| content |
HEADER HYDROLASE 09-NOV-12 4HXG
TITLE PYROCOCCUS HORIKOSHII ACYLAMINOACYL PEPTIDASE (ORTHORHOMBIC CRYSTAL
TITLE 2 FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN PH0594;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 EC: 3.4.19.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 70601;
SOURCE 4 STRAIN: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
SOURCE 5 GENE: PH0594;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS SELF-COMPARTMENTALIZATION, BETA-PROPELLER, ALPHA/BETA HYRDOLASE FOLD,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KISS-SZEMAN,D.K.MENYHARD,E.TICHY-RACS,B.HORNUNG,K.RADI,Z.SZELTNER,
AUTHOR 2 K.DOMOKOS,I.SZAMOSI,G.NARAY-SZABO,L.POLGAR,V.HARMAT
REVDAT 2 15-MAY-13 4HXG 1 JRNL
REVDAT 1 08-MAY-13 4HXG 0
JRNL AUTH D.K.MENYHARD,A.KISS-SZEMAN,E.TICHY-RACS,B.HORNUNG,K.RADI,
JRNL AUTH 2 Z.SZELTNER,K.DOMOKOS,I.SZAMOSI,G.NARAY-SZABO,L.POLGAR,
JRNL AUTH 3 V.HARMAT
JRNL TITL A SELF-COMPARTMENTALIZING HEXAMER SERINE PROTEASE FROM
JRNL TITL 2 PYROCOCCUS HORIKOSHII - SUBSTRATE SELECTION ACHIEVED THROUGH
JRNL TITL 3 MULTIMERIZATION.
JRNL REF J.BIOL.CHEM. 2013
JRNL REFN ESSN 1083-351X
JRNL PMID 23632025
JRNL DOI 10.1074/JBC.M113.451534
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.SZELTNER,A.L.KISS,K.DOMOKOS,V.HARMAT,G.NARAY-SZABO,
REMARK 1 AUTH 2 L.POLGAR
REMARK 1 TITL CHARACTERIZATION OF A NOVEL ACYLAMINOACYL PEPTIDASE WITH
REMARK 1 TITL 2 HEXAMERIC STRUCTURE AND ENDOPEPTIDASE ACTIVITY.
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1794 1204 2009
REMARK 1 REFN ISSN 0006-3002
REMARK 1 PMID 19303951
REMARK 1 DOI 10.1016/J.BBAPAP.2009.03.004
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.6
REMARK 3 NUMBER OF REFLECTIONS : 222127
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.790
REMARK 3 FREE R VALUE TEST SET COUNT : 1751
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 19.9807 - 6.2872 0.91 18193 185 0.1718 0.2015
REMARK 3 2 6.2872 - 5.0163 0.93 18159 94 0.1752 0.2384
REMARK 3 3 5.0163 - 4.3899 0.93 18119 192 0.1368 0.1675
REMARK 3 4 4.3899 - 3.9920 0.93 18048 91 0.1588 0.1964
REMARK 3 5 3.9920 - 3.7078 0.92 17905 190 0.1901 0.2589
REMARK 3 6 3.7078 - 3.4904 0.92 17761 92 0.2101 0.2452
REMARK 3 7 3.4904 - 3.3165 0.91 17458 183 0.2138 0.2551
REMARK 3 8 3.3165 - 3.1727 0.89 17115 86 0.2235 0.2572
REMARK 3 9 3.1727 - 3.0510 0.87 16648 181 0.2349 0.2871
REMARK 3 10 3.0510 - 2.9460 0.83 16076 86 0.2674 0.2931
REMARK 3 11 2.9460 - 2.8542 0.80 15350 154 0.3043 0.3724
REMARK 3 12 2.8542 - 2.7728 0.78 15080 74 0.3227 0.3787
REMARK 3 13 2.7728 - 2.7000 0.76 14464 143 0.3393 0.3845
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.28
REMARK 3 B_SOL : 40.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.850
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.77050
REMARK 3 B22 (A**2) : -8.72630
REMARK 3 B33 (A**2) : -21.16620
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 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 : 0.005 60324
REMARK 3 ANGLE : 0.979 81727
REMARK 3 CHIRALITY : 0.077 8515
REMARK 3 PLANARITY : 0.005 10492
REMARK 3 DIHEDRAL : 14.136 21378
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resseq 4:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 66.8984 -13.1890 -32.1439
REMARK 3 T TENSOR
REMARK 3 T11: 0.3557 T22: 0.3075
REMARK 3 T33: 0.3957 T12: 0.0181
REMARK 3 T13: 0.1207 T23: -0.0959
REMARK 3 L TENSOR
REMARK 3 L11: 0.0244 L22: 0.0140
REMARK 3 L33: 0.0798 L12: -0.0257
REMARK 3 L13: -0.0501 L23: 0.0235
REMARK 3 S TENSOR
REMARK 3 S11: -0.1266 S12: 0.0308 S13: -0.1833
REMARK 3 S21: -0.0305 S22: 0.0233 S23: -0.0180
REMARK 3 S31: 0.2125 S32: 0.0955 S33: -0.0650
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 350:618)
REMARK 3 ORIGIN FOR THE GROUP (A): 58.8604 12.4611 -45.6647
REMARK 3 T TENSOR
REMARK 3 T11: -0.0246 T22: 0.0980
REMARK 3 T33: -0.4382 T12: -0.1030
REMARK 3 T13: 0.0003 T23: -0.3364
REMARK 3 L TENSOR
REMARK 3 L11: 0.0397 L22: 0.0686
REMARK 3 L33: 0.0231 L12: -0.0027
REMARK 3 L13: 0.0035 L23: -0.0129
REMARK 3 S TENSOR
REMARK 3 S11: -0.0737 S12: 0.2249 S13: -0.0493
REMARK 3 S21: -0.2498 S22: -0.0487 S23: -0.0197
REMARK 3 S31: 0.0318 S32: 0.0297 S33: -0.1609
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'B' and (resseq 4:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7687 -21.0762 -21.0321
REMARK 3 T TENSOR
REMARK 3 T11: 0.4629 T22: 0.3373
REMARK 3 T33: 0.4808 T12: -0.1766
REMARK 3 T13: 0.0928 T23: -0.1336
REMARK 3 L TENSOR
REMARK 3 L11: 0.0199 L22: 0.0084
REMARK 3 L33: 0.0283 L12: 0.0094
REMARK 3 L13: -0.0059 L23: 0.0050
REMARK 3 S TENSOR
REMARK 3 S11: -0.0896 S12: 0.0814 S13: -0.1279
REMARK 3 S21: -0.0344 S22: -0.0096 S23: 0.0024
REMARK 3 S31: 0.1710 S32: -0.1386 S33: -0.1033
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'B' and (resseq 350:618)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7328 -18.0746 2.8106
REMARK 3 T TENSOR
REMARK 3 T11: 0.3938 T22: 0.3849
REMARK 3 T33: 0.4299 T12: -0.2062
REMARK 3 T13: 0.1230 T23: -0.0808
REMARK 3 L TENSOR
REMARK 3 L11: 0.0484 L22: 0.0203
REMARK 3 L33: 0.0445 L12: 0.0236
REMARK 3 L13: -0.0308 L23: 0.0037
REMARK 3 S TENSOR
REMARK 3 S11: -0.0872 S12: 0.0272 S13: -0.1435
REMARK 3 S21: 0.0331 S22: -0.0484 S23: 0.0763
REMARK 3 S31: 0.1830 S32: -0.1756 S33: -0.1442
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'C' and (resseq 4:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 55.4937 -37.1936 7.9718
REMARK 3 T TENSOR
REMARK 3 T11: 0.5959 T22: 0.1929
REMARK 3 T33: 0.5623 T12: 0.1267
REMARK 3 T13: 0.1892 T23: 0.0867
REMARK 3 L TENSOR
REMARK 3 L11: 0.0052 L22: 0.0141
REMARK 3 L33: 0.0186 L12: -0.0065
REMARK 3 L13: -0.0018 L23: 0.0107
REMARK 3 S TENSOR
REMARK 3 S11: -0.0267 S12: -0.0330 S13: -0.1810
REMARK 3 S21: -0.0346 S22: -0.0236 S23: 0.0004
REMARK 3 S31: 0.2683 S32: 0.0629 S33: 0.0076
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'C' and (resseq 350:618)
REMARK 3 ORIGIN FOR THE GROUP (A): 80.3449 -26.5040 21.0682
REMARK 3 T TENSOR
REMARK 3 T11: 0.5331 T22: 0.5680
REMARK 3 T33: 0.6333 T12: 0.3436
REMARK 3 T13: 0.1251 T23: 0.2130
REMARK 3 L TENSOR
REMARK 3 L11: 0.0259 L22: 0.0132
REMARK 3 L33: 0.0315 L12: -0.0170
REMARK 3 L13: 0.0318 L23: -0.0139
REMARK 3 S TENSOR
REMARK 3 S11: -0.0306 S12: -0.0715 S13: -0.1033
REMARK 3 S21: 0.0479 S22: -0.0210 S23: -0.1727
REMARK 3 S31: 0.2120 S32: 0.1131 S33: -0.0124
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'D' and (resseq 4:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.6612 39.6913 -7.2414
REMARK 3 T TENSOR
REMARK 3 T11: 0.0974 T22: 0.1655
REMARK 3 T33: 0.1511 T12: -0.0271
REMARK 3 T13: -0.0040 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.0334 L22: 0.0059
REMARK 3 L33: 0.0161 L12: -0.0127
REMARK 3 L13: -0.0188 L23: -0.0108
REMARK 3 S TENSOR
REMARK 3 S11: -0.0083 S12: 0.0053 S13: 0.0060
REMARK 3 S21: 0.0076 S22: -0.0225 S23: 0.0305
REMARK 3 S31: -0.0351 S32: 0.0176 S33: -0.0366
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'D' and (resseq 350:618)
REMARK 3 ORIGIN FOR THE GROUP (A): 83.0272 28.7535 -16.9945
REMARK 3 T TENSOR
REMARK 3 T11: 0.1586 T22: 0.3189
REMARK 3 T33: 0.2710 T12: -0.0646
REMARK 3 T13: 0.0070 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.0175 L22: 0.0263
REMARK 3 L33: 0.0148 L12: 0.0173
REMARK 3 L13: -0.0208 L23: -0.0059
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: 0.0061 S13: -0.0172
REMARK 3 S21: -0.0397 S22: 0.0009 S23: -0.0952
REMARK 3 S31: -0.0338 S32: 0.1155 S33: 0.0008
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'E' and (resseq 4:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8718 24.0266 17.6477
REMARK 3 T TENSOR
REMARK 3 T11: 0.1797 T22: 0.3073
REMARK 3 T33: 0.2832 T12: 0.0550
REMARK 3 T13: 0.0032 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.0120 L22: 0.0073
REMARK 3 L33: 0.0649 L12: -0.0025
REMARK 3 L13: -0.0168 L23: 0.0068
REMARK 3 S TENSOR
REMARK 3 S11: -0.0277 S12: -0.1175 S13: 0.0079
REMARK 3 S21: 0.0408 S22: 0.0382 S23: -0.0145
REMARK 3 S31: 0.0308 S32: -0.0670 S33: 0.0074
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'E' and (resseq 350:618)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7306 21.1601 -8.3810
REMARK 3 T TENSOR
REMARK 3 T11: 0.1372 T22: 0.3875
REMARK 3 T33: 0.2765 T12: 0.0269
REMARK 3 T13: -0.0310 T23: -0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 0.0620 L22: 0.0064
REMARK 3 L33: 0.0254 L12: -0.0059
REMARK 3 L13: 0.0116 L23: 0.0212
REMARK 3 S TENSOR
REMARK 3 S11: -0.0395 S12: -0.0018 S13: 0.0345
REMARK 3 S21: -0.0247 S22: -0.0023 S23: 0.0949
REMARK 3 S31: -0.0151 S32: -0.2439 S33: -0.0870
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain 'F' and (resseq 4:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 63.2226 15.7244 33.8560
REMARK 3 T TENSOR
REMARK 3 T11: 0.1483 T22: 0.3807
REMARK 3 T33: 0.2157 T12: 0.0084
REMARK 3 T13: -0.0284 T23: 0.0731
REMARK 3 L TENSOR
REMARK 3 L11: 0.0241 L22: 0.0148
REMARK 3 L33: 0.0437 L12: 0.0335
REMARK 3 L13: -0.0178 L23: -0.0222
REMARK 3 S TENSOR
REMARK 3 S11: -0.0241 S12: -0.1563 S13: -0.0338
REMARK 3 S21: 0.0290 S22: -0.0740 S23: -0.0537
REMARK 3 S31: 0.0077 S32: 0.1777 S33: -0.0845
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain 'F' and (resseq 350:618)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.1793 -9.6912 46.5829
REMARK 3 T TENSOR
REMARK 3 T11: 0.2039 T22: 0.2767
REMARK 3 T33: 0.0904 T12: 0.1569
REMARK 3 T13: -0.0316 T23: 0.3153
REMARK 3 L TENSOR
REMARK 3 L11: 0.0214 L22: 0.0641
REMARK 3 L33: 0.0475 L12: 0.0122
REMARK 3 L13: 0.0183 L23: 0.0359
REMARK 3 S TENSOR
REMARK 3 S11: -0.0619 S12: -0.2157 S13: 0.0085
REMARK 3 S21: 0.1750 S22: -0.1865 S23: 0.0080
REMARK 3 S31: 0.1040 S32: 0.0199 S33: -0.0915
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain 'G' and (resseq 4:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 121.7459 -17.2731 34.3139
REMARK 3 T TENSOR
REMARK 3 T11: 0.6432 T22: 0.3143
REMARK 3 T33: 0.2216 T12: 0.0436
REMARK 3 T13: 0.0616 T23: -0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.0402 L22: 0.0647
REMARK 3 L33: 0.1353 L12: 0.0220
REMARK 3 L13: -0.0444 L23: 0.0036
REMARK 3 S TENSOR
REMARK 3 S11: -0.0625 S12: 0.0120 S13: -0.0574
REMARK 3 S21: -0.0706 S22: -0.0686 S23: 0.0154
REMARK 3 S31: 0.1276 S32: 0.0743 S33: -0.1314
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain 'G' and (resseq 350:618)
REMARK 3 ORIGIN FOR THE GROUP (A): 147.0101 -7.2071 21.6940
REMARK 3 T TENSOR
REMARK 3 T11: 0.5833 T22: 0.6505
REMARK 3 T33: 0.2914 T12: 0.0893
REMARK 3 T13: 0.1059 T23: 0.0743
REMARK 3 L TENSOR
REMARK 3 L11: 0.0981 L22: 0.0531
REMARK 3 L33: 0.1189 L12: 0.0184
REMARK 3 L13: 0.0336 L23: -0.0259
REMARK 3 S TENSOR
REMARK 3 S11: -0.0609 S12: 0.0818 S13: -0.0187
REMARK 3 S21: -0.1472 S22: -0.0739 S23: -0.0571
REMARK 3 S31: -0.0844 S32: 0.1384 S33: -0.0246
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: chain 'H' and (resseq 4:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 113.3939 26.7585 51.5068
REMARK 3 T TENSOR
REMARK 3 T11: 0.8306 T22: 0.2466
REMARK 3 T33: 0.2747 T12: -0.0074
REMARK 3 T13: 0.0075 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: -0.0040 L22: 0.0509
REMARK 3 L33: 0.0699 L12: -0.0141
REMARK 3 L13: 0.0089 L23: -0.0599
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: 0.0429 S13: 0.0373
REMARK 3 S21: 0.0881 S22: -0.0115 S23: 0.0023
REMARK 3 S31: -0.1832 S32: 0.0631 S33: 0.0246
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: chain 'H' and (resseq 350:618)
REMARK 3 ORIGIN FOR THE GROUP (A): 116.5471 41.3520 77.4116
REMARK 3 T TENSOR
REMARK 3 T11: 1.2329 T22: 0.1353
REMARK 3 T33: 0.2581 T12: -0.0981
REMARK 3 T13: -0.0722 T23: -0.0644
REMARK 3 L TENSOR
REMARK 3 L11: 0.0028 L22: 0.0424
REMARK 3 L33: 0.0271 L12: 0.0031
REMARK 3 L13: 0.0162 L23: 0.0142
REMARK 3 S TENSOR
REMARK 3 S11: 0.0138 S12: -0.0612 S13: 0.0557
REMARK 3 S21: 0.1493 S22: -0.0152 S23: 0.0106
REMARK 3 S31: -0.1953 S32: 0.0143 S33: 0.0176
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: chain 'I' and (resseq 4:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 97.9796 -11.5128 75.6908
REMARK 3 T TENSOR
REMARK 3 T11: 0.6758 T22: 0.3327
REMARK 3 T33: 0.3321 T12: -0.0136
REMARK 3 T13: 0.0457 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.0136 L22: 0.0397
REMARK 3 L33: 0.0211 L12: 0.0126
REMARK 3 L13: -0.0045 L23: 0.0009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0173 S12: -0.0346 S13: 0.0012
REMARK 3 S21: 0.1165 S22: -0.0302 S23: 0.0578
REMARK 3 S31: 0.0123 S32: -0.0357 S33: -0.0047
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: chain 'I' and (resseq 350:618)
REMARK 3 ORIGIN FOR THE GROUP (A): 109.0762 -37.8099 85.3511
REMARK 3 T TENSOR
REMARK 3 T11: 0.8299 T22: 0.2111
REMARK 3 T33: 0.2544 T12: -0.0289
REMARK 3 T13: 0.0455 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.0136 L22: 0.0367
REMARK 3 L33: 0.0229 L12: 0.0023
REMARK 3 L13: 0.0005 L23: -0.0277
REMARK 3 S TENSOR
REMARK 3 S11: 0.0207 S12: -0.0541 S13: -0.0451
REMARK 3 S21: 0.1105 S22: -0.0079 S23: 0.0503
REMARK 3 S31: 0.1404 S32: -0.0270 S33: 0.0145
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: chain 'J' and (resseq 4:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 174.2594 -10.1292 60.2677
REMARK 3 T TENSOR
REMARK 3 T11: 0.3435 T22: 0.9940
REMARK 3 T33: 0.4073 T12: 0.0548
REMARK 3 T13: -0.0596 T23: 0.2858
REMARK 3 L TENSOR
REMARK 3 L11: 0.0402 L22: 0.0422
REMARK 3 L33: 0.1113 L12: -0.0115
REMARK 3 L13: 0.0595 L23: -0.0063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0109 S12: 0.0831 S13: 0.0345
REMARK 3 S21: -0.0003 S22: 0.0047 S23: -0.1548
REMARK 3 S31: 0.0062 S32: 0.2011 S33: 0.0800
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: chain 'J' and (resseq 350:618)
REMARK 3 ORIGIN FOR THE GROUP (A): 163.7937 -34.5056 46.5798
REMARK 3 T TENSOR
REMARK 3 T11: 0.7422 T22: 0.7967
REMARK 3 T33: 0.4944 T12: 0.3929
REMARK 3 T13: 0.1153 T23: 0.1520
REMARK 3 L TENSOR
REMARK 3 L11: 0.0263 L22: 0.0340
REMARK 3 L33: 0.0331 L12: 0.0007
REMARK 3 L13: 0.0069 L23: 0.0365
REMARK 3 S TENSOR
REMARK 3 S11: 0.0570 S12: 0.0847 S13: -0.0519
REMARK 3 S21: -0.0113 S22: -0.0023 S23: -0.0937
REMARK 3 S31: 0.0820 S32: 0.1405 S33: 0.0147
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: chain 'K' and (resseq 4:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 158.2336 24.1616 89.6227
REMARK 3 T TENSOR
REMARK 3 T11: 0.9141 T22: 0.7168
REMARK 3 T33: 0.4966 T12: -0.4558
REMARK 3 T13: -0.3692 T23: 0.1825
REMARK 3 L TENSOR
REMARK 3 L11: 0.0428 L22: 0.0037
REMARK 3 L33: 0.0118 L12: 0.0178
REMARK 3 L13: 0.0241 L23: 0.0107
REMARK 3 S TENSOR
REMARK 3 S11: -0.0311 S12: -0.0106 S13: 0.0014
REMARK 3 S21: 0.0726 S22: -0.0533 S23: -0.1225
REMARK 3 S31: -0.1841 S32: 0.1266 S33: -0.0296
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: chain 'K' and (resseq 350:618)
REMARK 3 ORIGIN FOR THE GROUP (A): 155.4129 42.3302 66.0871
REMARK 3 T TENSOR
REMARK 3 T11: 1.0008 T22: 0.5098
REMARK 3 T33: 0.5600 T12: -0.5836
REMARK 3 T13: -0.2775 T23: 0.2197
REMARK 3 L TENSOR
REMARK 3 L11: 0.0051 L22: 0.0315
REMARK 3 L33: 0.0103 L12: 0.0150
REMARK 3 L13: 0.0059 L23: -0.0065
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: 0.0226 S13: 0.0777
REMARK 3 S21: 0.0585 S22: -0.0369 S23: -0.0969
REMARK 3 S31: -0.1111 S32: 0.0874 S33: 0.0093
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: chain 'L' and (resseq 4:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 151.0265 -21.8975 100.2318
REMARK 3 T TENSOR
REMARK 3 T11: 0.7506 T22: 0.8132
REMARK 3 T33: 0.4787 T12: 0.0469
REMARK 3 T13: -0.1362 T23: 0.2037
REMARK 3 L TENSOR
REMARK 3 L11: 0.0382 L22: 0.0061
REMARK 3 L33: 0.0212 L12: -0.0101
REMARK 3 L13: -0.0086 L23: -0.0025
REMARK 3 S TENSOR
REMARK 3 S11: -0.0461 S12: -0.0004 S13: -0.0123
REMARK 3 S21: -0.0147 S22: -0.0690 S23: -0.0565
REMARK 3 S31: 0.1291 S32: 0.2016 S33: -0.0782
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: chain 'L' and (resseq 350:618)
REMARK 3 ORIGIN FOR THE GROUP (A): 125.4053 -14.0332 114.0552
REMARK 3 T TENSOR
REMARK 3 T11: 0.6442 T22: 0.4204
REMARK 3 T33: 0.0768 T12: -0.0623
REMARK 3 T13: -0.0736 T23: 0.0387
REMARK 3 L TENSOR
REMARK 3 L11: 0.1565 L22: 0.0604
REMARK 3 L33: 0.0171 L12: 0.0421
REMARK 3 L13: -0.0264 L23: -0.0080
REMARK 3 S TENSOR
REMARK 3 S11: -0.0741 S12: -0.2502 S13: -0.0121
REMARK 3 S21: 0.1200 S22: -0.0743 S23: -0.0730
REMARK 3 S31: 0.0874 S32: 0.1116 S33: 0.0145
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RAMACHANDRAN RESTRAINTS WERE APPLIED
REMARK 4
REMARK 4 4HXG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-12.
