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casp_data / casp15 /experiment_structures /T1132.pdb
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HEADER CYTOSOLIC PROTEIN 02-SEP-22 8ECX
TITLE PA0709 WITH GLYOXAL AND BME MODIFICATIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIBIOTIC BIOSYNTHESIS MONOOXYGENASE;
COMPND 3 CHAIN: B;
COMPND 4 SYNONYM: QUINOL MONOOXYGENASE YGIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: C/D/E SUBUNITS HAVE HEM/CAR MODIFICATIONS MODELLED
COMPND 7 ALONGSIDE UNMODIFIED ARG AT ARG49 POSITION
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLYOXAL, CYTOSOLIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.J.CUTHBERT,C.W.GOULDING
REVDAT 4 23-OCT-24 8ECX 1 FORMUL LINK
REVDAT 3 27-DEC-23 8ECX 1 REMARK SEQRES HET HETNAM
REVDAT 3 2 1 FORMUL LINK ATOM
REVDAT 2 15-NOV-23 8ECX 1 LINK
REVDAT 1 27-SEP-23 8ECX 0
JRNL AUTH B.J.CUTHBERT,C.W.GOULDING,A.T.ULIJASZ
JRNL TITL STRUCTURAL CHARACTERIZATION OF PA0709
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 63344
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6335
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 49.6400 - 6.3100 1.00 2034 227 0.1932 0.1997
REMARK 3 2 6.3000 - 5.0100 1.00 1954 216 0.1716 0.1655
REMARK 3 3 5.0000 - 4.3700 1.00 1936 216 0.1247 0.1318
REMARK 3 4 4.3700 - 3.9700 1.00 1936 215 0.1342 0.1659
REMARK 3 5 3.9700 - 3.6900 1.00 1901 211 0.1382 0.1687
REMARK 3 6 3.6900 - 3.4700 1.00 1926 214 0.1425 0.1670
REMARK 3 7 3.4700 - 3.3000 1.00 1887 210 0.1425 0.1788
REMARK 3 8 3.3000 - 3.1500 1.00 1917 213 0.1560 0.1694
REMARK 3 9 3.1500 - 3.0300 1.00 1892 210 0.1671 0.1889
REMARK 3 10 3.0300 - 2.9300 1.00 1917 213 0.1633 0.1784
REMARK 3 11 2.9300 - 2.8400 1.00 1909 212 0.1587 0.1841
REMARK 3 12 2.8400 - 2.7600 1.00 1885 210 0.1626 0.2059
REMARK 3 13 2.7600 - 2.6800 1.00 1899 211 0.1623 0.1860
REMARK 3 14 2.6800 - 2.6200 1.00 1860 206 0.1639 0.1919
REMARK 3 15 2.6200 - 2.5600 1.00 1900 212 0.1686 0.1872
REMARK 3 16 2.5600 - 2.5000 1.00 1890 209 0.1722 0.2214
REMARK 3 17 2.5000 - 2.4500 1.00 1893 211 0.1848 0.2183
REMARK 3 18 2.4500 - 2.4100 1.00 1889 210 0.1891 0.2134
REMARK 3 19 2.4100 - 2.3600 1.00 1861 206 0.1878 0.2259
REMARK 3 20 2.3600 - 2.3200 1.00 1896 211 0.1903 0.2141
REMARK 3 21 2.3200 - 2.2900 1.00 1904 212 0.1850 0.2306
REMARK 3 22 2.2900 - 2.2500 1.00 1858 206 0.1784 0.2209
REMARK 3 23 2.2500 - 2.2200 1.00 1893 210 0.1768 0.2393
REMARK 3 24 2.2200 - 2.1900 1.00 1887 210 0.1931 0.2121
REMARK 3 25 2.1900 - 2.1600 1.00 1876 208 0.1981 0.2370
REMARK 3 26 2.1600 - 2.1300 1.00 1873 209 0.2177 0.2290
REMARK 3 27 2.1300 - 2.1000 1.00 1872 208 0.2243 0.2742
REMARK 3 28 2.1000 - 2.0800 1.00 1881 209 0.2205 0.2579
REMARK 3 29 2.0800 - 2.0500 1.00 1887 209 0.2401 0.2809
REMARK 3 30 2.0500 - 2.0300 1.00 1896 211 0.2476 0.2657
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.203
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.278
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.39
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 : 0.003 5271
REMARK 3 ANGLE : 0.775 7116
REMARK 3 CHIRALITY : 0.044 706
REMARK 3 PLANARITY : 0.004 973
REMARK 3 DIHEDRAL : 24.556 763
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 29
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 5:16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.504 11.982 0.295
REMARK 3 T TENSOR
REMARK 3 T11: 0.2226 T22: 0.2053
REMARK 3 T33: 0.1549 T12: 0.0207
REMARK 3 T13: 0.0047 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 4.1392 L22: 2.1899
REMARK 3 L33: 0.2513 L12: 0.7999
REMARK 3 L13: -1.0094 L23: -0.3770
REMARK 3 S TENSOR
REMARK 3 S11: 0.0024 S12: -0.0195 S13: 0.0971
REMARK 3 S21: -0.3684 S22: -0.0498 S23: 0.1396
REMARK 3 S31: -0.0635 S32: -0.0359 S33: 0.0102
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 17:37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.921 6.226 6.114
REMARK 3 T TENSOR
REMARK 3 T11: 0.2342 T22: 0.1907
REMARK 3 T33: 0.2240 T12: 0.0001
REMARK 3 T13: 0.0308 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 2.0644 L22: 3.5391
REMARK 3 L33: 3.8073 L12: 1.9287
REMARK 3 L13: 3.7410 L23: 1.5914
REMARK 3 S TENSOR
REMARK 3 S11: 0.2274 S12: -0.1423 S13: -0.1753
REMARK 3 S21: -0.0270 S22: -0.0530 S23: -0.2337
REMARK 3 S31: 0.1613 S32: 0.1491 S33: -0.2279
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 38:62 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.320 15.037 7.579
REMARK 3 T TENSOR
REMARK 3 T11: 0.1576 T22: 0.1060
REMARK 3 T33: 0.1247 T12: 0.0095
REMARK 3 T13: 0.0229 T23: -0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 4.3533 L22: 2.6545
REMARK 3 L33: 2.8567 L12: -1.0063
REMARK 3 L13: 0.8158 L23: 0.7378
REMARK 3 S TENSOR
REMARK 3 S11: 0.1633 S12: -0.0696 S13: 0.0856
REMARK 3 S21: -0.1025 S22: 0.0023 S23: -0.1380
REMARK 3 S31: -0.0542 S32: 0.1227 S33: -0.1470
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 63:74 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.553 12.606 -0.458
REMARK 3 T TENSOR
REMARK 3 T11: 0.3146 T22: 0.2473
REMARK 3 T33: 0.2960 T12: 0.0421
REMARK 3 T13: 0.0910 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 9.5538 L22: 2.0261
REMARK 3 L33: 6.5862 L12: 2.8278
REMARK 3 L13: 0.5120 L23: 6.4147
REMARK 3 S TENSOR
REMARK 3 S11: 0.3089 S12: 0.4382 S13: 0.2214
REMARK 3 S21: -0.7327 S22: 0.1402 S23: -0.7027
REMARK 3 S31: -0.1952 S32: 0.1766 S33: -0.3652
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 75:84 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.932 6.108 -5.275
REMARK 3 T TENSOR
REMARK 3 T11: 0.2968 T22: 0.1478
REMARK 3 T33: 0.1849 T12: 0.0257
REMARK 3 T13: 0.0145 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 8.2914 L22: 2.6019
REMARK 3 L33: 8.1214 L12: 2.4767
REMARK 3 L13: 5.4841 L23: -1.2458
REMARK 3 S TENSOR
REMARK 3 S11: 0.2432 S12: 0.5119 S13: -0.2727
REMARK 3 S21: -0.6112 S22: -0.0590 S23: -0.1600
REMARK 3 S31: 0.5129 S32: 0.4084 S33: -0.1774
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN A AND ( RESID 85:98 OR RESID 101:102 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.379 23.102 5.235
REMARK 3 T TENSOR
REMARK 3 T11: 0.2387 T22: 0.2251
REMARK 3 T33: 0.2337 T12: -0.0047
REMARK 3 T13: 0.0597 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 2.9349 L22: 3.7889
REMARK 3 L33: 5.4896 L12: 1.8773
REMARK 3 L13: 2.5145 L23: 3.0063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0991 S12: -0.1114 S13: -0.0254
REMARK 3 S21: -0.3315 S22: 0.2412 S23: -0.3124
REMARK 3 S31: -0.5345 S32: 0.2463 S33: -0.0954
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN B AND RESID 4:16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.873 34.629 11.485
REMARK 3 T TENSOR
REMARK 3 T11: 0.2396 T22: 0.1994
REMARK 3 T33: 0.2141 T12: -0.0009
REMARK 3 T13: 0.0218 T23: -0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 2.1820 L22: 3.7196
REMARK 3 L33: 3.1790 L12: 1.2479
REMARK 3 L13: -0.2404 L23: -1.6116
REMARK 3 S TENSOR
REMARK 3 S11: -0.0148 S12: -0.0390 S13: 0.3134
REMARK 3 S21: -0.2253 S22: -0.0637 S23: 0.0870
REMARK 3 S31: -0.3129 S32: 0.1202 S33: 0.0914
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN B AND RESID 17:48 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.833 28.169 19.333
REMARK 3 T TENSOR
REMARK 3 T11: 0.1916 T22: 0.2432
REMARK 3 T33: 0.1877 T12: 0.0162
REMARK 3 T13: -0.0278 T23: -0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 1.4421 L22: 3.5991
REMARK 3 L33: 3.2547 L12: 0.0842
REMARK 3 L13: -0.5509 L23: -0.1915
REMARK 3 S TENSOR
REMARK 3 S11: 0.0216 S12: -0.1835 S13: 0.0939
REMARK 3 S21: 0.1572 S22: 0.0042 S23: -0.0683
REMARK 3 S31: -0.1148 S32: 0.3040 S33: -0.0156
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ( CHAIN B AND RESID 49:64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.144 24.779 15.710
REMARK 3 T TENSOR
REMARK 3 T11: 0.1718 T22: 0.1967
REMARK 3 T33: 0.1322 T12: 0.0119
REMARK 3 T13: -0.0120 T23: -0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 3.0747 L22: 6.7975
REMARK 3 L33: 4.7228 L12: 1.4637
REMARK 3 L13: -1.3935 L23: -2.3308
REMARK 3 S TENSOR
REMARK 3 S11: -0.0730 S12: -0.1822 S13: -0.0765
REMARK 3 S21: 0.1918 S22: 0.0666 S23: -0.1329
REMARK 3 S31: -0.0673 S32: -0.0883 S33: 0.0418
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ( CHAIN B AND ( RESID 65:98 OR RESID 101:102 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.941 28.692 18.335
REMARK 3 T TENSOR
REMARK 3 T11: 0.1848 T22: 0.2256
REMARK 3 T33: 0.1756 T12: 0.0274
REMARK 3 T13: 0.0142 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 1.1114 L22: 2.1494
REMARK 3 L33: 1.9168 L12: 0.6022
REMARK 3 L13: -0.1272 L23: -0.2356
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: -0.2297 S13: 0.0878
REMARK 3 S21: 0.2777 S22: 0.0411 S23: 0.2668
REMARK 3 S31: -0.1259 S32: -0.0994 S33: -0.0088
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ( CHAIN C AND RESID 1:37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.676 24.815 -22.125
REMARK 3 T TENSOR
REMARK 3 T11: 0.1916 T22: 0.2304
REMARK 3 T33: 0.1660 T12: -0.0411
REMARK 3 T13: -0.0266 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.0362 L22: 4.2527
REMARK 3 L33: 2.2875 L12: -0.8033
REMARK 3 L13: -0.0593 L23: -1.5393
REMARK 3 S TENSOR
REMARK 3 S11: -0.0068 S12: 0.1466 S13: 0.0301
REMARK 3 S21: -0.3095 S22: -0.0069 S23: -0.0001
REMARK 3 S31: 0.1680 S32: 0.0138 S33: 0.0132
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ( CHAIN C AND RESID 38:62 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.150 25.292 -16.797
REMARK 3 T TENSOR
REMARK 3 T11: 0.2325 T22: 0.2213
REMARK 3 T33: 0.1530 T12: -0.0052
REMARK 3 T13: -0.0210 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 1.8679 L22: 2.9896
REMARK 3 L33: 3.5888 L12: -0.4089
REMARK 3 L13: 0.5285 L23: -1.9846
REMARK 3 S TENSOR
REMARK 3 S11: -0.0597 S12: 0.0852 S13: -0.0836
REMARK 3 S21: -0.1592 S22: -0.0320 S23: -0.0817
REMARK 3 S31: 0.1437 S32: 0.2604 S33: 0.1113
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: ( CHAIN C AND RESID 63:84 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.073 24.183 -24.206
REMARK 3 T TENSOR
REMARK 3 T11: 0.2578 T22: 0.2836
REMARK 3 T33: 0.2282 T12: -0.0394
REMARK 3 T13: -0.0594 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 0.9105 L22: 7.8497
REMARK 3 L33: 1.7970 L12: 0.5033
REMARK 3 L13: -0.2975 L23: -3.1289
REMARK 3 S TENSOR
REMARK 3 S11: -0.0515 S12: 0.2407 S13: -0.0571
REMARK 3 S21: -0.5077 S22: 0.2289 S23: 0.5225
REMARK 3 S31: 0.3272 S32: -0.2758 S33: -0.1937
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: ( CHAIN C AND ( RESID 85:98 OR RESID 101:102 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.168 35.104 -14.307
REMARK 3 T TENSOR
REMARK 3 T11: 0.2103 T22: 0.2394
REMARK 3 T33: 0.2188 T12: -0.0041
REMARK 3 T13: 0.0094 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 2.3348 L22: 5.6665
REMARK 3 L33: 1.0286 L12: 1.4713
REMARK 3 L13: 1.2153 L23: 0.5801
REMARK 3 S TENSOR
REMARK 3 S11: -0.1715 S12: 0.2973 S13: 0.2149
REMARK 3 S21: -0.4124 S22: 0.1216 S23: 0.1182
REMARK 3 S31: -0.0805 S32: 0.1526 S33: 0.0814
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: ( CHAIN D AND RESID 4:37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.270 42.852 -9.565
REMARK 3 T TENSOR
REMARK 3 T11: 0.2438 T22: 0.2365
REMARK 3 T33: 0.2214 T12: -0.0548
REMARK 3 T13: -0.0486 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 2.9785 L22: 2.0635
REMARK 3 L33: 1.7121 L12: -0.2261
REMARK 3 L13: 0.2722 L23: 0.2715
REMARK 3 S TENSOR
REMARK 3 S11: -0.1078 S12: 0.0815 S13: 0.3829
REMARK 3 S21: -0.0113 S22: 0.0868 S23: -0.1631
REMARK 3 S31: -0.2800 S32: 0.1876 S33: 0.0043
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: ( CHAIN D AND RESID 38:62 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.862 38.663 -11.725
