HEADER STRUCTURAL PROTEIN 09-AUG-10 3OBV
TITLE AUTOINHIBITED FORMIN MDIA1 STRUCTURE
CAVEAT 3OBV GLC I 1 HAS WRONG CHIRALITY AT ATOM C2 GLC I 1 HAS WRONG
CAVEAT 2 3OBV CHIRALITY AT ATOM C3 FRU I 2 HAS WRONG CHIRALITY AT ATOM C4
CAVEAT 3 3OBV FRU I 2 HAS WRONG CHIRALITY AT ATOM C5 GLC J 1 HAS WRONG
CAVEAT 4 3OBV CHIRALITY AT ATOM C2 GLC J 1 HAS WRONG CHIRALITY AT ATOM C3
CAVEAT 5 3OBV GLC J 1 HAS WRONG CHIRALITY AT ATOM C5 FRU J 2 HAS WRONG
CAVEAT 6 3OBV CHIRALITY AT ATOM C4 FRU J 2 HAS WRONG CHIRALITY AT ATOM C5
CAVEAT 7 3OBV GLC K 1 HAS WRONG CHIRALITY AT ATOM C2 GLC K 1 HAS WRONG
CAVEAT 8 3OBV CHIRALITY AT ATOM C3 FRU K 2 HAS WRONG CHIRALITY AT ATOM C4
CAVEAT 9 3OBV FRU K 2 HAS WRONG CHIRALITY AT ATOM C5 GLC L 1 HAS WRONG
CAVEAT 10 3OBV CHIRALITY AT ATOM C2 GLC L 1 HAS WRONG CHIRALITY AT ATOM C3
CAVEAT 11 3OBV FRU L 2 HAS WRONG CHIRALITY AT ATOM C4 FRU L 2 HAS WRONG
CAVEAT 12 3OBV CHIRALITY AT ATOM C5 GLC M 1 HAS WRONG CHIRALITY AT ATOM C2
CAVEAT 13 3OBV GLC M 1 HAS WRONG CHIRALITY AT ATOM C3 FRU M 2 HAS WRONG
CAVEAT 14 3OBV CHIRALITY AT ATOM C4 FRU M 2 HAS WRONG CHIRALITY AT ATOM C5
CAVEAT 15 3OBV GLC N 1 HAS WRONG CHIRALITY AT ATOM C2 GLC N 1 HAS WRONG
CAVEAT 16 3OBV CHIRALITY AT ATOM C3 GLC N 1 HAS WRONG CHIRALITY AT ATOM C4
CAVEAT 17 3OBV FRU N 2 HAS WRONG CHIRALITY AT ATOM C4 FRU N 2 HAS WRONG
CAVEAT 18 3OBV CHIRALITY AT ATOM C5 GLC O 1 HAS WRONG CHIRALITY AT ATOM C2
CAVEAT 19 3OBV GLC O 1 HAS WRONG CHIRALITY AT ATOM C3 FRU O 2 HAS WRONG
CAVEAT 20 3OBV CHIRALITY AT ATOM C4 FRU O 2 HAS WRONG CHIRALITY AT ATOM C5
CAVEAT 21 3OBV GLC P 1 HAS WRONG CHIRALITY AT ATOM C2 GLC P 1 HAS WRONG
CAVEAT 22 3OBV CHIRALITY AT ATOM C3 GLC P 1 HAS WRONG CHIRALITY AT ATOM C4
CAVEAT 23 3OBV FRU P 2 HAS WRONG CHIRALITY AT ATOM C4 FRU P 2 HAS WRONG
CAVEAT 24 3OBV CHIRALITY AT ATOM C5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN DIAPHANOUS HOMOLOG 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: N-TERMINAL FRAGMENT, UNP RESIDUES 131-457;
COMPND 5 SYNONYM: DIAPHANOUS-RELATED FORMIN-1, DRF1, P140MDIA, MDIA1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEIN DIAPHANOUS HOMOLOG 1;
COMPND 9 CHAIN: E, F, G, H;
COMPND 10 FRAGMENT: C-TERMINAL FRAGMENT, UNP RESIDUES 753-1209;
COMPND 11 SYNONYM: DIAPHANOUS-RELATED FORMIN-1, DRF1, P140MDIA, MDIA1;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: DIAPH1, DIAP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 GENE: DIAPH1, DIAP1;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS AUTOINHIBITION, ACTIN, NUCLEATION, CYTOSKELETON, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.TOMCHICK,M.K.ROSEN,T.OTOMO
REVDAT 5 21-FEB-24 3OBV 1 HETSYN
REVDAT 4 29-JUL-20 3OBV 1 CAVEAT COMPND REMARK HET
REVDAT 4 2 1 HETNAM FORMUL LINK SITE
REVDAT 4 3 1 ATOM
REVDAT 3 08-NOV-17 3OBV 1 REMARK
REVDAT 2 25-APR-12 3OBV 1 JRNL VERSN
REVDAT 1 24-NOV-10 3OBV 0
JRNL AUTH T.OTOMO,D.R.TOMCHICK,C.OTOMO,M.MACHIUS,M.K.ROSEN
JRNL TITL CRYSTAL STRUCTURE OF THE FORMIN MDIA1 IN AUTOINHIBITED
JRNL TITL 2 CONFORMATION.
JRNL REF PLOS ONE V. 5 12896 2010
JRNL REFN ESSN 1932-6203
JRNL PMID 20927343
JRNL DOI 10.1371/JOURNAL.PONE.0012896
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.4_486
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 122258
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.470
REMARK 3 FREE R VALUE TEST SET COUNT : 1799
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 29.9476 - 5.9110 0.99 12683 158 0.1761 0.2118
REMARK 3 2 5.9110 - 4.6976 1.00 12589 179 0.1891 0.2666
REMARK 3 3 4.6976 - 4.1055 1.00 12559 201 0.1585 0.2435
REMARK 3 4 4.1055 - 3.7309 1.00 12564 205 0.1801 0.2434
REMARK 3 5 3.7309 - 3.4639 1.00 12521 201 0.2116 0.2583
REMARK 3 6 3.4639 - 3.2599 1.00 12548 188 0.2296 0.2785
REMARK 3 7 3.2599 - 3.0968 1.00 12586 191 0.2654 0.3089
REMARK 3 8 3.0968 - 2.9622 1.00 12465 179 0.2736 0.3961
REMARK 3 9 2.9622 - 2.8482 0.92 11509 173 0.3026 0.3771
REMARK 3 10 2.8482 - 2.7500 0.67 8435 124 0.3524 0.4261
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 63.74
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 102.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.53600
REMARK 3 B22 (A**2) : 8.07510
REMARK 3 B33 (A**2) : -13.61110
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -8.34330
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 24585
REMARK 3 ANGLE : 1.350 33045
REMARK 3 CHIRALITY : 0.192 3716
REMARK 3 PLANARITY : 0.004 4293
REMARK 3 DIHEDRAL : 17.341 9940
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 35
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 131:196)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3642 4.5182 35.6115
REMARK 3 T TENSOR
REMARK 3 T11: 0.8199 T22: 0.6911
REMARK 3 T33: 0.7606 T12: 0.1593
REMARK 3 T13: 0.4517 T23: 0.1273
REMARK 3 L TENSOR
REMARK 3 L11: 0.4573 L22: 0.9241
REMARK 3 L33: 0.4505 L12: -0.1051
REMARK 3 L13: -0.4500 L23: -0.1454
REMARK 3 S TENSOR
REMARK 3 S11: -0.1035 S12: -0.1913 S13: -0.2532
REMARK 3 S21: 0.6706 S22: 0.0097 S23: 0.7434
REMARK 3 S31: -0.1682 S32: 0.0383 S33: 0.0002
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 197:452)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.9282 -6.4320 9.8969
REMARK 3 T TENSOR
REMARK 3 T11: 0.3132 T22: 0.2988
REMARK 3 T33: 0.4463 T12: 0.0830
REMARK 3 T13: 0.0622 T23: 0.0982
REMARK 3 L TENSOR
REMARK 3 L11: 0.2329 L22: 1.7049
REMARK 3 L33: 2.0179 L12: -0.5855
REMARK 3 L13: -0.8983 L23: 1.3654
REMARK 3 S TENSOR
REMARK 3 S11: 0.0873 S12: 0.0036 S13: -0.1013
REMARK 3 S21: 0.2132 S22: 0.0008 S23: 0.0335
REMARK 3 S31: 0.1473 S32: -0.0109 S33: -0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN E AND RESID 754:805)
REMARK 3 ORIGIN FOR THE GROUP (A): 75.9906 -62.9661 15.3700
REMARK 3 T TENSOR
REMARK 3 T11: 0.6678 T22: 0.5989
REMARK 3 T33: 0.4732 T12: 0.1216
REMARK 3 T13: -0.2165 T23: -0.2296
REMARK 3 L TENSOR
REMARK 3 L11: 0.1192 L22: 0.2630
REMARK 3 L33: 0.3685 L12: -0.2328
REMARK 3 L13: 0.2546 L23: -0.3034
REMARK 3 S TENSOR
REMARK 3 S11: 0.1907 S12: -0.7586 S13: -0.2419
REMARK 3 S21: 1.1365 S22: 0.0397 S23: -0.6864
REMARK 3 S31: -0.2750 S32: 0.3306 S33: -0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN E AND RESID 829:937)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6773 -72.8829 30.9930
REMARK 3 T TENSOR
REMARK 3 T11: 0.8269 T22: 1.1713
REMARK 3 T33: 0.6218 T12: 0.1890
REMARK 3 T13: 0.1822 T23: 0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 0.4933 L22: 0.6933
REMARK 3 L33: 0.5434 L12: -0.2062
REMARK 3 L13: 0.3479 L23: 0.6101
REMARK 3 S TENSOR
REMARK 3 S11: -0.1010 S12: 0.0052 S13: -0.1994
REMARK 3 S21: 0.3712 S22: 0.0403 S23: -0.0872
REMARK 3 S31: 0.0893 S32: -0.3486 S33: 0.0001
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN E AND RESID 938:1118)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5049 -58.4560 -10.2904
REMARK 3 T TENSOR
REMARK 3 T11: 0.3905 T22: 0.7891
REMARK 3 T33: 0.4761 T12: 0.0618
REMARK 3 T13: -0.1237 T23: 0.0610
REMARK 3 L TENSOR
REMARK 3 L11: 0.8590 L22: 0.2938
REMARK 3 L33: 1.4380 L12: -0.5317
REMARK 3 L13: 0.5490 L23: 0.3047
REMARK 3 S TENSOR
REMARK 3 S11: -0.1301 S12: 0.0919 S13: 0.1803