REMARK 100 THE RCSB ID CODE IS RCSB076041.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0715
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 255208
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 200 DATA REDUNDANCY : 4.390
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.4700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.33
REMARK 200 R MERGE FOR SHELL (I) : 0.69000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.360
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4HXF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 91.65500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 137.87000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 91.90000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 137.87000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 91.65500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 91.90000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 34060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 121200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -152.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, C, F, B, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 27630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 122010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -162.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, J, H, K, I, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 MET A 1
REMARK 465 THR A 2
REMARK 465 SER A 3
REMARK 465 GLY A 53
REMARK 465 GLU A 80
REMARK 465 GLU A 81
REMARK 465 LYS A 82
REMARK 465 LYS A 83
REMARK 465 GLU A 374
REMARK 465 GLY A 375
REMARK 465 GLU A 619
REMARK 465 GLU A 620
REMARK 465 LYS A 621
REMARK 465 LYS A 622
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 SER B 3
REMARK 465 GLU B 80
REMARK 465 GLU B 81
REMARK 465 LYS B 82
REMARK 465 GLU B 619
REMARK 465 GLU B 620
REMARK 465 LYS B 621
REMARK 465 LYS B 622
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 SER C 3
REMARK 465 GLU C 80
REMARK 465 GLU C 81
REMARK 465 LYS C 82
REMARK 465 GLU C 619
REMARK 465 GLU C 620
REMARK 465 LYS C 621
REMARK 465 LYS C 622
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 SER D 3
REMARK 465 GLU D 80
REMARK 465 GLU D 81
REMARK 465 LYS D 82
REMARK 465 GLU D 619
REMARK 465 GLU D 620
REMARK 465 LYS D 621
REMARK 465 LYS D 622
REMARK 465 MET E 1
REMARK 465 THR E 2
REMARK 465 GLU E 80
REMARK 465 GLU E 81
REMARK 465 LYS E 82
REMARK 465 GLU E 619
REMARK 465 GLU E 620
REMARK 465 LYS E 621
REMARK 465 LYS E 622
REMARK 465 MET F 1
REMARK 465 THR F 2
REMARK 465 SER F 3
REMARK 465 GLU F 80
REMARK 465 GLU F 619
REMARK 465 GLU F 620
REMARK 465 LYS F 621
REMARK 465 LYS F 622
REMARK 465 MET G 1
REMARK 465 THR G 2
REMARK 465 SER G 3
REMARK 465 GLU G 80
REMARK 465 GLU G 81
REMARK 465 LYS G 82
REMARK 465 LYS G 83
REMARK 465 LYS G 373
REMARK 465 GLU G 374
REMARK 465 GLY G 375
REMARK 465 GLU G 619
REMARK 465 GLU G 620
REMARK 465 LYS G 621
REMARK 465 LYS G 622
REMARK 465 MET H 1
REMARK 465 THR H 2
REMARK 465 SER H 3
REMARK 465 GLU H 80
REMARK 465 GLU H 81
REMARK 465 LYS H 82
REMARK 465 LYS H 83
REMARK 465 GLU H 374
REMARK 465 GLY H 375
REMARK 465 GLU H 619
REMARK 465 GLU H 620
REMARK 465 LYS H 621
REMARK 465 LYS H 622
REMARK 465 MET I 1
REMARK 465 THR I 2
REMARK 465 SER I 3
REMARK 465 GLU I 80
REMARK 465 GLU I 81
REMARK 465 LYS I 82
REMARK 465 LYS I 83
REMARK 465 GLU I 619
REMARK 465 GLU I 620
REMARK 465 LYS I 621
REMARK 465 LYS I 622
REMARK 465 MET J 1
REMARK 465 THR J 2
REMARK 465 SER J 3
REMARK 465 GLU J 51
REMARK 465 GLU J 80
REMARK 465 GLU J 81
REMARK 465 LYS J 82
REMARK 465 LYS J 83
REMARK 465 VAL J 240
REMARK 465 GLU J 619
REMARK 465 GLU J 620
REMARK 465 LYS J 621
REMARK 465 LYS J 622
REMARK 465 MET K 1
REMARK 465 THR K 2
REMARK 465 SER K 3
REMARK 465 GLU K 80
REMARK 465 GLU K 81
REMARK 465 LYS K 82
REMARK 465 LYS K 83
REMARK 465 GLU K 374
REMARK 465 GLU K 619
REMARK 465 GLU K 620
REMARK 465 LYS K 621
REMARK 465 LYS K 622
REMARK 465 MET L 1
REMARK 465 THR L 2
REMARK 465 SER L 3
REMARK 465 GLU L 80
REMARK 465 GLU L 81
REMARK 465 LYS L 82
REMARK 465 LYS L 83
REMARK 465 GLU L 619
REMARK 465 GLU L 620
REMARK 465 LYS L 621
REMARK 465 LYS L 622
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 ILE A 4 CD1
REMARK 470 GLU A 5 CG CD OE1 OE2
REMARK 470 LYS A 13 CE NZ
REMARK 470 ARG A 23 CZ NH1 NH2
REMARK 470 ASN A 25 CG OD1 ND2
REMARK 470 LYS A 40 CE NZ
REMARK 470 GLU A 51 CG CD OE1 OE2
REMARK 470 ASP A 52 CG OD1 OD2
REMARK 470 ASP A 60 CG OD1 OD2
REMARK 470 LYS A 71 CG CD CE NZ
REMARK 470 ASN A 79 CG OD1 ND2
REMARK 470 LYS A 93 CG CD CE NZ
REMARK 470 LYS A 99 CE NZ
REMARK 470 LYS A 104 CG CD CE NZ
REMARK 470 GLN A 113 CG CD OE1 NE2
REMARK 470 LYS A 124 CG CD CE NZ
REMARK 470 GLU A 129 CG CD OE1 OE2
REMARK 470 LYS A 206 NZ
REMARK 470 GLU A 211 CG CD OE1 OE2
REMARK 470 LYS A 245 NZ
REMARK 470 GLU A 252 CG CD OE1 OE2
REMARK 470 LYS A 254 CG CD CE NZ
REMARK 470 LEU A 257 CG CD1 CD2
REMARK 470 ASP A 258 CG OD1 OD2
REMARK 470 ARG A 270 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 271 CG OD1 ND2
REMARK 470 LYS A 273 CE NZ
REMARK 470 GLU A 292 CG CD OE1 OE2
REMARK 470 LYS A 300 NZ
REMARK 470 ASP A 329 CG OD1 OD2
REMARK 470 GLU A 331 CG CD OE1 OE2
REMARK 470 ARG A 333 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 342 CD1
REMARK 470 LYS A 344 CD CE NZ
REMARK 470 LYS A 345 CG CD CE NZ
REMARK 470 LYS A 347 CD CE NZ
REMARK 470 LYS A 357 CD CE NZ
REMARK 470 GLU A 371 CG CD OE1 OE2
REMARK 470 LYS A 373 CG CD CE NZ
REMARK 470 LYS A 377 CE NZ
REMARK 470 ASP A 480 CG OD1 OD2
REMARK 470 LYS A 524 CG CD CE NZ
REMARK 470 LYS A 532 CG CD CE NZ
REMARK 470 LYS A 535 CE NZ
REMARK 470 LYS A 575 CE NZ
REMARK 470 LYS A 606 CG CD CE NZ
REMARK 470 GLU A 614 CG CD OE1 OE2
REMARK 470 LYS A 615 CD CE NZ
REMARK 470 LYS A 618 CG CD CE NZ
REMARK 470 ILE B 4 CD1
REMARK 470 GLU B 5 CG CD OE1 OE2
REMARK 470 LYS B 13 CE NZ
REMARK 470 ARG B 23 CZ NH1 NH2
REMARK 470 LYS B 24 CG CD CE NZ
REMARK 470 ASN B 25 CG OD1 ND2
REMARK 470 LYS B 40 CE NZ
REMARK 470 GLU B 51 CB CG CD OE1 OE2
REMARK 470 LYS B 56 CE NZ
REMARK 470 LYS B 71 CG CD CE NZ
REMARK 470 ASN B 79 CG OD1 ND2
REMARK 470 LYS B 83 CG CD CE NZ
REMARK 470 LYS B 93 CG CD CE NZ
REMARK 470 LYS B 99 CD CE NZ
REMARK 470 GLU B 102 CG CD OE1 OE2
REMARK 470 LYS B 104 CG CD CE NZ
REMARK 470 GLN B 113 CG CD OE1 NE2
REMARK 470 LYS B 124 CD CE NZ
REMARK 470 GLU B 211 CG CD OE1 OE2
REMARK 470 LYS B 212 NZ
REMARK 470 LYS B 238 CG CD CE NZ
REMARK 470 LYS B 245 CD CE NZ
REMARK 470 GLU B 252 CG CD OE1 OE2
REMARK 470 LYS B 254 CG CD CE NZ
REMARK 470 ASP B 259 CG OD1 OD2
REMARK 470 ASN B 271 CG OD1 ND2
REMARK 470 LYS B 273 CG CD CE NZ
REMARK 470 GLU B 292 CG CD OE1 OE2
REMARK 470 LYS B 298 NZ
REMARK 470 GLU B 331 CG CD OE1 OE2
REMARK 470 ARG B 333 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 342 CD1
REMARK 470 LYS B 344 CE NZ
REMARK 470 LYS B 345 CD CE NZ
REMARK 470 ARG B 352 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 357 CG CD CE NZ
REMARK 470 GLU B 371 CG CD OE1 OE2
REMARK 470 ILE B 372 CG1 CG2 CD1
REMARK 470 LYS B 373 CG CD CE NZ
REMARK 470 GLU B 374 CG CD OE1 OE2
REMARK 470 GLU B 376 CG CD OE1 OE2
REMARK 470 GLU B 446 CG CD OE1 OE2
REMARK 470 GLU B 458 CG CD OE1 OE2
REMARK 470 GLU B 518 CG CD OE1 OE2
REMARK 470 ARG B 523 NE CZ NH1 NH2
REMARK 470 LYS B 524 CG CD CE NZ
REMARK 470 LYS B 532 CG CD CE NZ
REMARK 470 LYS B 535 CD CE NZ
REMARK 470 LYS B 575 CE NZ
REMARK 470 LYS B 606 CG CD CE NZ
REMARK 470 GLU B 609 CG CD OE1 OE2
REMARK 470 GLU B 614 CG CD OE1 OE2
REMARK 470 LYS B 615 CG CD CE NZ
REMARK 470 LEU B 617 CG CD1 CD2
REMARK 470 LYS B 618 CG CD CE NZ
REMARK 470 ILE C 4 CG1 CG2 CD1
REMARK 470 GLU C 5 CG CD OE1 OE2
REMARK 470 LYS C 13 CE NZ
REMARK 470 ARG C 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 24 CG CD CE NZ
REMARK 470 LYS C 40 CE NZ
REMARK 470 LEU C 50 CG CD1 CD2
REMARK 470 GLU C 51 CG CD OE1 OE2
REMARK 470 ASP C 52 CG OD1 OD2
REMARK 470 LYS C 71 CD CE NZ
REMARK 470 LYS C 83 CD CE NZ
REMARK 470 THR C 84 OG1 CG2
REMARK 470 LYS C 93 CG CD CE NZ
REMARK 470 LYS C 99 CE NZ
REMARK 470 GLU C 102 CG CD OE1 OE2
REMARK 470 LYS C 104 CG CD CE NZ
REMARK 470 GLN C 113 CG CD OE1 NE2
REMARK 470 LYS C 124 CD CE NZ
REMARK 470 GLU C 127 CD OE1 OE2
REMARK 470 LYS C 151 CG CD CE NZ
REMARK 470 GLU C 211 CD OE1 OE2
REMARK 470 LYS C 212 NZ
REMARK 470 LYS C 238 CG CD CE NZ
REMARK 470 LYS C 245 CE NZ
REMARK 470 GLU C 252 CG CD OE1 OE2
REMARK 470 LYS C 254 CG CD CE NZ
REMARK 470 ASP C 258 CG OD1 OD2
REMARK 470 ILE C 269 CG1 CG2 CD1
REMARK 470 ARG C 270 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 271 CG OD1 ND2
REMARK 470 LYS C 273 CG CD CE NZ
REMARK 470 GLU C 292 CG CD OE1 OE2
REMARK 470 LYS C 298 NZ
REMARK 470 GLU C 331 CG CD OE1 OE2
REMARK 470 ARG C 333 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 342 CD1
REMARK 470 LYS C 344 CE NZ
REMARK 470 LYS C 345 CG CD CE NZ
REMARK 470 LYS C 347 CG CD CE NZ
REMARK 470 ARG C 352 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 357 CG CD CE NZ
REMARK 470 SER C 358 OG
REMARK 470 ASP C 360 CG OD1 OD2
REMARK 470 LEU C 361 CG CD1 CD2
REMARK 470 GLU C 371 CG CD OE1 OE2
REMARK 470 LYS C 373 CG CD CE NZ
REMARK 470 GLU C 374 CG CD OE1 OE2
REMARK 470 GLU C 376 CG CD OE1 OE2
REMARK 470 LYS C 377 CD CE NZ
REMARK 470 GLU C 446 CD OE1 OE2
REMARK 470 ARG C 457 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 458 CG CD OE1 OE2
REMARK 470 ASP C 480 CG OD1 OD2
REMARK 470 LYS C 483 CG CD CE NZ
REMARK 470 LYS C 524 CG CD CE NZ
REMARK 470 LYS C 532 CG CD CE NZ
REMARK 470 LYS C 535 CG CD CE NZ
REMARK 470 LYS C 575 CE NZ
REMARK 470 ILE C 582 CD1
REMARK 470 ARG C 583 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 594 CD CE NZ
REMARK 470 LYS C 606 CG CD CE NZ
REMARK 470 GLU C 614 CG CD OE1 OE2
REMARK 470 LYS C 615 CG CD CE NZ
REMARK 470 LEU C 617 CG CD1 CD2
REMARK 470 LYS C 618 CG CD CE NZ
REMARK 470 ILE D 4 N CG1 CG2 CD1
REMARK 470 GLU D 5 CG CD OE1 OE2
REMARK 470 LYS D 13 CE NZ
REMARK 470 ARG D 23 CZ NH1 NH2
REMARK 470 ASN D 25 CG OD1 ND2
REMARK 470 LYS D 40 CE NZ
REMARK 470 GLU D 51 CG CD OE1 OE2
REMARK 470 ASP D 60 CG OD1 OD2
REMARK 470 LYS D 71 CD CE NZ
REMARK 470 LYS D 72 CE NZ
REMARK 470 LYS D 83 CG CD CE NZ
REMARK 470 LYS D 93 CG CD CE NZ
REMARK 470 LYS D 104 CD CE NZ
REMARK 470 LYS D 124 CE NZ
REMARK 470 LYS D 151 CE NZ
REMARK 470 LYS D 245 CE NZ
REMARK 470 GLU D 252 CG CD OE1 OE2
REMARK 470 LYS D 254 CG CD CE NZ
REMARK 470 ARG D 270 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 271 CG OD1 ND2
REMARK 470 LYS D 273 CE NZ
REMARK 470 GLU D 292 CG CD OE1 OE2
REMARK 470 ARG D 311 CD NE CZ NH1 NH2
REMARK 470 GLU D 331 CG CD OE1 OE2
REMARK 470 ILE D 342 CD1
REMARK 470 LYS D 344 CE NZ
REMARK 470 LYS D 345 CE NZ
REMARK 470 GLU D 371 CG CD OE1 OE2
REMARK 470 LYS D 373 CG CD CE NZ
REMARK 470 GLU D 376 CG CD OE1 OE2
REMARK 470 GLU D 458 CG CD OE1 OE2
REMARK 470 ASP D 480 CG OD1 OD2
REMARK 470 GLU D 518 CG CD OE1 OE2
REMARK 470 GLU D 520 CD OE1 OE2
REMARK 470 LYS D 524 CE NZ
REMARK 470 LYS D 532 CG CD CE NZ
REMARK 470 LYS D 535 CG CD CE NZ
REMARK 470 LYS D 575 CE NZ
REMARK 470 LYS D 606 CG CD CE NZ
REMARK 470 GLU D 614 CG CD OE1 OE2
REMARK 470 LYS D 615 CD CE NZ
REMARK 470 LYS D 618 CG CD CE NZ
REMARK 470 ILE E 4 CD1
REMARK 470 GLU E 5 CG CD OE1 OE2
REMARK 470 LYS E 13 CE NZ
REMARK 470 LYS E 40 CE NZ
REMARK 470 GLU E 51 CG CD OE1 OE2
REMARK 470 ASP E 52 CG OD1 OD2
REMARK 470 LYS E 71 CD CE NZ
REMARK 470 ASN E 79 CG OD1 ND2
REMARK 470 LYS E 83 CG CD CE NZ
REMARK 470 THR E 84 OG1 CG2
REMARK 470 LYS E 93 CD CE NZ
REMARK 470 LYS E 99 CE NZ
REMARK 470 LYS E 104 CG CD CE NZ
REMARK 470 LYS E 124 CD CE NZ
REMARK 470 LYS E 151 CE NZ
REMARK 470 GLU E 211 CD OE1 OE2
REMARK 470 LYS E 238 CE NZ
REMARK 470 LYS E 254 CG CD CE NZ
REMARK 470 LYS E 273 CD CE NZ
REMARK 470 LYS E 300 CE NZ
REMARK 470 GLU E 331 CD OE1 OE2
REMARK 470 ARG E 333 CG CD NE CZ NH1 NH2
REMARK 470 ILE E 342 CD1
REMARK 470 LYS E 344 CD CE NZ
REMARK 470 LYS E 345 CE NZ
REMARK 470 LYS E 347 CG CD CE NZ
REMARK 470 LYS E 357 CD CE NZ
REMARK 470 GLU E 371 CG CD OE1 OE2
REMARK 470 LYS E 373 CG CD CE NZ
REMARK 470 GLU E 374 CG CD OE1 OE2
REMARK 470 LYS E 377 NZ
REMARK 470 ASP E 480 CG OD1 OD2
REMARK 470 LYS E 532 CG CD CE NZ
REMARK 470 LYS E 535 CG CD CE NZ
REMARK 470 LYS E 575 CE NZ
REMARK 470 LYS E 606 CD CE NZ
REMARK 470 GLU E 614 CG CD OE1 OE2
REMARK 470 LYS E 615 CG CD CE NZ
REMARK 470 LYS E 618 CG CD CE NZ
REMARK 470 ILE F 4 CG1 CG2 CD1
REMARK 470 GLU F 5 CG CD OE1 OE2
REMARK 470 LYS F 13 CE NZ
REMARK 470 ARG F 23 CZ NH1 NH2
REMARK 470 ASN F 25 CG OD1 ND2
REMARK 470 LYS F 40 CE NZ
REMARK 470 GLU F 51 CG CD OE1 OE2
REMARK 470 ASP F 60 CG OD1 OD2
REMARK 470 LYS F 71 CD CE NZ
REMARK 470 GLU F 81 CG CD OE1 OE2
REMARK 470 LYS F 82 CG CD CE NZ
REMARK 470 LYS F 83 CG CD CE NZ
REMARK 470 LYS F 93 CE NZ
REMARK 470 LYS F 99 CE NZ
REMARK 470 LYS F 104 CG CD CE NZ
REMARK 470 GLN F 113 CG CD OE1 NE2
REMARK 470 LYS F 124 CG CD CE NZ
REMARK 470 GLU F 129 CG CD OE1 OE2
REMARK 470 LYS F 151 CE NZ
REMARK 470 LYS F 238 CG CD CE NZ
REMARK 470 LYS F 254 CG CD CE NZ
REMARK 470 ARG F 270 CG CD NE CZ NH1 NH2
REMARK 470 ASN F 271 CG OD1 ND2
REMARK 470 LYS F 273 CD CE NZ
REMARK 470 GLU F 331 CD OE1 OE2
REMARK 470 ARG F 333 CG CD NE CZ NH1 NH2
REMARK 470 ILE F 342 CD1
REMARK 470 LYS F 344 CD CE NZ
REMARK 470 LYS F 347 CE NZ
REMARK 470 LYS F 357 CG CD CE NZ
REMARK 470 GLU F 371 CD OE1 OE2
REMARK 470 GLU F 374 CG CD OE1 OE2
REMARK 470 ASP F 480 CG OD1 OD2
REMARK 470 ASP F 514 CG OD1 OD2
REMARK 470 GLU F 518 CG CD OE1 OE2
REMARK 470 GLU F 520 CG CD OE1 OE2
REMARK 470 LYS F 532 CG CD CE NZ
REMARK 470 LYS F 535 CG CD CE NZ
REMARK 470 LYS F 575 CE NZ
REMARK 470 LYS F 606 CG CD CE NZ
REMARK 470 VAL F 613 CG1 CG2
REMARK 470 GLU F 614 CG CD OE1 OE2
REMARK 470 LYS F 615 CG CD CE NZ
REMARK 470 LEU F 617 CG CD1 CD2
REMARK 470 LYS F 618 CG CD CE NZ
REMARK 470 ILE G 4 CG1 CG2 CD1
REMARK 470 GLU G 5 CG CD OE1 OE2
REMARK 470 LYS G 13 CG CD CE NZ
REMARK 470 ARG G 23 CZ NH1 NH2
REMARK 470 ASN G 25 CG OD1 ND2
REMARK 470 GLU G 37 CG CD OE1 OE2
REMARK 470 LYS G 40 CD CE NZ
REMARK 470 ASN G 49 CG OD1 ND2
REMARK 470 GLU G 51 CG CD OE1 OE2
REMARK 470 ASP G 52 CG OD1 OD2
REMARK 470 LYS G 71 CE NZ
REMARK 470 ASN G 79 CG OD1 ND2
REMARK 470 THR G 84 OG1 CG2
REMARK 470 LYS G 93 CE NZ
REMARK 470 LYS G 99 CE NZ
REMARK 470 LEU G 101 CG CD1 CD2
REMARK 470 LYS G 104 CG CD CE NZ
REMARK 470 GLN G 113 CG CD OE1 NE2
REMARK 470 LYS G 124 CG CD CE NZ
REMARK 470 GLU G 129 CG CD OE1 OE2
REMARK 470 GLN G 167 CD OE1 NE2
REMARK 470 GLU G 211 CG CD OE1 OE2
REMARK 470 LYS G 238 CD CE NZ
REMARK 470 LYS G 245 CE NZ
REMARK 470 GLU G 252 CG CD OE1 OE2
REMARK 470 LYS G 254 CD CE NZ
REMARK 470 ARG G 270 CG CD NE CZ NH1 NH2
REMARK 470 ASN G 271 CG OD1 ND2
REMARK 470 LYS G 273 CD CE NZ
REMARK 470 GLU G 292 CG CD OE1 OE2
REMARK 470 LYS G 298 NZ
REMARK 470 LYS G 300 CD CE NZ
REMARK 470 GLU G 331 CD OE1 OE2
REMARK 470 ILE G 342 CD1
REMARK 470 LYS G 344 CD CE NZ
REMARK 470 LYS G 345 CG CD CE NZ
REMARK 470 ARG G 352 CG CD NE CZ NH1 NH2
REMARK 470 LYS G 357 CG CD CE NZ
REMARK 470 GLU G 371 CD OE1 OE2
REMARK 470 GLU G 376 CG CD OE1 OE2
REMARK 470 LYS G 397 NZ
REMARK 470 LYS G 406 CD CE NZ
REMARK 470 ASP G 480 CG OD1 OD2
REMARK 470 LYS G 483 CG CD CE NZ
REMARK 470 GLU G 518 CG CD OE1 OE2
REMARK 470 GLU G 520 CD OE1 OE2
REMARK 470 ARG G 523 CG CD NE CZ NH1 NH2
REMARK 470 LYS G 524 CG CD CE NZ
REMARK 470 LYS G 532 CG CD CE NZ
REMARK 470 LYS G 535 CG CD CE NZ
REMARK 470 LYS G 566 CD CE NZ
REMARK 470 LYS G 575 CD CE NZ
REMARK 470 ARG G 583 NE CZ NH1 NH2
REMARK 470 LYS G 606 CG CD CE NZ
REMARK 470 GLU G 609 CG CD OE1 OE2
REMARK 470 GLU G 614 CG CD OE1 OE2
REMARK 470 LYS G 615 CG CD CE NZ
REMARK 470 ILE G 616 CG1 CG2 CD1
REMARK 470 LEU G 617 CG CD1 CD2
REMARK 470 LYS G 618 CG CD CE NZ