REMARK 3 T TENSOR
REMARK 3 T11: 0.1896 T22: 0.2073
REMARK 3 T33: 0.1697 T12: -0.0276
REMARK 3 T13: -0.0318 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 4.9449 L22: 2.0475
REMARK 3 L33: 2.4506 L12: -0.5940
REMARK 3 L13: -0.9017 L23: 0.4280
REMARK 3 S TENSOR
REMARK 3 S11: -0.0628 S12: 0.4159 S13: 0.0318
REMARK 3 S21: -0.0065 S22: 0.0015 S23: -0.0769
REMARK 3 S31: -0.1020 S32: 0.0098 S33: 0.0268
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: ( CHAIN D AND RESID 63:74 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.994 35.529 -8.451
REMARK 3 T TENSOR
REMARK 3 T11: 0.2019 T22: 0.3591
REMARK 3 T33: 0.2691 T12: -0.0091
REMARK 3 T13: -0.0204 T23: 0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 7.8540 L22: 2.0235
REMARK 3 L33: 3.0892 L12: 3.2697
REMARK 3 L13: 2.9027 L23: 4.1765
REMARK 3 S TENSOR
REMARK 3 S11: 0.0197 S12: 0.2504 S13: -0.3914
REMARK 3 S21: 0.2652 S22: 0.1737 S23: -0.7111
REMARK 3 S31: 0.0282 S32: 0.5932 S33: -0.1576
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: ( CHAIN D AND RESID 75:91 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.393 41.052 -2.291
REMARK 3 T TENSOR
REMARK 3 T11: 0.1860 T22: 0.2743
REMARK 3 T33: 0.2001 T12: -0.0149
REMARK 3 T13: -0.0452 T23: -0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 2.2048 L22: 2.6659
REMARK 3 L33: 1.6460 L12: -0.3851
REMARK 3 L13: -0.7902 L23: 0.0807
REMARK 3 S TENSOR
REMARK 3 S11: 0.1064 S12: -0.4371 S13: 0.2304
REMARK 3 S21: 0.4431 S22: -0.1046 S23: -0.3067
REMARK 3 S31: -0.1300 S32: 0.2525 S33: -0.0068
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: ( CHAIN D AND ( RESID 92:98 OR RESID 101:101 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.645 23.255 -19.168
REMARK 3 T TENSOR
REMARK 3 T11: 0.2733 T22: 0.3317
REMARK 3 T33: 0.2965 T12: 0.0469
REMARK 3 T13: 0.0684 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 6.6629 L22: 7.5006
REMARK 3 L33: 2.0058 L12: 2.5872
REMARK 3 L13: 4.5506 L23: 2.2273
REMARK 3 S TENSOR
REMARK 3 S11: -0.1035 S12: 0.7007 S13: -0.7073
REMARK 3 S21: -0.4700 S22: 0.0946 S23: -0.5948
REMARK 3 S31: 1.0320 S32: 0.8554 S33: 0.2327
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: ( CHAIN E AND RESID 3:16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.092 19.306 -2.061
REMARK 3 T TENSOR
REMARK 3 T11: 0.1668 T22: 0.1437
REMARK 3 T33: 0.1950 T12: -0.0089
REMARK 3 T13: -0.0141 T23: 0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 2.0464 L22: 1.5510
REMARK 3 L33: 4.7079 L12: -0.5920
REMARK 3 L13: -1.2687 L23: 2.0528
REMARK 3 S TENSOR
REMARK 3 S11: -0.0849 S12: 0.0484 S13: -0.0734
REMARK 3 S21: -0.0052 S22: 0.1155 S23: 0.3281
REMARK 3 S31: 0.1764 S32: 0.0039 S33: -0.0136
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: ( CHAIN E AND RESID 17:48 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.183 20.350 0.543
REMARK 3 T TENSOR
REMARK 3 T11: 0.1904 T22: 0.2753
REMARK 3 T33: 0.2927 T12: -0.0226
REMARK 3 T13: -0.0191 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 1.3234 L22: 1.2920
REMARK 3 L33: 2.2114 L12: -0.4917
REMARK 3 L13: -0.5033 L23: 0.4368
REMARK 3 S TENSOR
REMARK 3 S11: -0.0780 S12: 0.0287 S13: -0.1243
REMARK 3 S21: 0.0176 S22: 0.0363 S23: 0.2835
REMARK 3 S31: 0.0200 S32: -0.3072 S33: 0.0323
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: ( CHAIN E AND RESID 49:64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.373 22.905 0.853
REMARK 3 T TENSOR
REMARK 3 T11: 0.1680 T22: 0.1944
REMARK 3 T33: 0.2419 T12: 0.0017
REMARK 3 T13: 0.0021 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 2.7098 L22: 1.7676
REMARK 3 L33: 8.5454 L12: -0.5065
REMARK 3 L13: -2.3278 L23: 1.1906
REMARK 3 S TENSOR
REMARK 3 S11: -0.2271 S12: 0.0557 S13: -0.1652
REMARK 3 S21: 0.0216 S22: -0.1249 S23: 0.2949
REMARK 3 S31: -0.1659 S32: -0.5420 S33: 0.1858
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: ( CHAIN E AND RESID 65:74 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.356 15.306 13.147
REMARK 3 T TENSOR
REMARK 3 T11: 0.3103 T22: 0.3257
REMARK 3 T33: 0.3454 T12: -0.0209
REMARK 3 T13: 0.0518 T23: 0.0867
REMARK 3 L TENSOR
REMARK 3 L11: 1.5269 L22: 2.0294
REMARK 3 L33: 2.0172 L12: 0.4605
REMARK 3 L13: 2.4813 L23: 9.9433
REMARK 3 S TENSOR
REMARK 3 S11: 0.1238 S12: -0.2746 S13: -0.2787
REMARK 3 S21: 0.2547 S22: -0.0368 S23: -0.3147
REMARK 3 S31: 0.4770 S32: 0.2977 S33: -0.0931
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: ( CHAIN E AND RESID 75:84 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.005 8.767 1.411
REMARK 3 T TENSOR
REMARK 3 T11: 0.2777 T22: 0.2168
REMARK 3 T33: 0.3053 T12: -0.0359
REMARK 3 T13: -0.0171 T23: 0.0434
REMARK 3 L TENSOR
REMARK 3 L11: 7.7898 L22: 4.9773
REMARK 3 L33: 2.0145 L12: -4.7238
REMARK 3 L13: -3.1200 L23: 3.7412
REMARK 3 S TENSOR
REMARK 3 S11: 0.0601 S12: -0.2933 S13: -0.7224
REMARK 3 S21: 0.4734 S22: 0.0466 S23: 0.4140
REMARK 3 S31: 0.5560 S32: -0.1600 S33: 0.0075
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: ( CHAIN E AND RESID 85:91 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.552 21.659 2.959
REMARK 3 T TENSOR
REMARK 3 T11: 0.1549 T22: 0.1622
REMARK 3 T33: 0.1830 T12: 0.0036
REMARK 3 T13: 0.0318 T23: 0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 1.4387 L22: 6.6405
REMARK 3 L33: 1.5662 L12: 0.9443
REMARK 3 L13: 1.1923 L23: 2.6570
REMARK 3 S TENSOR
REMARK 3 S11: -0.0271 S12: -0.0984 S13: -0.1156
REMARK 3 S21: 0.1455 S22: 0.0226 S23: 0.2297
REMARK 3 S31: 0.0502 S32: -0.0509 S33: -0.0300
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: ( CHAIN E AND ( RESID 92:98 OR RESID 101:102 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.736 36.009 11.493
REMARK 3 T TENSOR
REMARK 3 T11: 0.1406 T22: 0.3186
REMARK 3 T33: 0.3599 T12: -0.0026
REMARK 3 T13: 0.0047 T23: -0.0687
REMARK 3 L TENSOR
REMARK 3 L11: 6.4114 L22: 8.3996
REMARK 3 L33: 9.1812 L12: -0.9979
REMARK 3 L13: -1.1339 L23: 1.4366
REMARK 3 S TENSOR
REMARK 3 S11: -0.4364 S12: -0.4616 S13: 0.3112
REMARK 3 S21: 0.5554 S22: -0.0028 S23: 1.2047
REMARK 3 S31: -0.0992 S32: -0.9122 S33: 0.3550
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: ( CHAIN F AND RESID 4:37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.993 43.914 2.661
REMARK 3 T TENSOR
REMARK 3 T11: 0.2238 T22: 0.2020
REMARK 3 T33: 0.4934 T12: 0.0249
REMARK 3 T13: -0.0460 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.8699 L22: 2.1625
REMARK 3 L33: 1.9748 L12: 1.2461
REMARK 3 L13: 0.2526 L23: 0.9838
REMARK 3 S TENSOR
REMARK 3 S11: -0.1173 S12: -0.0584 S13: 0.7121
REMARK 3 S21: -0.1167 S22: -0.1660 S23: 0.9091
REMARK 3 S31: -0.2005 S32: -0.2843 S33: 0.2548
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: ( CHAIN F AND RESID 38:91 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.725 41.346 -0.806
REMARK 3 T TENSOR
REMARK 3 T11: 0.2192 T22: 0.2269
REMARK 3 T33: 0.3452 T12: 0.0354
REMARK 3 T13: -0.0806 T23: 0.0387
REMARK 3 L TENSOR
REMARK 3 L11: 2.1471 L22: 2.5766
REMARK 3 L33: 0.7620 L12: 1.9500
REMARK 3 L13: 0.1812 L23: 1.0287
REMARK 3 S TENSOR
REMARK 3 S11: -0.2552 S12: 0.1829 S13: 0.5505
REMARK 3 S21: -0.4130 S22: 0.0813 S23: 0.6404
REMARK 3 S31: -0.2831 S32: -0.1710 S33: 0.1679
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: ( CHAIN F AND ( RESID 92:98 OR RESID 101:102 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.761 26.269 -7.639
REMARK 3 T TENSOR
REMARK 3 T11: 0.1742 T22: 0.3774
REMARK 3 T33: 0.3725 T12: -0.0103
REMARK 3 T13: -0.1013 T23: 0.0486
REMARK 3 L TENSOR
REMARK 3 L11: 1.6987 L22: 4.0261
REMARK 3 L33: 5.9384 L12: -1.5951
REMARK 3 L13: 0.5668 L23: 3.2810
REMARK 3 S TENSOR
REMARK 3 S11: -0.0454 S12: 0.5488 S13: -0.7140
REMARK 3 S21: 0.0096 S22: -0.0285 S23: 0.3445
REMARK 3 S31: 0.1776 S32: -0.7344 S33: -0.0775
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 8ECX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-22.
REMARK 100 THE DEPOSITION ID IS D_1000268199.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63379
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030
REMARK 200 RESOLUTION RANGE LOW (A) : 49.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.40
REMARK 200 R MERGE (I) : 0.14900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.40
REMARK 200 R MERGE FOR SHELL (I) : 1.30200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: UNPUBLISHED
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12 % PEG 4000, 0.1 M SODIUM ACETATE PH
REMARK 280 5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.09200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.09200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 54.50650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.49200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 54.50650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.49200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 60.09200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 54.50650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 74.49200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 60.09200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 54.50650
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 74.49200
REMARK 290 SMTRY3 8 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: 15640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 314 LIES ON A SPECIAL POSITION.
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 SER A -3
REMARK 465 GLY A -2
REMARK 465 GLY A -1
REMARK 465 GLY A 0
REMARK 465 SER B -3
REMARK 465 GLY B -2
REMARK 465 GLY B -1
REMARK 465 SER D -3
REMARK 465 GLY D -2
REMARK 465 GLY D -1
REMARK 465 SER E -3
REMARK 465 GLY E -2
REMARK 465 SER F -3
REMARK 465 GLY F -2
REMARK 465 GLY F -1
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 GLU A 97 CG CD OE1 OE2
REMARK 470 GLU B 97 CG CD OE1 OE2
REMARK 470 GLU C 17 CG CD OE1 OE2
REMARK 470 GLU D 17 CG CD OE1 OE2
REMARK 470 GLU E 17 CG CD OE1 OE2
REMARK 470 GLN E 32 CG CD OE1 NE2
REMARK 470 GLU E 71 CG CD OE1 OE2
REMARK 470 GLU F 17 CG CD OE1 OE2
REMARK 470 GLU F 59 CG CD OE1 OE2
REMARK 470 GLU F 71 CG CD OE1 OE2
REMARK 470 GLU F 97 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 246 O HOH B 257 2.18
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 TYR A 83 -31.69 -150.40
REMARK 500 TYR B 83 -30.52 -136.04
REMARK 500 TYR C 83 -28.41 -149.43
REMARK 500 TYR D 83 -30.44 -132.81
REMARK 500 TYR E 83 -33.94 -151.47
REMARK 500 MET F 1 -118.78 -79.33
REMARK 500 MET F 1 -95.04 -109.61
REMARK 500 TYR F 83 -31.40 -136.77
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8ECX A 1 98 UNP A0A072ZNL3_PSEAI
DBREF2 8ECX A A0A072ZNL3 1 98
DBREF1 8ECX B 1 98 UNP A0A072ZNL3_PSEAI
DBREF2 8ECX B A0A072ZNL3 1 98
DBREF1 8ECX C 1 98 UNP A0A072ZNL3_PSEAI
DBREF2 8ECX C A0A072ZNL3 1 98
DBREF1 8ECX D 1 98 UNP A0A072ZNL3_PSEAI
DBREF2 8ECX D A0A072ZNL3 1 98
DBREF1 8ECX E 1 98 UNP A0A072ZNL3_PSEAI
DBREF2 8ECX E A0A072ZNL3 1 98
DBREF1 8ECX F 1 98 UNP A0A072ZNL3_PSEAI
DBREF2 8ECX F A0A072ZNL3 1 98
SEQADV 8ECX SER A -3 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY A -2 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY A -1 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY A 0 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX SER B -3 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY B -2 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY B -1 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY B 0 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX SER C -3 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY C -2 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY C -1 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY C 0 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX SER D -3 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY D -2 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY D -1 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY D 0 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX SER E -3 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY E -2 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY E -1 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY E 0 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX SER F -3 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY F -2 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY F -1 UNP A0A072ZNL EXPRESSION TAG