REMARK 3 S21: -0.2789 S22: 0.2306 S23: 0.1929
REMARK 3 S31: 0.1721 S32: -0.8299 S33: -0.0015
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN E AND RESID 1119:1173)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.0772 -31.6057 -35.8582
REMARK 3 T TENSOR
REMARK 3 T11: 0.7014 T22: 0.5479
REMARK 3 T33: 0.4300 T12: 0.0098
REMARK 3 T13: -0.0665 T23: 0.1149
REMARK 3 L TENSOR
REMARK 3 L11: 0.1663 L22: 0.1235
REMARK 3 L33: 0.2499 L12: 0.1899
REMARK 3 L13: -0.7064 L23: 0.2728
REMARK 3 S TENSOR
REMARK 3 S11: -0.2385 S12: 0.1709 S13: -0.2937
REMARK 3 S21: -0.3738 S22: 0.1800 S23: -0.3025
REMARK 3 S31: 0.1354 S32: -0.2062 S33: -0.0003
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN E AND RESID 1174:1195)
REMARK 3 ORIGIN FOR THE GROUP (A): 66.8527 -1.9239 -55.2481
REMARK 3 T TENSOR
REMARK 3 T11: 0.9559 T22: 0.5786
REMARK 3 T33: 0.5220 T12: 0.0222
REMARK 3 T13: 0.1575 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 0.0335 L22: 0.0455
REMARK 3 L33: 0.0345 L12: 0.0566
REMARK 3 L13: 0.0353 L23: 0.0603
REMARK 3 S TENSOR
REMARK 3 S11: 0.3157 S12: 0.2247 S13: 0.5830
REMARK 3 S21: 0.4564 S22: -0.1841 S23: -0.8978
REMARK 3 S31: 0.0121 S32: 0.3104 S33: 0.0013
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 132:192)
REMARK 3 ORIGIN FOR THE GROUP (A): 90.5080 -2.8810 -57.4610
REMARK 3 T TENSOR
REMARK 3 T11: 0.7715 T22: 1.2358
REMARK 3 T33: 0.8451 T12: -0.1148
REMARK 3 T13: 0.5644 T23: -0.0432
REMARK 3 L TENSOR
REMARK 3 L11: 0.1651 L22: 0.1471
REMARK 3 L33: 0.0794 L12: 0.1997
REMARK 3 L13: 0.0983 L23: 0.1379
REMARK 3 S TENSOR
REMARK 3 S11: -0.5154 S12: 0.5882 S13: -0.3041
REMARK 3 S21: -1.1252 S22: 0.2408 S23: -0.9489
REMARK 3 S31: -0.7754 S32: 0.0946 S33: -0.0034
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 200:457)
REMARK 3 ORIGIN FOR THE GROUP (A): 64.4752 -8.3693 -30.2973
REMARK 3 T TENSOR
REMARK 3 T11: 0.2903 T22: 0.4768
REMARK 3 T33: 0.3938 T12: 0.1168
REMARK 3 T13: 0.1324 T23: -0.0656
REMARK 3 L TENSOR
REMARK 3 L11: 0.8128 L22: 1.4211
REMARK 3 L33: 1.6446 L12: 1.0504
REMARK 3 L13: -0.9381 L23: -0.7843
REMARK 3 S TENSOR
REMARK 3 S11: 0.0541 S12: 0.2082 S13: -0.1967
REMARK 3 S21: -0.1259 S22: 0.1467 S23: -0.1807
REMARK 3 S31: -0.0510 S32: 0.1395 S33: -0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN F AND RESID 754:805)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5478 -53.5174 -38.3801
REMARK 3 T TENSOR
REMARK 3 T11: 0.9444 T22: 1.2204
REMARK 3 T33: 0.6199 T12: 0.0762
REMARK 3 T13: -0.2518 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 0.1497 L22: -0.0289
REMARK 3 L33: 0.0681 L12: 0.2084
REMARK 3 L13: 0.1340 L23: 0.1192
REMARK 3 S TENSOR
REMARK 3 S11: -0.0381 S12: 0.1491 S13: -0.1475
REMARK 3 S21: -0.9998 S22: 0.0416 S23: 0.2847
REMARK 3 S31: -0.1169 S32: -0.0722 S33: -0.0001
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN F AND RESID 830:939)
REMARK 3 ORIGIN FOR THE GROUP (A): 66.0866 -77.7873 -53.6573
REMARK 3 T TENSOR
REMARK 3 T11: 1.0209 T22: 1.4803
REMARK 3 T33: 0.8008 T12: 0.2263
REMARK 3 T13: -0.0248 T23: -0.3255
REMARK 3 L TENSOR
REMARK 3 L11: 0.2984 L22: 0.5611
REMARK 3 L33: 0.2531 L12: -0.5785
REMARK 3 L13: 0.4825 L23: -0.5144
REMARK 3 S TENSOR
REMARK 3 S11: 0.4435 S12: 0.5574 S13: -0.3543
REMARK 3 S21: -0.6518 S22: -0.6175 S23: 0.0117
REMARK 3 S31: -0.3100 S32: -0.2145 S33: -0.0008
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN F AND RESID 940:1118)
REMARK 3 ORIGIN FOR THE GROUP (A): 76.6318 -67.6578 -12.6405
REMARK 3 T TENSOR
REMARK 3 T11: 0.5171 T22: 0.4565
REMARK 3 T33: 0.6786 T12: -0.0821
REMARK 3 T13: 0.0216 T23: -0.1094
REMARK 3 L TENSOR
REMARK 3 L11: 0.6241 L22: 0.1819
REMARK 3 L33: 0.9295 L12: -0.2287
REMARK 3 L13: -0.1339 L23: 0.3789
REMARK 3 S TENSOR
REMARK 3 S11: -0.0200 S12: 0.0219 S13: 0.1588
REMARK 3 S21: 0.0907 S22: 0.1047 S23: -0.3991
REMARK 3 S31: 0.0457 S32: -0.0832 S33: 0.0002
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN F AND RESID 1119:1170)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.4755 -36.3221 12.4729
REMARK 3 T TENSOR
REMARK 3 T11: 0.7686 T22: 0.4940
REMARK 3 T33: 0.5525 T12: 0.1788
REMARK 3 T13: -0.1455 T23: -0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 0.1699 L22: -0.0692
REMARK 3 L33: 0.4734 L12: -0.2025
REMARK 3 L13: -1.0604 L23: 0.0604
REMARK 3 S TENSOR
REMARK 3 S11: 0.0136 S12: 0.0988 S13: 0.1462
REMARK 3 S21: 0.5185 S22: 0.2559 S23: -0.6164
REMARK 3 S31: 0.1851 S32: -0.1977 S33: -0.0001
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN F AND RESID 1171:1196)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.3694 -3.7313 34.9292
REMARK 3 T TENSOR
REMARK 3 T11: 0.9372 T22: 0.4566
REMARK 3 T33: 0.5804 T12: 0.0679
REMARK 3 T13: 0.1321 T23: 0.2302
REMARK 3 L TENSOR
REMARK 3 L11: 0.1991 L22: 0.0578
REMARK 3 L33: 0.0181 L12: -0.0484
REMARK 3 L13: 0.0652 L23: 0.0228
REMARK 3 S TENSOR
REMARK 3 S11: -0.0105 S12: -0.8598 S13: 0.2870
REMARK 3 S21: 0.1915 S22: 0.1746 S23: 0.2289
REMARK 3 S31: 0.4802 S32: 0.2470 S33: 0.0004
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 131:196)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7646 13.5756 -39.6281
REMARK 3 T TENSOR
REMARK 3 T11: 0.6266 T22: 0.4502
REMARK 3 T33: 0.4686 T12: -0.0372
REMARK 3 T13: -0.2714 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.6593 L22: 1.1280
REMARK 3 L33: 0.5355 L12: -0.0181
REMARK 3 L13: 0.6240 L23: 0.1297
REMARK 3 S TENSOR
REMARK 3 S11: -0.0592 S12: 0.1379 S13: -0.0467
REMARK 3 S21: -0.6950 S22: -0.1426 S23: 0.4952
REMARK 3 S31: 0.0096 S32: 0.1248 S33: -0.0001
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN C AND RESID 197:452)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.4087 24.5084 -10.6802
REMARK 3 T TENSOR
REMARK 3 T11: 0.2342 T22: 0.2065
REMARK 3 T33: 0.3592 T12: -0.0253
REMARK 3 T13: -0.0283 T23: 0.0657
REMARK 3 L TENSOR
REMARK 3 L11: 0.3126 L22: 1.5075
REMARK 3 L33: 2.6027 L12: 0.4141
REMARK 3 L13: 0.9838 L23: 1.4632
REMARK 3 S TENSOR
REMARK 3 S11: 0.0369 S12: 0.0229 S13: 0.0535
REMARK 3 S21: -0.0963 S22: 0.0029 S23: 0.0607
REMARK 3 S31: -0.0738 S32: 0.0150 S33: -0.0001
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN G AND RESID 754:805)
REMARK 3 ORIGIN FOR THE GROUP (A): 78.0765 80.9479 -10.9355
REMARK 3 T TENSOR
REMARK 3 T11: 0.9557 T22: 1.0514
REMARK 3 T33: 0.8199 T12: -0.1077
REMARK 3 T13: 0.2215 T23: -0.2172
REMARK 3 L TENSOR
REMARK 3 L11: 0.0697 L22: 0.0435
REMARK 3 L33: 0.0906 L12: 0.0360
REMARK 3 L13: 0.0877 L23: -0.0904
REMARK 3 S TENSOR
REMARK 3 S11: 0.1231 S12: 0.6248 S13: 0.4695
REMARK 3 S21: -0.8384 S22: -0.3360 S23: -0.3731
REMARK 3 S31: 0.5653 S32: 0.1469 S33: -0.0002
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN G AND RESID 829:937)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7648 91.0239 -34.6279
REMARK 3 T TENSOR
REMARK 3 T11: 1.0420 T22: 0.8383
REMARK 3 T33: 0.4394 T12: -0.2962
REMARK 3 T13: -0.2876 T23: 0.1146
REMARK 3 L TENSOR
REMARK 3 L11: 0.4410 L22: 0.8155
REMARK 3 L33: 0.2195 L12: -0.3082
REMARK 3 L13: 0.0470 L23: 0.1728
REMARK 3 S TENSOR
REMARK 3 S11: -0.0341 S12: -0.1492 S13: -0.0343
REMARK 3 S21: -0.7408 S22: 0.2242 S23: 0.0223