REMARK 470 ILE H 4 CG1 CG2 CD1
REMARK 470 GLU H 5 CG CD OE1 OE2
REMARK 470 LYS H 9 CE NZ
REMARK 470 LYS H 13 CD CE NZ
REMARK 470 LYS H 40 CE NZ
REMARK 470 GLU H 51 CG CD OE1 OE2
REMARK 470 LYS H 71 CD CE NZ
REMARK 470 LYS H 93 CG CD CE NZ
REMARK 470 LYS H 99 CD CE NZ
REMARK 470 GLU H 102 CG CD OE1 OE2
REMARK 470 LYS H 104 CG CD CE NZ
REMARK 470 LYS H 124 CG CD CE NZ
REMARK 470 LYS H 151 CG CD CE NZ
REMARK 470 VAL H 192 CG1 CG2
REMARK 470 GLU H 209 CG CD OE1 OE2
REMARK 470 GLU H 211 CG CD OE1 OE2
REMARK 470 GLU H 236 CD OE1 OE2
REMARK 470 LYS H 238 CG CD CE NZ
REMARK 470 GLU H 252 CG CD OE1 OE2
REMARK 470 LYS H 254 CG CD CE NZ
REMARK 470 ARG H 270 CG CD NE CZ NH1 NH2
REMARK 470 ASN H 271 CG OD1 ND2
REMARK 470 LYS H 273 CE NZ
REMARK 470 LYS H 298 NZ
REMARK 470 LYS H 300 CG CD CE NZ
REMARK 470 GLU H 310 CG CD OE1 OE2
REMARK 470 GLU H 331 CG CD OE1 OE2
REMARK 470 ARG H 333 CG CD NE CZ NH1 NH2
REMARK 470 ILE H 342 CD1
REMARK 470 LYS H 344 CG CD CE NZ
REMARK 470 LYS H 345 CD CE NZ
REMARK 470 GLU H 350 CG CD OE1 OE2
REMARK 470 LYS H 357 CG CD CE NZ
REMARK 470 LEU H 361 CG CD1 CD2
REMARK 470 GLU H 371 CD OE1 OE2
REMARK 470 ILE H 372 CG1 CG2 CD1
REMARK 470 LYS H 373 CG CD CE NZ
REMARK 470 GLU H 376 CG CD OE1 OE2
REMARK 470 LYS H 377 CG CD CE NZ
REMARK 470 GLN H 439 CD OE1 NE2
REMARK 470 ASP H 440 CG OD1 OD2
REMARK 470 GLU H 446 CD OE1 OE2
REMARK 470 ARG H 457 CG CD NE CZ NH1 NH2
REMARK 470 ASP H 480 CG OD1 OD2
REMARK 470 LYS H 483 CG CD CE NZ
REMARK 470 SER H 487 OG
REMARK 470 ASP H 514 CG OD1 OD2
REMARK 470 GLU H 520 CG CD OE1 OE2
REMARK 470 ARG H 523 CD NE CZ NH1 NH2
REMARK 470 LYS H 524 CG CD CE NZ
REMARK 470 LYS H 532 CG CD CE NZ
REMARK 470 LYS H 535 CG CD CE NZ
REMARK 470 LYS H 566 CG CD CE NZ
REMARK 470 LYS H 575 CD CE NZ
REMARK 470 LYS H 606 CG CD CE NZ
REMARK 470 GLU H 609 CG CD OE1 OE2
REMARK 470 GLU H 614 CG CD OE1 OE2
REMARK 470 LYS H 615 CG CD CE NZ
REMARK 470 LEU H 617 CG CD1 CD2
REMARK 470 LYS H 618 CG CD CE NZ
REMARK 470 ILE I 4 CG1 CG2 CD1
REMARK 470 GLU I 5 CG CD OE1 OE2
REMARK 470 LYS I 13 CE NZ
REMARK 470 ARG I 23 CZ NH1 NH2
REMARK 470 ASN I 25 CG OD1 ND2
REMARK 470 LYS I 40 CE NZ
REMARK 470 GLU I 51 CG CD OE1 OE2
REMARK 470 LYS I 71 CE NZ
REMARK 470 ASN I 79 CG OD1 ND2
REMARK 470 LYS I 93 CG CD CE NZ
REMARK 470 LYS I 104 CG CD CE NZ
REMARK 470 GLN I 113 CG CD OE1 NE2
REMARK 470 LYS I 124 CG CD CE NZ
REMARK 470 GLU I 127 CG CD OE1 OE2
REMARK 470 LYS I 151 CD CE NZ
REMARK 470 GLU I 209 CG CD OE1 OE2
REMARK 470 GLU I 211 CG CD OE1 OE2
REMARK 470 LYS I 212 CE NZ
REMARK 470 LYS I 238 CE NZ
REMARK 470 LYS I 245 CE NZ
REMARK 470 GLU I 252 CG CD OE1 OE2
REMARK 470 LYS I 254 CG CD CE NZ
REMARK 470 ARG I 270 CG CD NE CZ NH1 NH2
REMARK 470 ASN I 271 CG OD1 ND2
REMARK 470 LYS I 273 CE NZ
REMARK 470 GLU I 292 CG CD OE1 OE2
REMARK 470 GLU I 295 CG CD OE1 OE2
REMARK 470 ARG I 311 NE CZ NH1 NH2
REMARK 470 GLU I 331 CG CD OE1 OE2
REMARK 470 ARG I 333 CG CD NE CZ NH1 NH2
REMARK 470 ILE I 342 CD1
REMARK 470 LYS I 344 CE NZ
REMARK 470 LYS I 345 CE NZ
REMARK 470 LYS I 347 CG CD CE NZ
REMARK 470 ARG I 352 CG CD NE CZ NH1 NH2
REMARK 470 GLU I 371 CG CD OE1 OE2
REMARK 470 LYS I 373 CG CD CE NZ
REMARK 470 GLU I 374 CG CD OE1 OE2
REMARK 470 LYS I 377 CG CD CE NZ
REMARK 470 LYS I 397 CG CD CE NZ
REMARK 470 GLU I 446 CG CD OE1 OE2
REMARK 470 GLU I 458 CG CD OE1 OE2
REMARK 470 ASP I 480 CG OD1 OD2
REMARK 470 GLU I 518 CG CD OE1 OE2
REMARK 470 LYS I 524 CG CD CE NZ
REMARK 470 LYS I 532 CG CD CE NZ
REMARK 470 LYS I 535 CG CD CE NZ
REMARK 470 LYS I 575 CG CD CE NZ
REMARK 470 ARG I 583 NE CZ NH1 NH2
REMARK 470 LYS I 606 CG CD CE NZ
REMARK 470 GLU I 614 CG CD OE1 OE2
REMARK 470 LYS I 615 CG CD CE NZ
REMARK 470 LEU I 617 CG CD1 CD2
REMARK 470 LYS I 618 CG CD CE NZ
REMARK 470 ILE J 4 CG1 CG2 CD1
REMARK 470 GLU J 5 CG CD OE1 OE2
REMARK 470 LYS J 9 CE NZ
REMARK 470 LYS J 13 CG CD CE NZ
REMARK 470 LEU J 17 CG CD1 CD2
REMARK 470 ARG J 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS J 24 CD CE NZ
REMARK 470 ASN J 25 CG OD1 ND2
REMARK 470 LEU J 26 CG CD1 CD2
REMARK 470 GLU J 37 CG CD OE1 OE2
REMARK 470 LYS J 40 CD CE NZ
REMARK 470 ASN J 49 CG OD1 ND2
REMARK 470 LEU J 50 CG CD1 CD2
REMARK 470 ASP J 52 CG OD1 OD2
REMARK 470 LYS J 56 CE NZ
REMARK 470 ASP J 60 CG OD1 OD2
REMARK 470 ILE J 66 CG1 CG2 CD1
REMARK 470 LYS J 71 CG CD CE NZ
REMARK 470 THR J 84 OG1 CG2
REMARK 470 LYS J 93 CG CD CE NZ
REMARK 470 LYS J 98 CG CD CE NZ
REMARK 470 LYS J 99 CG CD CE NZ
REMARK 470 GLU J 102 CG CD OE1 OE2
REMARK 470 LYS J 104 CG CD CE NZ
REMARK 470 ILE J 109 CG1 CG2 CD1
REMARK 470 GLU J 110 CG CD OE1 OE2
REMARK 470 GLN J 113 CG CD OE1 NE2
REMARK 470 LYS J 124 CD CE NZ
REMARK 470 GLU J 129 CG CD OE1 OE2
REMARK 470 LYS J 151 CG CD CE NZ
REMARK 470 LYS J 170 CE NZ
REMARK 470 ARG J 190 CG CD NE CZ NH1 NH2
REMARK 470 ASP J 191 CG OD1 OD2
REMARK 470 ILE J 193 CG1 CG2 CD1
REMARK 470 ARG J 195 CG CD NE CZ NH1 NH2
REMARK 470 LEU J 204 CG CD1 CD2
REMARK 470 LYS J 206 CG CD CE NZ
REMARK 470 ASP J 207 CG OD1 OD2
REMARK 470 GLU J 209 CG CD OE1 OE2
REMARK 470 GLU J 210 CG CD OE1 OE2
REMARK 470 GLU J 211 CG CD OE1 OE2
REMARK 470 LYS J 212 CG CD CE NZ
REMARK 470 LEU J 213 CG CD1 CD2
REMARK 470 GLU J 215 CG CD OE1 OE2
REMARK 470 LYS J 216 CG CD CE NZ
REMARK 470 VAL J 217 CG1 CG2
REMARK 470 ASP J 225 CG OD1 OD2
REMARK 470 GLU J 227 CG CD OE1 OE2
REMARK 470 ARG J 228 CG CD NE CZ NH1 NH2
REMARK 470 LYS J 234 CD CE NZ
REMARK 470 GLU J 236 CG CD OE1 OE2
REMARK 470 LYS J 237 CG CD CE NZ
REMARK 470 LYS J 238 CG CD CE NZ
REMARK 470 GLU J 242 CG CD OE1 OE2
REMARK 470 LYS J 245 CG CD CE NZ
REMARK 470 ILE J 246 CG1 CG2 CD1
REMARK 470 ILE J 248 CG1 CG2 CD1
REMARK 470 TYR J 249 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP J 250 CG OD1 OD2
REMARK 470 GLU J 252 CG CD OE1 OE2
REMARK 470 VAL J 253 CG1 CG2
REMARK 470 LYS J 254 CG CD CE NZ
REMARK 470 ILE J 256 CG1 CG2 CD1
REMARK 470 LEU J 257 CG CD1 CD2
REMARK 470 ASP J 258 CG OD1 OD2
REMARK 470 ILE J 260 CG1 CG2 CD1
REMARK 470 ARG J 262 NE CZ NH1 NH2
REMARK 470 ILE J 269 CG1 CG2 CD1
REMARK 470 ARG J 270 CG CD NE CZ NH1 NH2
REMARK 470 ASN J 271 CG OD1 ND2
REMARK 470 LYS J 273 CG CD CE NZ
REMARK 470 SER J 283 OG
REMARK 470 LEU J 286 CG CD1 CD2
REMARK 470 ASP J 290 CG OD1 OD2
REMARK 470 GLU J 292 CG CD OE1 OE2
REMARK 470 VAL J 293 CG1 CG2
REMARK 470 ARG J 294 CG CD NE CZ NH1 NH2
REMARK 470 LYS J 298 CG CD CE NZ
REMARK 470 LYS J 300 CD CE NZ
REMARK 470 ARG J 311 CG CD NE CZ NH1 NH2
REMARK 470 LEU J 312 CG CD1 CD2
REMARK 470 ILE J 313 CG1 CG2 CD1
REMARK 470 LEU J 327 CG CD1 CD2
REMARK 470 GLU J 331 CG CD OE1 OE2
REMARK 470 ARG J 333 CG CD NE CZ NH1 NH2
REMARK 470 ILE J 342 CD1
REMARK 470 LYS J 344 CG CD CE NZ
REMARK 470 LYS J 345 CG CD CE NZ
REMARK 470 LEU J 346 CG CD1 CD2
REMARK 470 LYS J 347 CG CD CE NZ
REMARK 470 ARG J 352 CG CD NE CZ NH1 NH2
REMARK 470 LYS J 357 CG CD CE NZ
REMARK 470 SER J 358 OG
REMARK 470 ILE J 359 CG1 CG2 CD1
REMARK 470 ASP J 360 CG OD1 OD2
REMARK 470 LEU J 361 CG CD1 CD2
REMARK 470 GLU J 362 CG CD OE1 OE2
REMARK 470 LEU J 363 CG CD1 CD2
REMARK 470 GLU J 371 CG CD OE1 OE2
REMARK 470 LYS J 373 CG CD CE NZ
REMARK 470 GLU J 374 CG CD OE1 OE2
REMARK 470 GLU J 376 CG CD OE1 OE2
REMARK 470 LYS J 377 CG CD CE NZ
REMARK 470 LYS J 397 CE NZ
REMARK 470 LYS J 406 CD CE NZ
REMARK 470 TYR J 421 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP J 424 CG OD1 OD2
REMARK 470 GLN J 439 CG CD OE1 NE2
REMARK 470 ILE J 441 CG1 CG2 CD1
REMARK 470 GLU J 446 CG CD OE1 OE2
REMARK 470 ARG J 450 CG CD NE CZ NH1 NH2
REMARK 470 ARG J 457 CG CD NE CZ NH1 NH2
REMARK 470 GLU J 458 CG CD OE1 OE2
REMARK 470 ASP J 480 CG OD1 OD2
REMARK 470 LYS J 483 CG CD CE NZ
REMARK 470 SER J 492 OG
REMARK 470 GLU J 520 CG CD OE1 OE2
REMARK 470 ARG J 523 CG CD NE CZ NH1 NH2
REMARK 470 LYS J 524 CG CD CE NZ
REMARK 470 LYS J 532 CG CD CE NZ
REMARK 470 LYS J 535 CG CD CE NZ
REMARK 470 LYS J 575 CD CE NZ
REMARK 470 LYS J 605 NZ
REMARK 470 LYS J 606 CD CE NZ
REMARK 470 VAL J 613 CG1 CG2
REMARK 470 GLU J 614 CG CD OE1 OE2
REMARK 470 LYS J 615 CD CE NZ
REMARK 470 LEU J 617 CG CD1 CD2
REMARK 470 LYS J 618 CG CD CE NZ
REMARK 470 ILE K 4 CG1 CG2 CD1
REMARK 470 GLU K 5 CG CD OE1 OE2
REMARK 470 LYS K 13 CE NZ
REMARK 470 ARG K 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS K 24 CG CD CE NZ
REMARK 470 ASN K 25 CG OD1 ND2
REMARK 470 LEU K 26 CG CD1 CD2
REMARK 470 LYS K 40 CE NZ
REMARK 470 ILE K 47 CG1 CG2 CD1
REMARK 470 GLU K 48 CG CD OE1 OE2
REMARK 470 ASN K 49 CG OD1 ND2
REMARK 470 LEU K 50 CG CD1 CD2
REMARK 470 GLU K 51 CG CD OE1 OE2
REMARK 470 ASP K 52 CG OD1 OD2
REMARK 470 SER K 54 OG
REMARK 470 LYS K 56 CG CD CE NZ
REMARK 470 LYS K 71 CG CD CE NZ
REMARK 470 ASN K 79 CG OD1 ND2
REMARK 470 THR K 84 OG1 CG2
REMARK 470 LYS K 93 CG CD CE NZ
REMARK 470 GLU K 102 CG CD OE1 OE2
REMARK 470 LYS K 104 CG CD CE NZ
REMARK 470 GLN K 113 CG CD OE1 NE2
REMARK 470 LYS K 124 CG CD CE NZ
REMARK 470 LYS K 151 CE NZ
REMARK 470 GLN K 167 CG CD OE1 NE2
REMARK 470 ARG K 195 NE CZ NH1 NH2
REMARK 470 LYS K 198 CG CD CE NZ
REMARK 470 GLU K 209 CG CD OE1 OE2
REMARK 470 GLU K 211 CG CD OE1 OE2
REMARK 470 LYS K 212 CE NZ
REMARK 470 ARG K 228 CZ NH1 NH2
REMARK 470 ILE K 229 CG1 CG2 CD1
REMARK 470 LYS K 234 CG CD CE NZ
REMARK 470 LYS K 238 CG CD CE NZ
REMARK 470 VAL K 240 CG1 CG2
REMARK 470 LYS K 245 CG CD CE NZ
REMARK 470 GLU K 252 CG CD OE1 OE2
REMARK 470 LYS K 254 CG CD CE NZ
REMARK 470 ILE K 256 CG1 CG2 CD1
REMARK 470 ASP K 259 CG OD1 OD2
REMARK 470 VAL K 264 CG1 CG2
REMARK 470 ILE K 269 CG1 CG2 CD1
REMARK 470 ARG K 270 CG CD NE CZ NH1 NH2
REMARK 470 ASN K 271 CG OD1 ND2
REMARK 470 LYS K 273 CE NZ
REMARK 470 PHE K 276 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU K 280 CG CD OE1 OE2
REMARK 470 VAL K 284 CG1 CG2
REMARK 470 LEU K 286 CG CD1 CD2
REMARK 470 TYR K 287 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU K 288 CG CD1 CD2
REMARK 470 GLU K 292 CG CD OE1 OE2
REMARK 470 VAL K 293 CG1 CG2
REMARK 470 ARG K 294 CG CD NE CZ NH1 NH2
REMARK 470 LYS K 298 CG CD CE NZ
REMARK 470 LYS K 300 CG CD CE NZ
REMARK 470 ILE K 303 CG1 CG2 CD1
REMARK 470 GLU K 310 CG CD OE1 OE2
REMARK 470 ARG K 311 CD NE CZ NH1 NH2
REMARK 470 TYR K 314 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU K 325 CG CD1 CD2
REMARK 470 LEU K 327 CG CD1 CD2
REMARK 470 TRP K 328 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP K 328 CZ3 CH2
REMARK 470 ASP K 329 CG OD1 OD2
REMARK 470 GLU K 331 CG CD OE1 OE2
REMARK 470 GLU K 332 CG CD OE1 OE2
REMARK 470 ARG K 333 CG CD NE CZ NH1 NH2
REMARK 470 GLN K 334 CG CD OE1 NE2
REMARK 470 LEU K 335 CG CD1 CD2
REMARK 470 ILE K 342 CD1
REMARK 470 LYS K 344 CG CD CE NZ
REMARK 470 LYS K 345 CG CD CE NZ
REMARK 470 LYS K 347 CG CD CE NZ
REMARK 470 GLU K 350 CD OE1 OE2
REMARK 470 ARG K 352 CG CD NE CZ NH1 NH2
REMARK 470 LYS K 357 CE NZ
REMARK 470 SER K 358 OG
REMARK 470 LEU K 361 CG CD1 CD2
REMARK 470 ASP K 364 CG OD1 OD2
REMARK 470 ILE K 368 CG1 CG2 CD1
REMARK 470 LYS K 369 CG CD CE NZ
REMARK 470 GLU K 371 CG CD OE1 OE2
REMARK 470 ILE K 372 CG1 CG2 CD1
REMARK 470 LYS K 373 CG CD CE NZ
REMARK 470 GLU K 376 CG CD OE1 OE2
REMARK 470 LYS K 377 CG CD CE NZ
REMARK 470 LEU K 427 CG CD1 CD2
REMARK 470 ARG K 428 CG CD NE CZ NH1 NH2
REMARK 470 LEU K 430 CG CD1 CD2
REMARK 470 ILE K 441 CG1 CG2 CD1
REMARK 470 ILE K 445 CG1 CG2 CD1
REMARK 470 GLU K 446 CG CD OE1 OE2
REMARK 470 GLU K 447 CG CD OE1 OE2
REMARK 470 ARG K 450 CG CD NE CZ NH1 NH2
REMARK 470 LEU K 451 CG CD1 CD2
REMARK 470 ARG K 457 CG CD NE CZ NH1 NH2
REMARK 470 GLU K 458 CG CD OE1 OE2
REMARK 470 ASP K 480 CG OD1 OD2
REMARK 470 LYS K 483 CG CD CE NZ
REMARK 470 SER K 492 OG
REMARK 470 LEU K 517 CG CD1 CD2
REMARK 470 GLU K 518 CG CD OE1 OE2
REMARK 470 GLU K 520 CG CD OE1 OE2
REMARK 470 ARG K 523 CG CD NE CZ NH1 NH2
REMARK 470 LYS K 524 CG CD CE NZ
REMARK 470 LEU K 525 CG CD1 CD2
REMARK 470 LYS K 532 CG CD CE NZ
REMARK 470 VAL K 534 CG1 CG2
REMARK 470 LYS K 535 CG CD CE NZ
REMARK 470 LEU K 561 CD1 CD2
REMARK 470 LYS K 575 CE NZ
REMARK 470 LYS K 603 CG CD CE NZ
REMARK 470 LYS K 606 CG CD CE NZ
REMARK 470 VAL K 613 CG1 CG2
REMARK 470 GLU K 614 CG CD OE1 OE2
REMARK 470 LYS K 615 CD CE NZ
REMARK 470 LEU K 617 CG CD1 CD2
REMARK 470 LYS K 618 CG CD CE NZ
REMARK 470 ILE L 4 CG1 CG2 CD1
REMARK 470 GLU L 5 CG CD OE1 OE2
REMARK 470 LYS L 13 CE NZ
REMARK 470 ARG L 23 CZ NH1 NH2
REMARK 470 ASN L 25 CG OD1 ND2
REMARK 470 GLU L 37 CG CD OE1 OE2
REMARK 470 LYS L 40 CE NZ
REMARK 470 LEU L 50 CG CD1 CD2
REMARK 470 GLU L 51 CG CD OE1 OE2
REMARK 470 ASP L 52 CG OD1 OD2
REMARK 470 LYS L 71 CG CD CE NZ
REMARK 470 LYS L 72 CE NZ
REMARK 470 ASN L 79 CG OD1 ND2
REMARK 470 THR L 84 OG1 CG2
REMARK 470 LEU L 92 CG CD1 CD2
REMARK 470 LYS L 93 CG CD CE NZ
REMARK 470 LYS L 99 CG CD CE NZ
REMARK 470 LYS L 104 CG CD CE NZ
REMARK 470 ILE L 106 CD1
REMARK 470 GLN L 113 CG CD OE1 NE2
REMARK 470 LYS L 124 CD CE NZ
REMARK 470 GLU L 129 CG CD OE1 OE2
REMARK 470 LYS L 151 CG CD CE NZ
REMARK 470 GLN L 167 CG CD OE1 NE2
REMARK 470 LYS L 170 CE NZ
REMARK 470 LYS L 206 CD CE NZ
REMARK 470 GLU L 209 CG CD OE1 OE2
REMARK 470 GLU L 211 CG CD OE1 OE2
REMARK 470 LYS L 238 CG CD CE NZ
REMARK 470 GLU L 252 CG CD OE1 OE2
REMARK 470 LYS L 254 CG CD CE NZ
REMARK 470 LYS L 268 CG CD CE NZ
REMARK 470 ARG L 270 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 273 CE NZ
REMARK 470 GLU L 292 CG CD OE1 OE2
REMARK 470 ARG L 294 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 298 CE NZ
REMARK 470 ARG L 311 CG CD NE CZ NH1 NH2
REMARK 470 GLU L 331 CD OE1 OE2
REMARK 470 ARG L 333 NE CZ NH1 NH2
REMARK 470 ILE L 342 CD1
REMARK 470 LYS L 344 CG CD CE NZ
REMARK 470 LYS L 345 CG CD CE NZ
REMARK 470 LYS L 347 CG CD CE NZ
REMARK 470 ARG L 352 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 357 CG CD CE NZ
REMARK 470 LYS L 373 CG CD CE NZ
REMARK 470 GLU L 374 CG CD OE1 OE2
REMARK 470 GLU L 376 CG CD OE1 OE2
REMARK 470 LYS L 377 CE NZ
REMARK 470 LYS L 397 CG CD CE NZ
REMARK 470 LYS L 406 CD CE NZ
REMARK 470 GLU L 458 CG CD OE1 OE2
REMARK 470 LYS L 483 CG CD CE NZ
REMARK 470 GLU L 520 CG CD OE1 OE2
REMARK 470 LYS L 532 CG CD CE NZ
REMARK 470 LYS L 535 CG CD CE NZ
REMARK 470 LYS L 575 CG CD CE NZ
REMARK 470 ARG L 583 NE CZ NH1 NH2
REMARK 470 LYS L 606 CG CD CE NZ
REMARK 470 GLU L 614 CG CD OE1 OE2
REMARK 470 LYS L 615 CG CD CE NZ
REMARK 470 LEU L 617 CG CD1 CD2
REMARK 470 LYS L 618 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 24 -124.13 51.48
REMARK 500 GLU A 51 -122.85 64.07
REMARK 500 LEU A 95 -2.02 80.84
REMARK 500 VAL A 100 -64.08 -103.60
REMARK 500 ARG A 116 -62.58 -120.15
REMARK 500 ASN A 143 -14.20 76.93
REMARK 500 ASP A 191 -75.84 -107.23
REMARK 500 VAL A 192 -61.99 -103.26
REMARK 500 LYS A 198 -63.73 -128.73
REMARK 500 ILE A 296 -72.34 -99.02
REMARK 500 HIS A 301 168.40 173.51
REMARK 500 ASP A 309 -78.77 -124.05
REMARK 500 ILE A 359 -116.49 51.74
REMARK 500 GLU A 431 -7.04 65.98
REMARK 500 LEU A 435 -78.88 -101.54
REMARK 500 ALA A 466 -121.84 61.76
REMARK 500 ILE A 512 -62.37 -101.62
REMARK 500 GLU A 518 -57.98 -126.71
REMARK 500 LEU A 604 -63.79 -128.59
REMARK 500 LYS B 24 -126.15 50.54
REMARK 500 GLU B 51 -14.60 82.92
REMARK 500 ASN B 143 -14.04 77.29
REMARK 500 ASP B 191 -77.93 -104.59
REMARK 500 VAL B 192 -61.68 -106.85
REMARK 500 PHE B 197 -4.94 70.63
REMARK 500 LYS B 198 -63.08 -103.41
REMARK 500 ILE B 296 -65.86 -98.51
REMARK 500 HIS B 301 167.10 173.45
REMARK 500 ASP B 309 -77.81 -124.77
REMARK 500 ILE B 359 -116.63 51.26
REMARK 500 GLU B 431 16.79 57.34
REMARK 500 LEU B 435 -78.34 -111.34
REMARK 500 ALA B 466 -123.91 60.20
REMARK 500 TRP B 506 -61.41 -104.98
REMARK 500 ILE B 512 -62.41 -109.36
REMARK 500 LEU B 604 -63.07 -126.99
REMARK 500 LYS C 24 -130.53 56.16
REMARK 500 ASP C 52 -13.78 67.37
REMARK 500 VAL C 100 -61.19 -101.22
REMARK 500 ARG C 116 -62.29 -122.09