SEQADV 8ECX GLY F 0 UNP A0A072ZNL EXPRESSION TAG
SEQRES 1 A 102 SER GLY GLY GLY MET THR TYR HIS VAL LEU VAL GLN PHE
SEQRES 2 A 102 ASP VAL PRO SER ASP LYS ARG GLU ALA PHE ALA ALA ALA
SEQRES 3 A 102 GLY LEU PHE ASP ALA ASN GLY SER LEU GLN ASN GLU PRO
SEQRES 4 A 102 GLY THR LEU ARG PHE GLU VAL ILE ARG ASP GLU ASN ASN
SEQRES 5 A 102 ARG ASN ARG PHE TYR LEU ASP GLU VAL TYR GLU ASP GLU
SEQRES 6 A 102 ALA ALA PHE LEU GLN HIS CME ARG ASN GLU THR ILE ALA
SEQRES 7 A 102 ARG PHE TYR GLU LEU ILE ASP SER TYR ALA PHE GLY PRO
SEQRES 8 A 102 LEU PHE LEU PHE LYS GLY TYR ARG VAL GLU GLY
SEQRES 1 B 102 SER GLY GLY GLY MET THR TYR HIS VAL LEU VAL GLN PHE
SEQRES 2 B 102 ASP VAL PRO SER ASP LYS ARG GLU ALA PHE ALA ALA ALA
SEQRES 3 B 102 GLY LEU PHE ASP ALA ASN GLY SER LEU GLN ASN GLU PRO
SEQRES 4 B 102 GLY THR LEU ARG PHE GLU VAL ILE ARG ASP GLU ASN ASN
SEQRES 5 B 102 ARG ASN ARG PHE TYR LEU ASP GLU VAL TYR GLU ASP GLU
SEQRES 6 B 102 ALA ALA PHE LEU GLN HIS CME ARG ASN GLU THR ILE ALA
SEQRES 7 B 102 ARG PHE TYR GLU LEU ILE ASP SER TYR ALA PHE GLY PRO
SEQRES 8 B 102 LEU PHE LEU PHE LYS GLY TYR ARG VAL GLU GLY
SEQRES 1 C 102 SER GLY GLY GLY MET THR TYR HIS VAL LEU VAL GLN PHE
SEQRES 2 C 102 ASP VAL PRO SER ASP LYS ARG GLU ALA PHE ALA ALA ALA
SEQRES 3 C 102 GLY LEU PHE ASP ALA ASN GLY SER LEU GLN ASN GLU PRO
SEQRES 4 C 102 GLY THR LEU ARG PHE GLU VAL ILE ARG ASP GLU ASN ASN
SEQRES 5 C 102 ARG ASN ARG PHE TYR LEU ASP GLU VAL TYR GLU ASP GLU
SEQRES 6 C 102 ALA ALA PHE LEU GLN HIS CME ARG ASN GLU THR ILE ALA
SEQRES 7 C 102 ARG PHE TYR GLU LEU ILE ASP SER TYR ALA PHE GLY PRO
SEQRES 8 C 102 LEU PHE LEU PHE LYS GLY TYR ARG VAL GLU GLY
SEQRES 1 D 102 SER GLY GLY GLY MET THR TYR HIS VAL LEU VAL GLN PHE
SEQRES 2 D 102 ASP VAL PRO SER ASP LYS ARG GLU ALA PHE ALA ALA ALA
SEQRES 3 D 102 GLY LEU PHE ASP ALA ASN GLY SER LEU GLN ASN GLU PRO
SEQRES 4 D 102 GLY THR LEU ARG PHE GLU VAL ILE ARG ASP GLU ASN ASN
SEQRES 5 D 102 ARG ASN ARG PHE TYR LEU ASP GLU VAL TYR GLU ASP GLU
SEQRES 6 D 102 ALA ALA PHE LEU GLN HIS CME ARG ASN GLU THR ILE ALA
SEQRES 7 D 102 ARG PHE TYR GLU LEU ILE ASP SER TYR ALA PHE GLY PRO
SEQRES 8 D 102 LEU PHE LEU PHE LYS GLY TYR ARG VAL GLU GLY
SEQRES 1 E 102 SER GLY GLY GLY MET THR TYR HIS VAL LEU VAL GLN PHE
SEQRES 2 E 102 ASP VAL PRO SER ASP LYS ARG GLU ALA PHE ALA ALA ALA
SEQRES 3 E 102 GLY LEU PHE ASP ALA ASN GLY SER LEU GLN ASN GLU PRO
SEQRES 4 E 102 GLY THR LEU ARG PHE GLU VAL ILE ARG ASP GLU ASN ASN
SEQRES 5 E 102 ARG ASN ARG PHE TYR LEU ASP GLU VAL TYR GLU ASP GLU
SEQRES 6 E 102 ALA ALA PHE LEU GLN HIS CME ARG ASN GLU THR ILE ALA
SEQRES 7 E 102 ARG PHE TYR GLU LEU ILE ASP SER TYR ALA PHE GLY PRO
SEQRES 8 E 102 LEU PHE LEU PHE LYS GLY TYR ARG VAL GLU GLY
SEQRES 1 F 102 SER GLY GLY GLY MET THR TYR HIS VAL LEU VAL GLN PHE
SEQRES 2 F 102 ASP VAL PRO SER ASP LYS ARG GLU ALA PHE ALA ALA ALA
SEQRES 3 F 102 GLY LEU PHE ASP ALA ASN GLY SER LEU GLN ASN GLU PRO
SEQRES 4 F 102 GLY THR LEU ARG PHE GLU VAL ILE ARG ASP GLU ASN ASN
SEQRES 5 F 102 ARG ASN ARG PHE TYR LEU ASP GLU VAL TYR GLU ASP GLU
SEQRES 6 F 102 ALA ALA PHE LEU GLN HIS CME ARG ASN GLU THR ILE ALA
SEQRES 7 F 102 ARG PHE TYR GLU LEU ILE ASP SER TYR ALA PHE GLY PRO
SEQRES 8 F 102 LEU PHE LEU PHE LYS GLY TYR ARG VAL GLU GLY
MODRES 8ECX CME A 68 CYS MODIFIED RESIDUE
MODRES 8ECX CME B 68 CYS MODIFIED RESIDUE
MODRES 8ECX CME C 68 CYS MODIFIED RESIDUE
MODRES 8ECX CME D 68 CYS MODIFIED RESIDUE
MODRES 8ECX CME E 68 CYS MODIFIED RESIDUE
MODRES 8ECX CME F 68 CYS MODIFIED RESIDUE
HET CME A 68 10
HET CME B 68 10
HET WEZ C 49 15
HET POK C 49 15
HET CME C 68 10
HET POK D 49 15
HET WEZ D 49 15
HET CME D 68 10
HET WEZ E 49 15
HET POK E 49 15
HET CME E 68 10
HET CME F 68 10
HET ACT A 101 4
HET ACT A 102 4
HET GOL A 103 6
HET ACT B 101 4
HET ACT B 102 4
HET ACT C 101 4
HET ACT C 102 4
HET ACT C 103 4
HET ACT D 101 4
HET ACT E 101 4
HET ACT E 102 4
HET ACT E 103 4
HET ACT F 101 4
HET ACT F 102 4
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM WEZ N-[(4S)-4-AMINO-5-OXOPENTYL]-N'-[(1S)-1-HYDROXY-2-
HETNAM 2 WEZ OXOETHYL]GUANIDINE
HETNAM POK 2-[[~{N}-[(4~{S})-4-AZANYL-5-OXIDANYLIDENE-
HETNAM 2 POK PENTYL]CARBAMIMIDOYL]AMINO]ETHANOIC ACID
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 CME 6(C5 H11 N O3 S2)
FORMUL 3 WEZ 3(C8 H16 N4 O4)
FORMUL 3 POK 3(C8 H16 N4 O4)
FORMUL 7 ACT 13(C2 H3 O2 1-)
FORMUL 9 GOL C3 H8 O3
FORMUL 21 HOH *774(H2 O)
HELIX 1 AA1 PRO A 12 ASP A 14 5 3
HELIX 2 AA2 LYS A 15 GLU A 34 1 20
HELIX 3 AA3 ASP A 60 ARG A 69 1 10
HELIX 4 AA4 ASN A 70 ASP A 81 1 12
HELIX 5 AA5 PRO B 12 ASP B 14 5 3
HELIX 6 AA6 LYS B 15 GLU B 34 1 20
HELIX 7 AA7 ASP B 60 ASN B 70 1 11
HELIX 8 AA8 ASN B 70 ASP B 81 1 12
HELIX 9 AA9 PRO C 12 ASP C 14 5 3
HELIX 10 AB1 LYS C 15 GLU C 34 1 20
HELIX 11 AB2 ASP C 60 ARG C 69 1 10
HELIX 12 AB3 ASN C 70 ASP C 81 1 12
HELIX 13 AB4 PRO D 12 ASP D 14 5 3
HELIX 14 AB5 LYS D 15 GLU D 34 1 20
HELIX 15 AB6 ASP D 60 ARG D 69 1 10
HELIX 16 AB7 ASN D 70 ASP D 81 1 12
HELIX 17 AB8 PRO E 12 ASP E 14 5 3
HELIX 18 AB9 LYS E 15 GLU E 34 1 20
HELIX 19 AC1 ASP E 60 ASN E 70 1 11
HELIX 20 AC2 ASN E 70 ASP E 81 1 12
HELIX 21 AC3 PRO F 12 ASP F 14 5 3
HELIX 22 AC4 LYS F 15 GLU F 34 1 20
HELIX 23 AC5 ASP F 60 ARG F 69 1 10
HELIX 24 AC6 ASN F 70 ASP F 81 1 12
SHEET 1 AA1 9 TYR A 3 ASP A 10 0
SHEET 2 AA1 9 ARG A 51 TYR A 58 -1 O PHE A 52 N PHE A 9
SHEET 3 AA1 9 THR A 37 ASP A 45 -1 N ILE A 43 O TYR A 53
SHEET 4 AA1 9 PHE B 85 ARG B 95 -1 O TYR B 94 N ARG A 44
SHEET 5 AA1 9 TYR B 3 ASP B 10 -1 N ASP B 10 O PHE B 85
SHEET 6 AA1 9 ARG B 51 TYR B 58 -1 O TYR B 58 N TYR B 3
SHEET 7 AA1 9 THR B 37 ASP B 45 -1 N ILE B 43 O TYR B 53
SHEET 8 AA1 9 PHE A 85 ARG A 95 -1 N TYR A 94 O ARG B 44
SHEET 9 AA1 9 TYR A 3 ASP A 10 -1 N HIS A 4 O GLY A 93
SHEET 1 AA2 9 TYR C 3 ASP C 10 0
SHEET 2 AA2 9 ARG C 51 TYR C 58 -1 O PHE C 52 N PHE C 9
SHEET 3 AA2 9 THR C 37 ASP C 45 -1 N ILE C 43 O TYR C 53
SHEET 4 AA2 9 PHE D 85 ARG D 95 -1 O TYR D 94 N ARG C 44
SHEET 5 AA2 9 TYR D 3 ASP D 10 -1 N HIS D 4 O GLY D 93
SHEET 6 AA2 9 ARG D 51 TYR D 58 -1 O PHE D 52 N PHE D 9
SHEET 7 AA2 9 THR D 37 ASP D 45 -1 N ILE D 43 O TYR D 53
SHEET 8 AA2 9 PHE C 85 ARG C 95 -1 N TYR C 94 O ARG D 44
SHEET 9 AA2 9 TYR C 3 ASP C 10 -1 N HIS C 4 O GLY C 93
SHEET 1 AA3 9 TYR E 3 ASP E 10 0
SHEET 2 AA3 9 ARG E 51 TYR E 58 -1 O GLU E 56 N VAL E 5
SHEET 3 AA3 9 THR E 37 ASP E 45 -1 N ILE E 43 O TYR E 53
SHEET 4 AA3 9 PHE F 85 ARG F 95 -1 O TYR F 94 N ARG E 44
SHEET 5 AA3 9 TYR F 3 ASP F 10 -1 N ASP F 10 O PHE F 85
SHEET 6 AA3 9 ARG F 51 TYR F 58 -1 O GLU F 56 N VAL F 5
SHEET 7 AA3 9 THR F 37 ASP F 45 -1 N ILE F 43 O TYR F 53
SHEET 8 AA3 9 PHE E 85 ARG E 95 -1 N TYR E 94 O ARG F 44
SHEET 9 AA3 9 TYR E 3 ASP E 10 -1 N ASP E 10 O PHE E 85
LINK C HIS A 67 N CME A 68 1555 1555 1.33
LINK C CME A 68 N ARG A 69 1555 1555 1.33
LINK C HIS B 67 N CME B 68 1555 1555 1.33
LINK C CME B 68 N ARG B 69 1555 1555 1.33
LINK C ASN C 48 N CWEZ C 49 1555 1555 1.33
LINK C ASN C 48 N BPOK C 49 1555 1555 1.33
LINK C CWEZ C 49 N ASN C 50 1555 1555 1.32
LINK C BPOK C 49 N ASN C 50 1555 1555 1.32
LINK C HIS C 67 N CME C 68 1555 1555 1.33
LINK C CME C 68 N ARG C 69 1555 1555 1.33
LINK C ASN D 48 N BPOK D 49 1555 1555 1.33
LINK C ASN D 48 N CWEZ D 49 1555 1555 1.33
LINK C BPOK D 49 N ASN D 50 1555 1555 1.32
LINK C CWEZ D 49 N ASN D 50 1555 1555 1.33
LINK C HIS D 67 N CME D 68 1555 1555 1.33
LINK C CME D 68 N ARG D 69 1555 1555 1.33
LINK C ASN E 48 N CWEZ E 49 1555 1555 1.33
LINK C ASN E 48 N BPOK E 49 1555 1555 1.33
LINK C CWEZ E 49 N ASN E 50 1555 1555 1.32
LINK C BPOK E 49 N ASN E 50 1555 1555 1.32
LINK C HIS E 67 N CME E 68 1555 1555 1.33
LINK C CME E 68 N ARG E 69 1555 1555 1.33
LINK C HIS F 67 N CME F 68 1555 1555 1.33
LINK C CME F 68 N ARG F 69 1555 1555 1.33
CISPEP 1 GLY A 86 PRO A 87 0 4.41
CISPEP 2 GLY B 86 PRO B 87 0 -1.48
CISPEP 3 GLY C 86 PRO C 87 0 2.40
CISPEP 4 GLY D 86 PRO D 87 0 1.81
CISPEP 5 GLY E 86 PRO E 87 0 3.67
CISPEP 6 GLY F 86 PRO F 87 0 0.41
CRYST1 109.013 148.984 120.184 90.00 90.00 90.00 C 2 2 21 48
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 0.009173 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006712 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008321 0.00000
TER 816 GLY A 98
ATOM 817 N GLY B 0 29.538 8.137 17.615 1.00 67.02 N
ATOM 818 CA GLY B 0 28.601 7.216 18.233 1.00 66.44 C
ATOM 819 C GLY B 0 27.192 7.769 18.292 1.00 47.57 C
ATOM 820 O GLY B 0 26.596 7.848 19.367 1.00 78.70 O
ATOM 821 N MET B 1 26.667 8.143 17.123 1.00 59.49 N
ATOM 822 CA AMET B 1 25.349 8.771 17.007 0.51 42.53 C
ATOM 823 CA BMET B 1 25.347 8.762 17.016 0.49 42.52 C
ATOM 824 C MET B 1 25.234 9.997 17.906 1.00 38.23 C
ATOM 825 O MET B 1 24.165 10.306 18.438 1.00 29.23 O
ATOM 826 CB AMET B 1 24.221 7.774 17.290 0.51 45.90 C
ATOM 827 CB BMET B 1 24.239 7.752 17.326 0.49 45.90 C
ATOM 828 CG AMET B 1 23.829 6.946 16.072 0.51 53.37 C
ATOM 829 CG BMET B 1 24.079 6.695 16.244 0.49 53.39 C
ATOM 830 SD AMET B 1 22.066 6.568 15.979 0.51 63.03 S
ATOM 831 SD BMET B 1 22.368 6.177 16.053 0.49 64.75 S
ATOM 832 CE AMET B 1 21.364 7.881 16.975 0.51 38.66 C
ATOM 833 CE BMET B 1 21.636 7.707 15.490 0.49 37.01 C
ATOM 834 N THR B 2 26.346 10.704 18.080 1.00 29.50 N
ATOM 835 CA THR B 2 26.302 12.018 18.689 1.00 26.30 C
ATOM 836 C THR B 2 25.600 12.983 17.735 1.00 21.47 C
ATOM 837 O THR B 2 25.407 12.695 16.550 1.00 21.88 O
ATOM 838 CB THR B 2 27.715 12.508 19.015 1.00 23.49 C
ATOM 839 OG1 THR B 2 28.591 12.217 17.917 1.00 25.15 O
ATOM 840 CG2 THR B 2 28.243 11.825 20.273 1.00 24.25 C
ATOM 841 N TYR B 3 25.214 14.138 18.261 1.00 18.88 N
ATOM 842 CA TYR B 3 24.424 15.112 17.518 1.00 20.84 C
ATOM 843 C TYR B 3 25.325 16.274 17.118 1.00 19.97 C
ATOM 844 O TYR B 3 25.896 16.947 17.983 1.00 20.59 O
ATOM 845 CB TYR B 3 23.237 15.578 18.359 1.00 18.38 C
ATOM 846 CG TYR B 3 22.203 16.403 17.630 1.00 18.50 C
ATOM 847 CD1 TYR B 3 21.397 15.840 16.647 1.00 22.92 C
ATOM 848 CD2 TYR B 3 22.000 17.734 17.959 1.00 18.26 C
ATOM 849 CE1 TYR B 3 20.434 16.595 15.992 1.00 23.39 C
ATOM 850 CE2 TYR B 3 21.045 18.495 17.312 1.00 19.06 C
ATOM 851 CZ TYR B 3 20.264 17.925 16.329 1.00 26.05 C
ATOM 852 OH TYR B 3 19.312 18.691 15.689 1.00 23.90 O
ATOM 853 N HIS B 4 25.455 16.501 15.814 1.00 22.26 N
ATOM 854 CA HIS B 4 26.386 17.481 15.271 1.00 19.45 C
ATOM 855 C HIS B 4 25.611 18.645 14.671 1.00 20.01 C
ATOM 856 O HIS B 4 24.685 18.438 13.881 1.00 21.52 O
ATOM 857 CB HIS B 4 27.294 16.846 14.216 1.00 18.47 C
ATOM 858 CG HIS B 4 28.242 15.829 14.769 1.00 22.89 C
ATOM 859 ND1 HIS B 4 29.611 15.948 14.657 1.00 21.49 N
ATOM 860 CD2 HIS B 4 28.018 14.675 15.441 1.00 25.38 C
ATOM 861 CE1 HIS B 4 30.189 14.909 15.234 1.00 26.08 C
ATOM 862 NE2 HIS B 4 29.245 14.124 15.720 1.00 27.46 N
ATOM 863 N VAL B 5 25.992 19.862 15.050 1.00 21.26 N
ATOM 864 CA VAL B 5 25.350 21.080 14.576 1.00 18.82 C
ATOM 865 C VAL B 5 26.420 21.987 13.992 1.00 20.23 C
ATOM 866 O VAL B 5 27.423 22.278 14.653 1.00 17.07 O
ATOM 867 CB VAL B 5 24.590 21.803 15.704 1.00 26.71 C
ATOM 868 CG1 VAL B 5 24.009 23.117 15.203 1.00 18.63 C
