 S32: -0.0203 S33: -0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 152 THROUGH 171 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7333 -88.2382 62.3398
REMARK 3 T TENSOR
REMARK 3 T11: 1.0444 T22: 0.7455
REMARK 3 T33: 0.7868 T12: 0.1016
REMARK 3 T13: -0.2226 T23: 0.1943
REMARK 3 L TENSOR
REMARK 3 L11: 0.0020 L22: -0.0015
REMARK 3 L33: -0.0008 L12: -0.0008
REMARK 3 L13: 0.0005 L23: 0.0001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0089 S12: 0.0091 S13: -0.0082
REMARK 3 S21: 0.0600 S22: 0.0270 S23: -0.0643
REMARK 3 S31: -0.0445 S32: 0.0019 S33: -0.0000
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 172 THROUGH 210 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7028 -89.6669 68.1212
REMARK 3 T TENSOR
REMARK 3 T11: 1.0836 T22: 0.6194
REMARK 3 T33: 0.8968 T12: -0.3045
REMARK 3 T13: -0.0885 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.0100 L22: 0.0035
REMARK 3 L33: 0.0010 L12: -0.0083
REMARK 3 L13: -0.0009 L23: -0.0050
REMARK 3 S TENSOR
REMARK 3 S11: -0.0610 S12: -0.0688 S13: 0.0774
REMARK 3 S21: 0.0793 S22: -0.0556 S23: 0.1483
REMARK 3 S31: -0.0277 S32: -0.0926 S33: -0.0000
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 211 THROUGH 220 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2723 -82.1408 71.2929
REMARK 3 T TENSOR
REMARK 3 T11: 1.1135 T22: 1.0295
REMARK 3 T33: 1.0205 T12: 0.1715
REMARK 3 T13: -0.1144 T23: 0.0492
REMARK 3 L TENSOR
REMARK 3 L11: 0.0021 L22: 0.0005
REMARK 3 L33: -0.0004 L12: -0.0020
REMARK 3 L13: 0.0007 L23: -0.0004
REMARK 3 S TENSOR
REMARK 3 S11: 0.0456 S12: 0.0204 S13: 0.0019
REMARK 3 S21: 0.0085 S22: 0.0260 S23: -0.0319
REMARK 3 S31: -0.0253 S32: -0.0224 S33: -0.0000
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'M' AND (RESID 1 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.0310 -81.5203 -9.7163
REMARK 3 T TENSOR
REMARK 3 T11: 0.1542 T22: 0.2539
REMARK 3 T33: 0.3363 T12: 0.1243
REMARK 3 T13: -0.1677 T23: -0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 0.0328 L22: 0.0028
REMARK 3 L33: 0.0277 L12: 0.0110
REMARK 3 L13: 0.0251 L23: 0.0065
REMARK 3 S TENSOR
REMARK 3 S11: 0.0314 S12: 0.0706 S13: -0.0610
REMARK 3 S21: -0.0224 S22: 0.0464 S23: 0.0134
REMARK 3 S31: 0.0482 S32: -0.0570 S33: 0.0296
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'M' AND (RESID 26 THROUGH 79 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0422 -82.1561 -1.7002
REMARK 3 T TENSOR
REMARK 3 T11: 0.1437 T22: 0.4133
REMARK 3 T33: 0.2841 T12: 0.0175
REMARK 3 T13: 0.1032 T23: -0.1387
REMARK 3 L TENSOR
REMARK 3 L11: 0.5122 L22: 0.0596
REMARK 3 L33: 0.2071 L12: -0.1750
REMARK 3 L13: 0.3195 L23: -0.1106
REMARK 3 S TENSOR
REMARK 3 S11: -0.1115 S12: -0.0567 S13: 0.1024
REMARK 3 S21: 0.0534 S22: -0.0780 S23: 0.0543
REMARK 3 S31: 0.0761 S32: -0.1463 S33: -0.3265
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'M' AND (RESID 80 THROUGH 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.6544 -81.3878 -7.8904
REMARK 3 T TENSOR
REMARK 3 T11: 0.3041 T22: 0.2936
REMARK 3 T33: 0.5231 T12: -0.1356
REMARK 3 T13: -0.2532 T23: 0.0664
REMARK 3 L TENSOR
REMARK 3 L11: 0.0530 L22: 0.0098
REMARK 3 L33: 0.0348 L12: 0.0026
REMARK 3 L13: 0.0246 L23: 0.0063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0263 S12: -0.0295 S13: 0.0423
REMARK 3 S21: -0.0096 S22: -0.0453 S23: 0.0218
REMARK 3 S31: -0.0372 S32: -0.0531 S33: -0.1248
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'M' AND (RESID 107 THROUGH 117 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.6374 -63.2807 -17.2843
REMARK 3 T TENSOR
REMARK 3 T11: 0.9910 T22: 0.5166
REMARK 3 T33: 0.6517 T12: -0.1039
REMARK 3 T13: -0.2206 T23: -0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 0.0030 L22: 0.0023
REMARK 3 L33: 0.0069 L12: 0.0033
REMARK 3 L13: 0.0061 L23: 0.0041
REMARK 3 S TENSOR
REMARK 3 S11: 0.0443 S12: 0.0214 S13: -0.0146
REMARK 3 S21: 0.0142 S22: 0.0774 S23: 0.0073
REMARK 3 S31: 0.0368 S32: 0.0003 S33: 0.0000
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'M' AND (RESID 118 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.8912 -53.0745 -38.2326
REMARK 3 T TENSOR
REMARK 3 T11: 1.2420 T22: 0.8754
REMARK 3 T33: 0.8217 T12: -0.0963
REMARK 3 T13: -0.0568 T23: 0.1879
REMARK 3 L TENSOR
REMARK 3 L11: 0.0067 L22: 0.0054
REMARK 3 L33: 0.0061 L12: -0.0055
REMARK 3 L13: 0.0014 L23: -0.0047
REMARK 3 S TENSOR
REMARK 3 S11: -0.0143 S12: -0.0178 S13: 0.0237
REMARK 3 S21: -0.0008 S22: -0.0285 S23: -0.0366
REMARK 3 S31: -0.0024 S32: 0.0238 S33: -0.0000
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'M' AND (RESID 136 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5758 -60.9001 -33.6352
REMARK 3 T TENSOR
REMARK 3 T11: 1.1019 T22: 0.8660
REMARK 3 T33: 0.7571 T12: 0.1833
REMARK 3 T13: -0.5907 T23: -0.1636
REMARK 3 L TENSOR
REMARK 3 L11: 0.0129 L22: 0.0033
REMARK 3 L33: 0.0143 L12: -0.0094
REMARK 3 L13: 0.0142 L23: -0.0080
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: -0.0092 S13: -0.0557
REMARK 3 S21: -0.0469 S22: 0.0217 S23: 0.0181
REMARK 3 S31: -0.0553 S32: -0.0170 S33: -0.0280
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'M' AND (RESID 168 THROUGH 178 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1809 -63.1271 -17.7368
REMARK 3 T TENSOR
REMARK 3 T11: 0.8245 T22: 0.4854
REMARK 3 T33: 0.5534 T12: -0.0038
REMARK 3 T13: -0.1549 T23: 0.2082
REMARK 3 L TENSOR
REMARK 3 L11: 0.0009 L22: 0.0022
REMARK 3 L33: 0.0035 L12: 0.0008
REMARK 3 L13: 0.0008 L23: -0.0020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0003 S12: -0.0159 S13: 0.0109
REMARK 3 S21: -0.0088 S22: 0.0103 S23: -0.0045
REMARK 3 S31: 0.0318 S32: -0.0107 S33: -0.0000
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'M' AND (RESID 179 THROUGH 195 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1530 -58.7685 -41.1597