REMARK 500 ASN C 143 -11.75 78.22
REMARK 500 GLU C 160 -62.69 -90.87
REMARK 500 ASP C 191 -76.99 -113.74
REMARK 500 VAL C 192 -62.44 -98.57
REMARK 500 PHE C 197 -4.10 71.13
REMARK 500 LYS C 198 -64.24 -105.21
REMARK 500 ILE C 296 -63.14 -102.57
REMARK 500 HIS C 301 174.17 172.60
REMARK 500 ASP C 309 -77.89 -123.41
REMARK 500 ILE C 359 -116.86 52.53
REMARK 500
REMARK 500 THIS ENTRY HAS 229 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP A 337 24.5 L L OUTSIDE RANGE
REMARK 500 ASP I 337 23.7 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 838 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH B 834 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH D 956 DISTANCE = 5.59 ANGSTROMS
REMARK 525 HOH D1019 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH E 915 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH E 933 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH F 874 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH F 882 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH F 886 DISTANCE = 5.44 ANGSTROMS
REMARK 525 HOH F 902 DISTANCE = 5.51 ANGSTROMS
REMARK 525 HOH F 905 DISTANCE = 5.13 ANGSTROMS
REMARK 525 HOH I 835 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH I 836 DISTANCE = 5.32 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 162 OE1
REMARK 620 2 LYS G 99 O 70.0
REMARK 620 3 HOH I 875 O 150.7 82.5
REMARK 620 4 HOH G 827 O 87.6 68.8 72.7
REMARK 620 5 HOH I 808 O 108.3 155.7 92.5 87.0
REMARK 620 6 HOH G 875 O 77.5 78.5 107.4 147.1 125.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 710 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 162 OE1
REMARK 620 2 HOH D1021 O 81.3
REMARK 620 3 HOH E 902 O 127.9 73.7
REMARK 620 4 HOH E 832 O 122.2 148.2 101.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 705 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 162 OE1
REMARK 620 2 LYS F 99 O 76.7
REMARK 620 3 HOH D 856 O 111.7 164.6
REMARK 620 4 HOH F 879 O 79.0 88.3 81.0
REMARK 620 5 HOH D 939 O 98.6 80.8 109.7 169.1
REMARK 620 6 HOH D 940 O 141.3 76.2 90.0 73.1 103.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 704 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 99 O
REMARK 620 2 GLU A 162 OE1 77.6
REMARK 620 3 HOH A 938 O 143.3 72.8
REMARK 620 4 HOH C 858 O 107.5 84.1 90.6
REMARK 620 5 HOH A 949 O 77.6 69.1 72.0 151.2
REMARK 620 6 HOH C 841 O 91.4 154.1 106.1 121.7 85.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 704 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 244 OD2
REMARK 620 2 GLU I 263 OE2 72.2
REMARK 620 3 HOH I 871 O 68.7 137.8
REMARK 620 4 HOH I 803 O 84.2 78.0 82.9
REMARK 620 5 HOH I 876 O 131.3 105.3 112.0 144.2
REMARK 620 6 HOH I 877 O 157.9 95.7 115.3 75.1 69.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 703 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS H 99 O
REMARK 620 2 GLU H 162 OE1 74.0
REMARK 620 3 HOH H 801 O 70.0 67.1
REMARK 620 4 HOH G 876 O 92.9 158.9 124.6
REMARK 620 5 HOH G 828 O 168.7 96.1 101.3 98.1
REMARK 620 6 HOH H 808 O 95.8 77.1 143.8 88.1 87.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 705 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 162 OE1
REMARK 620 2 LYS E 99 O 79.5
REMARK 620 3 HOH F 872 O 94.7 75.9
REMARK 620 4 HOH E 919 O 68.6 88.9 159.5
REMARK 620 5 HOH F 871 O 151.5 82.0 101.5 89.6
REMARK 620 6 HOH F 873 O 103.4 170.6 112.6 83.9 91.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 703 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU I 162 OE1
REMARK 620 2 LYS I 99 O 78.4
REMARK 620 3 GLU H 42 OE1 122.1 137.4
REMARK 620 4 HOH I 834 O 65.2 75.1 145.9
REMARK 620 5 HOH I 833 O 100.8 79.3 61.2 152.8
REMARK 620 6 HOH H 858 O 140.8 90.3 91.4 75.7 113.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 703 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS B 99 O
REMARK 620 2 GLU B 162 OE1 94.2
REMARK 620 3 HOH A 854 O 78.4 146.0
REMARK 620 4 HOH A 853 O 75.0 100.7 109.1
REMARK 620 5 HOH B 828 O 87.4 78.4 68.3 162.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 709 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 244 OD2
REMARK 620 2 GLU D 263 OE1 114.9
REMARK 620 3 GLU D 263 OE2 80.6 43.7
REMARK 620 4 HOH D 802 O 89.4 97.2 70.2
REMARK 620 5 HOH D 936 O 102.9 75.8 109.4 167.5
REMARK 620 6 HOH D 935 O 174.4 61.6 94.2 86.9 80.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 703 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 263 OE2
REMARK 620 2 ASP C 244 OD2 78.9
REMARK 620 3 HOH C 802 O 106.1 172.0
REMARK 620 4 HOH C 810 O 71.8 86.4 89.3
REMARK 620 5 HOH C 859 O 129.1 104.2 77.6 157.7
REMARK 620 6 HOH C 857 O 151.4 79.8 93.3 88.1 74.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 162 OE1
REMARK 620 2 LYS C 99 O 63.6
REMARK 620 3 GLU B 42 OE1 144.3 137.1
REMARK 620 4 HOH C 801 O 71.2 78.1 132.6
REMARK 620 5 HOH B 829 O 130.0 75.6 85.5 73.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 244 OD2
REMARK 620 2 GLU H 263 OE2 93.3
REMARK 620 3 GLU H 263 OE1 134.1 47.1
REMARK 620 4 HOH H 857 O 111.5 108.4 71.4
REMARK 620 5 HOH H 856 O 160.7 99.9 64.3 77.5
REMARK 620 6 HOH H 802 O 84.4 149.4 141.3 100.7 77.0
REMARK 620 7 HOH H 818 O 78.4 68.8 101.1 170.0 93.3 80.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 704 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 244 OD2
REMARK 620 2 GLU E 263 OE2 88.8
REMARK 620 3 GLU E 263 OE1 132.4 45.4
REMARK 620 4 HOH E 987 O 138.9 79.2 57.2
REMARK 620 5 HOH E 842 O 84.2 65.9 86.5 55.0
REMARK 620 6 HOH E 801 O 80.1 122.8 130.8 74.2 57.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 704 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 244 OD2
REMARK 620 2 GLU F 263 OE2 74.4
REMARK 620 3 HOH F 802 O 102.2 57.0
REMARK 620 4 HOH F 878 O 134.1 64.0 71.1
REMARK 620 5 HOH F 954 O 61.6 64.1 121.0 82.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 705 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 244 OD2
REMARK 620 2 GLU A 263 OE2 59.0
REMARK 620 3 HOH A 947 O 83.5 68.3
REMARK 620 4 HOH A 812 O 73.6 77.8 145.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L 703 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS L 99 O
REMARK 620 2 GLU L 162 OE1 54.2
REMARK 620 3 GLU L 162 OE2 84.6 45.7
REMARK 620 4 HOH J 707 O 156.5 105.4 87.6
REMARK 620 5 HOH J 706 O 76.7 58.4 96.3 82.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 703 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 244 OD2
REMARK 620 2 GLU G 263 OE2 72.0
REMARK 620 3 HOH G 804 O 74.5 51.1
REMARK 620 4 HOH G 810 O 78.8 120.9 72.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU L 263 OE1
REMARK 620 2 HOH L 851 O 79.2
REMARK 620 3 HOH L 820 O 102.5 123.9
REMARK 620 4 HOH L 809 O 163.3 93.9 68.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 706 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E 946 O
REMARK 620 2 HOH E 901 O 80.8
REMARK 620 3 HOH E 896 O 152.3 95.5
REMARK 620 4 HOH D 915 O 59.9 66.1 93.3
REMARK 620 5 HOH D1006 O 84.3 162.5 93.5 98.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 706 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E 988 O
REMARK 620 2 HOH E 841 O 58.2
REMARK 620 3 HOH F 955 O 103.5 161.5
REMARK 620 4 HOH E 979 O 141.6 97.3 96.8
REMARK 620 5 HOH E 840 O 72.7 101.6 67.6 85.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ D 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ D 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ D 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ D 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ D 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ D 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ E 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ E 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ E 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ F 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ F 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ F 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ G 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ H 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ I 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ I 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ K 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ L 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HXE RELATED DB: PDB
REMARK 900 RELATED ID: 4HXG RELATED DB: PDB
DBREF 4HXG A 1 622 UNP O58323 O58323_PYRHO 1 622
DBREF 4HXG B 1 622 UNP O58323 O58323_PYRHO 1 622
DBREF 4HXG C 1 622 UNP O58323 O58323_PYRHO 1 622
DBREF 4HXG D 1 622 UNP O58323 O58323_PYRHO 1 622
DBREF 4HXG E 1 622 UNP O58323 O58323_PYRHO 1 622
DBREF 4HXG F 1 622 UNP O58323 O58323_PYRHO 1 622
DBREF 4HXG G 1 622 UNP O58323 O58323_PYRHO 1 622
DBREF 4HXG H 1 622 UNP O58323 O58323_PYRHO 1 622
DBREF 4HXG I 1 622 UNP O58323 O58323_PYRHO 1 622
DBREF 4HXG J 1 622 UNP O58323 O58323_PYRHO 1 622
DBREF 4HXG K 1 622 UNP O58323 O58323_PYRHO 1 622
DBREF 4HXG L 1 622 UNP O58323 O58323_PYRHO 1 622
SEQADV 4HXG ALA A 466 UNP O58323 SER 466 ENGINEERED MUTATION
SEQADV 4HXG ALA B 466 UNP O58323 SER 466 ENGINEERED MUTATION
SEQADV 4HXG ALA C 466 UNP O58323 SER 466 ENGINEERED MUTATION
SEQADV 4HXG ALA D 466 UNP O58323 SER 466 ENGINEERED MUTATION
SEQADV 4HXG ALA E 466 UNP O58323 SER 466 ENGINEERED MUTATION
SEQADV 4HXG ALA F 466 UNP O58323 SER 466 ENGINEERED MUTATION
SEQADV 4HXG ALA G 466 UNP O58323 SER 466 ENGINEERED MUTATION
SEQADV 4HXG ALA H 466 UNP O58323 SER 466 ENGINEERED MUTATION
SEQADV 4HXG ALA I 466 UNP O58323 SER 466 ENGINEERED MUTATION
SEQADV 4HXG ALA J 466 UNP O58323 SER 466 ENGINEERED MUTATION
SEQADV 4HXG ALA K 466 UNP O58323 SER 466 ENGINEERED MUTATION
SEQADV 4HXG ALA L 466 UNP O58323 SER 466 ENGINEERED MUTATION
SEQRES 1 A 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 A 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 A 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 A 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 A 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 A 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 A 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 A 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 A 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 A 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 A 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 A 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 A 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 A 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 A 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 A 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 A 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 A 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 A 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 A 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 A 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 A 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 A 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 A 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 A 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 A 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 A 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 A 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 A 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 A 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 A 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 A 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 A 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 A 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 A 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 A 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE ALA TYR GLY
SEQRES 37 A 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 A 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 A 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 A 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 A 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 A 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 A 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 A 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 A 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 A 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 A 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 A 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
SEQRES 1 B 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 B 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 B 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 B 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 B 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 B 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 B 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 B 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 B 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 B 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 B 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 B 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 B 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 B 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 B 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 B 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 B 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 B 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 B 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 B 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 B 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 B 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 B 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 B 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 B 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 B 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 B 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 B 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 B 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 B 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 B 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 B 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 B 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 B 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 B 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 B 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE ALA TYR GLY
SEQRES 37 B 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 B 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 B 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 B 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 B 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 B 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 B 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 B 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 B 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 B 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 B 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 B 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