ATOM 869 CG2 VAL B 5 23.498 20.907 16.269 1.00 21.15 C
ATOM 870 N LEU B 6 26.205 22.438 12.761 1.00 20.04 N
ATOM 871 CA LEU B 6 27.143 23.317 12.078 1.00 18.23 C
ATOM 872 C LEU B 6 26.466 24.644 11.772 1.00 24.13 C
ATOM 873 O LEU B 6 25.415 24.674 11.124 1.00 22.35 O
ATOM 874 CB LEU B 6 27.646 22.701 10.784 1.00 16.99 C
ATOM 875 CG LEU B 6 28.917 23.446 10.411 1.00 44.97 C
ATOM 876 CD1 LEU B 6 30.141 22.847 11.112 1.00 27.90 C
ATOM 877 CD2 LEU B 6 29.043 23.515 8.942 1.00 46.39 C
ATOM 878 N VAL B 7 27.090 25.739 12.200 1.00 19.64 N
ATOM 879 CA VAL B 7 26.477 27.061 12.165 1.00 19.36 C
ATOM 880 C VAL B 7 27.419 28.034 11.468 1.00 21.12 C
ATOM 881 O VAL B 7 28.642 27.926 11.601 1.00 23.56 O
ATOM 882 CB VAL B 7 26.143 27.552 13.588 1.00 22.44 C
ATOM 883 CG1 VAL B 7 25.138 28.663 13.525 1.00 22.85 C
ATOM 884 CG2 VAL B 7 25.619 26.402 14.441 1.00 27.29 C
ATOM 885 N GLN B 8 26.848 28.989 10.733 1.00 22.20 N
ATOM 886 CA GLN B 8 27.608 29.947 9.939 1.00 20.41 C
ATOM 887 C GLN B 8 27.245 31.374 10.333 1.00 19.51 C
ATOM 888 O GLN B 8 26.065 31.702 10.499 1.00 17.63 O
ATOM 889 CB GLN B 8 27.350 29.725 8.442 1.00 18.18 C
ATOM 890 CG GLN B 8 28.013 30.728 7.508 1.00 17.61 C
ATOM 891 CD GLN B 8 27.743 30.413 6.050 1.00 25.89 C
ATOM 892 OE1 GLN B 8 28.232 29.416 5.518 1.00 21.02 O
ATOM 893 NE2 GLN B 8 26.950 31.254 5.399 1.00 19.62 N
ATOM 894 N PHE B 9 28.269 32.218 10.482 1.00 20.76 N
ATOM 895 CA PHE B 9 28.103 33.619 10.849 1.00 18.29 C
ATOM 896 C PHE B 9 28.954 34.498 9.944 1.00 22.29 C
ATOM 897 O PHE B 9 30.054 34.107 9.544 1.00 23.38 O
ATOM 898 CB PHE B 9 28.508 33.880 12.307 1.00 18.63 C
ATOM 899 CG PHE B 9 27.545 33.338 13.322 1.00 21.72 C
ATOM 900 CD1 PHE B 9 26.492 34.113 13.779 1.00 20.97 C
ATOM 901 CD2 PHE B 9 27.708 32.065 13.843 1.00 23.44 C
ATOM 902 CE1 PHE B 9 25.607 33.625 14.724 1.00 26.63 C
ATOM 903 CE2 PHE B 9 26.824 31.567 14.787 1.00 23.45 C
ATOM 904 CZ PHE B 9 25.773 32.350 15.230 1.00 20.33 C
ATOM 905 N ASP B 10 28.450 35.692 9.640 1.00 19.48 N
ATOM 906 CA ASP B 10 29.194 36.700 8.898 1.00 22.09 C
ATOM 907 C ASP B 10 29.271 37.973 9.729 1.00 23.10 C
ATOM 908 O ASP B 10 28.299 38.346 10.393 1.00 22.02 O
ATOM 909 CB ASP B 10 28.547 36.995 7.540 1.00 22.15 C
ATOM 910 CG ASP B 10 28.443 35.762 6.664 1.00 33.10 C
ATOM 911 OD1 ASP B 10 27.474 35.660 5.883 1.00 23.86 O
ATOM 912 OD2 ASP B 10 29.339 34.896 6.751 1.00 28.76 O
ATOM 913 N VAL B 11 30.427 38.630 9.697 1.00 20.81 N
ATOM 914 CA VAL B 11 30.681 39.803 10.535 1.00 23.23 C
ATOM 915 C VAL B 11 31.364 40.882 9.705 1.00 23.12 C
ATOM 916 O VAL B 11 31.992 40.599 8.678 1.00 22.53 O
ATOM 917 CB VAL B 11 31.549 39.457 11.763 1.00 23.59 C
ATOM 918 CG1 VAL B 11 30.849 38.438 12.652 1.00 20.82 C
ATOM 919 CG2 VAL B 11 32.916 38.946 11.323 1.00 25.67 C
ATOM 920 N PRO B 12 31.241 42.139 10.129 1.00 26.50 N
ATOM 921 CA PRO B 12 31.994 43.215 9.472 1.00 28.62 C
ATOM 922 C PRO B 12 33.495 43.035 9.643 1.00 31.62 C
ATOM 923 O PRO B 12 33.971 42.299 10.510 1.00 25.21 O
ATOM 924 CB PRO B 12 31.501 44.482 10.180 1.00 29.91 C
ATOM 925 CG PRO B 12 30.165 44.116 10.723 1.00 31.75 C
ATOM 926 CD PRO B 12 30.263 42.665 11.096 1.00 27.34 C
ATOM 927 N ASER B 13 34.246 43.743 8.795 0.57 28.57 N
ATOM 928 N BSER B 13 34.243 43.741 8.791 0.43 28.63 N
ATOM 929 CA ASER B 13 35.695 43.568 8.756 0.57 31.59 C
ATOM 930 CA BSER B 13 35.693 43.575 8.757 0.43 31.59 C
ATOM 931 C ASER B 13 36.360 43.983 10.062 0.57 31.81 C
ATOM 932 C BSER B 13 36.332 43.950 10.088 0.43 31.80 C
ATOM 933 O ASER B 13 37.374 43.394 10.455 0.57 33.13 O
ATOM 934 O BSER B 13 37.289 43.304 10.529 0.43 33.05 O
ATOM 935 CB ASER B 13 36.286 44.358 7.589 0.57 31.86 C
ATOM 936 CB BSER B 13 36.290 44.412 7.625 0.43 31.84 C
ATOM 937 OG ASER B 13 35.632 44.039 6.373 0.57 38.32 O
ATOM 938 OG BSER B 13 36.177 45.798 7.902 0.43 29.62 O
ATOM 939 N ASP B 14 35.817 44.987 10.745 1.00 28.18 N
ATOM 940 CA ASP B 14 36.377 45.453 12.005 1.00 29.24 C
ATOM 941 C ASP B 14 35.874 44.665 13.212 1.00 29.90 C
ATOM 942 O ASP B 14 36.192 45.032 14.348 1.00 29.53 O
ATOM 943 CB ASP B 14 36.082 46.944 12.195 1.00 35.08 C
ATOM 944 CG ASP B 14 34.602 47.233 12.368 1.00 35.89 C
ATOM 945 OD1 ASP B 14 33.773 46.405 11.937 1.00 35.75 O
ATOM 946 OD2 ASP B 14 34.268 48.293 12.939 1.00 52.38 O
ATOM 947 N LYS B 15 35.104 43.596 12.996 1.00 27.54 N
ATOM 948 CA LYS B 15 34.566 42.785 14.083 1.00 28.69 C
ATOM 949 C LYS B 15 35.085 41.351 14.041 1.00 31.24 C
ATOM 950 O LYS B 15 34.511 40.469 14.688 1.00 27.06 O
ATOM 951 CB LYS B 15 33.038 42.792 14.049 1.00 25.89 C
ATOM 952 CG LYS B 15 32.413 44.116 14.453 1.00 30.07 C
ATOM 953 CD LYS B 15 32.986 44.630 15.761 1.00 35.15 C
ATOM 954 CE LYS B 15 32.201 45.828 16.264 1.00 52.06 C
ATOM 955 NZ LYS B 15 32.280 45.956 17.742 1.00 57.23 N
ATOM 956 N ARG B 16 36.164 41.102 13.294 1.00 26.76 N
ATOM 957 CA ARG B 16 36.698 39.747 13.193 1.00 26.70 C
ATOM 958 C ARG B 16 37.233 39.258 14.534 1.00 27.09 C
ATOM 959 O ARG B 16 36.964 38.122 14.941 1.00 25.91 O
ATOM 960 CB ARG B 16 37.792 39.693 12.124 1.00 25.37 C
ATOM 961 CG ARG B 16 37.283 39.931 10.711 1.00 33.21 C
ATOM 962 CD ARG B 16 38.409 40.239 9.734 1.00 32.67 C
ATOM 963 NE ARG B 16 37.896 40.621 8.422 1.00 34.50 N
ATOM 964 CZ ARG B 16 38.598 41.255 7.493 1.00 32.51 C
ATOM 965 NH1 ARG B 16 39.865 41.582 7.685 1.00 30.83 N
ATOM 966 NH2 ARG B 16 38.015 41.565 6.338 1.00 30.31 N
ATOM 967 N GLU B 17 37.988 40.105 15.237 1.00 25.50 N
ATOM 968 CA GLU B 17 38.535 39.710 16.531 1.00 31.22 C
ATOM 969 C GLU B 17 37.436 39.570 17.576 1.00 30.83 C
ATOM 970 O GLU B 17 37.453 38.632 18.381 1.00 29.12 O
ATOM 971 CB GLU B 17 39.583 40.722 16.992 1.00 34.85 C
ATOM 972 CG GLU B 17 40.718 40.926 16.005 1.00 49.65 C
ATOM 973 CD GLU B 17 41.404 39.627 15.639 1.00 66.48 C
ATOM 974 OE1 GLU B 17 41.455 39.296 14.436 1.00 73.17 O
ATOM 975 OE2 GLU B 17 41.890 38.934 16.556 1.00 70.29 O
ATOM 976 N ALA B 18 36.471 40.493 17.575 1.00 28.08 N
ATOM 977 CA ALA B 18 35.414 40.458 18.579 1.00 28.03 C
ATOM 978 C ALA B 18 34.554 39.210 18.434 1.00 26.56 C
ATOM 979 O ALA B 18 34.162 38.602 19.437 1.00 25.17 O
ATOM 980 CB ALA B 18 34.554 41.718 18.486 1.00 25.88 C
ATOM 981 N PHE B 19 34.249 38.805 17.198 1.00 23.29 N
ATOM 982 CA PHE B 19 33.458 37.590 17.030 1.00 28.66 C
ATOM 983 C PHE B 19 34.251 36.356 17.432 1.00 26.12 C
ATOM 984 O PHE B 19 33.698 35.430 18.036 1.00 26.03 O
ATOM 985 CB PHE B 19 32.962 37.433 15.595 1.00 24.67 C
ATOM 986 CG PHE B 19 32.091 36.224 15.412 1.00 22.53 C
ATOM 987 CD1 PHE B 19 30.738 36.288 15.692 1.00 23.41 C
ATOM 988 CD2 PHE B 19 32.632 35.008 15.028 1.00 22.67 C
ATOM 989 CE1 PHE B 19 29.934 35.174 15.552 1.00 22.59 C
ATOM 990 CE2 PHE B 19 31.833 33.892 14.892 1.00 25.90 C
ATOM 991 CZ PHE B 19 30.484 33.975 15.153 1.00 19.34 C
ATOM 992 N ALA B 20 35.539 36.312 17.083 1.00 21.70 N
ATOM 993 CA ALA B 20 36.378 35.192 17.491 1.00 29.35 C
ATOM 994 C ALA B 20 36.364 35.033 19.005 1.00 27.09 C
ATOM 995 O ALA B 20 36.225 33.920 19.527 1.00 23.35 O
ATOM 996 CB ALA B 20 37.805 35.388 16.979 1.00 27.46 C
ATOM 997 N ALA B 21 36.482 36.150 19.728 1.00 25.02 N
ATOM 998 CA ALA B 21 36.450 36.100 21.186 1.00 24.03 C
ATOM 999 C ALA B 21 35.085 35.650 21.692 1.00 25.86 C
ATOM 1000 O ALA B 21 34.997 34.838 22.621 1.00 25.97 O
ATOM 1001 CB ALA B 21 36.817 37.467 21.763 1.00 27.50 C
ATOM 1002 N ALA B 22 34.009 36.162 21.089 1.00 25.69 N
ATOM 1003 CA ALA B 22 32.667 35.755 21.496 1.00 21.90 C
ATOM 1004 C ALA B 22 32.426 34.279 21.206 1.00 24.57 C
ATOM 1005 O ALA B 22 31.814 33.570 22.014 1.00 26.80 O
ATOM 1006 CB ALA B 22 31.620 36.621 20.794 1.00 21.70 C
ATOM 1007 N GLY B 23 32.904 33.796 20.057 1.00 18.94 N
ATOM 1008 CA GLY B 23 32.727 32.391 19.730 1.00 17.69 C
ATOM 1009 C GLY B 23 33.522 31.478 20.642 1.00 20.91 C
ATOM 1010 O GLY B 23 33.056 30.397 21.013 1.00 21.98 O
ATOM 1011 N LEU B 24 34.729 31.899 21.022 1.00 19.97 N
ATOM 1012 CA LEU B 24 35.524 31.102 21.949 1.00 21.04 C
ATOM 1013 C LEU B 24 34.898 31.082 23.337 1.00 23.40 C
ATOM 1014 O LEU B 24 34.929 30.053 24.022 1.00 20.85 O
ATOM 1015 CB LEU B 24 36.955 31.631 22.005 1.00 22.35 C
ATOM 1016 CG LEU B 24 37.801 31.255 20.790 1.00 30.05 C
ATOM 1017 CD1 LEU B 24 39.180 31.884 20.873 1.00 25.50 C
ATOM 1018 CD2 LEU B 24 37.900 29.740 20.660 1.00 25.99 C
ATOM 1019 N PHE B 25 34.325 32.209 23.770 1.00 22.36 N
ATOM 1020 CA PHE B 25 33.586 32.224 25.029 1.00 28.24 C
ATOM 1021 C PHE B 25 32.438 31.229 24.990 1.00 22.86 C
ATOM 1022 O PHE B 25 32.208 30.483 25.950 1.00 26.30 O
ATOM 1023 CB PHE B 25 33.046 33.623 25.320 1.00 21.70 C
ATOM 1024 CG PHE B 25 31.977 33.640 26.378 1.00 26.71 C
ATOM 1025 CD1 PHE B 25 32.321 33.700 27.719 1.00 25.31 C
ATOM 1026 CD2 PHE B 25 30.632 33.566 26.037 1.00 24.91 C
ATOM 1027 CE1 PHE B 25 31.348 33.702 28.702 1.00 32.01 C
ATOM 1028 CE2 PHE B 25 29.655 33.560 27.014 1.00 28.21 C
ATOM 1029 CZ PHE B 25 30.012 33.632 28.350 1.00 28.85 C
ATOM 1030 N ASP B 26 31.684 31.233 23.891 1.00 20.63 N
ATOM 1031 CA ASP B 26 30.570 30.307 23.736 1.00 20.62 C
ATOM 1032 C ASP B 26 31.047 28.865 23.849 1.00 26.20 C
ATOM 1033 O ASP B 26 30.458 28.057 24.577 1.00 22.98 O
ATOM 1034 CB ASP B 26 29.889 30.559 22.393 1.00 21.40 C
ATOM 1035 CG ASP B 26 28.591 29.803 22.239 1.00 32.52 C
ATOM 1036 OD1 ASP B 26 28.163 29.124 23.196 1.00 25.75 O
ATOM 1037 OD2 ASP B 26 27.993 29.898 21.150 1.00 23.39 O
ATOM 1038 N ALA B 27 32.133 28.533 23.148 1.00 21.49 N
ATOM 1039 CA ALA B 27 32.670 27.177 23.194 1.00 22.45 C
ATOM 1040 C ALA B 27 33.109 26.802 24.603 1.00 22.94 C
ATOM 1041 O ALA B 27 32.697 25.768 25.141 1.00 23.16 O
ATOM 1042 CB ALA B 27 33.839 27.050 22.218 1.00 21.46 C
ATOM 1043 N ASN B 28 33.948 27.637 25.219 1.00 21.73 N
ATOM 1044 CA ASN B 28 34.511 27.295 26.521 1.00 23.35 C
ATOM 1045 C ASN B 28 33.447 27.315 27.613 1.00 26.07 C
ATOM 1046 O ASN B 28 33.448 26.457 28.502 1.00 24.57 O
ATOM 1047 CB ASN B 28 35.656 28.251 26.858 1.00 27.94 C
ATOM 1048 CG ASN B 28 36.858 28.065 25.948 1.00 34.04 C
ATOM 1049 OD1 ASN B 28 37.200 26.943 25.570 1.00 30.35 O
ATOM 1050 ND2 ASN B 28 37.500 29.170 25.583 1.00 34.24 N
ATOM 1051 N GLY B 29 32.530 28.283 27.563 1.00 26.26 N
ATOM 1052 CA GLY B 29 31.448 28.307 28.534 1.00 25.42 C
ATOM 1053 C GLY B 29 30.533 27.103 28.417 1.00 25.63 C
ATOM 1054 O GLY B 29 30.126 26.519 29.425 1.00 24.71 O
ATOM 1055 N SER B 30 30.202 26.710 27.184 1.00 22.86 N
ATOM 1056 CA SER B 30 29.309 25.574 26.982 1.00 26.12 C
ATOM 1057 C SER B 30 29.974 24.265 27.388 1.00 21.89 C
ATOM 1058 O SER B 30 29.341 23.413 28.020 1.00 25.80 O
ATOM 1059 CB SER B 30 28.857 25.509 25.524 1.00 21.37 C
ATOM 1060 OG SER B 30 28.124 26.668 25.168 1.00 24.82 O
ATOM 1061 N LEU B 31 31.248 24.086 27.031 1.00 22.69 N
ATOM 1062 CA LEU B 31 31.942 22.849 27.375 1.00 25.10 C
ATOM 1063 C LEU B 31 32.100 22.707 28.883 1.00 30.92 C
ATOM 1064 O LEU B 31 32.041 21.594 29.420 1.00 30.77 O
ATOM 1065 CB LEU B 31 33.303 22.801 26.682 1.00 20.60 C
ATOM 1066 CG LEU B 31 33.244 22.623 25.164 1.00 26.37 C
ATOM 1067 CD1 LEU B 31 34.576 22.975 24.519 1.00 21.96 C
ATOM 1068 CD2 LEU B 31 32.829 21.203 24.814 1.00 25.98 C
ATOM 1069 N GLN B 32 32.289 23.824 29.584 1.00 28.58 N
ATOM 1070 CA GLN B 32 32.515 23.769 31.023 1.00 30.80 C
ATOM 1071 C GLN B 32 31.224 23.519 31.794 1.00 35.03 C
ATOM 1072 O GLN B 32 31.223 22.773 32.779 1.00 30.91 O
ATOM 1073 CB GLN B 32 33.170 25.068 31.496 1.00 32.41 C
ATOM 1074 CG GLN B 32 33.334 25.170 33.005 1.00 43.28 C
ATOM 1075 CD GLN B 32 34.357 24.190 33.545 1.00 57.21 C
ATOM 1076 OE1 GLN B 32 35.491 24.140 33.072 1.00 61.33 O
ATOM 1077 NE2 GLN B 32 33.959 23.404 34.539 1.00 56.28 N
ATOM 1078 N ASN B 33 30.116 24.117 31.355 1.00 26.99 N
ATOM 1079 CA ASN B 33 28.902 24.172 32.158 1.00 29.94 C
ATOM 1080 C ASN B 33 27.779 23.268 31.668 1.00 33.02 C