REMARK 3 S31: 0.3133 S32: -0.2846 S33: 0.0004
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN G AND RESID 938:1118)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4465 76.6421 5.1441
REMARK 3 T TENSOR
REMARK 3 T11: 0.3196 T22: 0.8531
REMARK 3 T33: 0.7490 T12: -0.2430
REMARK 3 T13: -0.0275 T23: 0.3175
REMARK 3 L TENSOR
REMARK 3 L11: 0.2477 L22: 0.1975
REMARK 3 L33: 1.1072 L12: 0.0585
REMARK 3 L13: -0.3654 L23: 0.3049
REMARK 3 S TENSOR
REMARK 3 S11: 0.0055 S12: 0.0178 S13: -0.0430
REMARK 3 S21: 0.0029 S22: 0.4286 S23: 0.4441
REMARK 3 S31: 0.1041 S32: -0.4945 S33: 0.0002
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN G AND RESID 1119:1173)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7767 49.7306 34.7126
REMARK 3 T TENSOR
REMARK 3 T11: 0.6224 T22: 0.7189
REMARK 3 T33: 0.5415 T12: 0.0860
REMARK 3 T13: 0.1512 T23: 0.0870
REMARK 3 L TENSOR
REMARK 3 L11: 0.2154 L22: 0.0002
REMARK 3 L33: 0.3853 L12: 0.1042
REMARK 3 L13: 0.4740 L23: 0.1434
REMARK 3 S TENSOR
REMARK 3 S11: -0.1791 S12: 0.0295 S13: -0.1052
REMARK 3 S21: 0.1619 S22: 0.3644 S23: 0.2247
REMARK 3 S31: 0.1036 S32: -0.0525 S33: -0.0002
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN G AND RESID 1174:1196)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.5989 19.9772 56.7867
REMARK 3 T TENSOR
REMARK 3 T11: 0.6702 T22: 0.4739
REMARK 3 T33: 0.4336 T12: 0.0638
REMARK 3 T13: -0.0353 T23: -0.0323
REMARK 3 L TENSOR
REMARK 3 L11: 0.0355 L22: 0.0861
REMARK 3 L33: 0.0291 L12: -0.0515
REMARK 3 L13: 0.0393 L23: 0.0369
REMARK 3 S TENSOR
REMARK 3 S11: 0.0480 S12: -0.6775 S13: -0.3266
REMARK 3 S21: -0.1008 S22: -0.0781 S23: -0.3551
REMARK 3 S31: 0.1139 S32: -0.0608 S33: 0.0010
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN D AND RESID 131:196)
REMARK 3 ORIGIN FOR THE GROUP (A): 81.6142 21.1335 62.2283
REMARK 3 T TENSOR
REMARK 3 T11: 0.7549 T22: 0.8070
REMARK 3 T33: 0.5217 T12: 0.1681
REMARK 3 T13: -0.3242 T23: 0.0797
REMARK 3 L TENSOR
REMARK 3 L11: 0.4558 L22: 0.7168
REMARK 3 L33: 0.3801 L12: -0.0527
REMARK 3 L13: 0.5010 L23: 0.0763
REMARK 3 S TENSOR
REMARK 3 S11: -0.7090 S12: -0.0844 S13: 0.2481
REMARK 3 S21: 0.7869 S22: 0.2381 S23: -0.4928
REMARK 3 S31: 0.1445 S32: -0.1765 S33: -0.0001
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN D AND RESID 197:457)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.9548 26.3321 32.7022
REMARK 3 T TENSOR
REMARK 3 T11: 0.2904 T22: 0.2703
REMARK 3 T33: 0.2490 T12: -0.0150
REMARK 3 T13: -0.0685 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.6571 L22: 1.0648
REMARK 3 L33: 2.5430 L12: -1.0437
REMARK 3 L13: 1.3065 L23: -1.3234
REMARK 3 S TENSOR
REMARK 3 S11: 0.0297 S12: -0.0999 S13: 0.0943
REMARK 3 S21: 0.0753 S22: 0.0709 S23: 0.0437
REMARK 3 S31: 0.0572 S32: 0.0607 S33: -0.0000
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN H AND RESID 753:804)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4957 71.6040 32.8806
REMARK 3 T TENSOR
REMARK 3 T11: 0.9357 T22: 1.3986
REMARK 3 T33: 0.8966 T12: -0.0542
REMARK 3 T13: 0.1715 T23: 0.1588
REMARK 3 L TENSOR
REMARK 3 L11: 0.1473 L22: 0.0051
REMARK 3 L33: 0.0413 L12: -0.0866
REMARK 3 L13: -0.1521 L23: 0.0665
REMARK 3 S TENSOR
REMARK 3 S11: -0.0473 S12: 0.4916 S13: 0.6426
REMARK 3 S21: 1.0482 S22: -0.1048 S23: 0.5929
REMARK 3 S31: -0.3197 S32: 0.2269 S33: -0.0006
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN H AND RESID 830:937)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.4551 96.1564 56.2745
REMARK 3 T TENSOR
REMARK 3 T11: 0.7187 T22: 0.8032
REMARK 3 T33: 0.5685 T12: -0.1472
REMARK 3 T13: 0.1460 T23: -0.2126
REMARK 3 L TENSOR
REMARK 3 L11: 0.4660 L22: 0.4782
REMARK 3 L33: 0.2821 L12: 0.5879
REMARK 3 L13: -0.1169 L23: -0.0494
REMARK 3 S TENSOR
REMARK 3 S11: 0.1072 S12: 0.2730 S13: 0.0879
REMARK 3 S21: 0.3184 S22: -0.4018 S23: -0.0413
REMARK 3 S31: 0.0760 S32: -0.2086 S33: -0.0001
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN H AND RESID 938:1118)
REMARK 3 ORIGIN FOR THE GROUP (A): 74.2532 85.6805 16.9168
REMARK 3 T TENSOR
REMARK 3 T11: 0.3794 T22: 0.4639
REMARK 3 T33: 0.6082 T12: -0.0580
REMARK 3 T13: 0.0588 T23: -0.1015
REMARK 3 L TENSOR
REMARK 3 L11: 0.3835 L22: 0.3129
REMARK 3 L33: 1.1976 L12: -0.2344
REMARK 3 L13: 0.0221 L23: 0.1814
REMARK 3 S TENSOR
REMARK 3 S11: 0.0908 S12: 0.0297 S13: -0.0264
REMARK 3 S21: -0.1474 S22: 0.0207 S23: -0.2728
REMARK 3 S31: -0.1293 S32: -0.1439 S33: 0.0001
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN H AND RESID 1119:1173)
REMARK 3 ORIGIN FOR THE GROUP (A): 58.3058 53.0413 -12.3410
REMARK 3 T TENSOR
REMARK 3 T11: 0.6617 T22: 0.5826
REMARK 3 T33: 0.6221 T12: -0.2464
REMARK 3 T13: 0.1293 T23: -0.0675
REMARK 3 L TENSOR
REMARK 3 L11: 0.0436 L22: 0.9644
REMARK 3 L33: 1.2731 L12: 0.8245
REMARK 3 L13: 1.2570 L23: 1.0814
REMARK 3 S TENSOR
REMARK 3 S11: 0.0454 S12: -0.0164 S13: -0.0653
REMARK 3 S21: -0.2450 S22: 0.4320 S23: -0.6274
REMARK 3 S31: -0.0108 S32: -0.0811 S33: 0.0572
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN A AND RESID 2001:2001)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6156 -9.4948 4.7996
REMARK 3 T TENSOR
REMARK 3 T11: 2.1835 T22: 2.2803
REMARK 3 T33: 1.7221 T12: 0.2728
REMARK 3 T13: 0.5505 T23: 0.2496
REMARK 3 L TENSOR
REMARK 3 L11: 0.0004 L22: 0.0016
REMARK 3 L33: -0.0004 L12: -0.0014
REMARK 3 L13: -0.0002 L23: 0.0005
REMARK 3 S TENSOR
REMARK 3 S11: -0.0392 S12: -0.0091 S13: 0.0199
REMARK 3 S21: -0.0970 S22: -0.0811 S23: -0.0452
REMARK 3 S31: 0.0150 S32: 0.0216 S33: -0.0005
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN B AND RESID 2002:2002)
REMARK 3 ORIGIN FOR THE GROUP (A): 73.8500 -14.9538 -25.5541
REMARK 3 T TENSOR
REMARK 3 T11: 2.0555 T22: 2.3211
REMARK 3 T33: 1.2330 T12: -0.2216
REMARK 3 T13: -0.4534 T23: -0.2872
REMARK 3 L TENSOR
REMARK 3 L11: 0.0015 L22: 0.0018
REMARK 3 L33: -0.0005 L12: 0.0021
REMARK 3 L13: -0.0003 L23: 0.0013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0647 S12: -0.0235 S13: 0.0315
REMARK 3 S21: -0.0271 S22: -0.0529 S23: 0.0375
REMARK 3 S31: 0.1094 S32: -0.1019 S33: 0.0004
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: (CHAIN D AND RESID 2003:2003)
REMARK 3 ORIGIN FOR THE GROUP (A): 69.5681 33.1770 29.6847
REMARK 3 T TENSOR
REMARK 3 T11: 1.7966 T22: 2.2848
REMARK 3 T33: 1.7640 T12: -0.0395
REMARK 3 T13: 0.5323 T23: -0.5641
REMARK 3 L TENSOR
REMARK 3 L11: 0.0014 L22: 0.0011
REMARK 3 L33: -0.0007 L12: -0.0021
REMARK 3 L13: -0.0001 L23: 0.0012
REMARK 3 S TENSOR
REMARK 3 S11: -0.0321 S12: 0.0038 S13: -0.0148
REMARK 3 S21: -0.0330 S22: -0.0974 S23: -0.0148
REMARK 3 S31: -0.1575 S32: 0.0059 S33: 0.0004
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: (CHAIN C AND RESID 2004:2004)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.5591 27.8654 -6.9880
REMARK 3 T TENSOR
REMARK 3 T11: 2.1244 T22: 2.5277
REMARK 3 T33: 1.9587 T12: -0.3801
REMARK 3 T13: 0.2439 T23: 0.2499
REMARK 3 L TENSOR
REMARK 3 L11: 0.0015 L22: 0.0011
REMARK 3 L33: -0.0004 L12: 0.0014
REMARK 3 L13: 0.0002 L23: -0.0005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0139 S12: -0.0111 S13: -0.0480
REMARK 3 S21: 0.0893 S22: -0.0192 S23: 0.0247