SEQRES 1 C 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 C 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 C 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 C 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 C 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 C 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 C 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 C 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 C 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 C 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 C 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 C 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 C 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 C 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 C 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 C 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 C 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 C 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 C 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 C 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 C 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 C 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 C 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 C 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 C 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 C 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 C 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 C 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 C 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 C 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 C 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 C 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 C 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 C 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 C 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 C 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE ALA TYR GLY
SEQRES 37 C 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 C 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 C 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 C 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 C 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 C 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 C 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 C 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 C 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 C 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 C 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 C 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
SEQRES 1 D 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 D 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 D 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 D 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 D 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 D 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 D 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 D 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 D 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 D 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 D 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 D 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 D 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 D 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 D 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 D 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 D 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 D 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 D 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 D 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 D 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 D 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 D 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 D 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 D 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 D 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 D 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 D 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 D 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 D 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 D 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 D 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 D 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 D 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 D 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 D 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE ALA TYR GLY
SEQRES 37 D 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 D 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 D 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 D 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 D 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 D 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 D 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 D 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 D 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 D 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 D 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 D 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
SEQRES 1 E 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 E 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 E 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 E 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 E 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 E 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 E 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 E 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 E 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 E 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 E 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 E 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 E 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 E 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 E 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 E 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 E 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 E 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 E 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 E 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 E 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 E 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 E 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 E 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 E 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 E 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 E 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 E 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 E 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 E 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 E 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 E 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 E 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 E 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 E 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 E 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE ALA TYR GLY
SEQRES 37 E 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 E 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 E 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 E 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 E 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 E 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 E 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 E 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 E 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 E 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 E 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 E 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
SEQRES 1 F 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 F 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 F 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 F 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 F 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 F 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 F 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 F 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 F 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 F 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 F 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 F 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 F 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 F 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 F 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 F 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 F 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 F 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 F 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 F 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 F 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 F 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 F 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 F 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 F 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 F 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 F 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 F 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 F 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 F 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 F 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 F 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 F 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 F 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 F 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 F 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE ALA TYR GLY
SEQRES 37 F 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 F 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 F 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 F 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 F 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 F 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 F 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 F 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 F 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 F 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 F 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 F 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
SEQRES 1 G 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 G 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 G 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 G 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 G 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 G 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 G 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 G 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 G 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 G 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 G 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 G 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 G 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 G 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 G 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 G 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 G 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 G 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 G 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 G 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 G 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 G 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 G 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 G 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 G 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 G 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 G 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 G 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 G 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 G 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 G 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 G 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 G 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 G 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 G 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 G 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE ALA TYR GLY
SEQRES 37 G 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 G 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 G 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 G 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 G 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 G 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 G 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 G 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 G 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 G 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 G 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 G 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
SEQRES 1 H 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 H 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 H 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 H 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 H 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 H 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 H 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 H 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 H 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 H 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 H 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 H 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 H 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 H 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 H 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 H 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 H 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 H 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 H 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 H 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 H 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 H 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 H 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 H 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 H 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 H 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 H 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 H 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 H 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 H 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 H 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 H 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 H 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 H 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 H 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 H 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE ALA TYR GLY
SEQRES 37 H 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 H 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 H 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 H 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 H 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 H 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 H 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 H 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 H 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 H 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 H 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 H 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