ATOM 1081 O ASN B 33 26.769 23.138 32.368 1.00 28.47 O
ATOM 1082 CB ASN B 33 28.386 25.616 32.219 1.00 27.57 C
ATOM 1083 CG ASN B 33 29.339 26.543 32.942 1.00 36.00 C
ATOM 1084 OD1 ASN B 33 30.016 26.140 33.888 1.00 38.90 O
ATOM 1085 ND2 ASN B 33 29.399 27.793 32.499 1.00 33.14 N
ATOM 1086 N GLU B 34 27.916 22.641 30.508 1.00 24.10 N
ATOM 1087 CA GLU B 34 26.841 21.824 29.946 1.00 29.17 C
ATOM 1088 C GLU B 34 27.316 20.392 29.750 1.00 29.85 C
ATOM 1089 O GLU B 34 28.116 20.128 28.832 1.00 27.05 O
ATOM 1090 CB GLU B 34 26.359 22.425 28.626 1.00 22.94 C
ATOM 1091 CG GLU B 34 25.903 23.872 28.766 1.00 27.32 C
ATOM 1092 CD GLU B 34 25.604 24.535 27.437 1.00 26.40 C
ATOM 1093 OE1 GLU B 34 26.019 23.992 26.392 1.00 26.56 O
ATOM 1094 OE2 GLU B 34 24.961 25.606 27.441 1.00 27.42 O
ATOM 1095 N PRO B 35 26.865 19.442 30.575 1.00 25.41 N
ATOM 1096 CA PRO B 35 27.351 18.058 30.436 1.00 28.00 C
ATOM 1097 C PRO B 35 27.013 17.431 29.098 1.00 29.02 C
ATOM 1098 O PRO B 35 27.734 16.533 28.646 1.00 27.93 O
ATOM 1099 CB PRO B 35 26.658 17.321 31.593 1.00 27.73 C
ATOM 1100 CG PRO B 35 26.191 18.390 32.529 1.00 37.89 C
ATOM 1101 CD PRO B 35 25.901 19.585 31.677 1.00 27.00 C
ATOM 1102 N GLY B 36 25.937 17.875 28.450 1.00 27.00 N
ATOM 1103 CA GLY B 36 25.560 17.343 27.155 1.00 24.29 C
ATOM 1104 C GLY B 36 26.310 17.922 25.978 1.00 22.02 C
ATOM 1105 O GLY B 36 26.173 17.410 24.863 1.00 21.58 O
ATOM 1106 N THR B 37 27.100 18.971 26.197 1.00 22.60 N
ATOM 1107 CA THR B 37 27.893 19.592 25.142 1.00 20.69 C
ATOM 1108 C THR B 37 29.286 18.974 25.164 1.00 22.77 C
ATOM 1109 O THR B 37 30.042 19.162 26.124 1.00 25.22 O
ATOM 1110 CB THR B 37 27.958 21.104 25.334 1.00 20.62 C
ATOM 1111 OG1 THR B 37 26.629 21.641 25.372 1.00 22.85 O
ATOM 1112 CG2 THR B 37 28.719 21.744 24.184 1.00 20.27 C
ATOM 1113 N LEU B 38 29.629 18.249 24.101 1.00 19.75 N
ATOM 1114 CA LEU B 38 30.832 17.426 24.078 1.00 25.57 C
ATOM 1115 C LEU B 38 31.991 18.054 23.322 1.00 20.79 C
ATOM 1116 O LEU B 38 33.150 17.794 23.665 1.00 21.30 O
ATOM 1117 CB LEU B 38 30.517 16.061 23.458 1.00 25.34 C
ATOM 1118 CG LEU B 38 29.251 15.398 24.000 1.00 27.46 C
ATOM 1119 CD1 LEU B 38 28.881 14.173 23.179 1.00 28.47 C
ATOM 1120 CD2 LEU B 38 29.419 15.043 25.468 1.00 26.22 C
ATOM 1121 N ARG B 39 31.712 18.864 22.304 1.00 23.50 N
ATOM 1122 CA ARG B 39 32.758 19.471 21.496 1.00 22.15 C
ATOM 1123 C ARG B 39 32.205 20.754 20.893 1.00 19.78 C
ATOM 1124 O ARG B 39 31.019 20.838 20.566 1.00 19.81 O
ATOM 1125 CB ARG B 39 33.243 18.506 20.407 1.00 21.54 C
ATOM 1126 CG ARG B 39 34.570 18.869 19.757 1.00 22.10 C
ATOM 1127 CD ARG B 39 34.999 17.781 18.782 1.00 21.84 C
ATOM 1128 NE ARG B 39 34.298 17.899 17.509 1.00 26.75 N
ATOM 1129 CZ ARG B 39 34.022 16.881 16.705 1.00 29.50 C
ATOM 1130 NH1 ARG B 39 34.365 15.641 17.015 1.00 27.16 N
ATOM 1131 NH2 ARG B 39 33.382 17.112 15.563 1.00 26.55 N
ATOM 1132 N PHE B 40 33.074 21.754 20.755 1.00 21.95 N
ATOM 1133 CA PHE B 40 32.638 23.073 20.302 1.00 25.11 C
ATOM 1134 C PHE B 40 33.851 23.801 19.743 1.00 24.10 C
ATOM 1135 O PHE B 40 34.728 24.207 20.513 1.00 20.48 O
ATOM 1136 CB PHE B 40 32.015 23.853 21.452 1.00 23.83 C
ATOM 1137 CG PHE B 40 30.967 24.838 21.025 1.00 19.70 C
ATOM 1138 CD1 PHE B 40 31.289 25.928 20.231 1.00 18.11 C
ATOM 1139 CD2 PHE B 40 29.657 24.679 21.434 1.00 19.59 C
ATOM 1140 CE1 PHE B 40 30.317 26.836 19.846 1.00 19.48 C
ATOM 1141 CE2 PHE B 40 28.683 25.578 21.053 1.00 21.14 C
ATOM 1142 CZ PHE B 40 29.012 26.659 20.259 1.00 23.62 C
ATOM 1143 N GLU B 41 33.898 23.978 18.425 1.00 22.33 N
ATOM 1144 CA GLU B 41 35.039 24.596 17.764 1.00 23.70 C
ATOM 1145 C GLU B 41 34.595 25.782 16.921 1.00 21.09 C
ATOM 1146 O GLU B 41 33.505 25.776 16.341 1.00 18.34 O
ATOM 1147 CB GLU B 41 35.785 23.582 16.889 1.00 25.69 C
ATOM 1148 CG GLU B 41 36.163 22.305 17.619 1.00 23.01 C
ATOM 1149 CD GLU B 41 36.692 21.231 16.690 1.00 30.02 C
ATOM 1150 OE1 GLU B 41 36.108 21.035 15.604 1.00 26.86 O
ATOM 1151 OE2 GLU B 41 37.696 20.584 17.050 1.00 26.09 O
ATOM 1152 N VAL B 42 35.446 26.802 16.868 1.00 21.34 N
ATOM 1153 CA VAL B 42 35.237 27.980 16.037 1.00 18.49 C
ATOM 1154 C VAL B 42 36.188 27.881 14.855 1.00 20.26 C
ATOM 1155 O VAL B 42 37.399 27.713 15.042 1.00 20.82 O
ATOM 1156 CB VAL B 42 35.472 29.279 16.829 1.00 24.79 C
ATOM 1157 CG1 VAL B 42 35.132 30.495 15.976 1.00 20.61 C
ATOM 1158 CG2 VAL B 42 34.665 29.266 18.120 1.00 22.62 C
ATOM 1159 N ILE B 43 35.641 27.971 13.645 1.00 18.86 N
ATOM 1160 CA ILE B 43 36.406 27.822 12.413 1.00 23.86 C
ATOM 1161 C ILE B 43 36.261 29.097 11.593 1.00 23.88 C
ATOM 1162 O ILE B 43 35.151 29.616 11.435 1.00 19.79 O
ATOM 1163 CB ILE B 43 35.943 26.601 11.595 1.00 24.98 C
ATOM 1164 CG1 ILE B 43 35.785 25.369 12.490 1.00 27.07 C
ATOM 1165 CG2 ILE B 43 36.921 26.315 10.461 1.00 22.80 C
ATOM 1166 CD1 ILE B 43 37.089 24.828 13.027 1.00 33.84 C
ATOM 1167 N ARG B 44 37.380 29.601 11.081 1.00 21.68 N
ATOM 1168 CA AARG B 44 37.373 30.743 10.179 0.53 25.39 C
ATOM 1169 CA BARG B 44 37.383 30.745 10.180 0.47 25.40 C
ATOM 1170 C ARG B 44 37.534 30.255 8.746 1.00 23.78 C
ATOM 1171 O ARG B 44 38.268 29.299 8.482 1.00 29.80 O
ATOM 1172 CB AARG B 44 38.482 31.737 10.533 0.53 32.60 C
ATOM 1173 CB BARG B 44 38.508 31.728 10.532 0.47 32.58 C
ATOM 1174 CG AARG B 44 39.892 31.220 10.312 0.53 33.20 C
ATOM 1175 CG BARG B 44 39.927 31.199 10.323 0.47 33.21 C
ATOM 1176 CD AARG B 44 40.926 32.260 10.708 0.53 34.89 C
ATOM 1177 CD BARG B 44 40.976 32.289 10.535 0.47 35.05 C
ATOM 1178 NE AARG B 44 42.277 31.857 10.336 0.53 34.05 N
ATOM 1179 NE BARG B 44 41.536 32.272 11.882 0.47 36.37 N
ATOM 1180 CZ AARG B 44 42.765 31.918 9.105 0.53 27.57 C
ATOM 1181 CZ BARG B 44 41.315 33.205 12.799 0.47 33.81 C
ATOM 1182 NH1AARG B 44 42.045 32.380 8.096 0.53 29.51 N
ATOM 1183 NH1BARG B 44 41.874 33.142 13.997 0.47 27.53 N
ATOM 1184 NH2AARG B 44 44.010 31.508 8.880 0.53 29.12 N
ATOM 1185 NH2BARG B 44 40.511 34.223 12.509 0.47 34.07 N
ATOM 1186 N ASP B 45 36.823 30.901 7.827 1.00 20.27 N
ATOM 1187 CA ASP B 45 36.888 30.504 6.427 1.00 20.84 C
ATOM 1188 C ASP B 45 38.266 30.821 5.857 1.00 22.94 C
ATOM 1189 O ASP B 45 38.849 31.868 6.151 1.00 24.34 O
ATOM 1190 CB ASP B 45 35.802 31.216 5.621 1.00 22.52 C
ATOM 1191 CG ASP B 45 35.622 30.626 4.234 1.00 22.00 C
ATOM 1192 OD1 ASP B 45 34.847 29.657 4.099 1.00 26.47 O
ATOM 1193 OD2 ASP B 45 36.259 31.126 3.283 1.00 24.40 O
ATOM 1194 N GLU B 46 38.791 29.903 5.038 1.00 22.95 N
ATOM 1195 CA GLU B 46 40.152 30.057 4.531 1.00 25.13 C
ATOM 1196 C GLU B 46 40.272 31.229 3.565 1.00 30.10 C
ATOM 1197 O GLU B 46 41.346 31.833 3.458 1.00 28.64 O
ATOM 1198 CB GLU B 46 40.619 28.767 3.854 1.00 27.18 C
ATOM 1199 CG GLU B 46 39.964 28.478 2.511 1.00 27.96 C
ATOM 1200 CD GLU B 46 40.597 27.299 1.802 1.00 43.69 C
ATOM 1201 OE1 GLU B 46 41.676 26.854 2.246 1.00 29.91 O
ATOM 1202 OE2 GLU B 46 40.021 26.821 0.801 1.00 34.58 O
ATOM 1203 N ASN B 47 39.194 31.570 2.866 1.00 25.71 N
ATOM 1204 CA ASN B 47 39.207 32.644 1.880 1.00 31.47 C
ATOM 1205 C ASN B 47 38.435 33.876 2.322 1.00 26.79 C
ATOM 1206 O ASN B 47 38.858 34.996 2.031 1.00 38.75 O
ATOM 1207 CB ASN B 47 38.633 32.147 0.546 1.00 31.53 C
ATOM 1208 CG ASN B 47 39.440 31.009 -0.055 1.00 45.25 C
ATOM 1209 OD1 ASN B 47 38.882 30.012 -0.515 1.00 41.99 O
ATOM 1210 ND2 ASN B 47 40.759 31.148 -0.045 1.00 40.81 N
ATOM 1211 N ASN B 48 37.314 33.703 3.019 1.00 25.30 N
ATOM 1212 CA ASN B 48 36.461 34.814 3.428 1.00 25.13 C
ATOM 1213 C ASN B 48 36.812 35.181 4.865 1.00 24.30 C
ATOM 1214 O ASN B 48 36.453 34.463 5.804 1.00 22.92 O
ATOM 1215 CB ASN B 48 34.987 34.440 3.289 1.00 30.46 C
ATOM 1216 CG ASN B 48 34.060 35.639 3.391 1.00 24.88 C
ATOM 1217 OD1 ASN B 48 34.400 36.663 3.985 1.00 28.90 O
ATOM 1218 ND2 ASN B 48 32.885 35.521 2.786 1.00 27.95 N
ATOM 1219 N ARG B 49 37.508 36.306 5.035 1.00 26.59 N
ATOM 1220 CA ARG B 49 37.937 36.744 6.357 1.00 28.13 C
ATOM 1221 C ARG B 49 36.783 37.223 7.228 1.00 28.47 C
ATOM 1222 O ARG B 49 37.000 37.500 8.413 1.00 29.84 O
ATOM 1223 CB ARG B 49 38.978 37.854 6.215 1.00 34.22 C
ATOM 1224 CG ARG B 49 40.162 37.475 5.339 1.00 33.56 C
ATOM 1225 CD ARG B 49 41.423 38.215 5.750 1.00 54.85 C
ATOM 1226 NE ARG B 49 41.880 39.117 4.700 1.00 61.99 N
ATOM 1227 CZ ARG B 49 42.376 40.327 4.915 1.00 71.93 C
ATOM 1228 NH1 ARG B 49 42.504 40.813 6.139 1.00 65.72 N
ATOM 1229 NH2 ARG B 49 42.750 41.070 3.877 1.00 57.27 N
ATOM 1230 N ASN B 50 35.572 37.321 6.683 1.00 25.12 N
ATOM 1231 CA ASN B 50 34.409 37.780 7.430 1.00 23.00 C
ATOM 1232 C ASN B 50 33.436 36.660 7.774 1.00 22.55 C
ATOM 1233 O ASN B 50 32.397 36.931 8.384 1.00 21.08 O
ATOM 1234 CB ASN B 50 33.672 38.869 6.641 1.00 24.33 C
ATOM 1235 CG ASN B 50 34.401 40.198 6.658 1.00 29.50 C
ATOM 1236 OD1 ASN B 50 35.482 40.322 7.237 1.00 34.37 O
ATOM 1237 ND2 ASN B 50 33.808 41.205 6.023 1.00 27.84 N
ATOM 1238 N ARG B 51 33.741 35.419 7.408 1.00 20.15 N
ATOM 1239 CA ARG B 51 32.835 34.296 7.606 1.00 18.62 C
ATOM 1240 C ARG B 51 33.435 33.322 8.608 1.00 23.87 C
ATOM 1241 O ARG B 51 34.603 32.938 8.486 1.00 18.55 O
ATOM 1242 CB ARG B 51 32.545 33.586 6.282 1.00 19.02 C
ATOM 1243 CG ARG B 51 31.656 32.363 6.422 1.00 22.18 C
ATOM 1244 CD ARG B 51 30.939 32.044 5.125 1.00 21.75 C
ATOM 1245 NE ARG B 51 29.860 32.985 4.850 1.00 22.97 N
ATOM 1246 CZ ARG B 51 29.063 32.918 3.793 1.00 21.05 C
ATOM 1247 NH1 ARG B 51 29.200 31.965 2.884 1.00 21.18 N
ATOM 1248 NH2 ARG B 51 28.103 33.827 3.644 1.00 21.53 N
ATOM 1249 N PHE B 52 32.633 32.927 9.593 1.00 17.27 N
ATOM 1250 CA PHE B 52 33.055 32.001 10.630 1.00 19.65 C
ATOM 1251 C PHE B 52 32.039 30.879 10.762 1.00 25.05 C
ATOM 1252 O PHE B 52 30.860 31.042 10.432 1.00 20.56 O
ATOM 1253 CB PHE B 52 33.219 32.701 11.984 1.00 16.97 C
ATOM 1254 CG PHE B 52 34.290 33.752 12.001 1.00 18.71 C
ATOM 1255 CD1 PHE B 52 34.051 35.016 11.485 1.00 20.85 C
ATOM 1256 CD2 PHE B 52 35.534 33.478 12.545 1.00 20.93 C
ATOM 1257 CE1 PHE B 52 35.038 35.985 11.503 1.00 26.95 C
ATOM 1258 CE2 PHE B 52 36.523 34.440 12.566 1.00 27.60 C
ATOM 1259 CZ PHE B 52 36.276 35.696 12.044 1.00 26.77 C
ATOM 1260 N TYR B 53 32.507 29.736 11.256 1.00 14.88 N
ATOM 1261 CA TYR B 53 31.655 28.578 11.469 1.00 19.32 C
ATOM 1262 C TYR B 53 31.811 28.069 12.894 1.00 19.81 C
ATOM 1263 O TYR B 53 32.891 28.140 13.486 1.00 21.34 O
ATOM 1264 CB TYR B 53 31.976 27.454 10.480 1.00 18.22 C
ATOM 1265 CG TYR B 53 32.150 27.927 9.056 1.00 24.90 C
ATOM 1266 CD1 TYR B 53 31.052 28.107 8.225 1.00 15.80 C
ATOM 1267 CD2 TYR B 53 33.411 28.198 8.544 1.00 23.35 C
ATOM 1268 CE1 TYR B 53 31.206 28.537 6.923 1.00 20.05 C
ATOM 1269 CE2 TYR B 53 33.575 28.632 7.248 1.00 23.60 C
ATOM 1270 CZ TYR B 53 32.469 28.801 6.440 1.00 19.31 C
ATOM 1271 OH TYR B 53 32.630 29.229 5.142 1.00 21.12 O
ATOM 1272 N LEU B 54 30.711 27.563 13.440 1.00 17.96 N
ATOM 1273 CA LEU B 54 30.709 26.875 14.722 1.00 19.82 C
ATOM 1274 C LEU B 54 30.394 25.406 14.486 1.00 20.63 C
ATOM 1275 O LEU B 54 29.372 25.076 13.875 1.00 25.95 O
ATOM 1276 CB LEU B 54 29.689 27.483 15.686 1.00 18.25 C
ATOM 1277 CG LEU B 54 29.739 28.990 15.942 1.00 28.87 C
ATOM 1278 CD1 LEU B 54 28.693 29.381 16.974 1.00 21.67 C
ATOM 1279 CD2 LEU B 54 31.128 29.428 16.383 1.00 22.87 C
ATOM 1280 N ASP B 55 31.271 24.533 14.969 1.00 19.84 N
ATOM 1281 CA ASP B 55 31.142 23.090 14.793 1.00 16.77 C
ATOM 1282 C ASP B 55 30.896 22.495 16.176 1.00 19.91 C
ATOM 1283 O ASP B 55 31.818 22.388 16.991 1.00 22.80 O
ATOM 1284 CB ASP B 55 32.393 22.522 14.132 1.00 19.53 C
ATOM 1285 CG ASP B 55 32.208 21.103 13.645 1.00 30.97 C
ATOM 1286 OD1 ASP B 55 31.248 20.428 14.074 1.00 19.93 O
ATOM 1287 OD2 ASP B 55 33.036 20.666 12.821 1.00 26.66 O
ATOM 1288 N GLU B 56 29.652 22.101 16.434 1.00 19.46 N
ATOM 1289 CA GLU B 56 29.199 21.724 17.765 1.00 23.47 C