REMARK 3 S31: -0.0033 S32: -0.0052 S33: -0.0002
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: (CHAIN A AND RESID 2005:2005)
REMARK 3 ORIGIN FOR THE GROUP (A): 61.6902 -13.9861 -0.2335
REMARK 3 T TENSOR
REMARK 3 T11: 2.1085 T22: 2.6467
REMARK 3 T33: 2.1397 T12: -0.1235
REMARK 3 T13: 0.0614 T23: 0.1551
REMARK 3 L TENSOR
REMARK 3 L11: 0.0005 L22: 0.0007
REMARK 3 L33: 0.0014 L12: 0.0002
REMARK 3 L13: 0.0005 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: -0.0326 S13: -0.0085
REMARK 3 S21: -0.0148 S22: 0.0197 S23: -0.0257
REMARK 3 S31: -0.0264 S32: -0.0085 S33: -0.0005
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: (CHAIN B AND RESID 2006:2006)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.1712 -9.7798 -20.5871
REMARK 3 T TENSOR
REMARK 3 T11: 2.6407 T22: 2.5133
REMARK 3 T33: 1.6628 T12: 0.4723
REMARK 3 T13: 0.2298 T23: 0.8114
REMARK 3 L TENSOR
REMARK 3 L11: 0.0017 L22: 0.0020
REMARK 3 L33: 0.0010 L12: 0.0007
REMARK 3 L13: 0.0010 L23: 0.0021
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: -0.0234 S13: 0.0310
REMARK 3 S21: -0.0027 S22: 0.0017 S23: 0.0060
REMARK 3 S31: -0.0505 S32: 0.0014 S33: 0.0001
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: (CHAIN D AND RESID 2007:2007)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.3846 28.1832 20.1186
REMARK 3 T TENSOR
REMARK 3 T11: 3.0803 T22: 1.8218
REMARK 3 T33: 1.7017 T12: -0.0534
REMARK 3 T13: -0.4888 T23: 0.7405
REMARK 3 L TENSOR
REMARK 3 L11: 0.0012 L22: 0.0012
REMARK 3 L33: 0.0010 L12: -0.0010
REMARK 3 L13: -0.0003 L23: 0.0006
REMARK 3 S TENSOR
REMARK 3 S11: -0.0195 S12: -0.0016 S13: 0.0338
REMARK 3 S21: 0.0214 S22: 0.0380 S23: -0.0434
REMARK 3 S31: 0.0097 S32: 0.0218 S33: -0.0004
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: (CHAIN C AND RESID 2008:2008)
REMARK 3 ORIGIN FOR THE GROUP (A): 61.7059 32.4148 1.9585
REMARK 3 T TENSOR
REMARK 3 T11: 2.0488 T22: 2.3148
REMARK 3 T33: 2.7138 T12: 0.2318
REMARK 3 T13: 0.3355 T23: -0.1313
REMARK 3 L TENSOR
REMARK 3 L11: 0.0014 L22: 0.0002
REMARK 3 L33: 0.0005 L12: 0.0001
REMARK 3 L13: 0.0000 L23: 0.0005
REMARK 3 S TENSOR
REMARK 3 S11: -0.0111 S12: 0.0487 S13: 0.0214
REMARK 3 S21: -0.0164 S22: -0.0529 S23: -0.0206
REMARK 3 S31: 0.0043 S32: 0.0296 S33: -0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 138:161 OR RESSEQ
REMARK 3 177:192 OR RESSEQ 201:444) AND CHAIN E
REMARK 3 AND (RESSEQ 754: 805 OR RESSEQ 835:879 OR
REMARK 3 RESSEQ 881:898 OR RESSEQ 900:1195 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 138:161 OR RESSEQ
REMARK 3 177:192 OR RESSEQ 201:444) AND CHAIN G
REMARK 3 AND (RESSEQ 754: 805 OR RESSEQ 835:879 OR
REMARK 3 RESSEQ 881:898 OR RESSEQ 900::1195 )
REMARK 3 ATOM PAIRS NUMBER : 5633
REMARK 3 RMSD : 0.039
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 138:161 OR RESSEQ
REMARK 3 177:192 OR RESSEQ 201:444) AND CHAIN F
REMARK 3 AND (RESSEQ 754: 805 OR RESSEQ 835:879 OR
REMARK 3 RESSEQ 881:898 OR RESSEQ 900:1195 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 138:161 OR RESSEQ
REMARK 3 177:192 OR RESSEQ 201:444) AND CHAIN H
REMARK 3 AND (RESSEQ 754: 805 OR RESSEQ 835:879 OR
REMARK 3 RESSEQ 881:898 OR RESSEQ 900:1195 )
REMARK 3 ATOM PAIRS NUMBER : 5626
REMARK 3 RMSD : 0.068
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3OBV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000060919.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.75
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97937
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-3
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123292
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.54100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD, MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE, MLPHARE, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 1500, 25% SUCROSE, 0.1 M MES
REMARK 280 PH 6.75, 0.15 M NACL, 1 MM DTT, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 104.25950
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: THE BIOMOLECULE IS A DIMER. THERE ARE TWO BIOMOLECULE IN
REMARK 300 THE ASYMMETRIC UNIT. BIOMOLECULE ONE WHICH CONTAINS CHAIN A, E, B,
REMARK 300 AND F, BIOMOLECULE TWO CONTAINS CHAIN C, G, D AND H
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 76780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -137.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, B, F, I, J, K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 22040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 77630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -136.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G, D, H, M, N, O, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 AUTHOR STATE THAT THE LOOP REGION OF PROTEIN DIAPHANOUS HOMOLOG 1
REMARK 400 WAS REMOVED FOR CRYSTALLIZATION. THERE ARE FOUR COPIES OF PROTEIN
REMARK 400 DIAPHANOUS HOMOLOG 1 IN THE ASYMMETRIC UNTI MADE OF N-
REMARK 400 TERMINAL(CHAIN A,B,C,D) AND C-TERMINAL(E,F,G,H) OF THE PROTEIN
REMARK 400 RESPECTIVELY
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 GLU A 453
REMARK 465 ARG A 454
REMARK 465 LEU A 455
REMARK 465 VAL A 456
REMARK 465 ASP A 457
REMARK 465 LYS E 753
REMARK 465 THR E 806
REMARK 465 LYS E 807
REMARK 465 THR E 808
REMARK 465 SER E 809
REMARK 465 LYS E 810
REMARK 465 ALA E 811
REMARK 465 LYS E 812
REMARK 465 LYS E 813
REMARK 465 ASP E 814
REMARK 465 GLN E 815
REMARK 465 GLU E 816
REMARK 465 GLY E 817
REMARK 465 GLY E 818
REMARK 465 GLU E 819
REMARK 465 GLU E 820
REMARK 465 LYS E 821
REMARK 465 LYS E 822
REMARK 465 SER E 823
REMARK 465 VAL E 824
REMARK 465 GLN E 825
REMARK 465 LYS E 826
REMARK 465 LYS E 827
REMARK 465 LYS E 828
REMARK 465 ARG E 1196
REMARK 465 ARG E 1197
REMARK 465 LYS E 1198
REMARK 465 ARG E 1199
REMARK 465 GLY E 1200
REMARK 465 PRO E 1201
REMARK 465 ARG E 1202
REMARK 465 GLN E 1203
REMARK 465 VAL E 1204
REMARK 465 ASN E 1205
REMARK 465 ARG E 1206
REMARK 465 LYS E 1207
REMARK 465 ALA E 1208
REMARK 465 GLY E 1209
REMARK 465 GLU B 131
REMARK 465 LYS B 193
REMARK 465 GLU B 194
REMARK 465 GLU B 195
REMARK 465 THR B 196
REMARK 465 SER B 197
REMARK 465 GLY B 198
REMARK 465 ASN B 199
REMARK 465 LYS F 753
REMARK 465 THR F 806
REMARK 465 LYS F 807
REMARK 465 THR F 808
REMARK 465 SER F 809
REMARK 465 LYS F 810
REMARK 465 ALA F 811
REMARK 465 LYS F 812
REMARK 465 LYS F 813
REMARK 465 ASP F 814
REMARK 465 GLN F 815
REMARK 465 GLU F 816
REMARK 465 GLY F 817
REMARK 465 GLY F 818
REMARK 465 GLU F 819
REMARK 465 GLU F 820
REMARK 465 LYS F 821
REMARK 465 LYS F 822
REMARK 465 SER F 823
REMARK 465 VAL F 824
REMARK 465 GLN F 825
REMARK 465 LYS F 826
REMARK 465 LYS F 827
REMARK 465 LYS F 828
REMARK 465 VAL F 829
REMARK 465 ARG F 1197
REMARK 465 LYS F 1198
REMARK 465 ARG F 1199
REMARK 465 GLY F 1200
REMARK 465 PRO F 1201
REMARK 465 ARG F 1202
REMARK 465 GLN F 1203
REMARK 465 VAL F 1204
REMARK 465 ASN F 1205
REMARK 465 ARG F 1206
REMARK 465 LYS F 1207
REMARK 465 ALA F 1208
REMARK 465 GLY F 1209
REMARK 465 GLU C 453
REMARK 465 ARG C 454
REMARK 465 LEU C 455
REMARK 465 VAL C 456
REMARK 465 ASP C 457
REMARK 465 LYS G 753
REMARK 465 THR G 806