REMARK 3 T TENSOR
REMARK 3 T11: 1.0159 T22: 0.9081
REMARK 3 T33: 0.8775 T12: -0.2080
REMARK 3 T13: -0.1026 T23: 0.1996
REMARK 3 L TENSOR
REMARK 3 L11: 0.0072 L22: 0.0036
REMARK 3 L33: 0.0061 L12: 0.0025
REMARK 3 L13: -0.0037 L23: 0.0034
REMARK 3 S TENSOR
REMARK 3 S11: 0.0597 S12: 0.1293 S13: 0.0130
REMARK 3 S21: -0.0386 S22: 0.0536 S23: 0.0077
REMARK 3 S31: -0.0477 S32: -0.0448 S33: -0.0001
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'M' AND (RESID 196 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.1798 -52.8331 -35.8112
REMARK 3 T TENSOR
REMARK 3 T11: 0.9480 T22: 0.8187
REMARK 3 T33: 0.8206 T12: 0.1997
REMARK 3 T13: -0.1253 T23: 0.1596
REMARK 3 L TENSOR
REMARK 3 L11: 0.0103 L22: 0.0098
REMARK 3 L33: 0.0094 L12: -0.0104
REMARK 3 L13: 0.0100 L23: -0.0100
REMARK 3 S TENSOR
REMARK 3 S11: -0.0440 S12: -0.0611 S13: 0.0378
REMARK 3 S21: -0.0261 S22: -0.0491 S23: -0.0413
REMARK 3 S31: -0.0676 S32: -0.0502 S33: -0.0362
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1941-111.8673 44.1519
REMARK 3 T TENSOR
REMARK 3 T11: 0.3862 T22: 0.4583
REMARK 3 T33: 0.7076 T12: -0.0323
REMARK 3 T13: -0.0706 T23: 0.0969
REMARK 3 L TENSOR
REMARK 3 L11: 0.0032 L22: 0.0081
REMARK 3 L33: -0.0005 L12: -0.0062
REMARK 3 L13: 0.0006 L23: 0.0010
REMARK 3 S TENSOR
REMARK 3 S11: -0.0963 S12: -0.0142 S13: -0.0447
REMARK 3 S21: -0.0332 S22: -0.1129 S23: -0.0379
REMARK 3 S31: 0.1566 S32: -0.0747 S33: 0.0000
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 26 THROUGH 52 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1566-101.3896 38.3451
REMARK 3 T TENSOR
REMARK 3 T11: 0.2971 T22: 0.3644
REMARK 3 T33: 0.3923 T12: -0.0142
REMARK 3 T13: 0.0140 T23: 0.2506
REMARK 3 L TENSOR
REMARK 3 L11: 0.0279 L22: 0.0886
REMARK 3 L33: 0.0795 L12: -0.0266
REMARK 3 L13: 0.0052 L23: 0.0641
REMARK 3 S TENSOR
REMARK 3 S11: 0.0750 S12: -0.0344 S13: -0.0182
REMARK 3 S21: -0.0637 S22: -0.0761 S23: 0.0042
REMARK 3 S31: 0.0926 S32: -0.0099 S33: -0.0731
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 53 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3199-101.2383 33.2715
REMARK 3 T TENSOR
REMARK 3 T11: 0.9460 T22: 0.8617
REMARK 3 T33: 0.8130 T12: 0.0453
REMARK 3 T13: 0.2338 T23: 0.3126
REMARK 3 L TENSOR
REMARK 3 L11: 0.0017 L22: 0.0010
REMARK 3 L33: 0.0026 L12: -0.0002
REMARK 3 L13: -0.0025 L23: 0.0006
REMARK 3 S TENSOR
REMARK 3 S11: -0.0681 S12: 0.0296 S13: -0.0609
REMARK 3 S21: 0.0036 S22: -0.0059 S23: -0.0216
REMARK 3 S31: 0.0643 S32: -0.0084 S33: 0.0000
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 66 THROUGH 79 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2227-110.3139 35.5899
REMARK 3 T TENSOR
REMARK 3 T11: 0.6754 T22: 0.4822
REMARK 3 T33: 0.8523 T12: 0.0889
REMARK 3 T13: -0.0414 T23: 0.0359
REMARK 3 L TENSOR
REMARK 3 L11: 0.0048 L22: 0.0071
REMARK 3 L33: 0.0018 L12: -0.0051
REMARK 3 L13: 0.0028 L23: -0.0049
REMARK 3 S TENSOR
REMARK 3 S11: 0.0661 S12: 0.0344 S13: -0.0223
REMARK 3 S21: -0.0228 S22: 0.0627 S23: -0.0298
REMARK 3 S31: 0.0386 S32: 0.0779 S33: -0.0000
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 80 THROUGH 117 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7016-105.1592 45.8727
REMARK 3 T TENSOR
REMARK 3 T11: 0.2250 T22: 0.4142
REMARK 3 T33: 0.6197 T12: -0.0204
REMARK 3 T13: -0.0955 T23: 0.2147
REMARK 3 L TENSOR
REMARK 3 L11: 0.0342 L22: 0.2059
REMARK 3 L33: 0.3271 L12: -0.0832
REMARK 3 L13: -0.1051 L23: 0.2587
REMARK 3 S TENSOR
REMARK 3 S11: -0.0702 S12: -0.0115 S13: -0.0224
REMARK 3 S21: 0.1569 S22: -0.2615 S23: -0.0685
REMARK 3 S31: -0.0403 S32: 0.0641 S33: -0.1354
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 118 THROUGH 141 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9111 -95.9593 77.1556
REMARK 3 T TENSOR
REMARK 3 T11: 1.1443 T22: 0.6540
REMARK 3 T33: 0.6700 T12: -0.0362
REMARK 3 T13: -0.4561 T23: 0.0538
REMARK 3 L TENSOR
REMARK 3 L11: -0.0006 L22: 0.0019
REMARK 3 L33: 0.0033 L12: 0.0001
REMARK 3 L13: -0.0005 L23: -0.0027
REMARK 3 S TENSOR
REMARK 3 S11: -0.0160 S12: -0.0092 S13: -0.0451
REMARK 3 S21: -0.0296 S22: -0.0150 S23: -0.0461
REMARK 3 S31: 0.0168 S32: -0.0106 S33: 0.0000
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 142 THROUGH 178 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2180-106.4760 68.1207
REMARK 3 T TENSOR
REMARK 3 T11: 0.7460 T22: 0.4889
REMARK 3 T33: 0.8250 T12: -0.0501
REMARK 3 T13: -0.1986 T23: 0.1665
REMARK 3 L TENSOR
REMARK 3 L11: 0.0610 L22: 0.0492
REMARK 3 L33: 0.1439 L12: -0.0133
REMARK 3 L13: 0.0459 L23: 0.0619
REMARK 3 S TENSOR
REMARK 3 S11: 0.0541 S12: 0.0142 S13: 0.1057
REMARK 3 S21: 0.0463 S22: 0.0033 S23: -0.0612
REMARK 3 S31: -0.0147 S32: -0.0372 S33: 0.0715
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 179 THROUGH 194 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9580 -99.6620 83.0409
REMARK 3 T TENSOR
REMARK 3 T11: 0.9781 T22: 0.6220
REMARK 3 T33: 0.6039 T12: -0.2332
REMARK 3 T13: -0.2604 T23: 0.0919
REMARK 3 L TENSOR
REMARK 3 L11: 0.0054 L22: 0.0119
REMARK 3 L33: 0.0042 L12: -0.0059
REMARK 3 L13: -0.0040 L23: 0.0011
REMARK 3 S TENSOR
REMARK 3 S11: -0.0330 S12: -0.0246 S13: 0.0448
REMARK 3 S21: 0.0122 S22: 0.0263 S23: 0.0455
REMARK 3 S31: 0.0115 S32: -0.0056 S33: 0.0259
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 195 THROUGH 218 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.9619-106.9737 77.7789
REMARK 3 T TENSOR
REMARK 3 T11: 0.8929 T22: 0.5178
REMARK 3 T33: 0.6836 T12: -0.0437
REMARK 3 T13: -0.4963 T23: 0.0772
REMARK 3 L TENSOR
REMARK 3 L11: 0.0206 L22: 0.0111
REMARK 3 L33: 0.0077 L12: -0.0113
REMARK 3 L13: 0.0123 L23: -0.0092
REMARK 3 S TENSOR
REMARK 3 S11: 0.0177 S12: -0.0194 S13: 0.0348