SEQRES 1 I 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 I 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 I 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 I 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 I 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 I 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 I 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 I 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 I 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 I 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 I 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 I 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 I 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 I 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 I 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 I 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 I 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 I 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 I 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 I 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 I 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 I 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 I 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 I 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 I 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 I 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 I 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 I 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 I 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 I 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 I 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 I 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 I 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 I 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 I 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 I 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE ALA TYR GLY
SEQRES 37 I 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 I 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 I 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 I 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 I 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 I 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 I 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 I 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 I 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 I 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 I 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 I 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
SEQRES 1 J 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 J 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 J 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 J 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 J 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 J 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 J 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 J 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 J 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 J 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 J 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 J 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 J 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 J 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 J 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 J 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 J 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 J 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 J 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 J 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 J 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 J 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 J 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 J 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 J 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 J 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 J 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 J 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 J 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 J 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 J 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 J 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 J 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 J 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 J 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 J 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE ALA TYR GLY
SEQRES 37 J 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 J 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 J 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 J 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 J 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 J 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 J 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 J 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 J 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 J 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 J 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 J 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
SEQRES 1 K 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 K 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 K 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 K 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 K 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 K 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 K 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 K 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 K 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 K 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 K 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 K 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 K 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 K 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 K 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 K 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 K 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 K 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 K 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 K 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 K 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 K 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 K 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 K 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 K 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 K 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 K 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 K 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 K 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 K 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 K 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 K 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 K 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 K 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 K 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 K 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE ALA TYR GLY
SEQRES 37 K 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 K 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 K 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 K 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 K 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 K 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 K 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 K 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 K 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 K 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 K 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 K 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
SEQRES 1 L 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 L 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 L 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 L 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 L 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 L 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 L 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 L 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 L 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 L 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 L 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 L 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 L 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 L 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 L 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 L 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 L 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 L 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 L 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 L 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 L 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 L 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 L 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 L 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 L 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 L 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 L 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 L 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 L 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 L 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 L 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 L 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 L 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 L 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 L 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 L 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE ALA TYR GLY
SEQRES 37 L 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 L 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 L 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 L 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 L 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 L 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 L 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 L 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 L 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 L 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 L 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 L 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
HET HEZ A 701 8
HET HEZ A 702 8
HET HEZ A 703 8
HET MG A 704 1
HET MG A 705 1
HET HEZ B 701 8
HET HEZ B 702 8
HET MG B 703 1
HET HEZ C 701 8
HET MG C 702 1
HET MG C 703 1
HET HEZ D 701 8
HET HEZ D 702 8
HET HEZ D 703 8
HET HEZ D 704 8
HET HEZ D 705 8
HET HEZ D 706 8
HET HEZ D 707 8
HET HEZ D 708 8
HET MG D 709 1
HET MG D 710 1
HET CL D 711 1
HET HEZ E 701 8
HET HEZ E 702 8
HET HEZ E 703 8
HET MG E 704 1
HET MG E 705 1
HET MG E 706 1
HET HEZ F 701 8
HET HEZ F 702 8
HET HEZ F 703 8
HET MG F 704 1
HET MG F 705 1
HET MG F 706 1
HET CL F 707 1
HET HEZ G 701 8
HET MG G 702 1
HET MG G 703 1
HET HEZ H 701 8
HET MG H 702 1
HET MG H 703 1
HET HEZ I 701 8
HET HEZ I 702 8
HET MG I 703 1
HET MG I 704 1
HET HEZ K 701 8
HET HEZ L 701 8
HET MG L 702 1
HET MG L 703 1
HETNAM HEZ HEXANE-1,6-DIOL
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 13 HEZ 26(C6 H14 O2)
FORMUL 16 MG 21(MG 2+)
FORMUL 34 CL 2(CL 1-)
FORMUL 62 HOH *1147(H2 O)
HELIX 1 1 LYS A 9 PHE A 14 5 6
HELIX 2 2 ASN A 339 LYS A 345 1 7
HELIX 3 3 LYS A 397 LYS A 406 1 10
HELIX 4 4 SER A 422 ARG A 428 1 7
HELIX 5 5 LEU A 435 GLU A 452 1 18
HELIX 6 6 ALA A 466 SER A 479 1 14
HELIX 7 7 TYR A 493 SER A 501 1 9
HELIX 8 8 ILE A 503 ILE A 512 1 10
HELIX 9 9 GLU A 520 LEU A 525 1 6
HELIX 10 10 SER A 526 VAL A 534 5 9
HELIX 11 11 LEU A 551 LEU A 564 1 14
HELIX 12 12 GLY A 579 GLY A 584 1 6
HELIX 13 13 SER A 585 LEU A 604 1 20
HELIX 14 14 ASP A 612 LEU A 617 1 6
HELIX 15 15 LYS B 9 PHE B 14 5 6
HELIX 16 16 ASN B 339 LYS B 345 1 7
HELIX 17 17 LYS B 397 LYS B 406 1 10
HELIX 18 18 SER B 422 ARG B 428 1 7
HELIX 19 19 LEU B 435 GLU B 452 1 18
HELIX 20 20 ALA B 466 SER B 479 1 14
HELIX 21 21 TYR B 493 SER B 501 1 9
HELIX 22 22 ILE B 503 ILE B 512 1 10
HELIX 23 23 GLU B 520 LEU B 525 1 6
HELIX 24 24 SER B 526 VAL B 534 5 9
HELIX 25 25 LEU B 551 LEU B 564 1 14
HELIX 26 26 GLY B 579 GLY B 584 1 6
HELIX 27 27 SER B 585 LEU B 604 1 20
HELIX 28 28 ASP B 612 LYS B 618 1 7
HELIX 29 29 LYS C 9 PHE C 14 5 6
HELIX 30 30 ASN C 339 LYS C 345 1 7
HELIX 31 31 LYS C 397 LYS C 406 1 10
HELIX 32 32 SER C 422 ARG C 428 1 7
HELIX 33 33 LEU C 435 GLU C 452 1 18
HELIX 34 34 ALA C 466 SER C 479 1 14
HELIX 35 35 TYR C 493 PHE C 500 1 8
HELIX 36 36 ILE C 503 ILE C 512 1 10
HELIX 37 37 GLU C 520 LEU C 525 1 6
HELIX 38 38 SER C 526 VAL C 534 5 9
HELIX 39 39 PRO C 550 LEU C 564 1 15
HELIX 40 40 GLY C 579 GLY C 584 1 6
HELIX 41 41 SER C 585 LEU C 604 1 20
HELIX 42 42 ASP C 612 LYS C 618 1 7
HELIX 43 43 LYS D 9 PHE D 14 5 6
HELIX 44 44 ASN D 339 LYS D 345 1 7
HELIX 45 45 LYS D 397 LYS D 406 1 10
HELIX 46 46 SER D 422 ARG D 428 1 7
HELIX 47 47 LEU D 435 GLU D 452 1 18
HELIX 48 48 ALA D 466 SER D 479 1 14
HELIX 49 49 TYR D 493 SER D 501 1 9
HELIX 50 50 ILE D 503 ILE D 512 1 10
HELIX 51 51 GLU D 520 LEU D 525 1 6
HELIX 52 52 SER D 526 VAL D 534 5 9
HELIX 53 53 LEU D 551 LEU D 564 1 14
HELIX 54 54 GLY D 579 GLY D 584 1 6
HELIX 55 55 SER D 585 LEU D 604 1 20
HELIX 56 56 ASP D 612 LEU D 617 1 6
HELIX 57 57 LYS E 9 PHE E 14 5 6
HELIX 58 58 LEU E 341 LYS E 345 5 5
HELIX 59 59 LYS E 397 LYS E 406 1 10
HELIX 60 60 SER E 422 ARG E 428 1 7
HELIX 61 61 LEU E 435 GLU E 452 1 18
HELIX 62 62 ALA E 466 SER E 479 1 14
HELIX 63 63 TYR E 493 SER E 501 1 9
HELIX 64 64 ILE E 503 ILE E 512 1 10
HELIX 65 65 GLU E 520 LEU E 525 1 6
HELIX 66 66 SER E 526 VAL E 534 5 9
HELIX 67 67 LEU E 551 LEU E 564 1 14
HELIX 68 68 GLY E 579 GLY E 584 1 6
HELIX 69 69 SER E 585 LEU E 604 1 20
HELIX 70 70 ASP E 612 LEU E 617 1 6
HELIX 71 71 LYS F 9 PHE F 14 5 6
HELIX 72 72 LEU F 341 LYS F 345 5 5
HELIX 73 73 LYS F 397 LYS F 406 1 10
HELIX 74 74 SER F 422 ARG F 428 1 7
HELIX 75 75 LEU F 435 GLU F 452 1 18
HELIX 76 76 ALA F 466 SER F 479 1 14
HELIX 77 77 TYR F 493 SER F 501 1 9
HELIX 78 78 ILE F 503 ILE F 512 1 10
HELIX 79 79 GLU F 520 LEU F 525 1 6
HELIX 80 80 SER F 526 VAL F 534 5 9
HELIX 81 81 LEU F 551 LEU F 564 1 14
HELIX 82 82 GLY F 579 GLY F 584 1 6
HELIX 83 83 SER F 585 LEU F 604 1 20
HELIX 84 84 ASP F 612 LEU F 617 1 6
HELIX 85 85 LYS G 9 PHE G 14 5 6
HELIX 86 86 LEU G 341 LYS G 345 5 5
HELIX 87 87 LYS G 397 LYS G 406 1 10
HELIX 88 88 SER G 422 ARG G 428 1 7
HELIX 89 89 LEU G 435 GLU G 452 1 18
HELIX 90 90 ALA G 466 SER G 479 1 14
HELIX 91 91 TYR G 493 SER G 501 1 9
HELIX 92 92 ILE G 503 ILE G 512 1 10
HELIX 93 93 GLU G 520 LEU G 525 1 6
HELIX 94 94 SER G 526 VAL G 534 5 9
HELIX 95 95 LEU G 551 GLY G 565 1 15
HELIX 96 96 GLY G 579 GLY G 584 1 6
HELIX 97 97 SER G 585 LEU G 604 1 20
HELIX 98 98 ASP G 612 LEU G 617 1 6
HELIX 99 99 LYS H 9 PHE H 14 5 6
HELIX 100 100 LEU H 341 LYS H 345 5 5
HELIX 101 101 LYS H 397 LYS H 406 1 10
HELIX 102 102 SER H 422 ARG H 428 1 7
HELIX 103 103 LEU H 435 GLU H 452 1 18