REMARK 465 LYS G 807
REMARK 465 THR G 808
REMARK 465 SER G 809
REMARK 465 LYS G 810
REMARK 465 ALA G 811
REMARK 465 LYS G 812
REMARK 465 LYS G 813
REMARK 465 ASP G 814
REMARK 465 GLN G 815
REMARK 465 GLU G 816
REMARK 465 GLY G 817
REMARK 465 GLY G 818
REMARK 465 GLU G 819
REMARK 465 GLU G 820
REMARK 465 LYS G 821
REMARK 465 LYS G 822
REMARK 465 SER G 823
REMARK 465 VAL G 824
REMARK 465 GLN G 825
REMARK 465 LYS G 826
REMARK 465 LYS G 827
REMARK 465 LYS G 828
REMARK 465 ARG G 1197
REMARK 465 LYS G 1198
REMARK 465 ARG G 1199
REMARK 465 GLY G 1200
REMARK 465 PRO G 1201
REMARK 465 ARG G 1202
REMARK 465 GLN G 1203
REMARK 465 VAL G 1204
REMARK 465 ASN G 1205
REMARK 465 ARG G 1206
REMARK 465 LYS G 1207
REMARK 465 ALA G 1208
REMARK 465 GLY G 1209
REMARK 465 GLN H 805
REMARK 465 THR H 806
REMARK 465 LYS H 807
REMARK 465 THR H 808
REMARK 465 SER H 809
REMARK 465 LYS H 810
REMARK 465 ALA H 811
REMARK 465 LYS H 812
REMARK 465 LYS H 813
REMARK 465 ASP H 814
REMARK 465 GLN H 815
REMARK 465 GLU H 816
REMARK 465 GLY H 817
REMARK 465 GLY H 818
REMARK 465 GLU H 819
REMARK 465 GLU H 820
REMARK 465 LYS H 821
REMARK 465 LYS H 822
REMARK 465 SER H 823
REMARK 465 VAL H 824
REMARK 465 GLN H 825
REMARK 465 LYS H 826
REMARK 465 LYS H 827
REMARK 465 LYS H 828
REMARK 465 VAL H 829
REMARK 465 ARG H 1197
REMARK 465 LYS H 1198
REMARK 465 ARG H 1199
REMARK 465 GLY H 1200
REMARK 465 PRO H 1201
REMARK 465 ARG H 1202
REMARK 465 GLN H 1203
REMARK 465 VAL H 1204
REMARK 465 ASN H 1205
REMARK 465 ARG H 1206
REMARK 465 LYS H 1207
REMARK 465 ALA H 1208
REMARK 465 GLY H 1209
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN F 932 CD GLN F 932 OE1 -0.135
REMARK 500 GLN F 932 CD GLN F 932 NE2 -0.188
REMARK 500 GLN H 932 CD GLN H 932 OE1 -0.134
REMARK 500 GLN H 932 CD GLN H 932 NE2 -0.195
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 132 152.27 -46.03
REMARK 500 ASP A 149 -134.87 46.08
REMARK 500 GLU A 195 31.23 -94.06
REMARK 500 VAL A 243 69.73 -115.23
REMARK 500 LYS E 757 80.42 -153.41
REMARK 500 ASN E 766 37.74 -80.60
REMARK 500 TRP E 767 170.96 -54.25
REMARK 500 GLU E 773 -128.88 -52.45
REMARK 500 GLN E 777 -82.38 -142.85
REMARK 500 VAL E 834 -56.31 -130.95
REMARK 500 ARG E 851 77.96 58.41
REMARK 500 ASN E 865 95.45 -58.18
REMARK 500 ALA E 996 -84.67 -39.67
REMARK 500 GLN E 998 39.51 -68.49
REMARK 500 HIS E1014 55.37 -156.59
REMARK 500 LEU E1018 0.35 -68.68
REMARK 500 LEU E1024 55.71 -116.88
REMARK 500 PHE E1069 -71.47 -72.40
REMARK 500 VAL E1070 -16.99 -46.77
REMARK 500 VAL E1077 -19.28 -49.82
REMARK 500 VAL E1106 72.17 67.64
REMARK 500 MET E1172 36.36 -68.33
REMARK 500 ASN E1173 -18.76 -147.54
REMARK 500 ALA E1174 -94.15 -72.90
REMARK 500 ASP B 149 -123.43 34.86
REMARK 500 ASN B 165 -33.58 -132.18
REMARK 500 VAL B 243 71.90 -103.63
REMARK 500 ASN B 346 116.34 -163.06
REMARK 500 MET B 378 74.39 -105.19
REMARK 500 GLU F 773 -91.38 -23.19
REMARK 500 GLN F 777 -90.95 -151.96
REMARK 500 CYS F 779 -156.50 -79.73
REMARK 500 LYS F 783 35.29 -82.89
REMARK 500 ALA F 804 76.58 -109.23
REMARK 500 VAL F 834 -56.76 -148.29
REMARK 500 ILE F 845 -81.25 -70.37
REMARK 500 PHE F 846 -55.52 -25.63
REMARK 500 ARG F 851 87.26 63.58
REMARK 500 LYS F 894 4.34 -64.91
REMARK 500 ILE F 936 -47.93 -130.59
REMARK 500 ILE F 984 -15.09 -45.36
REMARK 500 ALA F 996 -72.33 -38.88
REMARK 500 GLN F 998 36.81 -62.89
REMARK 500 HIS F1014 54.21 -157.99
REMARK 500 LEU F1018 -12.15 -49.07
REMARK 500 LYS F1068 40.07 -77.77
REMARK 500 PHE F1069 -91.34 -78.76
REMARK 500 VAL F1070 -38.48 -28.48
REMARK 500 MET F1090 -38.56 -38.81
REMARK 500 VAL F1106 76.40 61.23
REMARK 500
REMARK 500 THIS ENTRY HAS 108 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V9D RELATED DB: PDB
REMARK 900 RELATED ID: 2BNX RELATED DB: PDB
DBREF 3OBV A 131 457 UNP O08808 DIAP1_MOUSE 131 457
DBREF 3OBV E 753 1209 UNP O08808 DIAP1_MOUSE 753 1209
DBREF 3OBV B 131 457 UNP O08808 DIAP1_MOUSE 131 457
DBREF 3OBV F 753 1209 UNP O08808 DIAP1_MOUSE 753 1209
DBREF 3OBV C 131 457 UNP O08808 DIAP1_MOUSE 131 457
DBREF 3OBV G 753 1209 UNP O08808 DIAP1_MOUSE 753 1209
DBREF 3OBV D 131 457 UNP O08808 DIAP1_MOUSE 131 457
DBREF 3OBV H 753 1209 UNP O08808 DIAP1_MOUSE 753 1209
SEQRES 1 A 327 GLU SER SER ARG SER ALA MET MET TYR ILE GLN GLU LEU
SEQRES 2 A 327 ARG SER GLY LEU ARG ASP MET HIS LEU LEU SER CYS LEU
SEQRES 3 A 327 GLU SER LEU ARG VAL SER LEU ASN ASN ASN PRO VAL SER
SEQRES 4 A 327 TRP VAL GLN THR PHE GLY ALA GLU GLY LEU ALA SER LEU
SEQRES 5 A 327 LEU ASP ILE LEU LYS ARG LEU HIS ASP GLU LYS GLU GLU
SEQRES 6 A 327 THR SER GLY ASN TYR ASP SER ARG ASN GLN HIS GLU ILE
SEQRES 7 A 327 ILE ARG CYS LEU LYS ALA PHE MET ASN ASN LYS PHE GLY
SEQRES 8 A 327 ILE LYS THR MET LEU GLU THR GLU GLU GLY ILE LEU LEU
SEQRES 9 A 327 LEU VAL ARG ALA MET ASP PRO ALA VAL PRO ASN MET MET
SEQRES 10 A 327 ILE ASP ALA ALA LYS LEU LEU SER ALA LEU CYS ILE LEU
SEQRES 11 A 327 PRO GLN PRO GLU ASP MET ASN GLU ARG VAL LEU GLU ALA
SEQRES 12 A 327 MET THR GLU ARG ALA GLU MET ASP GLU VAL GLU ARG PHE
SEQRES 13 A 327 GLN PRO LEU LEU ASP GLY LEU LYS SER GLY THR SER ILE
SEQRES 14 A 327 ALA LEU LYS VAL GLY CYS LEU GLN LEU ILE ASN ALA LEU
SEQRES 15 A 327 ILE THR PRO ALA GLU GLU LEU ASP PHE ARG VAL HIS ILE
SEQRES 16 A 327 ARG SER GLU LEU MET ARG LEU GLY LEU HIS GLN VAL LEU
SEQRES 17 A 327 GLN GLU LEU ARG GLU ILE GLU ASN GLU ASP MET LYS VAL
SEQRES 18 A 327 GLN LEU CYS VAL PHE ASP GLU GLN GLY ASP GLU ASP PHE
SEQRES 19 A 327 PHE ASP LEU LYS GLY ARG LEU ASP ASP ILE ARG MET GLU
SEQRES 20 A 327 MET ASP ASP PHE GLY GLU VAL PHE GLN ILE ILE LEU ASN
SEQRES 21 A 327 THR VAL LYS ASP SER LYS ALA GLU PRO HIS PHE LEU SER
SEQRES 22 A 327 ILE LEU GLN HIS LEU LEU LEU VAL ARG ASN ASP TYR GLU
SEQRES 23 A 327 ALA ARG PRO GLN TYR TYR LYS LEU ILE GLU GLU CYS VAL
SEQRES 24 A 327 SER GLN ILE VAL LEU HIS LYS ASN GLY THR ASP PRO ASP
SEQRES 25 A 327 PHE LYS CYS ARG HIS LEU GLN ILE ASP ILE GLU ARG LEU
SEQRES 26 A 327 VAL ASP
SEQRES 1 E 457 LYS LYS VAL TYR LYS PRO GLU VAL GLN LEU ARG ARG PRO
SEQRES 2 E 457 ASN TRP SER LYS PHE VAL ALA GLU ASP LEU SER GLN ASP
SEQRES 3 E 457 CYS PHE TRP THR LYS VAL LYS GLU ASP ARG PHE GLU ASN
SEQRES 4 E 457 ASN GLU LEU PHE ALA LYS LEU THR LEU ALA PHE SER ALA
SEQRES 5 E 457 GLN THR LYS THR SER LYS ALA LYS LYS ASP GLN GLU GLY
SEQRES 6 E 457 GLY GLU GLU LYS LYS SER VAL GLN LYS LYS LYS VAL LYS
SEQRES 7 E 457 GLU LEU LYS VAL LEU ASP SER LYS THR ALA GLN ASN LEU
SEQRES 8 E 457 SER ILE PHE LEU GLY SER PHE ARG MET PRO TYR GLN GLU
SEQRES 9 E 457 ILE LYS ASN VAL ILE LEU GLU VAL ASN GLU ALA VAL LEU
SEQRES 10 E 457 THR GLU SER MET ILE GLN ASN LEU ILE LYS GLN MET PRO
SEQRES 11 E 457 GLU PRO GLU GLN LEU LYS MET LEU SER GLU LEU LYS GLU
SEQRES 12 E 457 GLU TYR ASP ASP LEU ALA GLU SER GLU GLN PHE GLY VAL
SEQRES 13 E 457 VAL MET GLY THR VAL PRO ARG LEU ARG PRO ARG LEU ASN
SEQRES 14 E 457 ALA ILE LEU PHE LYS LEU GLN PHE SER GLU GLN VAL GLU
SEQRES 15 E 457 ASN ILE LYS PRO GLU ILE VAL SER VAL THR ALA ALA CYS
SEQRES 16 E 457 GLU GLU LEU ARG LYS SER GLU ASN PHE SER SER LEU LEU
SEQRES 17 E 457 GLU LEU THR LEU LEU VAL GLY ASN TYR MET ASN ALA GLY
SEQRES 18 E 457 SER ARG ASN ALA GLY ALA PHE GLY PHE ASN ILE SER PHE