ATOM 1290 C GLU B 56 28.750 20.271 17.784 1.00 22.06 C
ATOM 1291 O GLU B 56 28.080 19.805 16.857 1.00 23.74 O
ATOM 1292 CB GLU B 56 28.052 22.631 18.208 1.00 16.65 C
ATOM 1293 CG GLU B 56 28.248 24.074 17.781 1.00 17.54 C
ATOM 1294 CD GLU B 56 27.021 24.937 18.007 1.00 29.74 C
ATOM 1295 OE1 GLU B 56 26.002 24.418 18.508 1.00 27.62 O
ATOM 1296 OE2 GLU B 56 27.078 26.138 17.672 1.00 27.34 O
ATOM 1297 N VAL B 57 29.116 19.558 18.847 1.00 20.15 N
ATOM 1298 CA VAL B 57 28.756 18.157 19.025 1.00 23.28 C
ATOM 1299 C VAL B 57 28.087 17.997 20.380 1.00 25.38 C
ATOM 1300 O VAL B 57 28.602 18.481 21.393 1.00 24.16 O
ATOM 1301 CB VAL B 57 29.978 17.225 18.919 1.00 21.85 C
ATOM 1302 CG1 VAL B 57 29.543 15.772 19.058 1.00 19.87 C
ATOM 1303 CG2 VAL B 57 30.694 17.442 17.600 1.00 19.41 C
ATOM 1304 N TYR B 58 26.951 17.306 20.400 1.00 21.84 N
ATOM 1305 CA TYR B 58 26.174 17.135 21.615 1.00 21.01 C
ATOM 1306 C TYR B 58 25.889 15.661 21.849 1.00 22.22 C
ATOM 1307 O TYR B 58 25.984 14.831 20.941 1.00 21.05 O
ATOM 1308 CB TYR B 58 24.859 17.925 21.551 1.00 22.17 C
ATOM 1309 CG TYR B 58 25.076 19.408 21.384 1.00 21.19 C
ATOM 1310 CD1 TYR B 58 25.298 20.227 22.485 1.00 19.92 C
ATOM 1311 CD2 TYR B 58 25.106 19.985 20.123 1.00 19.59 C
ATOM 1312 CE1 TYR B 58 25.514 21.584 22.334 1.00 26.61 C
ATOM 1313 CE2 TYR B 58 25.320 21.338 19.962 1.00 24.53 C
ATOM 1314 CZ TYR B 58 25.526 22.134 21.069 1.00 25.56 C
ATOM 1315 OH TYR B 58 25.742 23.482 20.904 1.00 23.93 O
ATOM 1316 N GLU B 59 25.552 15.355 23.102 1.00 22.58 N
ATOM 1317 CA GLU B 59 25.119 14.015 23.478 1.00 29.00 C
ATOM 1318 C GLU B 59 23.999 13.525 22.569 1.00 27.69 C
ATOM 1319 O GLU B 59 24.039 12.403 22.050 1.00 27.16 O
ATOM 1320 CB GLU B 59 24.646 14.037 24.929 1.00 31.30 C
ATOM 1321 CG GLU B 59 25.216 12.973 25.831 1.00 48.90 C
ATOM 1322 CD GLU B 59 24.936 13.281 27.285 1.00 59.62 C
ATOM 1323 OE1 GLU B 59 23.750 13.464 27.633 1.00 67.93 O
ATOM 1324 OE2 GLU B 59 25.895 13.345 28.079 1.00 72.64 O
ATOM 1325 N ASP B 60 22.985 14.361 22.381 1.00 23.50 N
ATOM 1326 CA ASP B 60 21.811 14.044 21.581 1.00 23.88 C
ATOM 1327 C ASP B 60 21.124 15.360 21.238 1.00 29.34 C
ATOM 1328 O ASP B 60 21.595 16.438 21.611 1.00 25.77 O
ATOM 1329 CB ASP B 60 20.885 13.076 22.326 1.00 26.18 C
ATOM 1330 CG ASP B 60 20.567 13.540 23.744 1.00 30.04 C
ATOM 1331 OD1 ASP B 60 20.593 14.760 24.010 1.00 28.95 O
ATOM 1332 OD2 ASP B 60 20.297 12.674 24.603 1.00 38.12 O
ATOM 1333 N GLU B 61 19.996 15.268 20.529 1.00 29.24 N
ATOM 1334 CA GLU B 61 19.289 16.484 20.138 1.00 23.85 C
ATOM 1335 C GLU B 61 18.777 17.240 21.357 1.00 24.54 C
ATOM 1336 O GLU B 61 18.789 18.477 21.378 1.00 25.37 O
ATOM 1337 CB GLU B 61 18.127 16.162 19.200 1.00 32.75 C
ATOM 1338 CG GLU B 61 17.513 17.411 18.589 1.00 30.91 C
ATOM 1339 CD GLU B 61 16.070 17.225 18.167 1.00 51.18 C
ATOM 1340 OE1 GLU B 61 15.581 16.075 18.182 1.00 55.40 O
ATOM 1341 OE2 GLU B 61 15.421 18.238 17.832 1.00 47.67 O
ATOM 1342 N ALA B 62 18.316 16.513 22.378 1.00 26.41 N
ATOM 1343 CA ALA B 62 17.834 17.162 23.593 1.00 27.99 C
ATOM 1344 C ALA B 62 18.918 18.024 24.227 1.00 26.87 C
ATOM 1345 O ALA B 62 18.631 19.098 24.768 1.00 27.70 O
ATOM 1346 CB ALA B 62 17.332 16.112 24.585 1.00 30.36 C
ATOM 1347 N ALA B 63 20.174 17.576 24.158 1.00 25.44 N
ATOM 1348 CA ALA B 63 21.273 18.360 24.712 1.00 26.23 C
ATOM 1349 C ALA B 63 21.519 19.635 23.915 1.00 24.36 C
ATOM 1350 O ALA B 63 21.935 20.649 24.486 1.00 26.54 O
ATOM 1351 CB ALA B 63 22.545 17.517 24.768 1.00 26.56 C
ATOM 1352 N PHE B 64 21.280 19.606 22.602 1.00 22.95 N
ATOM 1353 CA PHE B 64 21.392 20.827 21.810 1.00 20.71 C
ATOM 1354 C PHE B 64 20.287 21.816 22.161 1.00 22.25 C
ATOM 1355 O PHE B 64 20.544 23.017 22.307 1.00 26.78 O
ATOM 1356 CB PHE B 64 21.359 20.500 20.319 1.00 19.48 C
ATOM 1357 CG PHE B 64 21.173 21.706 19.442 1.00 26.89 C
ATOM 1358 CD1 PHE B 64 22.138 22.700 19.393 1.00 22.97 C
ATOM 1359 CD2 PHE B 64 20.028 21.850 18.674 1.00 25.74 C
ATOM 1360 CE1 PHE B 64 21.968 23.815 18.588 1.00 24.97 C
ATOM 1361 CE2 PHE B 64 19.850 22.961 17.866 1.00 22.88 C
ATOM 1362 CZ PHE B 64 20.822 23.945 17.823 1.00 26.57 C
ATOM 1363 N LEU B 65 19.049 21.332 22.292 1.00 22.25 N
ATOM 1364 CA LEU B 65 17.954 22.213 22.685 1.00 28.26 C
ATOM 1365 C LEU B 65 18.167 22.784 24.080 1.00 28.34 C
ATOM 1366 O LEU B 65 17.787 23.931 24.344 1.00 27.63 O
ATOM 1367 CB LEU B 65 16.624 21.463 22.615 1.00 27.49 C
ATOM 1368 CG LEU B 65 16.245 20.885 21.251 1.00 30.91 C
ATOM 1369 CD1 LEU B 65 14.939 20.109 21.336 1.00 36.03 C
ATOM 1370 CD2 LEU B 65 16.152 21.994 20.217 1.00 30.47 C
ATOM 1371 N GLN B 66 18.773 22.009 24.981 1.00 26.23 N
ATOM 1372 CA GLN B 66 19.115 22.539 26.298 1.00 29.34 C
ATOM 1373 C GLN B 66 20.138 23.662 26.180 1.00 24.75 C
ATOM 1374 O GLN B 66 19.995 24.718 26.807 1.00 24.76 O
ATOM 1375 CB GLN B 66 19.645 21.422 27.195 1.00 26.00 C
ATOM 1376 CG GLN B 66 19.770 21.815 28.656 1.00 35.44 C
ATOM 1377 CD GLN B 66 18.473 22.352 29.221 1.00 40.86 C
ATOM 1378 OE1 GLN B 66 17.437 21.692 29.154 1.00 31.28 O
ATOM 1379 NE2 GLN B 66 18.523 23.556 29.780 1.00 30.90 N
ATOM 1380 N HIS B 67 21.181 23.443 25.384 1.00 21.08 N
ATOM 1381 CA HIS B 67 22.194 24.457 25.103 1.00 22.16 C
ATOM 1382 C HIS B 67 21.549 25.748 24.612 1.00 29.56 C
ATOM 1383 O HIS B 67 21.943 26.846 25.009 1.00 28.37 O
ATOM 1384 CB HIS B 67 23.190 23.930 24.063 1.00 18.69 C
ATOM 1385 CG HIS B 67 24.043 24.991 23.438 1.00 22.39 C
ATOM 1386 ND1 HIS B 67 25.201 25.457 24.023 1.00 22.95 N
ATOM 1387 CD2 HIS B 67 23.913 25.666 22.272 1.00 19.36 C
ATOM 1388 CE1 HIS B 67 25.744 26.377 23.247 1.00 24.66 C
ATOM 1389 NE2 HIS B 67 24.981 26.525 22.179 1.00 23.66 N
HETATM 1390 N CME B 68 20.536 25.597 23.767 1.00 21.06 N
HETATM 1391 CA CME B 68 19.860 26.721 23.159 1.00 19.75 C
HETATM 1392 CB CME B 68 18.899 26.291 22.048 1.00 23.06 C
HETATM 1393 SG CME B 68 19.710 25.769 20.578 1.00 28.64 S
HETATM 1394 SD CME B 68 20.056 27.502 19.437 1.00 64.29 S
HETATM 1395 CE CME B 68 18.812 27.540 18.196 1.00 57.82 C
HETATM 1396 CZ CME B 68 17.424 27.771 18.752 1.00 57.19 C
HETATM 1397 OH CME B 68 16.505 27.298 17.778 1.00 77.76 O
HETATM 1398 C CME B 68 19.073 27.535 24.183 1.00 22.20 C
HETATM 1399 O CME B 68 18.774 28.719 24.015 1.00 27.89 O
ATOM 1400 N ARG B 69 18.730 26.884 25.289 1.00 23.66 N
ATOM 1401 CA ARG B 69 17.970 27.545 26.350 1.00 25.48 C
ATOM 1402 C ARG B 69 18.854 28.024 27.499 1.00 29.94 C
ATOM 1403 O ARG B 69 18.364 28.637 28.447 1.00 29.56 O
ATOM 1404 CB ARG B 69 16.887 26.613 26.906 1.00 35.06 C
ATOM 1405 CG ARG B 69 15.821 26.196 25.907 1.00 47.66 C
ATOM 1406 CD ARG B 69 14.724 25.380 26.581 1.00 51.76 C
ATOM 1407 NE ARG B 69 15.223 24.136 27.154 1.00 43.07 N
ATOM 1408 CZ ARG B 69 15.112 22.950 26.570 1.00 48.60 C
ATOM 1409 NH1 ARG B 69 15.617 21.858 27.120 1.00 42.96 N
ATOM 1410 NH2 ARG B 69 14.473 22.857 25.407 1.00 39.24 N
ATOM 1411 N ASN B 70 20.154 27.758 27.408 1.00 27.55 N
ATOM 1412 CA ASN B 70 21.061 28.026 28.512 1.00 30.29 C
ATOM 1413 C ASN B 70 21.646 29.437 28.426 1.00 28.16 C
ATOM 1414 O ASN B 70 21.400 30.192 27.482 1.00 30.16 O
ATOM 1415 CB ASN B 70 22.162 26.969 28.559 1.00 23.22 C
ATOM 1416 CG ASN B 70 21.686 25.667 29.172 1.00 30.55 C
ATOM 1417 OD1 ASN B 70 20.605 25.604 29.758 1.00 28.85 O
ATOM 1418 ND2 ASN B 70 22.494 24.621 29.045 1.00 23.32 N
ATOM 1419 N GLU B 71 22.444 29.791 29.438 1.00 28.02 N
ATOM 1420 CA GLU B 71 22.903 31.167 29.601 1.00 34.02 C
ATOM 1421 C GLU B 71 24.117 31.494 28.739 1.00 27.53 C
ATOM 1422 O GLU B 71 24.310 32.661 28.379 1.00 27.10 O
ATOM 1423 CB GLU B 71 23.220 31.445 31.075 1.00 29.86 C
ATOM 1424 CG GLU B 71 21.979 31.607 31.949 1.00 30.38 C
ATOM 1425 CD GLU B 71 22.254 31.386 33.426 1.00 44.56 C
ATOM 1426 OE1 GLU B 71 23.312 31.836 33.918 1.00 43.82 O
ATOM 1427 OE2 GLU B 71 21.409 30.757 34.097 1.00 43.57 O
ATOM 1428 N THR B 72 24.943 30.500 28.402 1.00 22.97 N
ATOM 1429 CA THR B 72 26.137 30.775 27.606 1.00 23.67 C
ATOM 1430 C THR B 72 25.770 31.320 26.230 1.00 27.85 C
ATOM 1431 O THR B 72 26.314 32.340 25.790 1.00 27.21 O
ATOM 1432 CB THR B 72 26.996 29.517 27.473 1.00 26.87 C
ATOM 1433 OG1 THR B 72 27.384 29.059 28.774 1.00 26.10 O
ATOM 1434 CG2 THR B 72 28.245 29.803 26.644 1.00 27.00 C
ATOM 1435 N ILE B 73 24.842 30.655 25.535 1.00 26.53 N
ATOM 1436 CA ILE B 73 24.460 31.119 24.204 1.00 22.90 C
ATOM 1437 C ILE B 73 23.751 32.465 24.281 1.00 23.33 C
ATOM 1438 O ILE B 73 23.844 33.276 23.351 1.00 23.94 O
ATOM 1439 CB ILE B 73 23.598 30.066 23.481 1.00 26.07 C
ATOM 1440 CG1 ILE B 73 23.481 30.412 21.996 1.00 24.99 C
ATOM 1441 CG2 ILE B 73 22.220 29.950 24.113 1.00 21.96 C
ATOM 1442 CD1 ILE B 73 22.796 29.345 21.181 1.00 23.86 C
ATOM 1443 N ALA B 74 23.036 32.730 25.379 1.00 21.65 N
ATOM 1444 CA ALA B 74 22.389 34.028 25.544 1.00 23.66 C
ATOM 1445 C ALA B 74 23.422 35.143 25.640 1.00 28.59 C
ATOM 1446 O ALA B 74 23.262 36.204 25.025 1.00 25.30 O
ATOM 1447 CB ALA B 74 21.491 34.013 26.781 1.00 24.64 C
ATOM 1448 N ARG B 75 24.494 34.918 26.403 1.00 24.32 N
ATOM 1449 CA ARG B 75 25.576 35.894 26.468 1.00 27.61 C
ATOM 1450 C ARG B 75 26.272 36.029 25.119 1.00 24.00 C
ATOM 1451 O ARG B 75 26.692 37.127 24.734 1.00 25.70 O
ATOM 1452 CB ARG B 75 26.573 35.496 27.557 1.00 23.86 C
ATOM 1453 CG ARG B 75 27.823 36.356 27.603 1.00 30.33 C
ATOM 1454 CD ARG B 75 27.519 37.778 28.027 1.00 25.49 C
ATOM 1455 NE ARG B 75 28.725 38.598 28.065 1.00 26.76 N
ATOM 1456 CZ ARG B 75 28.763 39.888 27.758 1.00 29.44 C
ATOM 1457 NH1 ARG B 75 27.673 40.544 27.394 1.00 30.26 N
ATOM 1458 NH2 ARG B 75 29.924 40.535 27.814 1.00 26.93 N
ATOM 1459 N PHE B 76 26.401 34.921 24.387 1.00 22.68 N
ATOM 1460 CA PHE B 76 27.018 34.966 23.066 1.00 23.06 C
ATOM 1461 C PHE B 76 26.233 35.875 22.130 1.00 29.11 C
ATOM 1462 O PHE B 76 26.810 36.707 21.421 1.00 24.91 O
ATOM 1463 CB PHE B 76 27.121 33.552 22.493 1.00 21.54 C
ATOM 1464 CG PHE B 76 27.476 33.509 21.032 1.00 24.13 C
ATOM 1465 CD1 PHE B 76 28.772 33.765 20.611 1.00 23.15 C
ATOM 1466 CD2 PHE B 76 26.517 33.197 20.082 1.00 22.82 C
ATOM 1467 CE1 PHE B 76 29.103 33.722 19.267 1.00 19.73 C
ATOM 1468 CE2 PHE B 76 26.841 33.152 18.737 1.00 26.53 C
ATOM 1469 CZ PHE B 76 28.136 33.415 18.329 1.00 22.02 C
ATOM 1470 N TYR B 77 24.906 35.739 22.126 1.00 19.90 N
ATOM 1471 CA TYR B 77 24.092 36.553 21.231 1.00 22.85 C
ATOM 1472 C TYR B 77 24.004 37.996 21.702 1.00 28.49 C
ATOM 1473 O TYR B 77 23.829 38.902 20.882 1.00 25.41 O
ATOM 1474 CB TYR B 77 22.700 35.943 21.089 1.00 23.63 C
ATOM 1475 CG TYR B 77 22.667 34.847 20.059 1.00 29.68 C
ATOM 1476 CD1 TYR B 77 23.088 35.089 18.759 1.00 28.32 C
ATOM 1477 CD2 TYR B 77 22.241 33.569 20.386 1.00 37.41 C
ATOM 1478 CE1 TYR B 77 23.075 34.093 17.811 1.00 31.07 C
ATOM 1479 CE2 TYR B 77 22.224 32.564 19.443 1.00 34.36 C
ATOM 1480 CZ TYR B 77 22.640 32.832 18.158 1.00 32.99 C
ATOM 1481 OH TYR B 77 22.626 31.832 17.218 1.00 35.56 O
ATOM 1482 N GLU B 78 24.120 38.228 23.009 1.00 22.37 N
ATOM 1483 CA GLU B 78 24.214 39.595 23.508 1.00 29.17 C
ATOM 1484 C GLU B 78 25.462 40.287 22.975 1.00 25.56 C
ATOM 1485 O GLU B 78 25.425 41.472 22.624 1.00 31.69 O
ATOM 1486 CB GLU B 78 24.219 39.586 25.036 1.00 26.63 C
ATOM 1487 CG GLU B 78 23.720 40.862 25.689 1.00 45.52 C
ATOM 1488 CD GLU B 78 23.917 40.850 27.192 1.00 57.15 C
ATOM 1489 OE1 GLU B 78 23.721 41.905 27.829 1.00 70.83 O
ATOM 1490 OE2 GLU B 78 24.272 39.783 27.737 1.00 52.12 O
ATOM 1491 N LEU B 79 26.577 39.556 22.902 1.00 27.43 N
ATOM 1492 CA LEU B 79 27.837 40.148 22.465 1.00 33.53 C
ATOM 1493 C LEU B 79 27.786 40.553 20.997 1.00 28.17 C
ATOM 1494 O LEU B 79 28.256 41.635 20.625 1.00 28.33 O
ATOM 1495 CB LEU B 79 28.976 39.156 22.698 1.00 29.42 C
ATOM 1496 CG LEU B 79 29.515 39.017 24.120 1.00 28.27 C
ATOM 1497 CD1 LEU B 79 30.198 37.672 24.281 1.00 30.79 C