HELIX 104 104 ALA H 466 SER H 479 1 14
HELIX 105 105 TYR H 493 PHE H 500 1 8
HELIX 106 106 ILE H 503 ILE H 512 1 10
HELIX 107 107 GLU H 520 LEU H 525 1 6
HELIX 108 108 SER H 526 VAL H 534 5 9
HELIX 109 109 LEU H 551 LEU H 564 1 14
HELIX 110 110 GLY H 579 GLY H 584 1 6
HELIX 111 111 SER H 585 LYS H 603 1 19
HELIX 112 112 ASP H 612 LEU H 617 1 6
HELIX 113 113 LYS I 9 PHE I 14 5 6
HELIX 114 114 LEU I 341 LYS I 345 5 5
HELIX 115 115 LYS I 397 LYS I 406 1 10
HELIX 116 116 SER I 422 ARG I 428 1 7
HELIX 117 117 LEU I 435 GLU I 452 1 18
HELIX 118 118 ALA I 466 SER I 479 1 14
HELIX 119 119 TYR I 493 SER I 501 1 9
HELIX 120 120 ILE I 503 ILE I 512 1 10
HELIX 121 121 GLU I 520 LEU I 525 1 6
HELIX 122 122 SER I 526 VAL I 534 5 9
HELIX 123 123 LEU I 551 LEU I 564 1 14
HELIX 124 124 GLY I 579 GLY I 584 1 6
HELIX 125 125 SER I 585 LEU I 604 1 20
HELIX 126 126 ASP I 612 LEU I 617 1 6
HELIX 127 127 LYS J 9 PHE J 14 5 6
HELIX 128 128 ASN J 339 LEU J 346 1 8
HELIX 129 129 LYS J 397 LYS J 406 1 10
HELIX 130 130 SER J 422 ARG J 428 1 7
HELIX 131 131 LEU J 435 GLU J 452 1 18
HELIX 132 132 ALA J 466 SER J 479 1 14
HELIX 133 133 TYR J 493 SER J 501 1 9
HELIX 134 134 ILE J 503 ILE J 512 1 10
HELIX 135 135 GLU J 520 LEU J 525 1 6
HELIX 136 136 SER J 526 VAL J 534 5 9
HELIX 137 137 LEU J 551 LEU J 564 1 14
HELIX 138 138 GLY J 579 GLY J 584 1 6
HELIX 139 139 SER J 585 LEU J 604 1 20
HELIX 140 140 ASP J 612 LEU J 617 1 6
HELIX 141 141 LYS K 9 LYS K 13 5 5
HELIX 142 142 ASN K 339 LYS K 344 1 6
HELIX 143 143 LYS K 397 LYS K 406 1 10
HELIX 144 144 SER K 422 ARG K 428 1 7
HELIX 145 145 LEU K 435 GLU K 452 1 18
HELIX 146 146 ALA K 466 SER K 479 1 14
HELIX 147 147 TYR K 493 SER K 501 1 9
HELIX 148 148 ILE K 503 ILE K 512 1 10
HELIX 149 149 GLU K 520 LEU K 525 1 6
HELIX 150 150 SER K 526 VAL K 534 5 9
HELIX 151 151 LEU K 551 LEU K 564 1 14
HELIX 152 152 GLY K 579 GLY K 584 1 6
HELIX 153 153 SER K 585 LEU K 604 1 20
HELIX 154 154 ASP K 612 LYS K 618 1 7
HELIX 155 155 LYS L 9 PHE L 14 5 6
HELIX 156 156 ASN L 339 LYS L 345 1 7
HELIX 157 157 LYS L 397 LYS L 406 1 10
HELIX 158 158 SER L 422 ARG L 428 1 7
HELIX 159 159 LEU L 435 GLU L 452 1 18
HELIX 160 160 ALA L 466 SER L 479 1 14
HELIX 161 161 TYR L 493 SER L 501 1 9
HELIX 162 162 ILE L 503 ILE L 512 1 10
HELIX 163 163 GLU L 520 LEU L 525 1 6
HELIX 164 164 SER L 526 VAL L 534 5 9
HELIX 165 165 LEU L 551 LEU L 564 1 14
HELIX 166 166 GLY L 579 GLY L 584 1 6
HELIX 167 167 SER L 585 LEU L 604 1 20
HELIX 168 168 ASP L 612 LYS L 618 1 7
SHEET 1 A 4 TYR A 16 ARG A 23 0
SHEET 2 A 4 LEU A 26 ASN A 35 -1 O VAL A 30 N SER A 18
SHEET 3 A 4 LYS A 40 ASN A 49 -1 O GLU A 48 N VAL A 27
SHEET 4 A 4 ARG A 55 GLU A 59 -1 O ILE A 58 N ILE A 45
SHEET 1 B 4 SER A 62 ILE A 66 0
SHEET 2 B 4 LYS A 72 ARG A 77 -1 O ALA A 74 N ARG A 65
SHEET 3 B 4 GLN A 86 ASP A 91 -1 O ALA A 90 N ILE A 73
SHEET 4 B 4 ALA A 97 GLU A 102 -1 O LEU A 101 N ILE A 87
SHEET 1 C 4 ILE A 106 TRP A 111 0
SHEET 2 C 4 ARG A 117 LYS A 124 -1 O LEU A 119 N GLU A 110
SHEET 3 C 4 LYS A 151 ASP A 158 -1 O TRP A 155 N ALA A 120
SHEET 4 C 4 GLU A 163 LYS A 170 -1 O PHE A 168 N PHE A 154
SHEET 1 D 9 PHE A 131 GLU A 134 0
SHEET 2 D 9 VAL D 568 PHE D 573 -1 O ILE D 572 N ILE A 132
SHEET 3 D 9 LEU D 538 SER D 543 1 N HIS D 542 O PHE D 573
SHEET 4 D 9 ALA D 484 GLU D 488 1 N SER D 487 O LEU D 539
SHEET 5 D 9 ALA D 455 ILE D 465 1 N GLY D 464 O GLU D 488
SHEET 6 D 9 ALA D 378 VAL D 384 1 N VAL D 380 O GLY D 461
SHEET 7 D 9 TYR D 409 VAL D 413 1 O TYR D 409 N PRO D 379
SHEET 8 D 9 LEU D 361 ILE D 368 -1 N TRP D 366 O TYR D 412
SHEET 9 D 9 ARG D 352 SER D 358 -1 N SER D 358 O LEU D 361
SHEET 1 E 2 TRP A 140 PHE A 141 0
SHEET 2 E 2 GLY A 145 PHE A 146 -1 O GLY A 145 N PHE A 141
SHEET 1 F 4 SER A 175 HIS A 179 0
SHEET 2 F 4 SER A 182 PRO A 188 -1 O SER A 182 N HIS A 179
SHEET 3 F 4 TRP A 200 LYS A 206 -1 O TRP A 205 N ILE A 183
SHEET 4 F 4 GLU A 209 VAL A 217 -1 O GLU A 209 N LYS A 206
SHEET 1 G 4 PHE A 219 SER A 224 0
SHEET 2 G 4 ILE A 229 GLY A 233 -1 O TYR A 232 N TYR A 220
SHEET 3 G 4 LYS A 245 TYR A 249 -1 O TYR A 247 N LEU A 231
SHEET 4 G 4 VAL A 253 GLY A 255 -1 O LYS A 254 N ILE A 248
SHEET 1 H 4 GLU A 263 ARG A 270 0
SHEET 2 H 4 LYS A 273 GLU A 280 -1 O TYR A 275 N LYS A 268
SHEET 3 H 4 SER A 283 TRP A 289 -1 O TYR A 287 N PHE A 276
SHEET 4 H 4 VAL A 293 ALA A 297 -1 O ALA A 297 N LEU A 286
SHEET 1 I 4 TRP A 302 ALA A 308 0
SHEET 2 I 4 LEU A 312 GLU A 317 -1 O GLU A 317 N TRP A 302
SHEET 3 I 4 GLU A 324 TRP A 328 -1 O TYR A 326 N TYR A 314
SHEET 4 I 4 GLU A 332 GLN A 334 -1 O ARG A 333 N LEU A 327
SHEET 1 J 9 ARG A 352 SER A 358 0
SHEET 2 J 9 LEU A 361 ILE A 368 -1 O TYR A 367 N ARG A 352
SHEET 3 J 9 TYR A 409 VAL A 413 -1 O ILE A 410 N ILE A 368
SHEET 4 J 9 ALA A 378 VAL A 384 1 N ILE A 381 O TYR A 409
SHEET 5 J 9 ALA A 455 ILE A 465 1 O GLY A 461 N VAL A 380
SHEET 6 J 9 ALA A 484 GLU A 488 1 O ILE A 486 N ILE A 462
SHEET 7 J 9 LEU A 538 SER A 543 1 O ILE A 541 N SER A 487
SHEET 8 J 9 VAL A 568 PHE A 573 1 O TYR A 569 N LEU A 540
SHEET 9 J 9 PHE D 131 GLU D 134 -1 O ILE D 132 N ILE A 572
SHEET 1 K 4 TYR B 16 ARG B 23 0
SHEET 2 K 4 LEU B 26 ASN B 35 -1 O ALA B 28 N ARG B 21
SHEET 3 K 4 LYS B 40 ASN B 49 -1 O THR B 44 N LEU B 31
SHEET 4 K 4 ARG B 55 GLU B 59 -1 O ILE B 58 N ILE B 45
SHEET 1 L 4 SER B 62 ILE B 66 0
SHEET 2 L 4 LYS B 72 ARG B 77 -1 O ALA B 74 N ARG B 65
SHEET 3 L 4 ALA B 85 ASP B 91 -1 O ALA B 90 N ILE B 73
SHEET 4 L 4 ALA B 97 ALA B 103 -1 O ALA B 103 N ALA B 85
SHEET 1 M 4 ILE B 106 TRP B 111 0
SHEET 2 M 4 ARG B 117 LYS B 124 -1 O LEU B 119 N GLU B 110
SHEET 3 M 4 LYS B 151 ASP B 158 -1 O ILE B 157 N LEU B 118
SHEET 4 M 4 GLU B 163 LYS B 170 -1 O GLU B 166 N VAL B 156
SHEET 1 N 9 PHE B 131 GLU B 134 0
SHEET 2 N 9 VAL E 568 PHE E 573 -1 O ILE E 572 N ILE B 132
SHEET 3 N 9 LEU E 538 SER E 543 1 N LEU E 540 O ALA E 571
SHEET 4 N 9 ALA E 484 GLU E 488 1 N SER E 487 O LEU E 539
SHEET 5 N 9 ALA E 455 ILE E 465 1 N GLY E 464 O GLU E 488
SHEET 6 N 9 ALA E 378 VAL E 384 1 N VAL E 380 O GLY E 461
SHEET 7 N 9 TYR E 409 ASN E 414 1 O TYR E 409 N PRO E 379
SHEET 8 N 9 LEU E 361 ILE E 368 -1 N TRP E 366 O TYR E 412
SHEET 9 N 9 ARG E 352 SER E 358 -1 N ARG E 352 O TYR E 367
SHEET 1 O 2 TRP B 140 PHE B 141 0
SHEET 2 O 2 GLY B 145 PHE B 146 -1 O GLY B 145 N PHE B 141
SHEET 1 P 4 SER B 175 HIS B 179 0
SHEET 2 P 4 SER B 182 ARG B 190 -1 O SER B 182 N HIS B 179
SHEET 3 P 4 PRO B 194 LYS B 206 -1 O TYR B 203 N VAL B 185
SHEET 4 P 4 GLU B 209 VAL B 217 -1 O GLU B 211 N LEU B 204
SHEET 1 Q 4 PHE B 219 SER B 224 0
SHEET 2 Q 4 ILE B 229 GLY B 233 -1 O TYR B 232 N TYR B 220
SHEET 3 Q 4 LYS B 245 TYR B 249 -1 O LYS B 245 N GLY B 233
SHEET 4 Q 4 VAL B 253 GLY B 255 -1 O LYS B 254 N ILE B 248
SHEET 1 R 4 VAL B 264 ARG B 270 0
SHEET 2 R 4 LYS B 273 GLU B 280 -1 O TYR B 275 N LYS B 268
SHEET 3 R 4 SER B 283 TRP B 289 -1 O TYR B 287 N PHE B 276
SHEET 4 R 4 VAL B 293 ALA B 297 -1 O ARG B 294 N LEU B 288
SHEET 1 S 4 TRP B 302 ALA B 308 0
SHEET 2 S 4 LEU B 312 GLU B 317 -1 O ILE B 313 N ASP B 307
SHEET 3 S 4 GLU B 324 TRP B 328 -1 O TYR B 326 N TYR B 314
SHEET 4 S 4 GLU B 332 GLN B 334 -1 O ARG B 333 N LEU B 327
SHEET 1 T 9 ARG B 352 SER B 358 0
SHEET 2 T 9 LEU B 361 ILE B 368 -1 O TYR B 367 N ARG B 352
SHEET 3 T 9 TYR B 409 VAL B 413 -1 O TYR B 412 N TRP B 366
SHEET 4 T 9 ALA B 378 VAL B 384 1 N PRO B 379 O TYR B 409
SHEET 5 T 9 ALA B 455 ILE B 465 1 O THR B 463 N VAL B 382
SHEET 6 T 9 ALA B 484 GLU B 488 1 O GLU B 488 N GLY B 464
SHEET 7 T 9 LEU B 538 SER B 543 1 O ILE B 541 N SER B 487
SHEET 8 T 9 VAL B 568 PHE B 573 1 O TYR B 569 N LEU B 540
SHEET 9 T 9 PHE E 131 GLU E 134 -1 O ILE E 132 N ILE B 572
SHEET 1 U 4 TYR C 16 ARG C 23 0
SHEET 2 U 4 LEU C 26 ASN C 35 -1 O VAL C 30 N SER C 18
SHEET 3 U 4 LYS C 40 ASN C 49 -1 O GLU C 48 N VAL C 27
SHEET 4 U 4 ARG C 55 GLU C 59 -1 O ILE C 58 N ILE C 45
SHEET 1 V 4 SER C 62 ILE C 66 0
SHEET 2 V 4 LYS C 72 PHE C 78 -1 O ALA C 74 N ARG C 65
SHEET 3 V 4 ALA C 85 ASP C 91 -1 O TRP C 88 N PHE C 75
SHEET 4 V 4 ALA C 97 GLU C 102 -1 O LEU C 101 N ILE C 87
SHEET 1 W 4 ILE C 106 TRP C 111 0
SHEET 2 W 4 ARG C 117 LYS C 124 -1 O LEU C 119 N GLU C 110
SHEET 3 W 4 LYS C 151 ASP C 158 -1 O TRP C 155 N ALA C 120
SHEET 4 W 4 GLU C 163 LYS C 170 -1 O GLU C 163 N ASP C 158
SHEET 1 X 9 PHE C 131 GLU C 134 0
SHEET 2 X 9 VAL F 568 PHE F 573 -1 O ILE F 572 N ILE C 132
SHEET 3 X 9 LEU F 538 SER F 543 1 N LEU F 540 O TYR F 569
SHEET 4 X 9 ALA F 484 GLU F 488 1 N SER F 487 O ILE F 541
SHEET 5 X 9 ALA F 455 ILE F 465 1 N GLY F 464 O GLU F 488
SHEET 6 X 9 ALA F 378 VAL F 384 1 N VAL F 380 O GLY F 461
SHEET 7 X 9 TYR F 409 VAL F 413 1 O TYR F 409 N PRO F 379
SHEET 8 X 9 LEU F 361 ILE F 368 -1 N TRP F 366 O TYR F 412
SHEET 9 X 9 ARG F 352 SER F 358 -1 N SER F 358 O LEU F 361
SHEET 1 Y 2 TRP C 140 PHE C 141 0
SHEET 2 Y 2 GLY C 145 PHE C 146 -1 O GLY C 145 N PHE C 141
SHEET 1 Z 4 SER C 175 HIS C 179 0
SHEET 2 Z 4 SER C 182 ARG C 190 -1 O SER C 182 N HIS C 179
SHEET 3 Z 4 PRO C 194 LYS C 206 -1 O ARG C 195 N HIS C 189
SHEET 4 Z 4 GLU C 209 VAL C 217 -1 O VAL C 217 N TRP C 200
SHEET 1 AA 4 TYR C 220 SER C 224 0
SHEET 2 AA 4 ILE C 229 GLY C 233 -1 O TYR C 232 N TYR C 220
SHEET 3 AA 4 LYS C 245 TYR C 249 -1 O TYR C 249 N ILE C 229
SHEET 4 AA 4 VAL C 253 GLY C 255 -1 O LYS C 254 N ILE C 248
SHEET 1 AB 4 GLU C 263 ARG C 270 0
SHEET 2 AB 4 LYS C 273 GLU C 280 -1 O LYS C 273 N ARG C 270
SHEET 3 AB 4 SER C 283 TRP C 289 -1 O TYR C 287 N PHE C 276
SHEET 4 AB 4 VAL C 293 ALA C 297 -1 O ARG C 294 N LEU C 288
SHEET 1 AC 4 TRP C 302 ALA C 308 0
SHEET 2 AC 4 LEU C 312 GLU C 317 -1 O GLU C 317 N TRP C 302
SHEET 3 AC 4 GLU C 324 TRP C 328 -1 O TYR C 326 N TYR C 314
SHEET 4 AC 4 GLU C 332 GLN C 334 -1 O ARG C 333 N LEU C 327
SHEET 1 AD 9 ARG C 352 SER C 358 0
SHEET 2 AD 9 LEU C 361 ILE C 368 -1 O TYR C 367 N ARG C 352
SHEET 3 AD 9 TYR C 409 VAL C 413 -1 O ILE C 410 N ILE C 368
SHEET 4 AD 9 ALA C 378 VAL C 384 1 N ILE C 381 O TYR C 409
SHEET 5 AD 9 ALA C 455 ILE C 465 1 O GLY C 461 N VAL C 380
SHEET 6 AD 9 ALA C 484 GLU C 488 1 O GLU C 488 N GLY C 464
SHEET 7 AD 9 LEU C 538 SER C 543 1 O ILE C 541 N SER C 487
SHEET 8 AD 9 VAL C 568 PHE C 573 1 O PHE C 573 N HIS C 542
SHEET 9 AD 9 PHE F 131 GLU F 134 -1 O ILE F 132 N ILE C 572
SHEET 1 AE 4 TYR D 16 ARG D 23 0
SHEET 2 AE 4 LEU D 26 ASN D 35 -1 O LEU D 26 N ARG D 23
SHEET 3 AE 4 LYS D 40 ASN D 49 -1 O THR D 44 N LEU D 31
SHEET 4 AE 4 SER D 54 GLU D 59 -1 O LYS D 56 N ILE D 47
SHEET 1 AF 4 SER D 62 ILE D 66 0
SHEET 2 AF 4 LYS D 72 PHE D 78 -1 O ALA D 74 N ARG D 65
SHEET 3 AF 4 ALA D 85 ASP D 91 -1 O TRP D 88 N PHE D 75
SHEET 4 AF 4 ALA D 97 GLU D 102 -1 O LYS D 98 N VAL D 89
SHEET 1 AG 4 ILE D 106 TRP D 111 0
SHEET 2 AG 4 ARG D 117 LYS D 124 -1 O LEU D 119 N GLU D 110
SHEET 3 AG 4 LYS D 151 ASP D 158 -1 O TRP D 155 N ALA D 120
SHEET 4 AG 4 GLU D 163 LYS D 170 -1 O PHE D 168 N PHE D 154
SHEET 1 AH 2 TRP D 140 PHE D 141 0
SHEET 2 AH 2 GLY D 145 PHE D 146 -1 O GLY D 145 N PHE D 141
SHEET 1 AI 4 SER D 175 HIS D 179 0
SHEET 2 AI 4 SER D 182 PRO D 188 -1 O SER D 182 N HIS D 179
SHEET 3 AI 4 TRP D 200 LYS D 206 -1 O ASP D 201 N VAL D 187
SHEET 4 AI 4 GLU D 209 VAL D 217 -1 O GLU D 211 N LEU D 204
SHEET 1 AJ 4 PHE D 219 SER D 224 0
SHEET 2 AJ 4 ILE D 229 GLY D 233 -1 O LEU D 230 N ASP D 223
SHEET 3 AJ 4 LYS D 245 TYR D 249 -1 O TYR D 249 N ILE D 229
SHEET 4 AJ 4 VAL D 253 GLY D 255 -1 O LYS D 254 N ILE D 248
SHEET 1 AK 4 VAL D 264 ARG D 270 0
SHEET 2 AK 4 LYS D 273 GLU D 280 -1 O TYR D 275 N LYS D 268
SHEET 3 AK 4 SER D 283 TRP D 289 -1 O SER D 283 N GLU D 280
SHEET 4 AK 4 VAL D 293 ALA D 297 -1 O ILE D 296 N LEU D 286
SHEET 1 AL 4 TRP D 302 ALA D 308 0
SHEET 2 AL 4 LEU D 312 GLU D 317 -1 O GLU D 317 N TRP D 302
SHEET 3 AL 4 GLU D 324 TRP D 328 -1 O TRP D 328 N LEU D 312
SHEET 4 AL 4 GLU D 332 GLN D 334 -1 O ARG D 333 N LEU D 327
SHEET 1 AM 4 TYR E 16 ARG E 23 0
SHEET 2 AM 4 LEU E 26 ASN E 35 -1 O ALA E 28 N ARG E 21
SHEET 3 AM 4 LYS E 40 ASN E 49 -1 O GLU E 48 N VAL E 27
SHEET 4 AM 4 ARG E 55 GLU E 59 -1 O ILE E 58 N ILE E 45
SHEET 1 AN 4 SER E 62 ILE E 66 0
SHEET 2 AN 4 LYS E 72 ARG E 77 -1 O ALA E 74 N ARG E 65
SHEET 3 AN 4 ALA E 85 ASP E 91 -1 O ALA E 90 N ILE E 73
SHEET 4 AN 4 ALA E 97 ALA E 103 -1 O LEU E 101 N ILE E 87
SHEET 1 AO 4 ILE E 106 TRP E 111 0
SHEET 2 AO 4 ARG E 117 LYS E 124 -1 O LEU E 119 N GLU E 110
SHEET 3 AO 4 LYS E 151 ASP E 158 -1 O ILE E 157 N LEU E 118
SHEET 4 AO 4 GLU E 163 LYS E 170 -1 O GLU E 163 N ASP E 158
SHEET 1 AP 2 TRP E 140 PHE E 141 0
SHEET 2 AP 2 GLY E 145 PHE E 146 -1 O GLY E 145 N PHE E 141
SHEET 1 AQ 4 SER E 175 HIS E 179 0
SHEET 2 AQ 4 SER E 182 PRO E 188 -1 O SER E 182 N HIS E 179
SHEET 3 AQ 4 TRP E 200 LYS E 206 -1 O ASP E 201 N VAL E 187
SHEET 4 AQ 4 GLU E 209 VAL E 217 -1 O GLU E 209 N LYS E 206
SHEET 1 AR 4 PHE E 219 SER E 224 0
SHEET 2 AR 4 ILE E 229 GLY E 233 -1 O TYR E 232 N TYR E 220
SHEET 3 AR 4 LYS E 245 TYR E 249 -1 O TYR E 247 N LEU E 231
SHEET 4 AR 4 VAL E 253 GLY E 255 -1 O LYS E 254 N ILE E 248
SHEET 1 AS 4 GLU E 263 ARG E 270 0
SHEET 2 AS 4 LYS E 273 GLU E 280 -1 O TYR E 275 N LYS E 268
SHEET 3 AS 4 SER E 283 TRP E 289 -1 O TRP E 289 N VAL E 274
SHEET 4 AS 4 VAL E 293 ALA E 297 -1 O ARG E 294 N LEU E 288
SHEET 1 AT 4 TRP E 302 ALA E 308 0
SHEET 2 AT 4 LEU E 312 GLU E 317 -1 O GLU E 317 N TRP E 302
SHEET 3 AT 4 GLU E 324 TRP E 328 -1 O TRP E 328 N LEU E 312
SHEET 4 AT 4 GLU E 332 GLN E 334 -1 O ARG E 333 N LEU E 327
SHEET 1 AU 4 TYR F 16 ARG F 23 0
SHEET 2 AU 4 LEU F 26 ASN F 35 -1 O LEU F 26 N ARG F 23
SHEET 3 AU 4 LYS F 40 ASN F 49 -1 O THR F 44 N LEU F 31
SHEET 4 AU 4 ARG F 55 GLU F 59 -1 O LYS F 56 N ILE F 47
SHEET 1 AV 4 SER F 62 ILE F 66 0
SHEET 2 AV 4 LYS F 72 ARG F 77 -1 O ALA F 74 N ARG F 65
SHEET 3 AV 4 GLN F 86 ASP F 91 -1 O ALA F 90 N ILE F 73
SHEET 4 AV 4 ALA F 97 GLU F 102 -1 O LEU F 101 N ILE F 87
SHEET 1 AW 4 ILE F 106 TRP F 111 0
SHEET 2 AW 4 ARG F 117 LYS F 124 -1 O LEU F 119 N GLU F 110
SHEET 3 AW 4 LYS F 151 ASP F 158 -1 O ILE F 157 N LEU F 118
SHEET 4 AW 4 VAL F 164 LYS F 170 -1 O GLU F 166 N VAL F 156
SHEET 1 AX 2 TRP F 140 PHE F 141 0
SHEET 2 AX 2 GLY F 145 PHE F 146 -1 O GLY F 145 N PHE F 141
SHEET 1 AY 4 SER F 175 HIS F 179 0
SHEET 2 AY 4 SER F 182 PRO F 188 -1 O SER F 182 N HIS F 179
SHEET 3 AY 4 TRP F 200 LYS F 206 -1 O TRP F 205 N ILE F 183
SHEET 4 AY 4 GLU F 209 VAL F 217 -1 O GLU F 211 N LEU F 204
SHEET 1 AZ 4 PHE F 219 SER F 224 0
SHEET 2 AZ 4 ILE F 229 GLY F 233 -1 O LEU F 230 N ASP F 223
SHEET 3 AZ 4 LYS F 245 TYR F 249 -1 O TYR F 247 N LEU F 231
SHEET 4 AZ 4 VAL F 253 GLY F 255 -1 O LYS F 254 N ILE F 248
SHEET 1 BA 4 VAL F 264 ARG F 270 0
SHEET 2 BA 4 LYS F 273 GLU F 280 -1 O TYR F 275 N LYS F 268
SHEET 3 BA 4 SER F 283 TRP F 289 -1 O TYR F 287 N PHE F 276
SHEET 4 BA 4 VAL F 293 ALA F 297 -1 O ARG F 294 N LEU F 288
SHEET 1 BB 4 TRP F 302 ALA F 308 0
SHEET 2 BB 4 LEU F 312 GLU F 317 -1 O GLU F 317 N TRP F 302
SHEET 3 BB 4 GLU F 324 TRP F 328 -1 O TYR F 326 N TYR F 314
SHEET 4 BB 4 GLU F 332 GLN F 334 -1 O ARG F 333 N LEU F 327
SHEET 1 BC 4 TYR G 16 ARG G 23 0
SHEET 2 BC 4 LEU G 26 ASN G 35 -1 O THR G 32 N TYR G 16
SHEET 3 BC 4 LYS G 40 ASN G 49 -1 O THR G 44 N LEU G 31
SHEET 4 BC 4 ARG G 55 GLU G 59 -1 O ILE G 58 N ILE G 45
SHEET 1 BD 4 SER G 62 ILE G 66 0
SHEET 2 BD 4 LYS G 72 ARG G 77 -1 O ALA G 74 N ARG G 65
SHEET 3 BD 4 ALA G 85 ASP G 91 -1 O GLN G 86 N ARG G 77
SHEET 4 BD 4 ALA G 97 ALA G 103 -1 O LEU G 101 N ILE G 87
SHEET 1 BE 4 ILE G 106 TRP G 111 0
SHEET 2 BE 4 ARG G 117 LYS G 124 -1 O LEU G 119 N GLU G 110
SHEET 3 BE 4 LYS G 151 ASP G 158 -1 O TRP G 155 N ALA G 120
SHEET 4 BE 4 GLU G 163 LYS G 170 -1 O PHE G 168 N PHE G 154
SHEET 1 BF 8 PHE G 131 GLU G 134 0
SHEET 2 BF 8 VAL J 568 PHE J 573 -1 O ILE J 572 N ILE G 132
SHEET 3 BF 8 LEU J 538 SER J 543 1 N LEU J 540 O TYR J 569