SEQRES 19 E 457 LEU CYS LYS LEU ARG ASP THR LYS SER ALA ASP GLN LYS
SEQRES 20 E 457 MET THR LEU LEU HIS PHE LEU ALA GLU LEU CYS GLU ASN
SEQRES 21 E 457 ASP HIS PRO GLU VAL LEU LYS PHE PRO ASP GLU LEU ALA
SEQRES 22 E 457 HIS VAL GLU LYS ALA SER ARG VAL SER ALA GLU ASN LEU
SEQRES 23 E 457 GLN LYS SER LEU ASP GLN MET LYS LYS GLN ILE ALA ASP
SEQRES 24 E 457 VAL GLU ARG ASP VAL GLN ASN PHE PRO ALA ALA THR ASP
SEQRES 25 E 457 GLU LYS ASP LYS PHE VAL GLU LYS MET THR SER PHE VAL
SEQRES 26 E 457 LYS ASP ALA GLN GLU GLN TYR ASN LYS LEU ARG MET MET
SEQRES 27 E 457 HIS SER ASN MET GLU THR LEU TYR LYS GLU LEU GLY ASP
SEQRES 28 E 457 TYR PHE VAL PHE ASP PRO LYS LYS LEU SER VAL GLU GLU
SEQRES 29 E 457 PHE PHE MET ASP LEU HIS ASN PHE ARG ASN MET PHE LEU
SEQRES 30 E 457 GLN ALA VAL LYS GLU ASN GLN LYS ARG ARG GLU THR GLU
SEQRES 31 E 457 GLU LYS MET ARG ARG ALA LYS LEU ALA LYS GLU LYS ALA
SEQRES 32 E 457 GLU LYS GLU ARG LEU GLU LYS GLN GLN LYS ARG GLU GLN
SEQRES 33 E 457 LEU ILE ASP MET ASN ALA GLU GLY ASP GLU THR GLY VAL
SEQRES 34 E 457 MET ASP SER LEU LEU GLU ALA LEU GLN SER GLY ALA ALA
SEQRES 35 E 457 PHE ARG ARG LYS ARG GLY PRO ARG GLN VAL ASN ARG LYS
SEQRES 36 E 457 ALA GLY
SEQRES 1 B 327 GLU SER SER ARG SER ALA MET MET TYR ILE GLN GLU LEU
SEQRES 2 B 327 ARG SER GLY LEU ARG ASP MET HIS LEU LEU SER CYS LEU
SEQRES 3 B 327 GLU SER LEU ARG VAL SER LEU ASN ASN ASN PRO VAL SER
SEQRES 4 B 327 TRP VAL GLN THR PHE GLY ALA GLU GLY LEU ALA SER LEU
SEQRES 5 B 327 LEU ASP ILE LEU LYS ARG LEU HIS ASP GLU LYS GLU GLU
SEQRES 6 B 327 THR SER GLY ASN TYR ASP SER ARG ASN GLN HIS GLU ILE
SEQRES 7 B 327 ILE ARG CYS LEU LYS ALA PHE MET ASN ASN LYS PHE GLY
SEQRES 8 B 327 ILE LYS THR MET LEU GLU THR GLU GLU GLY ILE LEU LEU
SEQRES 9 B 327 LEU VAL ARG ALA MET ASP PRO ALA VAL PRO ASN MET MET
SEQRES 10 B 327 ILE ASP ALA ALA LYS LEU LEU SER ALA LEU CYS ILE LEU
SEQRES 11 B 327 PRO GLN PRO GLU ASP MET ASN GLU ARG VAL LEU GLU ALA
SEQRES 12 B 327 MET THR GLU ARG ALA GLU MET ASP GLU VAL GLU ARG PHE
SEQRES 13 B 327 GLN PRO LEU LEU ASP GLY LEU LYS SER GLY THR SER ILE
SEQRES 14 B 327 ALA LEU LYS VAL GLY CYS LEU GLN LEU ILE ASN ALA LEU
SEQRES 15 B 327 ILE THR PRO ALA GLU GLU LEU ASP PHE ARG VAL HIS ILE
SEQRES 16 B 327 ARG SER GLU LEU MET ARG LEU GLY LEU HIS GLN VAL LEU
SEQRES 17 B 327 GLN GLU LEU ARG GLU ILE GLU ASN GLU ASP MET LYS VAL
SEQRES 18 B 327 GLN LEU CYS VAL PHE ASP GLU GLN GLY ASP GLU ASP PHE
SEQRES 19 B 327 PHE ASP LEU LYS GLY ARG LEU ASP ASP ILE ARG MET GLU
SEQRES 20 B 327 MET ASP ASP PHE GLY GLU VAL PHE GLN ILE ILE LEU ASN
SEQRES 21 B 327 THR VAL LYS ASP SER LYS ALA GLU PRO HIS PHE LEU SER
SEQRES 22 B 327 ILE LEU GLN HIS LEU LEU LEU VAL ARG ASN ASP TYR GLU
SEQRES 23 B 327 ALA ARG PRO GLN TYR TYR LYS LEU ILE GLU GLU CYS VAL
SEQRES 24 B 327 SER GLN ILE VAL LEU HIS LYS ASN GLY THR ASP PRO ASP
SEQRES 25 B 327 PHE LYS CYS ARG HIS LEU GLN ILE ASP ILE GLU ARG LEU
SEQRES 26 B 327 VAL ASP
SEQRES 1 F 457 LYS LYS VAL TYR LYS PRO GLU VAL GLN LEU ARG ARG PRO
SEQRES 2 F 457 ASN TRP SER LYS PHE VAL ALA GLU ASP LEU SER GLN ASP
SEQRES 3 F 457 CYS PHE TRP THR LYS VAL LYS GLU ASP ARG PHE GLU ASN
SEQRES 4 F 457 ASN GLU LEU PHE ALA LYS LEU THR LEU ALA PHE SER ALA
SEQRES 5 F 457 GLN THR LYS THR SER LYS ALA LYS LYS ASP GLN GLU GLY
SEQRES 6 F 457 GLY GLU GLU LYS LYS SER VAL GLN LYS LYS LYS VAL LYS
SEQRES 7 F 457 GLU LEU LYS VAL LEU ASP SER LYS THR ALA GLN ASN LEU
SEQRES 8 F 457 SER ILE PHE LEU GLY SER PHE ARG MET PRO TYR GLN GLU
SEQRES 9 F 457 ILE LYS ASN VAL ILE LEU GLU VAL ASN GLU ALA VAL LEU
SEQRES 10 F 457 THR GLU SER MET ILE GLN ASN LEU ILE LYS GLN MET PRO
SEQRES 11 F 457 GLU PRO GLU GLN LEU LYS MET LEU SER GLU LEU LYS GLU
SEQRES 12 F 457 GLU TYR ASP ASP LEU ALA GLU SER GLU GLN PHE GLY VAL
SEQRES 13 F 457 VAL MET GLY THR VAL PRO ARG LEU ARG PRO ARG LEU ASN
SEQRES 14 F 457 ALA ILE LEU PHE LYS LEU GLN PHE SER GLU GLN VAL GLU
SEQRES 15 F 457 ASN ILE LYS PRO GLU ILE VAL SER VAL THR ALA ALA CYS
SEQRES 16 F 457 GLU GLU LEU ARG LYS SER GLU ASN PHE SER SER LEU LEU
SEQRES 17 F 457 GLU LEU THR LEU LEU VAL GLY ASN TYR MET ASN ALA GLY
SEQRES 18 F 457 SER ARG ASN ALA GLY ALA PHE GLY PHE ASN ILE SER PHE
SEQRES 19 F 457 LEU CYS LYS LEU ARG ASP THR LYS SER ALA ASP GLN LYS
SEQRES 20 F 457 MET THR LEU LEU HIS PHE LEU ALA GLU LEU CYS GLU ASN
SEQRES 21 F 457 ASP HIS PRO GLU VAL LEU LYS PHE PRO ASP GLU LEU ALA
SEQRES 22 F 457 HIS VAL GLU LYS ALA SER ARG VAL SER ALA GLU ASN LEU
SEQRES 23 F 457 GLN LYS SER LEU ASP GLN MET LYS LYS GLN ILE ALA ASP
SEQRES 24 F 457 VAL GLU ARG ASP VAL GLN ASN PHE PRO ALA ALA THR ASP
SEQRES 25 F 457 GLU LYS ASP LYS PHE VAL GLU LYS MET THR SER PHE VAL
SEQRES 26 F 457 LYS ASP ALA GLN GLU GLN TYR ASN LYS LEU ARG MET MET
SEQRES 27 F 457 HIS SER ASN MET GLU THR LEU TYR LYS GLU LEU GLY ASP
SEQRES 28 F 457 TYR PHE VAL PHE ASP PRO LYS LYS LEU SER VAL GLU GLU
SEQRES 29 F 457 PHE PHE MET ASP LEU HIS ASN PHE ARG ASN MET PHE LEU
SEQRES 30 F 457 GLN ALA VAL LYS GLU ASN GLN LYS ARG ARG GLU THR GLU
SEQRES 31 F 457 GLU LYS MET ARG ARG ALA LYS LEU ALA LYS GLU LYS ALA
SEQRES 32 F 457 GLU LYS GLU ARG LEU GLU LYS GLN GLN LYS ARG GLU GLN
SEQRES 33 F 457 LEU ILE ASP MET ASN ALA GLU GLY ASP GLU THR GLY VAL
SEQRES 34 F 457 MET ASP SER LEU LEU GLU ALA LEU GLN SER GLY ALA ALA
SEQRES 35 F 457 PHE ARG ARG LYS ARG GLY PRO ARG GLN VAL ASN ARG LYS
SEQRES 36 F 457 ALA GLY
SEQRES 1 C 327 GLU SER SER ARG SER ALA MET MET TYR ILE GLN GLU LEU
SEQRES 2 C 327 ARG SER GLY LEU ARG ASP MET HIS LEU LEU SER CYS LEU
SEQRES 3 C 327 GLU SER LEU ARG VAL SER LEU ASN ASN ASN PRO VAL SER
SEQRES 4 C 327 TRP VAL GLN THR PHE GLY ALA GLU GLY LEU ALA SER LEU
SEQRES 5 C 327 LEU ASP ILE LEU LYS ARG LEU HIS ASP GLU LYS GLU GLU
SEQRES 6 C 327 THR SER GLY ASN TYR ASP SER ARG ASN GLN HIS GLU ILE
SEQRES 7 C 327 ILE ARG CYS LEU LYS ALA PHE MET ASN ASN LYS PHE GLY
SEQRES 8 C 327 ILE LYS THR MET LEU GLU THR GLU GLU GLY ILE LEU LEU
SEQRES 9 C 327 LEU VAL ARG ALA MET ASP PRO ALA VAL PRO ASN MET MET
SEQRES 10 C 327 ILE ASP ALA ALA LYS LEU LEU SER ALA LEU CYS ILE LEU
SEQRES 11 C 327 PRO GLN PRO GLU ASP MET ASN GLU ARG VAL LEU GLU ALA
SEQRES 12 C 327 MET THR GLU ARG ALA GLU MET ASP GLU VAL GLU ARG PHE
SEQRES 13 C 327 GLN PRO LEU LEU ASP GLY LEU LYS SER GLY THR SER ILE
SEQRES 14 C 327 ALA LEU LYS VAL GLY CYS LEU GLN LEU ILE ASN ALA LEU
SEQRES 15 C 327 ILE THR PRO ALA GLU GLU LEU ASP PHE ARG VAL HIS ILE
SEQRES 16 C 327 ARG SER GLU LEU MET ARG LEU GLY LEU HIS GLN VAL LEU
SEQRES 17 C 327 GLN GLU LEU ARG GLU ILE GLU ASN GLU ASP MET LYS VAL
SEQRES 18 C 327 GLN LEU CYS VAL PHE ASP GLU GLN GLY ASP GLU ASP PHE
SEQRES 19 C 327 PHE ASP LEU LYS GLY ARG LEU ASP ASP ILE ARG MET GLU
SEQRES 20 C 327 MET ASP ASP PHE GLY GLU VAL PHE GLN ILE ILE LEU ASN
SEQRES 21 C 327 THR VAL LYS ASP SER LYS ALA GLU PRO HIS PHE LEU SER
SEQRES 22 C 327 ILE LEU GLN HIS LEU LEU LEU VAL ARG ASN ASP TYR GLU
SEQRES 23 C 327 ALA ARG PRO GLN TYR TYR LYS LEU ILE GLU GLU CYS VAL
SEQRES 24 C 327 SER GLN ILE VAL LEU HIS LYS ASN GLY THR ASP PRO ASP
SEQRES 25 C 327 PHE LYS CYS ARG HIS LEU GLN ILE ASP ILE GLU ARG LEU
SEQRES 26 C 327 VAL ASP
SEQRES 1 G 457 LYS LYS VAL TYR LYS PRO GLU VAL GLN LEU ARG ARG PRO