REMARK 3 S21: -0.0314 S22: -0.0512 S23: -0.0016
REMARK 3 S31: 0.0016 S32: 0.0784 S33: 0.0256
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6EYO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1200007105.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20732
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.700
REMARK 200 RESOLUTION RANGE LOW (A) : 88.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.22400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.69100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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: 2WQR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH8.0 AND 45% (V/V)
REMARK 280 PENTAERYTHRITOL PROPOXYLATE (5/4PO/OH), VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
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 59.74150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.49700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.80050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.49700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 59.74150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.80050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 66380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, H, M, L, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 222
REMARK 465 ILE A 223
REMARK 465 VAL A 224
REMARK 465 ALA A 225
REMARK 465 SER A 226
REMARK 465 ARG A 227
REMARK 465 ASP A 228
REMARK 465 PHE A 229
REMARK 465 THR A 230
REMARK 465 GLU A 287
REMARK 465 GLY A 288
REMARK 465 GLU A 289
REMARK 465 GLY A 318
REMARK 465 HIS A 319
REMARK 465 GLY A 500
REMARK 465 SER A 501
REMARK 465 GLY A 502
REMARK 465 PRO A 545
REMARK 465 GLY A 546
REMARK 465 LYS A 547
REMARK 465 ASP B 222
REMARK 465 ILE B 223
REMARK 465 VAL B 224
REMARK 465 ALA B 225
REMARK 465 SER B 226
REMARK 465 ARG B 227
REMARK 465 ASP B 228
REMARK 465 PHE B 229
REMARK 465 THR B 230
REMARK 465 SER B 257
REMARK 465 GLY B 258
REMARK 465 GLU B 287
REMARK 465 GLY B 288
REMARK 465 GLU B 289
REMARK 465 LEU B 290
REMARK 465 PRO B 545
REMARK 465 GLY B 546
REMARK 465 LYS B 547
REMARK 465 GLN I 1
REMARK 465 LYS I 135
REMARK 465 SER I 136
REMARK 465 THR I 137
REMARK 465 SER I 138
REMARK 465 GLY I 139
REMARK 465 GLY I 140
REMARK 465 LEU I 195
REMARK 465 GLY I 196
REMARK 465 GLU I 218
REMARK 465 PRO I 219
REMARK 465 LYS I 220
REMARK 465 SER I 221
REMARK 465 CYS I 222
REMARK 465 ASP I 223
REMARK 465 LYS I 224
REMARK 465 THR I 225
REMARK 465 HIS I 226
REMARK 465 THR I 227
REMARK 465 GLN H 1
REMARK 465 SER H 133
REMARK 465 SER H 134
REMARK 465 LYS H 135
REMARK 465 SER H 136
REMARK 465 THR H 137
REMARK 465 SER H 138
REMARK 465 GLY H 139
REMARK 465 SER H 192
REMARK 465 SER H 193
REMARK 465 SER H 194
REMARK 465 LEU H 195
REMARK 465 GLY H 196
REMARK 465 THR H 197
REMARK 465 GLN H 198
REMARK 465 THR H 199
REMARK 465 SER H 221
REMARK 465 CYS H 222
REMARK 465 ASP H 223
REMARK 465 LYS H 224
REMARK 465 THR H 225
REMARK 465 HIS H 226
REMARK 465 THR H 227
REMARK 465 LYS M 130
REMARK 465 SER M 131
REMARK 465 GLY M 132
REMARK 465 THR M 133
REMARK 465 ALA M 134
REMARK 465 GLN M 151
REMARK 465 TRP M 152
REMARK 465 LYS M 153
REMARK 465 VAL M 154
REMARK 465 ALA M 188
REMARK 465 ASP M 189
REMARK 465 TYR M 190
REMARK 465 GLU M 191
REMARK 465 LYS M 192
REMARK 465 HIS M 193
REMARK 465 GLU M 217
REMARK 465 CYS M 218
REMARK 465 SER L 125
REMARK 465 ASP L 126
REMARK 465 SER L 160
REMARK 465 GLY L 161
REMARK 465 LEU L 185
REMARK 465 SER L 186
REMARK 465 LYS L 187
REMARK 465 ALA L 188
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 LYS A 235 CD CE NZ
REMARK 470 SER A 240 OG
REMARK 470 SER A 257 OG
REMARK 470 GLU A 270 OE1 OE2
REMARK 470 GLN A 273 CD OE1 NE2
REMARK 470 ASP A 278 CG OD1 OD2
REMARK 470 GLN A 286 CG CD OE1 NE2
REMARK 470 LEU A 290 CG CD1 CD2
REMARK 470 SER A 292 OG
REMARK 470 GLN A 294 CG CD OE1 NE2
REMARK 470 LYS A 302 CG CD CE NZ
REMARK 470 ASP A 307 OD1 OD2
REMARK 470 ARG A 308 CZ NH1 NH2
REMARK 470 GLN A 317 CD OE1 NE2
REMARK 470 LYS A 326 CG CD CE NZ
REMARK 470 LYS A 327 CG CD CE NZ
REMARK 470 ARG A 334 NE CZ NH1 NH2
REMARK 470 LYS A 352 CG CD CE NZ
REMARK 470 LEU A 363 CG CD1 CD2
REMARK 470 GLN A 371 CG CD OE1 NE2
REMARK 470 LEU A 372 CD1 CD2
REMARK 470 SER A 378 OG
REMARK 470 LYS A 380 CG CD CE NZ
REMARK 470 ASN A 383 OD1 ND2
REMARK 470 LYS A 388 CG CD CE NZ
REMARK 470 GLU A 389 CG CD OE1 OE2
REMARK 470 LYS A 391 CE NZ
REMARK 470 ARG A 408 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 431 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 435 CG CD CE NZ
REMARK 470 GLU A 452 CG CD OE1 OE2
REMARK 470 ARG A 457 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 458 OD1 OD2
REMARK 470 LYS A 459 CG CD CE NZ
REMARK 470 ARG A 460 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 481 CG OD1 ND2
REMARK 470 GLU A 482 CG CD OE1 OE2
REMARK 470 GLN A 484 CG CD OE1 NE2
REMARK 470 GLN A 494 CG CD OE1 NE2
REMARK 470 LYS A 497 NZ
REMARK 470 LYS A 499 CG CD CE NZ
REMARK 470 THR A 512 OG1 CG2
REMARK 470 ARG A 513 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 515 CG CD OE1 OE2
REMARK 470 GLU A 517 CG CD OE1 OE2
REMARK 470 LYS A 519 CG CD CE NZ
REMARK 470 GLU A 521 CG CD OE1 OE2
REMARK 470 ILE A 523 CG1 CG2 CD1
REMARK 470 ARG A 525 CZ NH1 NH2
REMARK 470 GLU A 529 CG CD OE1 OE2
REMARK 470 GLN A 535 CG CD OE1 NE2
REMARK 470 ARG A 539 CZ NH1 NH2
REMARK 470 SER A 542 OG
REMARK 470 ILE B 251 CD1
REMARK 470 GLN B 252 OE1 NE2
REMARK 470 ILE B 264 CD1
REMARK 470 ILE B 266 CD1
REMARK 470 ASP B 278 OD1 OD2
REMARK 470 GLN B 286 CG CD OE1 NE2
REMARK 470 LYS B 302 CG CD CE NZ
REMARK 470 SER B 306 OG
REMARK 470 ARG B 308 NH1 NH2
REMARK 470 GLN B 317 CG CD OE1 NE2
REMARK 470 SER B 324 OG