ATOM 1498 CD2 LEU B 79 30.481 40.149 24.426 1.00 25.86 C
ATOM 1499 N ILE B 80 27.208 39.699 20.149 1.00 24.24 N
ATOM 1500 CA ILE B 80 27.320 39.834 18.702 1.00 36.30 C
ATOM 1501 C ILE B 80 26.108 40.497 18.070 1.00 28.04 C
ATOM 1502 O ILE B 80 26.105 40.718 16.851 1.00 26.01 O
ATOM 1503 CB ILE B 80 27.547 38.457 18.050 1.00 29.61 C
ATOM 1504 CG1 ILE B 80 26.256 37.638 18.112 1.00 25.96 C
ATOM 1505 CG2 ILE B 80 28.680 37.721 18.743 1.00 25.97 C
ATOM 1506 CD1 ILE B 80 26.294 36.371 17.296 1.00 26.54 C
ATOM 1507 N ASP B 81 25.077 40.822 18.855 1.00 24.15 N
ATOM 1508 CA ASP B 81 23.797 41.219 18.274 1.00 24.62 C
ATOM 1509 C ASP B 81 23.931 42.456 17.395 1.00 32.58 C
ATOM 1510 O ASP B 81 23.259 42.570 16.363 1.00 29.17 O
ATOM 1511 CB ASP B 81 22.769 41.466 19.378 1.00 25.27 C
ATOM 1512 CG ASP B 81 21.426 41.906 18.830 1.00 32.29 C
ATOM 1513 OD1 ASP B 81 20.802 41.115 18.094 1.00 35.37 O
ATOM 1514 OD2 ASP B 81 21.000 43.042 19.123 1.00 38.57 O
ATOM 1515 N SER B 82 24.800 43.390 17.776 1.00 28.30 N
ATOM 1516 CA SER B 82 24.866 44.660 17.066 1.00 29.03 C
ATOM 1517 C SER B 82 25.604 44.571 15.735 1.00 28.35 C
ATOM 1518 O SER B 82 25.499 45.502 14.931 1.00 27.78 O
ATOM 1519 CB SER B 82 25.523 45.724 17.950 1.00 36.30 C
ATOM 1520 OG SER B 82 26.913 45.492 18.101 1.00 31.10 O
ATOM 1521 N TYR B 83 26.330 43.485 15.465 1.00 25.95 N
ATOM 1522 CA TYR B 83 27.139 43.472 14.250 1.00 25.11 C
ATOM 1523 C TYR B 83 27.071 42.172 13.451 1.00 27.14 C
ATOM 1524 O TYR B 83 27.212 42.194 12.224 1.00 30.25 O
ATOM 1525 CB TYR B 83 28.601 43.790 14.586 1.00 29.60 C
ATOM 1526 CG TYR B 83 29.286 42.808 15.513 1.00 25.79 C
ATOM 1527 CD1 TYR B 83 29.842 41.630 15.029 1.00 24.72 C
ATOM 1528 CD2 TYR B 83 29.408 43.079 16.869 1.00 28.13 C
ATOM 1529 CE1 TYR B 83 30.475 40.736 15.873 1.00 24.86 C
ATOM 1530 CE2 TYR B 83 30.043 42.193 17.721 1.00 28.66 C
ATOM 1531 CZ TYR B 83 30.573 41.022 17.217 1.00 29.34 C
ATOM 1532 OH TYR B 83 31.208 40.138 18.058 1.00 26.83 O
ATOM 1533 N ALA B 84 26.867 41.042 14.119 1.00 27.42 N
ATOM 1534 CA ALA B 84 27.009 39.756 13.449 1.00 26.55 C
ATOM 1535 C ALA B 84 25.764 39.402 12.644 1.00 31.60 C
ATOM 1536 O ALA B 84 24.640 39.761 13.004 1.00 27.17 O
ATOM 1537 CB ALA B 84 27.298 38.648 14.462 1.00 27.47 C
ATOM 1538 N PHE B 85 25.981 38.697 11.531 1.00 26.23 N
ATOM 1539 CA APHE B 85 24.891 38.164 10.728 0.67 24.08 C
ATOM 1540 CA BPHE B 85 24.917 38.162 10.680 0.33 24.10 C
ATOM 1541 C PHE B 85 24.826 36.659 10.935 1.00 25.03 C
ATOM 1542 O PHE B 85 25.762 35.926 10.597 1.00 20.91 O
ATOM 1543 CB APHE B 85 25.042 38.489 9.244 0.67 22.90 C
ATOM 1544 CB BPHE B 85 25.214 38.414 9.199 0.33 23.03 C
ATOM 1545 CG APHE B 85 23.945 37.907 8.406 0.67 26.21 C
ATOM 1546 CG BPHE B 85 24.646 39.696 8.645 0.33 25.16 C
ATOM 1547 CD1APHE B 85 22.682 38.473 8.415 0.67 22.88 C
ATOM 1548 CD1BPHE B 85 24.271 40.739 9.470 0.33 36.69 C
ATOM 1549 CD2APHE B 85 24.162 36.772 7.644 0.67 23.13 C
ATOM 1550 CD2BPHE B 85 24.488 39.846 7.275 0.33 35.63 C
ATOM 1551 CE1APHE B 85 21.663 37.937 7.660 0.67 18.13 C
ATOM 1552 CE1BPHE B 85 23.751 41.914 8.935 0.33 19.82 C
ATOM 1553 CE2APHE B 85 23.146 36.230 6.888 0.67 24.28 C
ATOM 1554 CE2BPHE B 85 23.967 41.013 6.738 0.33 24.72 C
ATOM 1555 CZ APHE B 85 21.894 36.813 6.897 0.67 25.23 C
ATOM 1556 CZ BPHE B 85 23.599 42.048 7.570 0.33 23.58 C
ATOM 1557 N GLY B 86 23.714 36.198 11.499 1.00 27.27 N
ATOM 1558 CA GLY B 86 23.527 34.788 11.747 1.00 21.17 C
ATOM 1559 C GLY B 86 22.501 34.541 12.831 1.00 20.44 C
ATOM 1560 O GLY B 86 21.862 35.470 13.323 1.00 20.35 O
ATOM 1561 N PRO B 87 22.310 33.276 13.224 1.00 19.99 N
ATOM 1562 CA PRO B 87 22.960 32.073 12.709 1.00 20.29 C
ATOM 1563 C PRO B 87 22.321 31.562 11.425 1.00 24.07 C
ATOM 1564 O PRO B 87 21.115 31.709 11.227 1.00 22.09 O
ATOM 1565 CB PRO B 87 22.747 31.069 13.837 1.00 21.34 C
ATOM 1566 CG PRO B 87 21.423 31.454 14.398 1.00 21.29 C
ATOM 1567 CD PRO B 87 21.383 32.959 14.325 1.00 22.35 C
ATOM 1568 N LEU B 88 23.135 30.980 10.555 1.00 21.37 N
ATOM 1569 CA LEU B 88 22.655 30.155 9.457 1.00 17.83 C
ATOM 1570 C LEU B 88 23.120 28.736 9.729 1.00 20.96 C
ATOM 1571 O LEU B 88 24.326 28.467 9.739 1.00 21.25 O
ATOM 1572 CB LEU B 88 23.175 30.642 8.105 1.00 23.90 C
ATOM 1573 CG LEU B 88 22.753 29.759 6.926 1.00 23.20 C
ATOM 1574 CD1 LEU B 88 21.253 29.886 6.660 1.00 21.86 C
ATOM 1575 CD2 LEU B 88 23.553 30.092 5.677 1.00 32.00 C
ATOM 1576 N PHE B 89 22.172 27.840 9.972 1.00 19.34 N
ATOM 1577 CA PHE B 89 22.510 26.451 10.241 1.00 23.98 C
ATOM 1578 C PHE B 89 22.810 25.741 8.930 1.00 22.06 C
ATOM 1579 O PHE B 89 21.940 25.636 8.057 1.00 22.53 O
ATOM 1580 CB PHE B 89 21.379 25.769 11.002 1.00 20.81 C
ATOM 1581 CG PHE B 89 21.250 26.242 12.418 1.00 22.77 C
ATOM 1582 CD1 PHE B 89 22.018 25.672 13.420 1.00 23.77 C
ATOM 1583 CD2 PHE B 89 20.392 27.279 12.744 1.00 25.64 C
ATOM 1584 CE1 PHE B 89 21.917 26.113 14.726 1.00 28.53 C
ATOM 1585 CE2 PHE B 89 20.285 27.725 14.049 1.00 32.47 C
ATOM 1586 CZ PHE B 89 21.049 27.141 15.041 1.00 27.98 C
ATOM 1587 N LEU B 90 24.050 25.272 8.784 1.00 23.00 N
ATOM 1588 CA LEU B 90 24.412 24.521 7.590 1.00 18.61 C
ATOM 1589 C LEU B 90 23.854 23.105 7.650 1.00 19.46 C
ATOM 1590 O LEU B 90 23.349 22.596 6.643 1.00 23.43 O
ATOM 1591 CB LEU B 90 25.932 24.519 7.409 1.00 24.06 C
ATOM 1592 CG LEU B 90 26.534 25.908 7.147 1.00 25.49 C
ATOM 1593 CD1 LEU B 90 27.985 25.849 6.669 1.00 25.41 C
ATOM 1594 CD2 LEU B 90 25.686 26.688 6.159 1.00 21.17 C
ATOM 1595 N PHE B 91 23.913 22.463 8.816 1.00 18.83 N
ATOM 1596 CA PHE B 91 23.182 21.219 9.020 1.00 22.32 C
ATOM 1597 C PHE B 91 23.079 20.914 10.507 1.00 24.33 C
ATOM 1598 O PHE B 91 23.775 21.498 11.342 1.00 19.44 O
ATOM 1599 CB PHE B 91 23.825 20.041 8.273 1.00 16.23 C
ATOM 1600 CG PHE B 91 25.205 19.659 8.762 1.00 20.02 C
ATOM 1601 CD1 PHE B 91 25.372 18.917 9.925 1.00 24.14 C
ATOM 1602 CD2 PHE B 91 26.329 19.995 8.024 1.00 25.18 C
ATOM 1603 CE1 PHE B 91 26.633 18.554 10.360 1.00 25.99 C
ATOM 1604 CE2 PHE B 91 27.593 19.633 8.452 1.00 21.68 C
ATOM 1605 CZ PHE B 91 27.747 18.912 9.621 1.00 20.85 C
ATOM 1606 N LYS B 92 22.178 19.986 10.816 1.00 18.14 N
ATOM 1607 CA LYS B 92 22.153 19.250 12.069 1.00 18.62 C
ATOM 1608 C LYS B 92 21.992 17.779 11.722 1.00 18.45 C
ATOM 1609 O LYS B 92 21.219 17.432 10.824 1.00 22.75 O
ATOM 1610 CB LYS B 92 21.014 19.708 12.984 1.00 22.23 C
ATOM 1611 CG LYS B 92 20.858 21.212 13.080 1.00 23.21 C
ATOM 1612 CD LYS B 92 19.767 21.587 14.068 1.00 27.92 C
ATOM 1613 CE LYS B 92 19.420 23.059 13.962 1.00 40.35 C
ATOM 1614 NZ LYS B 92 18.291 23.296 13.024 1.00 46.34 N
ATOM 1615 N GLY B 93 22.731 16.917 12.408 1.00 21.55 N
ATOM 1616 CA GLY B 93 22.671 15.514 12.048 1.00 19.93 C
ATOM 1617 C GLY B 93 23.321 14.642 13.095 1.00 22.98 C
ATOM 1618 O GLY B 93 23.763 15.110 14.148 1.00 22.00 O
ATOM 1619 N TYR B 94 23.373 13.351 12.780 1.00 20.91 N
ATOM 1620 CA TYR B 94 23.889 12.337 13.685 1.00 17.40 C
ATOM 1621 C TYR B 94 25.107 11.671 13.069 1.00 21.17 C
ATOM 1622 O TYR B 94 25.131 11.384 11.868 1.00 21.16 O
ATOM 1623 CB TYR B 94 22.826 11.285 13.998 1.00 18.96 C
ATOM 1624 CG TYR B 94 21.660 11.847 14.765 1.00 26.05 C
ATOM 1625 CD1 TYR B 94 21.662 11.868 16.152 1.00 21.37 C
ATOM 1626 CD2 TYR B 94 20.561 12.372 14.101 1.00 25.81 C
ATOM 1627 CE1 TYR B 94 20.596 12.392 16.858 1.00 32.18 C
ATOM 1628 CE2 TYR B 94 19.492 12.897 14.795 1.00 30.71 C
ATOM 1629 CZ TYR B 94 19.513 12.903 16.174 1.00 31.41 C
ATOM 1630 OH TYR B 94 18.444 13.424 16.867 1.00 33.43 O
ATOM 1631 N ARG B 95 26.117 11.431 13.899 1.00 23.35 N
ATOM 1632 CA ARG B 95 27.295 10.716 13.439 1.00 23.77 C
ATOM 1633 C ARG B 95 26.940 9.278 13.094 1.00 19.79 C
ATOM 1634 O ARG B 95 26.182 8.617 13.808 1.00 26.27 O
ATOM 1635 CB ARG B 95 28.391 10.738 14.502 1.00 24.39 C
ATOM 1636 CG ARG B 95 29.682 10.095 14.030 1.00 26.13 C
ATOM 1637 CD ARG B 95 30.780 10.181 15.066 1.00 29.91 C
ATOM 1638 NE ARG B 95 32.032 9.656 14.538 1.00 22.76 N
ATOM 1639 CZ ARG B 95 33.149 9.529 15.241 1.00 35.55 C
ATOM 1640 NH1 ARG B 95 33.213 9.903 16.508 1.00 29.81 N
ATOM 1641 NH2 ARG B 95 34.229 9.020 14.655 1.00 27.50 N
ATOM 1642 N VAL B 96 27.484 8.800 11.984 1.00 20.71 N
ATOM 1643 CA VAL B 96 27.328 7.411 11.579 1.00 23.00 C
ATOM 1644 C VAL B 96 28.405 6.594 12.278 1.00 28.33 C
ATOM 1645 O VAL B 96 29.599 6.891 12.156 1.00 25.75 O
ATOM 1646 CB VAL B 96 27.421 7.272 10.051 1.00 29.82 C
ATOM 1647 CG1 VAL B 96 27.418 5.807 9.647 1.00 27.14 C
ATOM 1648 CG2 VAL B 96 26.278 8.023 9.382 1.00 35.81 C
ATOM 1649 N GLU B 97 27.984 5.574 13.022 1.00 31.33 N
ATOM 1650 CA GLU B 97 28.887 4.807 13.869 1.00 41.71 C
ATOM 1651 C GLU B 97 29.621 3.750 13.057 1.00 44.02 C
ATOM 1652 O GLU B 97 29.051 3.136 12.150 1.00 36.87 O
ATOM 1653 CB GLU B 97 28.121 4.144 15.014 1.00 38.90 C
ATOM 1654 N GLY B 98 30.887 3.538 13.398 1.00 44.38 N
ATOM 1655 CA GLY B 98 31.735 2.603 12.684 1.00 42.98 C
ATOM 1656 C GLY B 98 33.164 3.101 12.606 1.00 59.14 C
ATOM 1657 O GLY B 98 33.487 4.155 13.158 1.00 54.74 O
TER 1658 GLY B 98
TER 2533 GLY C 98
TER 3403 GLY D 98
TER 4252 GLY E 98
TER 5090 GLY F 98
HETATM 5105 C ACT B 101 25.486 28.449 19.329 1.00 25.87 C
HETATM 5106 O ACT B 101 24.943 27.582 18.600 1.00 39.55 O
HETATM 5107 OXT ACT B 101 25.957 28.315 20.490 1.00 27.74 O
HETATM 5108 CH3 ACT B 101 25.576 29.889 18.735 1.00 27.22 C
HETATM 5109 C ACT B 102 41.693 36.870 0.706 1.00 61.10 C
HETATM 5110 O ACT B 102 42.834 37.335 0.444 1.00 67.22 O
HETATM 5111 OXT ACT B 102 40.773 37.380 1.408 1.00 58.77 O
HETATM 5112 CH3 ACT B 102 41.361 35.472 0.083 1.00 36.57 C
HETATM 5266 O HOH B 201 25.282 6.744 20.787 1.00 61.35 O
HETATM 5267 O HOH B 202 17.074 25.906 15.867 1.00 51.06 O
HETATM 5268 O HOH B 203 31.494 44.895 19.807 1.00 55.74 O
HETATM 5269 O HOH B 204 43.988 27.537 2.635 1.00 51.58 O
HETATM 5270 O HOH B 205 22.460 11.253 19.934 1.00 43.67 O
HETATM 5271 O HOH B 206 25.282 33.142 33.200 1.00 37.17 O
HETATM 5272 O HOH B 207 32.597 33.384 1.491 1.00 29.15 O
HETATM 5273 O HOH B 208 37.821 47.513 8.791 1.00 47.29 O
HETATM 5274 O HOH B 209 28.495 29.808 30.919 1.00 33.99 O
HETATM 5275 O HOH B 210 30.738 17.978 13.476 1.00 29.01 O
HETATM 5276 O HOH B 211 23.421 43.019 22.942 1.00 43.11 O
HETATM 5277 O HOH B 212 13.125 19.310 17.860 1.00 36.64 O
HETATM 5278 O HOH B 213 37.454 27.124 0.493 1.00 40.18 O
HETATM 5279 O HOH B 214 34.566 39.179 3.480 1.00 23.80 O
HETATM 5280 O HOH B 215 22.538 27.240 17.875 1.00 37.49 O
HETATM 5281 O HOH B 216 30.845 19.388 28.582 1.00 35.98 O
HETATM 5282 O HOH B 217 21.083 29.865 17.827 1.00 43.01 O
HETATM 5283 O HOH B 218 31.146 26.866 36.127 1.00 47.46 O
HETATM 5284 O HOH B 219 18.994 30.327 30.382 1.00 35.77 O
HETATM 5285 O HOH B 220 33.158 44.925 6.501 1.00 34.69 O
HETATM 5286 O HOH B 221 31.479 40.979 20.567 1.00 33.32 O
HETATM 5287 O HOH B 222 33.608 20.239 16.486 1.00 25.04 O
HETATM 5288 O HOH B 223 33.682 39.634 21.787 1.00 22.76 O
HETATM 5289 O HOH B 224 36.829 34.385 24.477 1.00 29.40 O
HETATM 5290 O HOH B 225 39.763 37.763 19.449 1.00 32.88 O
HETATM 5291 O HOH B 226 16.143 19.380 25.645 1.00 30.59 O
HETATM 5292 O HOH B 227 24.107 20.507 26.065 1.00 23.86 O
HETATM 5293 O HOH B 228 25.307 27.487 29.355 1.00 31.98 O
HETATM 5294 O HOH B 229 27.726 28.240 3.181 1.00 36.51 O
HETATM 5295 O HOH B 230 24.237 27.883 26.178 1.00 25.00 O
HETATM 5296 O HOH B 231 24.145 22.621 32.664 1.00 32.47 O
HETATM 5297 O HOH B 232 25.073 33.573 8.844 1.00 23.73 O
HETATM 5298 O HOH B 233 26.399 37.958 4.960 1.00 36.80 O
HETATM 5299 O HOH B 234 43.882 42.758 1.964 1.00 39.59 O
HETATM 5300 O HOH B 235 16.170 24.555 30.672 1.00 52.05 O
HETATM 5301 O HOH B 236 13.291 15.560 16.795 1.00 54.47 O
HETATM 5302 O HOH B 237 22.304 28.745 35.694 1.00 35.87 O