SEQRES 2 G 457 ASN TRP SER LYS PHE VAL ALA GLU ASP LEU SER GLN ASP
SEQRES 3 G 457 CYS PHE TRP THR LYS VAL LYS GLU ASP ARG PHE GLU ASN
SEQRES 4 G 457 ASN GLU LEU PHE ALA LYS LEU THR LEU ALA PHE SER ALA
SEQRES 5 G 457 GLN THR LYS THR SER LYS ALA LYS LYS ASP GLN GLU GLY
SEQRES 6 G 457 GLY GLU GLU LYS LYS SER VAL GLN LYS LYS LYS VAL LYS
SEQRES 7 G 457 GLU LEU LYS VAL LEU ASP SER LYS THR ALA GLN ASN LEU
SEQRES 8 G 457 SER ILE PHE LEU GLY SER PHE ARG MET PRO TYR GLN GLU
SEQRES 9 G 457 ILE LYS ASN VAL ILE LEU GLU VAL ASN GLU ALA VAL LEU
SEQRES 10 G 457 THR GLU SER MET ILE GLN ASN LEU ILE LYS GLN MET PRO
SEQRES 11 G 457 GLU PRO GLU GLN LEU LYS MET LEU SER GLU LEU LYS GLU
SEQRES 12 G 457 GLU TYR ASP ASP LEU ALA GLU SER GLU GLN PHE GLY VAL
SEQRES 13 G 457 VAL MET GLY THR VAL PRO ARG LEU ARG PRO ARG LEU ASN
SEQRES 14 G 457 ALA ILE LEU PHE LYS LEU GLN PHE SER GLU GLN VAL GLU
SEQRES 15 G 457 ASN ILE LYS PRO GLU ILE VAL SER VAL THR ALA ALA CYS
SEQRES 16 G 457 GLU GLU LEU ARG LYS SER GLU ASN PHE SER SER LEU LEU
SEQRES 17 G 457 GLU LEU THR LEU LEU VAL GLY ASN TYR MET ASN ALA GLY
SEQRES 18 G 457 SER ARG ASN ALA GLY ALA PHE GLY PHE ASN ILE SER PHE
SEQRES 19 G 457 LEU CYS LYS LEU ARG ASP THR LYS SER ALA ASP GLN LYS
SEQRES 20 G 457 MET THR LEU LEU HIS PHE LEU ALA GLU LEU CYS GLU ASN
SEQRES 21 G 457 ASP HIS PRO GLU VAL LEU LYS PHE PRO ASP GLU LEU ALA
SEQRES 22 G 457 HIS VAL GLU LYS ALA SER ARG VAL SER ALA GLU ASN LEU
SEQRES 23 G 457 GLN LYS SER LEU ASP GLN MET LYS LYS GLN ILE ALA ASP
SEQRES 24 G 457 VAL GLU ARG ASP VAL GLN ASN PHE PRO ALA ALA THR ASP
SEQRES 25 G 457 GLU LYS ASP LYS PHE VAL GLU LYS MET THR SER PHE VAL
SEQRES 26 G 457 LYS ASP ALA GLN GLU GLN TYR ASN LYS LEU ARG MET MET
SEQRES 27 G 457 HIS SER ASN MET GLU THR LEU TYR LYS GLU LEU GLY ASP
SEQRES 28 G 457 TYR PHE VAL PHE ASP PRO LYS LYS LEU SER VAL GLU GLU
SEQRES 29 G 457 PHE PHE MET ASP LEU HIS ASN PHE ARG ASN MET PHE LEU
SEQRES 30 G 457 GLN ALA VAL LYS GLU ASN GLN LYS ARG ARG GLU THR GLU
SEQRES 31 G 457 GLU LYS MET ARG ARG ALA LYS LEU ALA LYS GLU LYS ALA
SEQRES 32 G 457 GLU LYS GLU ARG LEU GLU LYS GLN GLN LYS ARG GLU GLN
SEQRES 33 G 457 LEU ILE ASP MET ASN ALA GLU GLY ASP GLU THR GLY VAL
SEQRES 34 G 457 MET ASP SER LEU LEU GLU ALA LEU GLN SER GLY ALA ALA
SEQRES 35 G 457 PHE ARG ARG LYS ARG GLY PRO ARG GLN VAL ASN ARG LYS
SEQRES 36 G 457 ALA GLY
SEQRES 1 D 327 GLU SER SER ARG SER ALA MET MET TYR ILE GLN GLU LEU
SEQRES 2 D 327 ARG SER GLY LEU ARG ASP MET HIS LEU LEU SER CYS LEU
SEQRES 3 D 327 GLU SER LEU ARG VAL SER LEU ASN ASN ASN PRO VAL SER
SEQRES 4 D 327 TRP VAL GLN THR PHE GLY ALA GLU GLY LEU ALA SER LEU
SEQRES 5 D 327 LEU ASP ILE LEU LYS ARG LEU HIS ASP GLU LYS GLU GLU
SEQRES 6 D 327 THR SER GLY ASN TYR ASP SER ARG ASN GLN HIS GLU ILE
SEQRES 7 D 327 ILE ARG CYS LEU LYS ALA PHE MET ASN ASN LYS PHE GLY
SEQRES 8 D 327 ILE LYS THR MET LEU GLU THR GLU GLU GLY ILE LEU LEU
SEQRES 9 D 327 LEU VAL ARG ALA MET ASP PRO ALA VAL PRO ASN MET MET
SEQRES 10 D 327 ILE ASP ALA ALA LYS LEU LEU SER ALA LEU CYS ILE LEU
SEQRES 11 D 327 PRO GLN PRO GLU ASP MET ASN GLU ARG VAL LEU GLU ALA
SEQRES 12 D 327 MET THR GLU ARG ALA GLU MET ASP GLU VAL GLU ARG PHE
SEQRES 13 D 327 GLN PRO LEU LEU ASP GLY LEU LYS SER GLY THR SER ILE
SEQRES 14 D 327 ALA LEU LYS VAL GLY CYS LEU GLN LEU ILE ASN ALA LEU
SEQRES 15 D 327 ILE THR PRO ALA GLU GLU LEU ASP PHE ARG VAL HIS ILE
SEQRES 16 D 327 ARG SER GLU LEU MET ARG LEU GLY LEU HIS GLN VAL LEU
SEQRES 17 D 327 GLN GLU LEU ARG GLU ILE GLU ASN GLU ASP MET LYS VAL
SEQRES 18 D 327 GLN LEU CYS VAL PHE ASP GLU GLN GLY ASP GLU ASP PHE
SEQRES 19 D 327 PHE ASP LEU LYS GLY ARG LEU ASP ASP ILE ARG MET GLU
SEQRES 20 D 327 MET ASP ASP PHE GLY GLU VAL PHE GLN ILE ILE LEU ASN
SEQRES 21 D 327 THR VAL LYS ASP SER LYS ALA GLU PRO HIS PHE LEU SER
SEQRES 22 D 327 ILE LEU GLN HIS LEU LEU LEU VAL ARG ASN ASP TYR GLU
SEQRES 23 D 327 ALA ARG PRO GLN TYR TYR LYS LEU ILE GLU GLU CYS VAL
SEQRES 24 D 327 SER GLN ILE VAL LEU HIS LYS ASN GLY THR ASP PRO ASP
SEQRES 25 D 327 PHE LYS CYS ARG HIS LEU GLN ILE ASP ILE GLU ARG LEU
SEQRES 26 D 327 VAL ASP
SEQRES 1 H 457 LYS LYS VAL TYR LYS PRO GLU VAL GLN LEU ARG ARG PRO
SEQRES 2 H 457 ASN TRP SER LYS PHE VAL ALA GLU ASP LEU SER GLN ASP
SEQRES 3 H 457 CYS PHE TRP THR LYS VAL LYS GLU ASP ARG PHE GLU ASN
SEQRES 4 H 457 ASN GLU LEU PHE ALA LYS LEU THR LEU ALA PHE SER ALA
SEQRES 5 H 457 GLN THR LYS THR SER LYS ALA LYS LYS ASP GLN GLU GLY
SEQRES 6 H 457 GLY GLU GLU LYS LYS SER VAL GLN LYS LYS LYS VAL LYS
SEQRES 7 H 457 GLU LEU LYS VAL LEU ASP SER LYS THR ALA GLN ASN LEU
SEQRES 8 H 457 SER ILE PHE LEU GLY SER PHE ARG MET PRO TYR GLN GLU
SEQRES 9 H 457 ILE LYS ASN VAL ILE LEU GLU VAL ASN GLU ALA VAL LEU
SEQRES 10 H 457 THR GLU SER MET ILE GLN ASN LEU ILE LYS GLN MET PRO
SEQRES 11 H 457 GLU PRO GLU GLN LEU LYS MET LEU SER GLU LEU LYS GLU
SEQRES 12 H 457 GLU TYR ASP ASP LEU ALA GLU SER GLU GLN PHE GLY VAL
SEQRES 13 H 457 VAL MET GLY THR VAL PRO ARG LEU ARG PRO ARG LEU ASN
SEQRES 14 H 457 ALA ILE LEU PHE LYS LEU GLN PHE SER GLU GLN VAL GLU
SEQRES 15 H 457 ASN ILE LYS PRO GLU ILE VAL SER VAL THR ALA ALA CYS
SEQRES 16 H 457 GLU GLU LEU ARG LYS SER GLU ASN PHE SER SER LEU LEU
SEQRES 17 H 457 GLU LEU THR LEU LEU VAL GLY ASN TYR MET ASN ALA GLY
SEQRES 18 H 457 SER ARG ASN ALA GLY ALA PHE GLY PHE ASN ILE SER PHE
SEQRES 19 H 457 LEU CYS LYS LEU ARG ASP THR LYS SER ALA ASP GLN LYS
SEQRES 20 H 457 MET THR LEU LEU HIS PHE LEU ALA GLU LEU CYS GLU ASN
SEQRES 21 H 457 ASP HIS PRO GLU VAL LEU LYS PHE PRO ASP GLU LEU ALA
SEQRES 22 H 457 HIS VAL GLU LYS ALA SER ARG VAL SER ALA GLU ASN LEU
SEQRES 23 H 457 GLN LYS SER LEU ASP GLN MET LYS LYS GLN ILE ALA ASP
SEQRES 24 H 457 VAL GLU ARG ASP VAL GLN ASN PHE PRO ALA ALA THR ASP
SEQRES 25 H 457 GLU LYS ASP LYS PHE VAL GLU LYS MET THR SER PHE VAL
SEQRES 26 H 457 LYS ASP ALA GLN GLU GLN TYR ASN LYS LEU ARG MET MET
SEQRES 27 H 457 HIS SER ASN MET GLU THR LEU TYR LYS GLU LEU GLY ASP
SEQRES 28 H 457 TYR PHE VAL PHE ASP PRO LYS LYS LEU SER VAL GLU GLU
SEQRES 29 H 457 PHE PHE MET ASP LEU HIS ASN PHE ARG ASN MET PHE LEU
SEQRES 30 H 457 GLN ALA VAL LYS GLU ASN GLN LYS ARG ARG GLU THR GLU
SEQRES 31 H 457 GLU LYS MET ARG ARG ALA LYS LEU ALA LYS GLU LYS ALA
SEQRES 32 H 457 GLU LYS GLU ARG LEU GLU LYS GLN GLN LYS ARG GLU GLN
SEQRES 33 H 457 LEU ILE ASP MET ASN ALA GLU GLY ASP GLU THR GLY VAL
SEQRES 34 H 457 MET ASP SER LEU LEU GLU ALA LEU GLN SER GLY ALA ALA
SEQRES 35 H 457 PHE ARG ARG LYS ARG GLY PRO ARG GLN VAL ASN ARG LYS
SEQRES 36 H 457 ALA GLY
HET GLC I 1 22
HET FRU I 2 23
HET GLC J 1 22
HET FRU J 2 23
HET GLC K 1 22
HET FRU K 2 23
HET GLC L 1 22
HET FRU L 2 23
HET GLC M 1 22
HET FRU M 2 23
HET GLC N 1 22
HET FRU N 2 23
HET GLC O 1 22
HET FRU O 2 23
HET GLC P 1 22
HET FRU P 2 23
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM FRU BETA-D-FRUCTOFURANOSE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN FRU BETA-D-FRUCTOSE; D-FRUCTOSE; FRUCTOSE
FORMUL 9 GLC 8(C6 H12 O6)
FORMUL 9 FRU 8(C6 H12 O6)
HELIX 1 1 ARG A 134 ARG A 144 1 11
HELIX 2 2 ARG A 148 ASN A 166 1 19
HELIX 3 3 PRO A 167 GLU A 195 1 29
HELIX 4 4 ASP A 201 MET A 216 1 16