REMARK 470 LYS B 326 CD CE NZ
REMARK 470 LYS B 327 CG CD CE NZ
REMARK 470 ASP B 330 CG OD1 OD2
REMARK 470 ILE B 350 CG1 CG2 CD1
REMARK 470 LYS B 352 CG CD CE NZ
REMARK 470 ASP B 362 CG OD1 OD2
REMARK 470 THR B 369 OG1 CG2
REMARK 470 VAL B 370 CG1 CG2
REMARK 470 LYS B 380 CG CD CE NZ
REMARK 470 ASN B 383 CG OD1 ND2
REMARK 470 LYS B 388 CG CD CE NZ
REMARK 470 ARG B 408 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 412 CD OE1 OE2
REMARK 470 ARG B 427 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 431 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 435 CG CD CE NZ
REMARK 470 GLU B 444 CG CD OE1 OE2
REMARK 470 GLU B 452 CG CD OE1 OE2
REMARK 470 ARG B 457 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 459 CG CD CE NZ
REMARK 470 ARG B 460 CD NE CZ NH1 NH2
REMARK 470 ASN B 468 OD1 ND2
REMARK 470 GLU B 472 CG CD OE1 OE2
REMARK 470 GLN B 477 CD OE1 NE2
REMARK 470 GLU B 482 CG CD OE1 OE2
REMARK 470 GLN B 484 CG CD OE1 NE2
REMARK 470 ARG B 489 CZ NH1 NH2
REMARK 470 ARG B 496 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 497 CD CE NZ
REMARK 470 LYS B 499 CG CD CE NZ
REMARK 470 ARG B 513 CZ NH1 NH2
REMARK 470 GLU B 515 CG CD OE1 OE2
REMARK 470 GLN B 518 CG CD OE1 NE2
REMARK 470 LYS B 519 CG CD CE NZ
REMARK 470 ILE B 523 CG1 CG2 CD1
REMARK 470 GLU B 529 CG CD OE1 OE2
REMARK 470 ARG B 539 CZ NH1 NH2
REMARK 470 VAL I 2 CG1 CG2
REMARK 470 GLN I 3 CG CD OE1 NE2
REMARK 470 GLU I 10 OE1 OE2
REMARK 470 LEU I 11 CG CD1 CD2
REMARK 470 LYS I 13 CG CD CE NZ
REMARK 470 LYS I 23 CG CD CE NZ
REMARK 470 LYS I 38 NZ
REMARK 470 GLN I 43 OE1 NE2
REMARK 470 LEU I 45 CD1 CD2
REMARK 470 GLN I 62 CG CD OE1 NE2
REMARK 470 LYS I 63 CE NZ
REMARK 470 LYS I 65 CG CD CE NZ
REMARK 470 ASP I 66 CG OD1 OD2
REMARK 470 LYS I 67 CE NZ
REMARK 470 LEU I 86 CD1 CD2
REMARK 470 ARG I 102 CZ NH1 NH2
REMARK 470 LEU I 114 CD1 CD2
REMARK 470 LYS I 123 CE NZ
REMARK 470 PHE I 128 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER I 134 CB OG
REMARK 470 LEU I 144 CG CD1 CD2
REMARK 470 LYS I 149 CG CD CE NZ
REMARK 470 GLU I 154 CG CD OE1 OE2
REMARK 470 VAL I 156 CG1 CG2
REMARK 470 ASN I 161 CG OD1 ND2
REMARK 470 SER I 167 OG
REMARK 470 VAL I 175 CG1 CG2
REMARK 470 SER I 179 OG
REMARK 470 LEU I 184 CG CD1 CD2
REMARK 470 VAL I 188 CG1 CG2
REMARK 470 SER I 192 OG
REMARK 470 SER I 194 OG
REMARK 470 THR I 197 OG1 CG2
REMARK 470 GLN I 198 CG CD OE1 NE2
REMARK 470 LYS I 207 CG CD CE NZ
REMARK 470 ASN I 210 CG OD1 ND2
REMARK 470 LYS I 212 CG CD CE NZ
REMARK 470 ASP I 214 CG OD1 OD2
REMARK 470 LYS I 216 CG CD CE NZ
REMARK 470 GLN H 3 CG CD OE1 NE2
REMARK 470 GLN H 5 CG CD OE1 NE2
REMARK 470 GLN H 6 OE1 NE2
REMARK 470 LYS H 13 CG CD CE NZ
REMARK 470 SER H 17 OG
REMARK 470 LYS H 23 CG CD CE NZ
REMARK 470 MET H 34 CE
REMARK 470 LYS H 38 NZ
REMARK 470 ARG H 40 CD NE CZ NH1 NH2
REMARK 470 GLN H 62 CG CD OE1 NE2
REMARK 470 LYS H 63 CE NZ
REMARK 470 LYS H 65 CG CD CE NZ
REMARK 470 LYS H 67 CG CD CE NZ
REMARK 470 ASP H 89 CG OD1 OD2
REMARK 470 ASP H 90 CG OD1 OD2
REMARK 470 GLN H 111 OE1 NE2
REMARK 470 LEU H 114 CD1 CD2
REMARK 470 SER H 118 OG
REMARK 470 SER H 121 OG
REMARK 470 LYS H 123 CG CD CE NZ
REMARK 470 LEU H 130 CG CD1 CD2
REMARK 470 THR H 141 OG1 CG2
REMARK 470 LEU H 144 CG CD1 CD2
REMARK 470 VAL H 148 CG1 CG2
REMARK 470 LYS H 149 CG CD CE NZ
REMARK 470 ASP H 150 CG OD1 OD2
REMARK 470 VAL H 156 CG1 CG2
REMARK 470 VAL H 158 CG1 CG2
REMARK 470 SER H 159 OG
REMARK 470 TRP H 160 CE3 CZ2 CZ3 CH2
REMARK 470 ASN H 161 CB CG OD1 ND2
REMARK 470 SER H 162 OG
REMARK 470 LEU H 165 CG CD1 CD2
REMARK 470 THR H 166 OG1 CG2
REMARK 470 VAL H 169 CG1 CG2
REMARK 470 VAL H 175 CG1 CG2
REMARK 470 GLN H 177 CD OE1 NE2
REMARK 470 LEU H 184 CG CD1 CD2
REMARK 470 SER H 185 OG
REMARK 470 SER H 186 CB OG
REMARK 470 VAL H 188 CG1 CG2
REMARK 470 TYR H 200 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE H 201 CG1 CG2 CD1
REMARK 470 ASN H 203 CG OD1 ND2
REMARK 470 ASN H 205 OD1 ND2
REMARK 470 LYS H 207 CG CD CE NZ
REMARK 470 LYS H 212 CE NZ
REMARK 470 ASP H 214 CG OD1 OD2
REMARK 470 LYS H 215 CG CD CE NZ
REMARK 470 LYS H 216 CG CD CE NZ
REMARK 470 ALA H 217 CB
REMARK 470 GLU H 218 CG CD OE1 OE2
REMARK 470 LYS H 220 CB CG CD CE NZ
REMARK 470 SER M 10 OG
REMARK 470 LEU M 15 CG CD1 CD2
REMARK 470 GLN M 17 CB CG CD OE1 NE2
REMARK 470 ARG M 18 CZ NH1 NH2
REMARK 470 LYS M 24 CE NZ
REMARK 470 SER M 28 OG
REMARK 470 VAL M 29 CG1 CG2
REMARK 470 ASP M 32 CB CG OD1 OD2
REMARK 470 LYS M 43 CG CD CE NZ
REMARK 470 GLN M 46 OE1 NE2
REMARK 470 LYS M 49 CG CD CE NZ
REMARK 470 LEU M 51 CD1 CD2
REMARK 470 ILE M 52 CG1 CG2 CD1
REMARK 470 SER M 56 OG
REMARK 470 LEU M 58 CD1 CD2
REMARK 470 GLU M 84 CG CD OE1 OE2
REMARK 470 GLU M 85 CD OE1 OE2
REMARK 470 LEU M 108 CD1 CD2
REMARK 470 ILE M 110 CG1 CG2 CD1
REMARK 470 LYS M 111 CB CG CD CE NZ
REMARK 470 THR M 113 OG1 CG2
REMARK 470 SER M 118 OG
REMARK 470 PHE M 120 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE M 121 CG1 CG2 CD1
REMARK 470 SER M 125 OG
REMARK 470 ASP M 126 CB CG OD1 OD2
REMARK 470 GLU M 127 CG CD OE1 OE2
REMARK 470 GLN M 128 OE1 NE2
REMARK 470 LEU M 129 CD1 CD2
REMARK 470 ASN M 141 OD1 ND2
REMARK 470 ARG M 146 CG CD NE CZ NH1 NH2
REMARK 470 GLU M 147 CG CD OE1 OE2
REMARK 470 LYS M 149 CG CD CE NZ
REMARK 470 ASP M 155 CG OD1 OD2
REMARK 470 LEU M 158 CD1 CD2
REMARK 470 SER M 160 OG
REMARK 470 ASN M 162 CG OD1 ND2
REMARK 470 SER M 163 OG
REMARK 470 LYS M 173 CD CE NZ
REMARK 470 ASP M 174 CG OD1 OD2
REMARK 470 THR M 184 OG1 CG2
REMARK 470 LEU M 185 CG CD1 CD2
REMARK 470 SER M 186 OG
REMARK 470 LYS M 187 CG CD CE NZ
REMARK 470 LYS M 194 CG CD CE NZ
REMARK 470 GLU M 199 CG CD OE1 OE2
REMARK 470 THR M 201 OG1 CG2
REMARK 470 GLN M 203 CG CD OE1 NE2
REMARK 470 LEU M 205 CG CD1 CD2
REMARK 470 SER M 206 OG