HETATM 5303 O HOH B 238 28.422 47.231 16.673 1.00 45.31 O
HETATM 5304 O HOH B 239 26.446 43.564 20.207 1.00 31.53 O
HETATM 5305 O HOH B 240 31.201 6.195 16.769 1.00 52.99 O
HETATM 5306 O HOH B 241 23.929 42.479 13.713 1.00 32.49 O
HETATM 5307 O HOH B 242 40.154 20.559 15.919 1.00 36.62 O
HETATM 5308 O HOH B 243 21.863 45.639 18.849 1.00 47.39 O
HETATM 5309 O HOH B 244 37.142 33.967 8.506 1.00 34.16 O
HETATM 5310 O HOH B 245 23.250 34.795 29.679 1.00 36.96 O
HETATM 5311 O HOH B 246 39.308 37.117 9.908 1.00 46.68 O
HETATM 5312 O HOH B 247 37.006 25.740 20.706 1.00 28.11 O
HETATM 5313 O HOH B 248 37.807 20.251 19.804 1.00 26.28 O
HETATM 5314 O HOH B 249 37.404 24.540 26.946 1.00 43.89 O
HETATM 5315 O HOH B 250 27.176 31.083 1.200 1.00 32.69 O
HETATM 5316 O HOH B 251 17.351 20.268 16.956 1.00 26.21 O
HETATM 5317 O HOH B 252 20.826 37.111 24.232 1.00 27.72 O
HETATM 5318 O HOH B 253 15.733 25.116 22.912 1.00 37.40 O
HETATM 5319 O HOH B 254 31.170 47.447 12.154 1.00 43.34 O
HETATM 5320 O HOH B 255 38.066 25.872 23.159 1.00 31.69 O
HETATM 5321 O HOH B 256 16.786 15.006 15.313 1.00 41.73 O
HETATM 5322 O HOH B 257 39.216 34.954 10.139 1.00 50.39 O
HETATM 5323 O HOH B 258 23.643 7.683 12.897 1.00 35.16 O
HETATM 5324 O HOH B 259 41.181 41.008 12.310 1.00 45.71 O
HETATM 5325 O HOH B 260 33.674 16.057 25.830 1.00 44.62 O
HETATM 5326 O HOH B 261 37.878 26.657 18.235 1.00 19.75 O
HETATM 5327 O HOH B 262 25.644 33.537 6.424 1.00 24.61 O
HETATM 5328 O HOH B 263 30.869 10.542 18.408 1.00 42.43 O
HETATM 5329 O HOH B 264 18.887 12.793 19.645 1.00 26.56 O
HETATM 5330 O HOH B 265 19.284 30.933 25.729 1.00 28.68 O
HETATM 5331 O HOH B 266 28.305 8.454 21.579 1.00 56.55 O
HETATM 5332 O HOH B 267 19.448 24.392 8.087 1.00 33.72 O
HETATM 5333 O HOH B 268 35.474 27.722 2.074 1.00 27.10 O
HETATM 5334 O HOH B 269 16.145 21.458 13.598 1.00 47.52 O
HETATM 5335 O HOH B 270 23.327 37.235 28.749 1.00 51.32 O
HETATM 5336 O HOH B 271 31.142 29.633 2.701 1.00 23.45 O
HETATM 5337 O HOH B 272 20.593 15.156 26.890 1.00 32.78 O
HETATM 5338 O HOH B 273 36.941 43.047 16.344 1.00 29.00 O
HETATM 5339 O HOH B 274 45.047 30.376 11.368 1.00 41.84 O
HETATM 5340 O HOH B 275 25.694 10.032 22.434 1.00 54.50 O
HETATM 5341 O HOH B 276 17.458 13.706 22.129 1.00 28.66 O
HETATM 5342 O HOH B 277 18.840 30.668 21.829 1.00 32.64 O
HETATM 5343 O HOH B 278 41.390 35.964 16.420 1.00 46.62 O
HETATM 5344 O HOH B 279 26.534 23.606 35.298 1.00 49.27 O
HETATM 5345 O HOH B 280 35.801 24.731 28.915 1.00 35.78 O
HETATM 5346 O HOH B 281 35.871 18.998 23.548 1.00 32.20 O
HETATM 5347 O HOH B 282 35.924 21.355 21.681 1.00 21.99 O
HETATM 5348 O HOH B 283 25.092 4.894 12.958 1.00 47.40 O
HETATM 5349 O HOH B 284 23.813 19.902 28.959 1.00 26.74 O
HETATM 5350 O HOH B 285 31.791 6.446 14.205 1.00 47.22 O
HETATM 5351 O HOH B 286 22.863 21.993 30.362 1.00 27.99 O
HETATM 5352 O HOH B 287 21.248 26.050 5.124 1.00 37.41 O
HETATM 5353 O HOH B 288 19.294 28.719 9.665 1.00 25.17 O
HETATM 5354 O HOH B 289 37.083 32.052 26.159 1.00 44.54 O
HETATM 5355 O HOH B 290 38.687 42.704 13.866 1.00 39.00 O
HETATM 5356 O HOH B 291 25.568 47.066 12.349 1.00 45.13 O
HETATM 5357 O HOH B 292 33.237 30.925 1.834 1.00 37.43 O
HETATM 5358 O HOH B 293 39.508 36.629 14.125 1.00 38.98 O
HETATM 5359 O HOH B 294 17.689 12.713 26.182 1.00 53.74 O
HETATM 5360 O HOH B 295 36.306 14.447 19.092 1.00 33.47 O
HETATM 5361 O HOH B 296 30.820 16.873 28.800 1.00 50.33 O
HETATM 5362 O HOH B 297 25.430 30.559 2.790 1.00 39.97 O
HETATM 5363 O HOH B 298 29.139 45.586 20.282 1.00 52.74 O
HETATM 5364 O HOH B 299 35.907 8.552 17.222 1.00 52.35 O
HETATM 5365 O HOH B 300 32.539 19.945 33.005 1.00 58.56 O
HETATM 5366 O HOH B 301 37.078 7.962 13.980 1.00 30.52 O
HETATM 5367 O HOH B 302 13.125 20.164 24.411 1.00 46.79 O
HETATM 5368 O HOH B 303 35.468 4.774 15.540 1.00 51.23 O
HETATM 5369 O HOH B 304 26.735 34.636 0.934 1.00 24.26 O
HETATM 5370 O HOH B 305 29.256 20.267 33.078 1.00 50.72 O
HETATM 5371 O HOH B 306 39.394 46.203 7.823 1.00 56.07 O
HETATM 5372 O HOH B 307 17.531 18.426 28.666 1.00 50.84 O
HETATM 5373 O HOH B 308 35.126 48.043 16.195 1.00 57.97 O
HETATM 5374 O HOH B 309 17.216 31.736 27.496 1.00 47.48 O
HETATM 5375 O HOH B 310 42.202 35.009 4.439 1.00 50.95 O
HETATM 5376 O HOH B 311 34.317 31.264 28.602 1.00 35.34 O
HETATM 5377 O HOH B 312 35.830 22.581 29.887 1.00 47.79 O
HETATM 5378 O HOH B 313 19.919 17.635 27.725 1.00 29.80 O
HETATM 5379 O HOH B 314 36.395 16.708 22.663 1.00 52.01 O
HETATM 5380 O HOH B 315 19.816 21.970 6.781 1.00 30.78 O
HETATM 5381 O HOH B 316 12.058 25.461 24.505 1.00 63.75 O
HETATM 5382 O HOH B 317 15.444 27.929 22.874 1.00 50.06 O
HETATM 5383 O HOH B 318 40.090 35.710 20.203 1.00 36.73 O
HETATM 5384 O HOH B 319 30.796 18.968 31.666 1.00 52.36 O
HETATM 5385 O HOH B 320 16.472 22.379 9.951 1.00 53.93 O
HETATM 5386 O HOH B 321 34.808 29.333 30.274 1.00 44.02 O
HETATM 5387 O HOH B 322 24.955 35.091 31.103 1.00 39.29 O
HETATM 5388 O HOH B 323 43.990 35.191 11.471 1.00 56.30 O
HETATM 5389 O HOH B 324 24.631 35.103 35.249 1.00 40.03 O
HETATM 5390 O HOH B 325 19.754 32.753 23.360 1.00 35.19 O
HETATM 5391 O HOH B 326 43.448 35.890 9.026 1.00 52.66 O
HETATM 5392 O HOH B 327 27.069 20.565 35.289 1.00 53.20 O
HETATM 5393 O HOH B 328 20.577 20.991 31.953 1.00 40.56 O
HETATM 5394 O HOH B 329 23.708 45.114 21.202 1.00 47.82 O
HETATM 5395 O HOH B 330 21.997 17.986 29.250 1.00 39.89 O
HETATM 5396 O HOH B 331 29.031 41.162 6.041 1.00 47.79 O
HETATM 5397 O HOH B 332 16.320 22.582 16.445 1.00 46.32 O
HETATM 5398 O HOH B 333 14.118 16.933 21.847 1.00 44.01 O
HETATM 5399 O HOH B 334 19.257 22.491 33.619 1.00 54.91 O
HETATM 5400 O HOH B 335 22.873 6.870 20.569 1.00 59.51 O
HETATM 5401 O HOH B 336 37.824 41.591 21.279 1.00 48.01 O
HETATM 5402 O HOH B 337 18.831 32.572 29.598 1.00 48.53 O
HETATM 5403 O HOH B 338 32.795 13.797 20.333 1.00 48.58 O
HETATM 5404 O HOH B 339 13.488 21.849 17.315 1.00 42.07 O
HETATM 5405 O HOH B 340 20.135 38.037 26.921 1.00 47.16 O
HETATM 5406 O HOH B 341 24.275 20.705 34.780 1.00 44.96 O
HETATM 5407 O HOH B 342 34.972 14.637 21.478 1.00 51.91 O
HETATM 5408 O HOH B 343 11.810 18.627 20.143 1.00 41.70 O
HETATM 5409 O HOH B 344 27.110 2.053 8.375 1.00 54.66 O
HETATM 5410 O HOH B 345 33.551 13.522 24.589 1.00 56.62 O
HETATM 5411 O HOH B 346 19.987 10.441 20.004 1.00 46.93 O
HETATM 5412 O HOH B 347 38.759 17.968 20.546 1.00 36.74 O
HETATM 5413 O HOH B 348 37.894 22.503 25.804 1.00 49.77 O
HETATM 5414 O HOH B 349 39.500 34.857 22.975 1.00 44.31 O
HETATM 5415 O HOH B 350 36.418 19.831 26.133 1.00 41.98 O
HETATM 5416 O HOH B 351 20.689 34.659 30.314 1.00 42.64 O
HETATM 5417 O HOH B 352 14.206 17.979 24.444 1.00 40.60 O
HETATM 5418 O HOH B 353 26.274 26.648 2.337 1.00 39.53 O
HETATM 5419 O HOH B 354 23.461 29.095 2.192 1.00 32.56 O
HETATM 5420 O HOH B 355 11.209 20.263 21.883 1.00 40.41 O
HETATM 5421 O HOH B 356 30.107 10.103 22.999 1.00 54.08 O
CONECT 548 556
CONECT 556 548 557
CONECT 557 556 558 564
CONECT 558 557 559
CONECT 559 558 560
CONECT 560 559 561
CONECT 561 560 562
CONECT 562 561 563
CONECT 563 562
CONECT 564 557 565 566
CONECT 565 564
CONECT 566 564
CONECT 1382 1390
CONECT 1390 1382 1391
CONECT 1391 1390 1392 1398
CONECT 1392 1391 1393
CONECT 1393 1392 1394
CONECT 1394 1393 1395
CONECT 1395 1394 1396
CONECT 1396 1395 1397
CONECT 1397 1396
CONECT 1398 1391 1399 1400
CONECT 1399 1398
CONECT 1400 1398
CONECT 2054 2071 2086
CONECT 2071 2054 2072
CONECT 2072 2071 2073 2075
CONECT 2073 2072 2074 2101
CONECT 2074 2073
CONECT 2075 2072 2076
CONECT 2076 2075 2077
CONECT 2077 2076 2078
CONECT 2078 2077 2079
CONECT 2079 2078 2082 2083
CONECT 2080 2081 2082 2085
CONECT 2081 2080 2084
CONECT 2082 2079 2080
CONECT 2083 2079
CONECT 2084 2081
CONECT 2085 2080
CONECT 2086 2054 2087
CONECT 2087 2086 2088 2090
CONECT 2088 2087 2089 2101
CONECT 2089 2088
CONECT 2090 2087 2091
CONECT 2091 2090 2092
CONECT 2092 2091 2093
CONECT 2093 2092 2094
CONECT 2094 2093 2095 2096
CONECT 2095 2094
CONECT 2096 2094 2097
CONECT 2097 2096 2098
CONECT 2098 2097 2099 2100
CONECT 2099 2098
CONECT 2100 2098
CONECT 2101 2073 2088
CONECT 2253 2261
CONECT 2261 2253 2262
CONECT 2262 2261 2263 2269
CONECT 2263 2262 2264
CONECT 2264 2263 2265
CONECT 2265 2264 2266
CONECT 2266 2265 2267
CONECT 2267 2266 2268
CONECT 2268 2267
CONECT 2269 2262 2270 2271
CONECT 2270 2269
CONECT 2271 2269
CONECT 2918 2935 2950
CONECT 2935 2918 2936
CONECT 2936 2935 2937 2939
CONECT 2937 2936 2938 2965
CONECT 2938 2937
CONECT 2939 2936 2940
CONECT 2940 2939 2941
CONECT 2941 2940 2942
CONECT 2942 2941 2943
CONECT 2943 2942 2944 2945
CONECT 2944 2943
CONECT 2945 2943 2946
CONECT 2946 2945 2947
CONECT 2947 2946 2948 2949
CONECT 2948 2947
CONECT 2949 2947
CONECT 2950 2918 2951
CONECT 2951 2950 2952 2954
CONECT 2952 2951 2953 2965
CONECT 2953 2952
CONECT 2954 2951 2955
CONECT 2955 2954 2956
CONECT 2956 2955 2957
CONECT 2957 2956 2958
CONECT 2958 2957 2961 2962
CONECT 2959 2960 2961 2964
CONECT 2960 2959 2963
CONECT 2961 2958 2959
CONECT 2962 2958
CONECT 2963 2960
CONECT 2964 2959
CONECT 2965 2937 2952
CONECT 3123 3131
CONECT 3131 3123 3132
CONECT 3132 3131 3133 3139
CONECT 3133 3132 3134
CONECT 3134 3133 3135
CONECT 3135 3134 3136
CONECT 3136 3135 3137
CONECT 3137 3136 3138
CONECT 3138 3137
CONECT 3139 3132 3140 3141
CONECT 3140 3139
CONECT 3141 3139
CONECT 3785 3802 3817
CONECT 3802 3785 3803
CONECT 3803 3802 3804 3806
CONECT 3804 3803 3805 3832
CONECT 3805 3804
CONECT 3806 3803 3807
CONECT 3807 3806 3808
CONECT 3808 3807 3809
CONECT 3809 3808 3810
CONECT 3810 3809 3813 3814
CONECT 3811 3812 3813 3816
CONECT 3812 3811 3815
CONECT 3813 3810 3811
CONECT 3814 3810
CONECT 3815 3812
CONECT 3816 3811
CONECT 3817 3785 3818
CONECT 3818 3817 3819 3821
CONECT 3819 3818 3820 3832
CONECT 3820 3819
CONECT 3821 3818 3822
CONECT 3822 3821 3823
CONECT 3823 3822 3824
CONECT 3824 3823 3825
CONECT 3825 3824 3826 3827
CONECT 3826 3825
CONECT 3827 3825 3828
CONECT 3828 3827 3829
CONECT 3829 3828 3830 3831
CONECT 3830 3829
CONECT 3831 3829
CONECT 3832 3804 3819
CONECT 3984 3992
CONECT 3992 3984 3993
CONECT 3993 3992 3994 4000
CONECT 3994 3993 3995
CONECT 3995 3994 3996
CONECT 3996 3995 3997
CONECT 3997 3996 3998
CONECT 3998 3997 3999
CONECT 3999 3998
CONECT 4000 3993 4001 4002
CONECT 4001 4000
CONECT 4002 4000
CONECT 4812 4826
CONECT 4826 4812 4827
CONECT 4827 4826 4828 4834
CONECT 4828 4827 4829
CONECT 4829 4828 4830
CONECT 4830 4829 4831
CONECT 4831 4830 4832
CONECT 4832 4831 4833
CONECT 4833 4832
CONECT 4834 4827 4835 4836
CONECT 4835 4834
CONECT 4836 4834
CONECT 5091 5092 5093 5094
CONECT 5092 5091
CONECT 5093 5091
CONECT 5094 5091
CONECT 5095 5096 5097 5098
CONECT 5096 5095
CONECT 5097 5095
CONECT 5098 5095
CONECT 5099 5100 5101
CONECT 5100 5099
CONECT 5101 5099 5102 5103
CONECT 5102 5101
CONECT 5103 5101 5104
CONECT 5104 5103
CONECT 5105 5106 5107 5108
CONECT 5106 5105
CONECT 5107 5105
CONECT 5108 5105
CONECT 5109 5110 5111 5112
CONECT 5110 5109
CONECT 5111 5109
CONECT 5112 5109
CONECT 5113 5114 5115 5116
CONECT 5114 5113
CONECT 5115 5113
CONECT 5116 5113
CONECT 5117 5118 5119 5120
CONECT 5118 5117
CONECT 5119 5117
CONECT 5120 5117
CONECT 5121 5122 5123 5124
CONECT 5122 5121
CONECT 5123 5121
CONECT 5124 5121
CONECT 5125 5126 5127 5128
CONECT 5126 5125
CONECT 5127 5125
CONECT 5128 5125
CONECT 5129 5130 5131 5132
CONECT 5130 5129
CONECT 5131 5129
CONECT 5132 5129
CONECT 5133 5134 5135 5136
CONECT 5134 5133
CONECT 5135 5133
CONECT 5136 5133
CONECT 5137 5138 5139 5140
CONECT 5138 5137
CONECT 5139 5137
CONECT 5140 5137
CONECT 5141 5142 5143 5144
CONECT 5142 5141
CONECT 5143 5141
CONECT 5144 5141
CONECT 5145 5146 5147 5148
CONECT 5146 5145
CONECT 5147 5145
CONECT 5148 5145
MASTER 754 0 26 24 27 0 0 6 5800 6 226 48
END