HELIX 5 5 ASN A 218 GLU A 227 1 10
HELIX 6 6 GLU A 230 ALA A 238 1 9
HELIX 7 7 VAL A 243 LEU A 260 1 18
HELIX 8 8 ASP A 265 GLU A 282 1 18
HELIX 9 9 PHE A 286 GLY A 292 1 7
HELIX 10 10 SER A 298 THR A 314 1 17
HELIX 11 11 GLU A 318 LEU A 332 1 15
HELIX 12 12 GLY A 333 ARG A 342 1 10
HELIX 13 13 ASN A 346 MET A 378 1 33
HELIX 14 14 ASP A 380 LYS A 393 1 14
HELIX 15 15 LYS A 396 LEU A 410 1 15
HELIX 16 16 GLU A 416 LEU A 434 1 19
HELIX 17 17 HIS A 435 THR A 439 5 5
HELIX 18 18 PHE E 780 VAL E 784 5 5
HELIX 19 19 LYS E 785 GLU E 790 5 6
HELIX 20 20 GLU E 793 PHE E 802 1 10
HELIX 21 21 ASP E 836 ARG E 851 1 16
HELIX 22 22 PRO E 853 VAL E 864 1 12
HELIX 23 23 THR E 870 MET E 881 1 12
HELIX 24 24 GLU E 883 GLU E 892 1 10
HELIX 25 25 GLU E 896 LEU E 900 5 5
HELIX 26 26 ALA E 901 GLY E 911 1 11
HELIX 27 27 ARG E 915 GLU E 934 1 20
HELIX 28 28 ILE E 936 LYS E 952 1 17
HELIX 29 29 SER E 953 ASN E 971 1 19
HELIX 30 30 ASN E 983 SER E 985 5 3
HELIX 31 31 PHE E 986 ARG E 991 1 6
HELIX 32 32 THR E 1001 HIS E 1014 1 14
HELIX 33 33 PRO E 1015 LEU E 1018 5 4
HELIX 34 34 LYS E 1019 LEU E 1024 1 6
HELIX 35 35 HIS E 1026 SER E 1031 1 6
HELIX 36 36 SER E 1034 ASN E 1058 1 25
HELIX 37 37 LYS E 1068 PHE E 1105 1 38
HELIX 38 38 SER E 1113 GLU E 1167 1 55
HELIX 39 39 GLY E 1180 GLY E 1192 1 13
HELIX 40 40 SER B 133 ARG B 144 1 12
HELIX 41 41 ARG B 148 ASN B 166 1 19
HELIX 42 42 PRO B 167 GLU B 192 1 26
HELIX 43 43 ASP B 201 MET B 216 1 16
HELIX 44 44 ASN B 218 THR B 228 1 11
HELIX 45 45 GLU B 230 ALA B 238 1 9
HELIX 46 46 VAL B 243 LEU B 260 1 18
HELIX 47 47 ASP B 265 GLU B 282 1 18
HELIX 48 48 PHE B 286 LYS B 294 1 9
HELIX 49 49 SER B 298 THR B 314 1 17
HELIX 50 50 GLU B 318 LEU B 332 1 15
HELIX 51 51 GLY B 333 ARG B 342 1 10
HELIX 52 52 ASN B 346 MET B 378 1 33
HELIX 53 53 ASP B 380 LYS B 393 1 14
HELIX 54 54 ALA B 397 LEU B 409 1 13
HELIX 55 55 GLU B 416 LEU B 434 1 19
HELIX 56 56 HIS B 435 THR B 439 5 5
HELIX 57 57 VAL F 771 SER F 776 1 6
HELIX 58 58 LYS F 785 GLU F 790 5 6
HELIX 59 59 ASN F 791 PHE F 802 1 12
HELIX 60 60 ASP F 836 ARG F 851 1 16
HELIX 61 61 PRO F 853 VAL F 864 1 12
HELIX 62 62 THR F 870 MET F 881 1 12
HELIX 63 63 GLU F 883 MET F 889 1 7
HELIX 64 64 ALA F 901 VAL F 913 1 13
HELIX 65 65 ARG F 915 GLU F 934 1 20
HELIX 66 66 ILE F 936 SER F 953 1 18
HELIX 67 67 SER F 953 ASN F 971 1 19
HELIX 68 68 ILE F 984 THR F 993 5 10
HELIX 69 69 THR F 1001 HIS F 1014 1 14
HELIX 70 70 PRO F 1015 GLU F 1023 5 9
HELIX 71 71 HIS F 1026 VAL F 1033 1 8
HELIX 72 72 SER F 1034 GLN F 1057 1 24
HELIX 73 73 LYS F 1068 PHE F 1105 1 38
HELIX 74 74 ASP F 1108 LEU F 1112 5 5
HELIX 75 75 SER F 1113 GLU F 1167 1 55
HELIX 76 76 GLY F 1180 GLY F 1192 1 13
HELIX 77 77 SER C 132 ARG C 144 1 13
HELIX 78 78 ARG C 148 ASN C 166 1 19
HELIX 79 79 PRO C 167 GLU C 194 1 28
HELIX 80 80 ASP C 201 MET C 216 1 16
HELIX 81 81 ASN C 218 GLU C 227 1 10
HELIX 82 82 GLU C 230 ALA C 238 1 9
HELIX 83 83 VAL C 243 LEU C 260 1 18
HELIX 84 84 ASP C 265 GLU C 282 1 18
HELIX 85 85 PHE C 286 GLY C 292 1 7
HELIX 86 86 SER C 298 THR C 314 1 17
HELIX 87 87 GLU C 318 LEU C 332 1 15
HELIX 88 88 GLY C 333 ARG C 342 1 10
HELIX 89 89 ASN C 346 MET C 378 1 33
HELIX 90 90 ASP C 380 LYS C 393 1 14
HELIX 91 91 LYS C 396 LEU C 410 1 15
HELIX 92 92 GLU C 416 LEU C 434 1 19
HELIX 93 93 HIS C 435 THR C 439 5 5
HELIX 94 94 PHE G 780 VAL G 784 5 5
HELIX 95 95 LYS G 785 GLU G 790 5 6
HELIX 96 96 GLU G 793 PHE G 802 1 10
HELIX 97 97 ASP G 836 ARG G 851 1 16
HELIX 98 98 PRO G 853 VAL G 864 1 12
HELIX 99 99 THR G 870 MET G 881 1 12
HELIX 100 100 GLU G 883 GLU G 892 1 10
HELIX 101 101 GLU G 896 LEU G 900 5 5
HELIX 102 102 ALA G 901 GLY G 911 1 11
HELIX 103 103 ARG G 915 GLU G 934 1 20
HELIX 104 104 ILE G 936 LYS G 952 1 17
HELIX 105 105 SER G 953 ASN G 971 1 19
HELIX 106 106 ILE G 984 THR G 993 5 10
HELIX 107 107 THR G 1001 HIS G 1014 1 14
HELIX 108 108 PRO G 1015 LEU G 1018 5 4
HELIX 109 109 LYS G 1019 LEU G 1024 1 6
HELIX 110 110 HIS G 1026 SER G 1031 1 6
HELIX 111 111 SER G 1034 ASN G 1058 1 25
HELIX 112 112 LYS G 1068 PHE G 1105 1 38
HELIX 113 113 SER G 1113 GLU G 1167 1 55
HELIX 114 114 GLY G 1180 GLY G 1192 1 13
HELIX 115 115 ARG D 134 ARG D 144 1 11
HELIX 116 116 ARG D 148 ASN D 166 1 19
HELIX 117 117 PRO D 167 GLU D 195 1 29
HELIX 118 118 TYR D 200 MET D 216 1 17
HELIX 119 119 ASN D 218 THR D 228 1 11
HELIX 120 120 GLU D 230 ALA D 238 1 9
HELIX 121 121 VAL D 243 LEU D 260 1 18
HELIX 122 122 ASP D 265 GLU D 282 1 18
HELIX 123 123 PHE D 286 LYS D 294 1 9
HELIX 124 124 SER D 298 THR D 314 1 17
HELIX 125 125 GLU D 318 LEU D 332 1 15
HELIX 126 126 GLY D 333 ARG D 342 1 10
HELIX 127 127 ASN D 346 MET D 378 1 33
HELIX 128 128 ASP D 380 LYS D 393 1 14
HELIX 129 129 ALA D 397 LEU D 409 1 13
HELIX 130 130 GLU D 416 LEU D 434 1 19
HELIX 131 131 HIS D 435 THR D 439 5 5
HELIX 132 132 VAL H 771 SER H 776 1 6
HELIX 133 133 LYS H 785 GLU H 790 5 6
HELIX 134 134 ASN H 791 PHE H 802 1 12
HELIX 135 135 ASP H 836 ARG H 851 1 16
HELIX 136 136 PRO H 853 VAL H 864 1 12
HELIX 137 137 THR H 870 MET H 881 1 12
HELIX 138 138 GLU H 883 MET H 889 1 7
HELIX 139 139 ALA H 901 VAL H 913 1 13
HELIX 140 140 ARG H 915 GLU H 934 1 20
HELIX 141 141 ILE H 936 SER H 953 1 18
HELIX 142 142 SER H 953 ASN H 971 1 19
HELIX 143 143 ILE H 984 THR H 993 5 10
HELIX 144 144 THR H 1001 HIS H 1014 1 14
HELIX 145 145 PRO H 1015 GLU H 1023 5 9
HELIX 146 146 HIS H 1026 SER H 1031 1 6
HELIX 147 147 SER H 1034 GLN H 1057 1 24
HELIX 148 148 LYS H 1068 PHE H 1105 1 38
HELIX 149 149 ASP H 1108 LEU H 1112 5 5
HELIX 150 150 SER H 1113 GLU H 1167 1 55
HELIX 151 151 GLY H 1180 GLY H 1192 1 13
SHEET 1 A 2 HIS A 447 ASP A 451 0
SHEET 2 A 2 HIS B 447 ASP B 451 -1 O ILE B 450 N LEU A 448
SHEET 1 B 2 LYS E 769 PHE E 770 0
SHEET 2 B 2 GLY F 981 PHE F 982 -1 O GLY F 981 N PHE E 770
SHEET 1 C 2 HIS C 447 ASP C 451 0
SHEET 2 C 2 HIS D 447 ASP D 451 -1 O ILE D 450 N LEU C 448
SHEET 1 D 2 LYS G 769 PHE G 770 0
SHEET 2 D 2 GLY H 981 PHE H 982 -1 O GLY H 981 N PHE G 770
SHEET 1 E 2 GLY G 981 PHE G 982 0
SHEET 2 E 2 LYS H 769 PHE H 770 -1 O PHE H 770 N GLY G 981
LINK C1 GLC I 1 O2 FRU I 2 1555 1555 1.43
LINK C1 GLC J 1 O2 FRU J 2 1555 1555 1.43
LINK C1 GLC K 1 O2 FRU K 2 1555 1555 1.41
LINK C1 GLC L 1 O2 FRU L 2 1555 1555 1.42
LINK C1 GLC M 1 O2 FRU M 2 1555 1555 1.42
LINK C1 GLC N 1 O2 FRU N 2 1555 1555 1.42
LINK C1 GLC O 1 O2 FRU O 2 1555 1555 1.42
LINK C1 GLC P 1 O2 FRU P 2 1555 1555 1.42
CISPEP 1 GLN A 262 PRO A 263 0 1.05
CISPEP 2 GLN B 262 PRO B 263 0 -0.09
CISPEP 3 GLN C 262 PRO C 263 0 0.12
CISPEP 4 GLN D 262 PRO D 263 0 -0.30
CRYST1 93.926 208.519 131.516 90.00 102.74 90.00 P 1 21 1 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 0.010647 0.000000 0.002407 0.00000
SCALE2 0.000000 0.004796 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007796 0.00000
MTRIX1 1 0.988766 -0.003049 0.149444 0.66873 1
MTRIX2 1 -0.003190 -0.999995 0.000706 18.22290 1
MTRIX3 1 0.149441 -0.001175 -0.988770 -6.97453 1
MTRIX1 2 0.988654 0.001787 0.150199 0.50500 1
MTRIX2 2 0.001369 -0.999995 0.002890 17.90640 1
MTRIX3 2 0.150204 -0.002652 -0.988652 -6.95406 1
(ATOM LINES ARE NOT SHOWN.)
END