REMARK 470 LYS M 211 CG CD CE NZ
REMARK 470 SER M 212 OG
REMARK 470 PHE M 213 CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN M 214 CG OD1 ND2
REMARK 470 ARG M 215 CG CD NE CZ NH1 NH2
REMARK 470 VAL L 3 CG1 CG2
REMARK 470 LEU L 4 CD1 CD2
REMARK 470 SER L 10 OG
REMARK 470 LEU L 15 CG CD1 CD2
REMARK 470 GLN L 17 CG CD OE1 NE2
REMARK 470 SER L 22 OG
REMARK 470 LYS L 24 CD CE NZ
REMARK 470 ASP L 32 CG OD1 OD2
REMARK 470 MET L 37 SD CE
REMARK 470 GLN L 46 OE1 NE2
REMARK 470 LYS L 49 CG CD CE NZ
REMARK 470 LEU L 51 CD1 CD2
REMARK 470 ILE L 52 CG1 CG2 CD1
REMARK 470 SER L 56 OG
REMARK 470 ASN L 57 CG OD1 ND2
REMARK 470 ASP L 59 CG OD1 OD2
REMARK 470 SER L 71 OG
REMARK 470 GLU L 83 CD OE1 OE2
REMARK 470 GLU L 84 CD OE1 OE2
REMARK 470 GLU L 85 CG CD OE1 OE2
REMARK 470 LYS L 107 CG CD CE NZ
REMARK 470 GLU L 109 CG CD OE1 OE2
REMARK 470 ILE L 110 CD1
REMARK 470 LYS L 111 CG CD CE NZ
REMARK 470 ARG L 112 CG CD NE CZ NH1 NH2
REMARK 470 GLU L 127 CG CD OE1 OE2
REMARK 470 GLN L 128 OE1 NE2
REMARK 470 LEU L 129 CG CD1 CD2
REMARK 470 LYS L 130 CG CD CE NZ
REMARK 470 SER L 131 OG
REMARK 470 LEU L 139 CG CD1 CD2
REMARK 470 LEU L 140 CD1 CD2
REMARK 470 ASN L 141 CG OD1 ND2
REMARK 470 ASN L 142 CG OD1 ND2
REMARK 470 LYS L 149 CG CD CE NZ
REMARK 470 GLN L 151 CG CD OE1 NE2
REMARK 470 TRP L 152 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP L 152 CZ3 CH2
REMARK 470 GLN L 159 CB CG CD OE1 NE2
REMARK 470 ASN L 162 CG OD1 ND2
REMARK 470 SER L 163 OG
REMARK 470 GLU L 165 CG CD OE1 OE2
REMARK 470 GLU L 169 CG CD OE1 OE2
REMARK 470 LYS L 173 CD CE NZ
REMARK 470 ASP L 174 CG OD1 OD2
REMARK 470 THR L 176 OG1 CG2
REMARK 470 ASP L 189 CG OD1 OD2
REMARK 470 GLU L 191 CG CD OE1 OE2
REMARK 470 LYS L 192 CD CE NZ
REMARK 470 LYS L 194 CG CD CE NZ
REMARK 470 GLU L 199 CG CD OE1 OE2
REMARK 470 LYS L 211 CD CE NZ
REMARK 470 ASN L 214 OD1 ND2
REMARK 470 ARG L 215 CZ NH1 NH2
REMARK 470 CYS L 218 CB SG
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 456 76.12 -118.44
REMARK 500 SER A 534 54.15 -111.64
REMARK 500 ASP B 362 83.05 62.37
REMARK 500 VAL B 370 105.96 -59.69
REMARK 500 ASN B 394 21.64 -72.11
REMARK 500 PRO B 471 -144.24 -82.25
REMARK 500 SER B 534 40.36 -92.39
REMARK 500 TYR I 32 143.67 -170.28
REMARK 500 PRO I 41 102.44 -52.78
REMARK 500 ILE I 48 -63.78 -101.68
REMARK 500 SER I 104 39.67 -97.41
REMARK 500 ASP I 150 71.10 54.80
REMARK 500 ALA H 16 -159.41 -96.77
REMARK 500 ALA H 92 -169.37 -164.66
REMARK 500 ASP H 150 77.17 57.65
REMARK 500 TYR M 36 65.88 -110.09
REMARK 500 ALA M 55 -53.36 66.33
REMARK 500 ARG M 215 25.17 -79.29
REMARK 500 TYR L 31 114.96 -163.82
REMARK 500 TYR L 36 79.21 -116.30
REMARK 500 ALA L 55 -14.53 72.61
REMARK 500 SER L 56 22.58 -155.27
REMARK 500 ASN L 142 76.79 57.23
REMARK 500 LYS L 194 -65.02 -95.17
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6EYO A 224 547 UNP P01854 IGHE_HUMAN 104 428
DBREF 6EYO B 224 547 UNP P01854 IGHE_HUMAN 104 428
DBREF 6EYO I 1 227 PDB 6EYO 6EYO 1 227
DBREF 6EYO H 1 227 PDB 6EYO 6EYO 1 227
DBREF 6EYO M 1 218 PDB 6EYO 6EYO 1 218
DBREF 6EYO L 1 218 PDB 6EYO 6EYO 1 218
SEQADV 6EYO ASP A 222 UNP P01854 EXPRESSION TAG
SEQADV 6EYO ILE A 223 UNP P01854 EXPRESSION TAG
SEQADV 6EYO ALA A 225 UNP P01854 CYS 105 CONFLICT
SEQADV 6EYO GLN A 265 UNP P01854 ASN 146 CONFLICT
SEQADV 6EYO GLN A 371 UNP P01854 ASN 252 CONFLICT
SEQADV 6EYO ASP B 222 UNP P01854 EXPRESSION TAG
SEQADV 6EYO ILE B 223 UNP P01854 EXPRESSION TAG
SEQADV 6EYO ALA B 225 UNP P01854 CYS 105 CONFLICT
SEQADV 6EYO GLN B 265 UNP P01854 ASN 146 CONFLICT
SEQADV 6EYO GLN B 371 UNP P01854 ASN 252 CONFLICT
SEQRES 1 A 327 ASP ILE VAL ALA SER ARG ASP PHE THR PRO PRO THR VAL
SEQRES 2 A 327 LYS ILE LEU GLN SER SER CYS ASP GLY GLY GLY HIS PHE
SEQRES 3 A 327 PRO PRO THR ILE GLN LEU LEU CYS LEU VAL SER GLY TYR
SEQRES 4 A 327 THR PRO GLY THR ILE GLN ILE THR TRP LEU GLU ASP GLY
SEQRES 5 A 327 GLN VAL MET ASP VAL ASP LEU SER THR ALA SER THR THR
SEQRES 6 A 327 GLN GLU GLY GLU LEU ALA SER THR GLN SER GLU LEU THR
SEQRES 7 A 327 LEU SER GLN LYS HIS TRP LEU SER ASP ARG THR TYR THR
SEQRES 8 A 327 CYS GLN VAL THR TYR GLN GLY HIS THR PHE GLU ASP SER
SEQRES 9 A 327 THR LYS LYS CYS ALA ASP SER ASN PRO ARG GLY VAL SER
SEQRES 10 A 327 ALA TYR LEU SER ARG PRO SER PRO PHE ASP LEU PHE ILE
SEQRES 11 A 327 ARG LYS SER PRO THR ILE THR CYS LEU VAL VAL ASP LEU
SEQRES 12 A 327 ALA PRO SER LYS GLY THR VAL GLN LEU THR TRP SER ARG
SEQRES 13 A 327 ALA SER GLY LYS PRO VAL ASN HIS SER THR ARG LYS GLU
SEQRES 14 A 327 GLU LYS GLN ARG ASN GLY THR LEU THR VAL THR SER THR
SEQRES 15 A 327 LEU PRO VAL GLY THR ARG ASP TRP ILE GLU GLY GLU THR
SEQRES 16 A 327 TYR GLN CYS ARG VAL THR HIS PRO HIS LEU PRO ARG ALA
SEQRES 17 A 327 LEU MET ARG SER THR THR LYS THR SER GLY PRO ARG ALA
SEQRES 18 A 327 ALA PRO GLU VAL TYR ALA PHE ALA THR PRO GLU TRP PRO
SEQRES 19 A 327 GLY SER ARG ASP LYS ARG THR LEU ALA CYS LEU ILE GLN
SEQRES 20 A 327 ASN PHE MET PRO GLU ASP ILE SER VAL GLN TRP LEU HIS
SEQRES 21 A 327 ASN GLU VAL GLN LEU PRO ASP ALA ARG HIS SER THR THR
SEQRES 22 A 327 GLN PRO ARG LYS THR LYS GLY SER GLY PHE PHE VAL PHE
SEQRES 23 A 327 SER ARG LEU GLU VAL THR ARG ALA GLU TRP GLU GLN LYS
SEQRES 24 A 327 ASP GLU PHE ILE CYS ARG ALA VAL HIS GLU ALA ALA SER
SEQRES 25 A 327 PRO SER GLN THR VAL GLN ARG ALA VAL SER VAL ASN PRO
SEQRES 26 A 327 GLY LYS
SEQRES 1 B 327 ASP ILE VAL ALA SER ARG ASP PHE THR PRO PRO THR VAL
SEQRES 2 B 327 LYS ILE LEU GLN SER SER CYS ASP GLY GLY GLY HIS PHE
SEQRES 3 B 327 PRO PRO THR ILE GLN LEU LEU CYS LEU VAL SER GLY TYR
SEQRES 4 B 327 THR PRO GLY THR ILE GLN ILE THR TRP LEU GLU ASP GLY
SEQRES 5 B 327 GLN VAL MET ASP VAL ASP LEU SER THR ALA SER THR THR
SEQRES 6 B 327 GLN GLU GLY GLU LEU ALA SER THR GLN SER GLU LEU THR
SEQRES 7 B 327 LEU SER GLN LYS HIS TRP LEU SER ASP ARG THR TYR THR
SEQRES 8 B 327 CYS GLN VAL THR TYR GLN GLY HIS THR PHE GLU ASP SER
SEQRES 9 B 327 THR LYS LYS CYS ALA ASP SER ASN PRO ARG GLY VAL SER
SEQRES 10 B 327 ALA TYR LEU SER ARG PRO SER PRO PHE ASP LEU PHE ILE
SEQRES 11 B 327 ARG LYS SER PRO THR ILE THR CYS LEU VAL VAL ASP LEU
SEQRES 12 B 327 ALA PRO SER LYS GLY THR VAL GLN LEU THR TRP SER ARG
SEQRES 13 B 327 ALA SER GLY LYS PRO VAL ASN HIS SER THR ARG LYS GLU
SEQRES 14 B 327 GLU LYS GLN ARG ASN GLY THR LEU THR VAL THR SER THR
SEQRES 15 B 327 LEU PRO VAL GLY THR ARG ASP TRP ILE GLU GLY GLU THR
SEQRES 16 B 327 TYR GLN CYS ARG VAL THR HIS PRO HIS LEU PRO ARG ALA
SEQRES 17 B 327 LEU MET ARG SER THR THR LYS THR SER GLY PRO ARG ALA
SEQRES 18 B 327 ALA PRO GLU VAL TYR ALA PHE ALA THR PRO GLU TRP PRO
SEQRES 19 B 327 GLY SER ARG ASP LYS ARG THR LEU ALA CYS LEU ILE GLN
SEQRES 20 B 327 ASN PHE MET PRO GLU ASP ILE SER VAL GLN TRP LEU HIS
SEQRES 21 B 327 ASN GLU VAL GLN LEU PRO ASP ALA ARG HIS SER THR THR
SEQRES 22 B 327 GLN PRO ARG LYS THR LYS GLY SER GLY PHE PHE VAL PHE
SEQRES 23 B 327 SER ARG LEU GLU VAL THR ARG ALA GLU TRP GLU GLN LYS
SEQRES 24 B 327 ASP GLU PHE ILE CYS ARG ALA VAL HIS GLU ALA ALA SER
SEQRES 25 B 327 PRO SER GLN THR VAL GLN ARG ALA VAL SER VAL ASN PRO
SEQRES 26 B 327 GLY LYS
SEQRES 1 I 227 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU ALA LYS
SEQRES 2 I 227 PRO GLY ALA SER VAL MET LEU SER CYS LYS ALA SER GLY
SEQRES 3 I 227 TYR THR PHE ASN GLY TYR TRP MET HIS TRP VAL LYS GLN
SEQRES 4 I 227 ARG PRO GLY GLN ASP LEU GLU TRP ILE GLY TYR ILE ASN
SEQRES 5 I 227 PRO THR THR GLY HIS THR GLU TYR ASN GLN LYS PHE LYS
SEQRES 6 I 227 ASP LYS ALA THR LEU THR ALA ASP GLU SER SER ASN THR
SEQRES 7 I 227 ALA TYR ILE GLU LEU SER SER LEU THR SER ASP ASP SER
SEQRES 8 I 227 ALA VAL TYR TYR CYS ALA ARG GLN GLU TYR ARG HIS SER
SEQRES 9 I 227 TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 I 227 SER ALA ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 I 227 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 I 227 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 I 227 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 I 227 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 I 227 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 I 227 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 I 227 SER ASN THR LYS VAL ASP LYS LYS ALA GLU PRO LYS SER
SEQRES 18 I 227 CYS ASP LYS THR HIS THR
SEQRES 1 H 227 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU ALA LYS
SEQRES 2 H 227 PRO GLY ALA SER VAL MET LEU SER CYS LYS ALA SER GLY
SEQRES 3 H 227 TYR THR PHE ASN GLY TYR TRP MET HIS TRP VAL LYS GLN
SEQRES 4 H 227 ARG PRO GLY GLN ASP LEU GLU TRP ILE GLY TYR ILE ASN
SEQRES 5 H 227 PRO THR THR GLY HIS THR GLU TYR ASN GLN LYS PHE LYS
SEQRES 6 H 227 ASP LYS ALA THR LEU THR ALA ASP GLU SER SER ASN THR
SEQRES 7 H 227 ALA TYR ILE GLU LEU SER SER LEU THR SER ASP ASP SER
SEQRES 8 H 227 ALA VAL TYR TYR CYS ALA ARG GLN GLU TYR ARG HIS SER
SEQRES 9 H 227 TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 H 227 SER ALA ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 H 227 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 H 227 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 H 227 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 H 227 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 H 227 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 H 227 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 H 227 SER ASN THR LYS VAL ASP LYS LYS ALA GLU PRO LYS SER
SEQRES 18 H 227 CYS ASP LYS THR HIS THR
SEQRES 1 M 218 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL
SEQRES 2 M 218 SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS ALA SER
SEQRES 3 M 218 GLN SER VAL ASP TYR ASP GLY ASP THR TYR MET ASN TRP
SEQRES 4 M 218 TYR HIS GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE
SEQRES 5 M 218 TYR ALA ALA SER ASN LEU ASP SER GLY ILE PRO ALA ARG
SEQRES 6 M 218 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN
SEQRES 7 M 218 ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR TYR TYR
SEQRES 8 M 218 CYS GLN GLN THR ASN GLU ASP PRO TRP THR PHE GLY GLY
SEQRES 9 M 218 GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA PRO
SEQRES 10 M 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS
SEQRES 11 M 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE
SEQRES 12 M 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN
SEQRES 13 M 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU
SEQRES 14 M 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR
SEQRES 15 M 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL
SEQRES 16 M 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO
SEQRES 17 M 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS
SEQRES 1 L 218 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL
SEQRES 2 L 218 SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS ALA SER
SEQRES 3 L 218 GLN SER VAL ASP TYR ASP GLY ASP THR TYR MET ASN TRP
SEQRES 4 L 218 TYR HIS GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE
SEQRES 5 L 218 TYR ALA ALA SER ASN LEU ASP SER GLY ILE PRO ALA ARG
SEQRES 6 L 218 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN
SEQRES 7 L 218 ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR TYR TYR
SEQRES 8 L 218 CYS GLN GLN THR ASN GLU ASP PRO TRP THR PHE GLY GLY
SEQRES 9 L 218 GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA PRO
SEQRES 10 L 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS
SEQRES 11 L 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE
SEQRES 12 L 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN
SEQRES 13 L 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU
SEQRES 14 L 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR
SEQRES 15 L 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL
SEQRES 16 L 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO
SEQRES 17 L 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET MAN C 4 11
HET MAN C 5 11
HET MAN C 6 11
HET MAN C 7 11
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET MAN D 4 11
HET MAN D 5 11
HET MAN D 6 11
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 7 NAG 4(C8 H15 N O6)
FORMUL 7 BMA 2(C6 H12 O6)
FORMUL 7 MAN 7(C6 H12 O6)
HELIX 1 AA1 ASP A 276 ASP A 278 5 3
HELIX 2 AA2 GLN A 301 LEU A 305 1 5
HELIX 3 AA3 SER A 344 ILE A 350 1 7
HELIX 4 AA4 GLY A 406 GLY A 413 1 8
HELIX 5 AA5 PRO A 486 ALA A 488 5 3
HELIX 6 AA6 ARG A 513 LYS A 519 1 7
HELIX 7 AA7 ASP B 276 ASP B 278 5 3
HELIX 8 AA8 GLN B 301 LEU B 305 1 5
HELIX 9 AA9 SER B 344 PHE B 349 1 6
HELIX 10 AB1 ALA B 364 THR B 369 5 6
HELIX 11 AB2 GLY B 406 GLU B 412 1 7
HELIX 12 AB3 PRO B 486 ALA B 488 5 3
HELIX 13 AB4 ARG B 513 LYS B 519 1 7
HELIX 14 AB5 THR I 87 SER I 91 5 5
HELIX 15 AB6 SER I 162 ALA I 164 5 3
HELIX 16 AB7 GLN H 62 LYS H 65 5 4
HELIX 17 AB8 THR H 87 SER H 91 5 5
HELIX 18 AB9 GLU M 83 ALA M 87 5 5
HELIX 19 AC1 GLU L 127 GLY L 132 5 6
SHEET 1 AA1 8 SER A 280 THR A 285 0
SHEET 2 AA1 8 SER A 292 SER A 300 -1 O GLN A 294 N SER A 283
SHEET 3 AA1 8 THR A 250 SER A 257 -1 N VAL A 256 O THR A 293
SHEET 4 AA1 8 THR A 233 SER A 239 -1 N LYS A 235 O LEU A 255
SHEET 5 AA1 8 LYS B 235 SER B 239 -1 O GLN B 238 N GLN A 238
SHEET 6 AA1 8 THR B 250 VAL B 256 -1 O LEU B 255 N LYS B 235
SHEET 7 AA1 8 SER B 292 SER B 300 -1 O LEU B 299 N ILE B 251
SHEET 8 AA1 8 SER B 280 THR B 285 -1 N THR B 285 O SER B 292
SHEET 1 AA2 4 GLN A 273 MET A 275 0
SHEET 2 AA2 4 GLN A 265 GLU A 270 -1 N TRP A 268 O MET A 275
SHEET 3 AA2 4 THR A 309 THR A 315 -1 O GLN A 313 N THR A 267
SHEET 4 AA2 4 PHE A 321 LYS A 326 -1 O THR A 325 N TYR A 310
SHEET 1 AA3 4 SER A 337 SER A 341 0
SHEET 2 AA3 4 THR A 355 LEU A 363 -1 O LEU A 359 N TYR A 339
SHEET 3 AA3 4 LEU A 397 PRO A 404 -1 O SER A 401 N CYS A 358
SHEET 4 AA3 4 LYS A 388 LYS A 391 -1 N LYS A 388 O THR A 400
SHEET 1 AA4 3 GLN A 371 ARG A 376 0
SHEET 2 AA4 3 TYR A 416 THR A 421 -1 O GLN A 417 N SER A 375
SHEET 3 AA4 3 LEU A 429 THR A 433 -1 O ARG A 431 N CYS A 418
SHEET 1 AA5 4 GLU A 444 ALA A 449 0
SHEET 2 AA5 4 LYS A 459 GLN A 467 -1 O LEU A 465 N TYR A 446
SHEET 3 AA5 4 PHE A 504 THR A 512 -1 O LEU A 509 N LEU A 462
SHEET 4 AA5 4 HIS A 490 THR A 492 -1 N SER A 491 O ARG A 508
SHEET 1 AA6 3 SER A 475 HIS A 480 0
SHEET 2 AA6 3 PHE A 522 VAL A 527 -1 O ILE A 523 N LEU A 479
SHEET 3 AA6 3 THR A 536 VAL A 541 -1 O ARG A 539 N CYS A 524
SHEET 1 AA7 4 GLN B 273 VAL B 274 0
SHEET 2 AA7 4 ILE B 264 GLU B 270 -1 N GLU B 270 O GLN B 273
SHEET 3 AA7 4 TYR B 310 TYR B 316 -1 O GLN B 313 N THR B 267
SHEET 4 AA7 4 HIS B 319 THR B 325 -1 O ASP B 323 N CYS B 312
SHEET 1 AA8 4 ALA B 338 SER B 341 0
SHEET 2 AA8 4 THR B 355 LEU B 363 -1 O LEU B 359 N TYR B 339
SHEET 3 AA8 4 LEU B 397 PRO B 404 -1 O SER B 401 N CYS B 358
SHEET 4 AA8 4 THR B 386 LYS B 391 -1 N LYS B 388 O THR B 400
SHEET 1 AA9 3 GLN B 371 ARG B 376 0
SHEET 2 AA9 3 THR B 415 HIS B 422 -1 O ARG B 419 N THR B 373
SHEET 3 AA9 3 LEU B 425 THR B 434 -1 O LEU B 429 N VAL B 420
SHEET 1 AB1 4 GLU B 444 ALA B 449 0
SHEET 2 AB1 4 LYS B 459 GLN B 467 -1 O LEU B 465 N TYR B 446
SHEET 3 AB1 4 PHE B 503 THR B 512 -1 O LEU B 509 N LEU B 462
SHEET 4 AB1 4 HIS B 490 THR B 492 -1 N SER B 491 O ARG B 508
SHEET 1 AB2 4 GLU B 444 ALA B 449 0
SHEET 2 AB2 4 LYS B 459 GLN B 467 -1 O LEU B 465 N TYR B 446
SHEET 3 AB2 4 PHE B 503 THR B 512 -1 O LEU B 509 N LEU B 462
SHEET 4 AB2 4 ARG B 496 LYS B 497 -1 N ARG B 496 O PHE B 504
SHEET 1 AB3 4 VAL B 483 GLN B 484 0
SHEET 2 AB3 4 SER B 475 HIS B 480 -1 N HIS B 480 O VAL B 483
SHEET 3 AB3 4 PHE B 522 VAL B 527 -1 O ILE B 523 N LEU B 479
SHEET 4 AB3 4 THR B 536 VAL B 537 -1 O VAL B 537 N ALA B 526
SHEET 1 AB4 4 VAL B 483 GLN B 484 0
SHEET 2 AB4 4 SER B 475 HIS B 480 -1 N HIS B 480 O VAL B 483
SHEET 3 AB4 4 PHE B 522 VAL B 527 -1 O ILE B 523 N LEU B 479
SHEET 4 AB4 4 ALA B 540 VAL B 541 -1 O VAL B 541 N PHE B 522
SHEET 1 AB5 4 LEU I 4 GLN I 6 0
SHEET 2 AB5 4 VAL I 18 ALA I 24 -1 O LYS I 23 N GLN I 5
SHEET 3 AB5 4 THR I 78 LEU I 83 -1 O LEU I 83 N VAL I 18
SHEET 4 AB5 4 ALA I 68 ASP I 73 -1 N THR I 71 O TYR I 80
SHEET 1 AB6 6 GLU I 10 ALA I 12 0
SHEET 2 AB6 6 THR I 113 VAL I 117 1 O THR I 116 N GLU I 10
SHEET 3 AB6 6 ALA I 92 TYR I 95 -1 N TYR I 94 O THR I 113
SHEET 4 AB6 6 TYR I 32 GLN I 39 -1 N VAL I 37 O TYR I 95
SHEET 5 AB6 6 LEU I 45 ILE I 51 -1 O GLU I 46 N LYS I 38
SHEET 6 AB6 6 THR I 58 TYR I 60 -1 O GLU I 59 N TYR I 50
SHEET 1 AB7 5 GLU I 10 ALA I 12 0
SHEET 2 AB7 5 THR I 113 VAL I 117 1 O THR I 116 N GLU I 10
SHEET 3 AB7 5 ALA I 92 TYR I 95 -1 N TYR I 94 O THR I 113
SHEET 4 AB7 5 TYR I 32 GLN I 39 -1 N VAL I 37 O TYR I 95
SHEET 5 AB7 5 ARG I 98 GLU I 100 -1 O GLN I 99 N TRP I 33
SHEET 1 AB8 4 SER I 126 PRO I 129 0
SHEET 2 AB8 4 ALA I 142 TYR I 151 -1 O LYS I 149 N SER I 126
SHEET 3 AB8 4 TYR I 182 VAL I 190 -1 O LEU I 184 N VAL I 148
SHEET 4 AB8 4 VAL I 169 THR I 171 -1 N HIS I 170 O VAL I 187
SHEET 1 AB9 4 SER I 126 PRO I 129 0
SHEET 2 AB9 4 ALA I 142 TYR I 151 -1 O LYS I 149 N SER I 126
SHEET 3 AB9 4 TYR I 182 VAL I 190 -1 O LEU I 184 N VAL I 148
SHEET 4 AB9 4 VAL I 175 LEU I 176 -1 N VAL I 175 O SER I 183
SHEET 1 AC1 3 VAL I 156 TRP I 160 0
SHEET 2 AC1 3 ILE I 201 HIS I 206 -1 O ASN I 205 N THR I 157
SHEET 3 AC1 3 THR I 211 LYS I 216 -1 O THR I 211 N HIS I 206
SHEET 1 AC2 4 LEU H 4 GLN H 6 0
SHEET 2 AC2 4 SER H 17 ALA H 24 -1 O LYS H 23 N GLN H 5
SHEET 3 AC2 4 THR H 78 SER H 84 -1 O ALA H 79 N CYS H 22
SHEET 4 AC2 4 ALA H 68 ASP H 73 -1 N THR H 71 O TYR H 80
SHEET 1 AC3 6 GLU H 10 ALA H 12 0
SHEET 2 AC3 6 THR H 113 VAL H 117 1 O LEU H 114 N GLU H 10
SHEET 3 AC3 6 VAL H 93 GLU H 100 -1 N TYR H 94 O THR H 113
SHEET 4 AC3 6 TYR H 32 GLN H 39 -1 N HIS H 35 O ALA H 97
SHEET 5 AC3 6 GLU H 46 ILE H 51 -1 O ILE H 48 N TRP H 36
SHEET 6 AC3 6 THR H 58 TYR H 60 -1 O GLU H 59 N TYR H 50
SHEET 1 AC4 4 GLU H 10 ALA H 12 0
SHEET 2 AC4 4 THR H 113 VAL H 117 1 O LEU H 114 N GLU H 10
SHEET 3 AC4 4 VAL H 93 GLU H 100 -1 N TYR H 94 O THR H 113
SHEET 4 AC4 4 PHE H 106 TRP H 109 -1 O ALA H 107 N ARG H 98
SHEET 1 AC5 4 SER H 126 LEU H 130 0
SHEET 2 AC5 4 ALA H 142 TYR H 151 -1 O LEU H 147 N PHE H 128
SHEET 3 AC5 4 TYR H 182 VAL H 190 -1 O TYR H 182 N TYR H 151
SHEET 4 AC5 4 VAL H 169 THR H 171 -1 N HIS H 170 O VAL H 187
SHEET 1 AC6 4 SER H 126 LEU H 130 0
SHEET 2 AC6 4 ALA H 142 TYR H 151 -1 O LEU H 147 N PHE H 128
SHEET 3 AC6 4 TYR H 182 VAL H 190 -1 O TYR H 182 N TYR H 151
SHEET 4 AC6 4 VAL H 175 LEU H 176 -1 N VAL H 175 O SER H 183
SHEET 1 AC7 3 THR H 157 TRP H 160 0
SHEET 2 AC7 3 ILE H 201 HIS H 206 -1 O ASN H 203 N SER H 159
SHEET 3 AC7 3 THR H 211 LYS H 216 -1 O LYS H 215 N CYS H 202
SHEET 1 AC8 4 LEU M 4 SER M 7 0
SHEET 2 AC8 4 ALA M 19 ALA M 25 -1 O LYS M 24 N THR M 5
SHEET 3 AC8 4 ASP M 74 ILE M 79 -1 O LEU M 77 N ILE M 21
SHEET 4 AC8 4 PHE M 66 SER M 71 -1 N SER M 67 O ASN M 78
SHEET 1 AC9 6 SER M 10 SER M 14 0
SHEET 2 AC9 6 THR M 106 LYS M 111 1 O LYS M 111 N VAL M 13
SHEET 3 AC9 6 THR M 89 GLN M 94 -1 N TYR M 90 O THR M 106
SHEET 4 AC9 6 MET M 37 GLN M 42 -1 N ASN M 38 O GLN M 93
SHEET 5 AC9 6 LYS M 49 TYR M 53 -1 O LEU M 51 N TRP M 39
SHEET 6 AC9 6 ASN M 57 LEU M 58 -1 O ASN M 57 N TYR M 53
SHEET 1 AD1 4 SER M 10 SER M 14 0
SHEET 2 AD1 4 THR M 106 LYS M 111 1 O LYS M 111 N VAL M 13
SHEET 3 AD1 4 THR M 89 GLN M 94 -1 N TYR M 90 O THR M 106
SHEET 4 AD1 4 THR M 101 PHE M 102 -1 O THR M 101 N GLN M 94
SHEET 1 AD2 2 ASP M 30 TYR M 31 0
SHEET 2 AD2 2 ASP M 34 THR M 35 -1 O ASP M 34 N TYR M 31
SHEET 1 AD3 4 SER M 118 PHE M 122 0
SHEET 2 AD3 4 VAL M 136 PHE M 143 -1 O LEU M 139 N PHE M 120
SHEET 3 AD3 4 TYR M 177 LEU M 183 -1 O LEU M 183 N VAL M 136
SHEET 4 AD3 4 SER M 163 VAL M 167 -1 N SER M 166 O SER M 180
SHEET 1 AD4 3 ALA M 148 LYS M 149 0
SHEET 2 AD4 3 TYR M 196 HIS M 202 -1 O THR M 201 N LYS M 149
SHEET 3 AD4 3 VAL M 209 PHE M 213 -1 O LYS M 211 N CYS M 198
SHEET 1 AD5 4 LEU L 4 SER L 7 0
SHEET 2 AD5 4 ALA L 19 ALA L 25 -1 O LYS L 24 N THR L 5
SHEET 3 AD5 4 ASP L 74 ILE L 79 -1 O LEU L 77 N ILE L 21
SHEET 4 AD5 4 PHE L 66 SER L 71 -1 N SER L 69 O THR L 76
SHEET 1 AD6 6 SER L 10 SER L 14 0
SHEET 2 AD6 6 THR L 106 LYS L 111 1 O GLU L 109 N LEU L 11
SHEET 3 AD6 6 THR L 89 GLN L 94 -1 N TYR L 90 O THR L 106
SHEET 4 AD6 6 MET L 37 GLN L 42 -1 N TYR L 40 O TYR L 91
SHEET 5 AD6 6 LYS L 49 TYR L 53 -1 O LEU L 51 N TRP L 39
SHEET 6 AD6 6 ASN L 57 LEU L 58 -1 O ASN L 57 N TYR L 53
SHEET 1 AD7 4 SER L 10 SER L 14 0
SHEET 2 AD7 4 THR L 106 LYS L 111 1 O GLU L 109 N LEU L 11
SHEET 3 AD7 4 THR L 89 GLN L 94 -1 N TYR L 90 O THR L 106
SHEET 4 AD7 4 THR L 101 PHE L 102 -1 O THR L 101 N GLN L 94
SHEET 1 AD8 2 ASP L 30 TYR L 31 0
SHEET 2 AD8 2 ASP L 34 THR L 35 -1 O ASP L 34 N TYR L 31
SHEET 1 AD9 4 SER L 118 PHE L 122 0
SHEET 2 AD9 4 VAL L 136 PHE L 143 -1 O LEU L 139 N PHE L 120
SHEET 3 AD9 4 TYR L 177 LEU L 183 -1 O LEU L 183 N VAL L 136
SHEET 4 AD9 4 SER L 163 VAL L 167 -1 N SER L 166 O SER L 180
SHEET 1 AE1 3 LYS L 149 VAL L 154 0
SHEET 2 AE1 3 VAL L 195 THR L 201 -1 O GLU L 199 N GLN L 151
SHEET 3 AE1 3 VAL L 209 ASN L 214 -1 O LYS L 211 N CYS L 198
SSBOND 1 CYS A 241 CYS B 328 1555 1555 2.03
SSBOND 2 CYS A 254 CYS A 312 1555 1555 2.03
SSBOND 3 CYS A 328 CYS B 241 1555 1555 2.03
SSBOND 4 CYS A 358 CYS A 418 1555 1555 2.04
SSBOND 5 CYS A 464 CYS A 524 1555 1555 2.03
SSBOND 6 CYS B 254 CYS B 312 1555 1555 2.03
SSBOND 7 CYS B 358 CYS B 418 1555 1555 2.03
SSBOND 8 CYS B 464 CYS B 524 1555 1555 2.04
SSBOND 9 CYS I 22 CYS I 96 1555 1555 2.03
SSBOND 10 CYS I 146 CYS I 202 1555 1555 2.03
SSBOND 11 CYS H 22 CYS H 96 1555 1555 2.03
SSBOND 12 CYS H 146 CYS H 202 1555 1555 2.03
SSBOND 13 CYS M 23 CYS M 92 1555 1555 2.04
SSBOND 14 CYS M 138 CYS M 198 1555 1555 2.03
SSBOND 15 CYS L 23 CYS L 92 1555 1555 2.03
SSBOND 16 CYS L 138 CYS L 198 1555 1555 2.03
LINK ND2 ASN A 394 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN B 394 C1 NAG D 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.44
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.44
LINK O6 BMA C 3 C1 MAN C 6 1555 1555 1.45
LINK O2 MAN C 4 C1 MAN C 5 1555 1555 1.47
LINK O3 MAN C 6 C1 MAN C 7 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44
LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.44
LINK O6 BMA D 3 C1 MAN D 6 1555 1555 1.44
LINK O2 MAN D 4 C1 MAN D 5 1555 1555 1.46
CISPEP 1 MET A 470 PRO A 471 0 -6.98
CISPEP 2 SER A 532 PRO A 533 0 2.37
CISPEP 3 MET B 470 PRO B 471 0 -6.11
CISPEP 4 SER B 532 PRO B 533 0 -1.20
CISPEP 5 PHE I 152 PRO I 153 0 -2.11
CISPEP 6 GLU I 154 PRO I 155 0 -3.72
CISPEP 7 PHE H 152 PRO H 153 0 -2.49
CISPEP 8 GLU H 154 PRO H 155 0 -2.56
CISPEP 9 SER M 7 PRO M 8 0 -1.33
CISPEP 10 HIS M 80 PRO M 81 0 -2.20
CISPEP 11 ASP M 98 PRO M 99 0 -1.86
CISPEP 12 TYR M 144 PRO M 145 0 -2.39
CISPEP 13 SER L 7 PRO L 8 0 -0.59
CISPEP 14 HIS L 80 PRO L 81 0 -3.55
CISPEP 15 ASP L 98 PRO L 99 0 -0.24
CISPEP 16 TYR L 144 PRO L 145 0 0.42
CRYST1 119.483 119.601 132.994 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008369 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008361 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007519 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