SHEET 4 BF 8 ALA J 484 GLU J 488 1 N SER J 487 O ILE J 541
SHEET 5 BF 8 ALA J 455 ILE J 465 1 N ILE J 462 O ILE J 486
SHEET 6 BF 8 ALA J 378 VAL J 384 1 N VAL J 382 O GLY J 461
SHEET 7 BF 8 TYR J 409 VAL J 413 1 O TYR J 409 N PRO J 379
SHEET 8 BF 8 GLY J 365 ILE J 368 -1 N TRP J 366 O TYR J 412
SHEET 1 BG 2 TRP G 140 PHE G 141 0
SHEET 2 BG 2 GLY G 145 PHE G 146 -1 O GLY G 145 N PHE G 141
SHEET 1 BH 7 SER G 175 HIS G 179 0
SHEET 2 BH 7 SER G 182 PRO G 188 -1 O SER G 182 N HIS G 179
SHEET 3 BH 7 TRP G 200 LYS G 206 -1 O ASP G 201 N VAL G 187
SHEET 4 BH 7 GLU G 209 SER G 224 -1 O GLU G 209 N LYS G 206
SHEET 5 BH 7 ILE G 229 LYS G 234 -1 O TYR G 232 N TYR G 220
SHEET 6 BH 7 LYS G 245 TYR G 249 -1 O TYR G 247 N LEU G 231
SHEET 7 BH 7 VAL G 253 GLY G 255 -1 O LYS G 254 N ILE G 248
SHEET 1 BI 4 VAL G 264 ARG G 270 0
SHEET 2 BI 4 LYS G 273 GLU G 280 -1 O TYR G 275 N LYS G 268
SHEET 3 BI 4 SER G 283 TRP G 289 -1 O TYR G 287 N PHE G 276
SHEET 4 BI 4 VAL G 293 ALA G 297 -1 O ILE G 296 N LEU G 286
SHEET 1 BJ 4 TRP G 302 ALA G 308 0
SHEET 2 BJ 4 LEU G 312 THR G 318 -1 O GLU G 317 N TRP G 302
SHEET 3 BJ 4 ARG G 321 TRP G 328 -1 O TYR G 326 N TYR G 314
SHEET 4 BJ 4 GLU G 332 GLN G 334 -1 O ARG G 333 N LEU G 327
SHEET 1 BK 9 ARG G 352 SER G 358 0
SHEET 2 BK 9 LEU G 361 ILE G 368 -1 O TYR G 367 N ARG G 352
SHEET 3 BK 9 TYR G 409 VAL G 413 -1 O TYR G 412 N TRP G 366
SHEET 4 BK 9 VAL G 380 VAL G 384 1 N ILE G 381 O TYR G 409
SHEET 5 BK 9 ILE G 460 ILE G 465 1 O GLY G 461 N VAL G 380
SHEET 6 BK 9 ALA G 484 GLU G 488 1 O GLU G 488 N GLY G 464
SHEET 7 BK 9 LEU G 538 SER G 543 1 O LEU G 539 N SER G 487
SHEET 8 BK 9 VAL G 568 PHE G 573 1 O PHE G 573 N HIS G 542
SHEET 9 BK 9 PHE J 131 GLU J 134 -1 O ILE J 132 N ILE G 572
SHEET 1 BL 4 TYR H 16 ARG H 23 0
SHEET 2 BL 4 LEU H 26 ASN H 35 -1 O VAL H 30 N SER H 18
SHEET 3 BL 4 LYS H 40 ASN H 49 -1 O GLU H 48 N VAL H 27
SHEET 4 BL 4 SER H 54 GLU H 59 -1 O LYS H 56 N ILE H 47
SHEET 1 BM 4 SER H 62 ILE H 66 0
SHEET 2 BM 4 LYS H 72 ARG H 77 -1 O ALA H 74 N ARG H 65
SHEET 3 BM 4 ALA H 85 ASP H 91 -1 O TRP H 88 N PHE H 75
SHEET 4 BM 4 ALA H 97 ALA H 103 -1 O VAL H 100 N ILE H 87
SHEET 1 BN 4 ILE H 106 TRP H 111 0
SHEET 2 BN 4 ARG H 117 LYS H 124 -1 O LEU H 119 N GLU H 110
SHEET 3 BN 4 LYS H 151 ASP H 158 -1 O TRP H 155 N ALA H 120
SHEET 4 BN 4 GLU H 163 LYS H 170 -1 O GLU H 163 N ASP H 158
SHEET 1 BO 9 PHE H 131 GLU H 134 0
SHEET 2 BO 9 VAL K 568 PHE K 573 -1 O ILE K 572 N ILE H 132
SHEET 3 BO 9 LEU K 538 SER K 543 1 N HIS K 542 O PHE K 573
SHEET 4 BO 9 ALA K 484 GLU K 488 1 N SER K 487 O ILE K 541
SHEET 5 BO 9 ALA K 455 ILE K 465 1 N ILE K 462 O ILE K 486
SHEET 6 BO 9 ALA K 378 VAL K 384 1 N VAL K 380 O GLY K 461
SHEET 7 BO 9 TYR K 409 VAL K 413 1 O TYR K 409 N ILE K 381
SHEET 8 BO 9 LEU K 361 ILE K 368 -1 N TRP K 366 O TYR K 412
SHEET 9 BO 9 ARG K 352 SER K 358 -1 N PHE K 356 O LEU K 363
SHEET 1 BP 2 TRP H 140 PHE H 141 0
SHEET 2 BP 2 GLY H 145 PHE H 146 -1 O GLY H 145 N PHE H 141
SHEET 1 BQ 4 SER H 175 HIS H 179 0
SHEET 2 BQ 4 SER H 182 PRO H 188 -1 O SER H 182 N HIS H 179
SHEET 3 BQ 4 TRP H 200 LYS H 206 -1 O ASP H 201 N VAL H 187
SHEET 4 BQ 4 GLU H 209 VAL H 217 -1 O GLU H 209 N LYS H 206
SHEET 1 BR 4 PHE H 219 SER H 224 0
SHEET 2 BR 4 ILE H 229 GLY H 233 -1 O LEU H 230 N ILE H 222
SHEET 3 BR 4 LYS H 245 TYR H 249 -1 O TYR H 247 N LEU H 231
SHEET 4 BR 4 VAL H 253 GLY H 255 -1 O LYS H 254 N ILE H 248
SHEET 1 BS 4 GLU H 263 ARG H 270 0
SHEET 2 BS 4 LYS H 273 GLU H 280 -1 O LYS H 273 N ARG H 270
SHEET 3 BS 4 SER H 283 TRP H 289 -1 O TYR H 287 N PHE H 276
SHEET 4 BS 4 VAL H 293 ALA H 297 -1 O ARG H 294 N LEU H 288
SHEET 1 BT 3 TRP H 302 ILE H 303 0
SHEET 2 BT 3 LEU H 312 GLU H 317 -1 O GLU H 317 N TRP H 302
SHEET 3 BT 3 ASP H 307 ALA H 308 -1 N ASP H 307 O ILE H 313
SHEET 1 BU 4 TRP H 302 ILE H 303 0
SHEET 2 BU 4 LEU H 312 GLU H 317 -1 O GLU H 317 N TRP H 302
SHEET 3 BU 4 GLU H 324 TRP H 328 -1 O TYR H 326 N TYR H 314
SHEET 4 BU 4 GLU H 332 GLN H 334 -1 O ARG H 333 N LEU H 327
SHEET 1 BV 9 ARG H 352 SER H 358 0
SHEET 2 BV 9 LEU H 361 ILE H 368 -1 O LEU H 363 N PHE H 356
SHEET 3 BV 9 TYR H 409 VAL H 413 -1 O ILE H 410 N ILE H 368
SHEET 4 BV 9 ALA H 378 VAL H 384 1 N ILE H 381 O TYR H 409
SHEET 5 BV 9 ALA H 455 ILE H 465 1 O GLY H 461 N VAL H 380
SHEET 6 BV 9 ALA H 484 GLU H 488 1 O GLU H 488 N GLY H 464
SHEET 7 BV 9 LEU H 538 SER H 543 1 O ILE H 541 N SER H 487
SHEET 8 BV 9 VAL H 568 PHE H 573 1 O TYR H 569 N LEU H 540
SHEET 9 BV 9 PHE K 131 GLU K 134 -1 O ILE K 132 N ILE H 572
SHEET 1 BW 4 TYR I 16 ARG I 23 0
SHEET 2 BW 4 LEU I 26 ASN I 35 -1 O ALA I 28 N ARG I 21
SHEET 3 BW 4 LYS I 40 ASN I 49 -1 O THR I 44 N LEU I 31
SHEET 4 BW 4 ARG I 55 GLU I 59 -1 O ILE I 58 N ILE I 45
SHEET 1 BX 4 SER I 62 ILE I 66 0
SHEET 2 BX 4 LYS I 72 ARG I 77 -1 O ALA I 74 N ARG I 65
SHEET 3 BX 4 ALA I 85 ASP I 91 -1 O TRP I 88 N PHE I 75
SHEET 4 BX 4 ALA I 97 ALA I 103 -1 O LEU I 101 N ILE I 87
SHEET 1 BY 4 ILE I 106 TRP I 111 0
SHEET 2 BY 4 ARG I 117 LYS I 124 -1 O LEU I 119 N GLU I 110
SHEET 3 BY 4 LYS I 151 ASP I 158 -1 O TRP I 155 N ALA I 120
SHEET 4 BY 4 GLU I 163 LYS I 170 -1 O GLU I 166 N VAL I 156
SHEET 1 BZ 9 PHE I 131 GLU I 134 0
SHEET 2 BZ 9 VAL L 568 PHE L 573 -1 O ILE L 572 N ILE I 132
SHEET 3 BZ 9 LEU L 538 SER L 543 1 N LEU L 540 O TYR L 569
SHEET 4 BZ 9 ALA L 484 GLU L 488 1 N SER L 487 O ILE L 541
SHEET 5 BZ 9 ALA L 455 ILE L 465 1 N GLY L 464 O GLU L 488
SHEET 6 BZ 9 ALA L 378 VAL L 384 1 N VAL L 380 O GLY L 461
SHEET 7 BZ 9 TYR L 409 VAL L 413 1 O TYR L 409 N ILE L 381
SHEET 8 BZ 9 LEU L 361 ILE L 368 -1 N TRP L 366 O TYR L 412
SHEET 9 BZ 9 ARG L 352 SER L 358 -1 N PHE L 354 O GLY L 365
SHEET 1 CA 2 TRP I 140 PHE I 141 0
SHEET 2 CA 2 GLY I 145 PHE I 146 -1 O GLY I 145 N PHE I 141
SHEET 1 CB 4 SER I 175 HIS I 179 0
SHEET 2 CB 4 SER I 182 PRO I 188 -1 O SER I 182 N HIS I 179
SHEET 3 CB 4 TRP I 200 LYS I 206 -1 O TRP I 205 N ILE I 183
SHEET 4 CB 4 GLU I 209 VAL I 217 -1 O GLU I 209 N LYS I 206
SHEET 1 CC 4 PHE I 219 SER I 224 0
SHEET 2 CC 4 ILE I 229 GLY I 233 -1 O LEU I 230 N ASP I 223
SHEET 3 CC 4 LYS I 245 TYR I 249 -1 O TYR I 247 N LEU I 231
SHEET 4 CC 4 VAL I 253 GLY I 255 -1 O LYS I 254 N ILE I 248
SHEET 1 CD 4 VAL I 264 ARG I 270 0
SHEET 2 CD 4 LYS I 273 GLU I 280 -1 O LYS I 273 N ARG I 270
SHEET 3 CD 4 SER I 283 TRP I 289 -1 O SER I 283 N GLU I 280
SHEET 4 CD 4 VAL I 293 ALA I 297 -1 O ILE I 296 N LEU I 286
SHEET 1 CE 4 TRP I 302 ALA I 308 0
SHEET 2 CE 4 LEU I 312 GLU I 317 -1 O GLU I 317 N TRP I 302
SHEET 3 CE 4 GLU I 324 TRP I 328 -1 O TYR I 326 N TYR I 314
SHEET 4 CE 4 GLU I 332 GLN I 334 -1 O ARG I 333 N LEU I 327
SHEET 1 CF 9 ARG I 352 SER I 358 0
SHEET 2 CF 9 LEU I 361 ILE I 368 -1 O TYR I 367 N ARG I 352
SHEET 3 CF 9 TYR I 409 VAL I 413 -1 O ILE I 410 N ILE I 368
SHEET 4 CF 9 ALA I 378 VAL I 384 1 N PRO I 379 O TYR I 409
SHEET 5 CF 9 ALA I 455 ILE I 465 1 O GLY I 461 N VAL I 380
SHEET 6 CF 9 ALA I 484 GLU I 488 1 O GLU I 488 N GLY I 464
SHEET 7 CF 9 LEU I 538 SER I 543 1 O ILE I 541 N SER I 487
SHEET 8 CF 9 VAL I 568 PHE I 573 1 O PHE I 573 N HIS I 542
SHEET 9 CF 9 PHE L 131 GLU L 134 -1 O ILE L 132 N ILE I 572
SHEET 1 CG 4 TYR J 16 ARG J 23 0
SHEET 2 CG 4 LEU J 26 ASN J 35 -1 O THR J 32 N TYR J 16
SHEET 3 CG 4 LYS J 40 ASN J 49 -1 O GLU J 48 N VAL J 27
SHEET 4 CG 4 ARG J 55 GLU J 59 -1 O ILE J 58 N ILE J 45
SHEET 1 CH 4 SER J 62 ILE J 66 0
SHEET 2 CH 4 LYS J 72 ARG J 77 -1 O MET J 76 N SER J 62
SHEET 3 CH 4 GLN J 86 ASP J 91 -1 O ALA J 90 N ILE J 73
SHEET 4 CH 4 ALA J 97 GLU J 102 -1 O LEU J 101 N ILE J 87
SHEET 1 CI 4 ILE J 106 TRP J 111 0
SHEET 2 CI 4 ARG J 117 LYS J 124 -1 O LEU J 119 N GLU J 110
SHEET 3 CI 4 LYS J 151 ASP J 158 -1 O LYS J 151 N LYS J 124
SHEET 4 CI 4 GLU J 163 LYS J 170 -1 O GLU J 166 N VAL J 156
SHEET 1 CJ 2 TRP J 140 PHE J 141 0
SHEET 2 CJ 2 GLY J 145 PHE J 146 -1 O GLY J 145 N PHE J 141
SHEET 1 CK 4 TRP J 178 HIS J 179 0
SHEET 2 CK 4 SER J 182 PRO J 188 -1 O SER J 182 N HIS J 179
SHEET 3 CK 4 TRP J 200 LYS J 206 -1 O ASP J 201 N VAL J 187
SHEET 4 CK 4 GLU J 209 GLU J 210 -1 O GLU J 209 N LYS J 206
SHEET 1 CL 4 PHE J 219 SER J 224 0
SHEET 2 CL 4 ILE J 229 GLY J 233 -1 O LEU J 230 N ASP J 223
SHEET 3 CL 4 LYS J 245 TYR J 249 -1 O TYR J 247 N LEU J 231
SHEET 4 CL 4 VAL J 253 GLY J 255 -1 O LYS J 254 N ILE J 248
SHEET 1 CM 4 VAL J 264 ARG J 270 0
SHEET 2 CM 4 LYS J 273 GLU J 280 -1 O LYS J 273 N ARG J 270
SHEET 3 CM 4 SER J 283 TRP J 289 -1 O SER J 283 N GLU J 280
SHEET 4 CM 4 VAL J 293 ALA J 297 -1 O ARG J 294 N LEU J 288
SHEET 1 CN 4 TRP J 302 ALA J 308 0
SHEET 2 CN 4 LEU J 312 GLU J 317 -1 O GLU J 317 N TRP J 302
SHEET 3 CN 4 GLU J 324 TRP J 328 -1 O TYR J 326 N TYR J 314
SHEET 4 CN 4 GLU J 332 GLN J 334 -1 O ARG J 333 N LEU J 327
SHEET 1 CO 2 PHE J 356 SER J 358 0
SHEET 2 CO 2 LEU J 361 LEU J 363 -1 O LEU J 361 N SER J 358
SHEET 1 CP 4 ALA K 15 ARG K 23 0
SHEET 2 CP 4 LEU K 26 ASN K 35 -1 O ALA K 28 N ARG K 21
SHEET 3 CP 4 LYS K 40 ASN K 49 -1 O GLU K 42 N LYS K 33
SHEET 4 CP 4 ARG K 55 GLU K 59 -1 O ILE K 58 N ILE K 45
SHEET 1 CQ 4 SER K 62 ILE K 66 0
SHEET 2 CQ 4 LYS K 72 ARG K 77 -1 O ALA K 74 N ARG K 65
SHEET 3 CQ 4 GLN K 86 ASP K 91 -1 O ALA K 90 N ILE K 73
SHEET 4 CQ 4 SER K 96 GLU K 102 -1 O LEU K 101 N ILE K 87
SHEET 1 CR 4 ILE K 106 TRP K 111 0
SHEET 2 CR 4 ARG K 117 LYS K 124 -1 O LEU K 119 N GLU K 110
SHEET 3 CR 4 LYS K 151 ASP K 158 -1 O TRP K 155 N ALA K 120
SHEET 4 CR 4 GLU K 163 LYS K 170 -1 O PHE K 168 N PHE K 154
SHEET 1 CS 2 TRP K 140 PHE K 141 0
SHEET 2 CS 2 GLY K 145 PHE K 146 -1 O GLY K 145 N PHE K 141
SHEET 1 CT 4 SER K 175 HIS K 179 0
SHEET 2 CT 4 SER K 182 ARG K 190 -1 O SER K 182 N HIS K 179
SHEET 3 CT 4 PRO K 194 LYS K 206 -1 O TRP K 205 N ILE K 183
SHEET 4 CT 4 GLU K 209 GLU K 215 -1 O GLU K 209 N LYS K 206
SHEET 1 CU 4 PHE K 219 SER K 224 0
SHEET 2 CU 4 ILE K 229 GLY K 233 -1 O TYR K 232 N TYR K 220
SHEET 3 CU 4 LYS K 245 TYR K 249 -1 O TYR K 247 N LEU K 231
SHEET 4 CU 4 VAL K 253 GLY K 255 -1 O LYS K 254 N ILE K 248
SHEET 1 CV 4 GLU K 263 ARG K 270 0
SHEET 2 CV 4 LYS K 273 GLU K 280 -1 O LYS K 273 N ARG K 270
SHEET 3 CV 4 SER K 283 TRP K 289 -1 O TRP K 289 N VAL K 274
SHEET 4 CV 4 VAL K 293 ALA K 297 -1 O ALA K 297 N LEU K 286
SHEET 1 CW 4 TRP K 302 ALA K 308 0
SHEET 2 CW 4 LEU K 312 GLU K 317 -1 O GLU K 317 N TRP K 302
SHEET 3 CW 4 GLU K 324 TRP K 328 -1 O TYR K 326 N TYR K 314
SHEET 4 CW 4 GLU K 332 GLN K 334 -1 O ARG K 333 N LEU K 327
SHEET 1 CX 4 TYR L 16 ARG L 23 0
SHEET 2 CX 4 LEU L 26 ASN L 35 -1 O ALA L 28 N ARG L 21
SHEET 3 CX 4 LYS L 40 ASN L 49 -1 O THR L 44 N LEU L 31
SHEET 4 CX 4 ARG L 55 GLU L 59 -1 O LYS L 56 N ILE L 47
SHEET 1 CY 4 SER L 62 ILE L 66 0
SHEET 2 CY 4 LYS L 72 ARG L 77 -1 O ALA L 74 N ARG L 65
SHEET 3 CY 4 GLN L 86 ASP L 91 -1 O ALA L 90 N ILE L 73
SHEET 4 CY 4 ALA L 97 GLU L 102 -1 O LEU L 101 N ILE L 87
SHEET 1 CZ 4 ILE L 106 TRP L 111 0
SHEET 2 CZ 4 ARG L 117 LYS L 124 -1 O LEU L 119 N GLU L 110
SHEET 3 CZ 4 LYS L 151 ASP L 158 -1 O THR L 153 N GLY L 122
SHEET 4 CZ 4 GLU L 163 LYS L 170 -1 O PHE L 168 N PHE L 154
SHEET 1 DA 2 TRP L 140 PHE L 141 0
SHEET 2 DA 2 GLY L 145 PHE L 146 -1 O GLY L 145 N PHE L 141
SHEET 1 DB 7 SER L 175 HIS L 179 0
SHEET 2 DB 7 SER L 182 PRO L 188 -1 O SER L 182 N HIS L 179
SHEET 3 DB 7 TRP L 200 LYS L 206 -1 O ASP L 201 N VAL L 187
SHEET 4 DB 7 GLU L 209 SER L 224 -1 O GLU L 211 N LEU L 204
SHEET 5 DB 7 ILE L 229 LYS L 234 -1 O TYR L 232 N TYR L 220
SHEET 6 DB 7 LYS L 245 TYR L 249 -1 O LYS L 245 N GLY L 233
SHEET 7 DB 7 VAL L 253 LYS L 254 -1 O LYS L 254 N ILE L 248
SHEET 1 DC 4 GLU L 263 ARG L 270 0
SHEET 2 DC 4 LYS L 273 GLU L 280 -1 O TYR L 275 N LYS L 268
SHEET 3 DC 4 SER L 283 TRP L 289 -1 O SER L 283 N GLU L 280
SHEET 4 DC 4 VAL L 293 ALA L 297 -1 O ARG L 294 N LEU L 288
SHEET 1 DD 4 TRP L 302 ALA L 308 0
SHEET 2 DD 4 LEU L 312 GLU L 317 -1 O GLU L 317 N TRP L 302
SHEET 3 DD 4 GLU L 324 TRP L 328 -1 O GLU L 324 N LYS L 316
SHEET 4 DD 4 GLU L 332 GLN L 334 -1 O ARG L 333 N LEU L 327
LINK OE1 GLU G 162 MG MG G 702 1555 1555 2.21
LINK OE1 GLU D 162 MG MG D 710 1555 1555 2.29
LINK OE1 GLU F 162 MG MG F 705 1555 1555 2.30
LINK O LYS A 99 MG MG A 704 1555 1555 2.33
LINK OD2 ASP I 244 MG MG I 704 1555 1555 2.35
LINK O LYS F 99 MG MG F 705 1555 1555 2.35
LINK O LYS H 99 MG MG H 703 1555 1555 2.35
LINK OE1 GLU E 162 MG MG E 705 1555 1555 2.38
LINK OE1 GLU I 162 MG MG I 703 1555 1555 2.38
LINK O LYS B 99 MG MG B 703 1555 1555 2.39
LINK OE1 GLU B 162 MG MG B 703 1555 1555 2.40
LINK OD2 ASP D 244 MG MG D 709 1555 1555 2.41
LINK OE1 GLU H 162 MG MG H 703 1555 1555 2.43
LINK OE2 GLU C 263 MG MG C 703 1555 1555 2.45
LINK OE1 GLU C 162 MG MG C 702 1555 1555 2.45
LINK OD2 ASP H 244 MG MG H 702 1555 1555 2.45
LINK OD2 ASP E 244 MG MG E 704 1555 1555 2.48
LINK O LYS I 99 MG MG I 703 1555 1555 2.52
LINK O LYS E 99 MG MG E 705 1555 1555 2.53
LINK OE1 GLU A 162 MG MG A 704 1555 1555 2.54
LINK OD2 ASP C 244 MG MG C 703 1555 1555 2.55
LINK OD2 ASP F 244 MG MG F 704 1555 1555 2.61
LINK O LYS G 99 MG MG G 702 1555 1555 2.64
LINK OD2 ASP A 244 MG MG A 705 1555 1555 2.67
LINK OE2 GLU H 263 MG MG H 702 1555 1555 2.69
LINK O LYS L 99 MG MG L 703 1555 1555 2.73
LINK OE2 GLU E 263 MG MG E 704 1555 1555 2.73
LINK O LYS C 99 MG MG C 702 1555 1555 2.75
LINK OE2 GLU I 263 MG MG I 704 1555 1555 2.75
LINK OE1 GLU L 162 MG MG L 703 1555 1555 2.80
LINK OE1 GLU H 263 MG MG H 702 1555 1555 2.80
LINK OE1 GLU H 42 MG MG I 703 1555 1555 2.82
LINK OD2 ASP G 244 MG MG G 703 1555 1555 2.84
LINK OE1 GLU L 263 MG MG L 702 1555 1555 2.86
LINK OE2 GLU L 162 MG MG L 703 1555 1555 2.86
LINK OE2 GLU A 263 MG MG A 705 1555 1555 2.87
LINK OE1 GLU D 263 MG MG D 709 1555 1555 2.88
LINK OE1 GLU E 263 MG MG E 704 1555 1555 2.91
LINK OE2 GLU G 263 MG MG G 703 1555 1555 2.94
LINK OE1 GLU B 42 MG MG C 702 1555 1555 2.94
LINK OE2 GLU F 263 MG MG F 704 1555 1555 2.95
LINK OE2 GLU D 263 MG MG D 709 1555 1555 2.99
LINK MG MG I 703 O HOH I 834 1555 1555 2.31
LINK MG MG B 703 O HOH A 854 1555 1555 2.33
LINK MG MG E 705 O HOH F 872 1555 1555 2.33
LINK MG MG C 702 O HOH C 801 1555 1555 2.34
LINK MG MG L 702 O HOH L 851 1555 1555 2.35
LINK MG MG E 705 O HOH E 919 1555 1555 2.35
LINK MG MG D 710 O HOH D1021 1555 1555 2.36
LINK MG MG A 704 O HOH A 938 1555 1555 2.36
LINK MG MG D 709 O HOH D 802 1555 1555 2.37
LINK MG MG F 705 O HOH D 856 1555 1555 2.38
LINK MG MG F 705 O HOH F 879 1555 1555 2.40
LINK MG MG F 705 O HOH D 939 1555 1555 2.42
LINK MG MG A 705 O HOH A 947 1555 1555 2.43
LINK MG MG L 703 O HOH J 707 1555 1555 2.43
LINK MG MG I 703 O BHOH I 833 1555 1555 2.44
LINK MG MG F 705 O HOH D 940 1555 1555 2.44
LINK MG MG A 704 O HOH C 858 1555 1555 2.45
LINK MG MG H 703 O HOH H 801 1555 1555 2.47
LINK MG MG A 704 O HOH A 949 1555 1555 2.48
LINK MG MG A 705 O HOH A 812 1555 1555 2.49
LINK MG MG G 702 O HOH I 875 1555 1555 2.49
LINK MG MG F 704 O HOH F 802 1555 1555 2.49
LINK MG MG F 704 O HOH F 878 1555 1555 2.50
LINK MG MG C 703 O HOH C 802 1555 1555 2.50
LINK MG MG H 703 O HOH G 876 1555 1555 2.51
LINK MG MG H 703 O HOH G 828 1555 1555 2.51
LINK MG MG A 704 O HOH C 841 1555 1555 2.51
LINK MG MG E 706 O HOH E 946 1555 1555 2.52
LINK MG MG C 702 O HOH B 829 1555 1555 2.53
LINK MG MG C 703 O HOH C 810 1555 1555 2.53
LINK MG MG E 706 O HOH E 901 1555 1555 2.54
LINK MG MG C 703 O HOH C 859 1555 1555 2.54
LINK MG MG E 705 O HOH F 871 1555 1555 2.56
LINK MG MG F 706 O HOH E 988 1555 1555 2.56
LINK MG MG D 710 O HOH E 902 1555 1555 2.56
LINK MG MG H 702 O HOH H 857 1555 1555 2.57
LINK MG MG G 702 O HOH G 827 1555 1555 2.57
LINK MG MG F 706 O HOH E 841 1555 1555 2.57
LINK MG MG I 703 O HOH H 858 1555 1555 2.57
LINK MG MG F 704 O HOH F 954 1555 1555 2.57
LINK MG MG B 703 O BHOH A 853 1555 1555 2.58
LINK MG MG E 704 O HOH E 987 1555 1555 2.58
LINK MG MG I 704 O HOH I 871 1555 1555 2.60
LINK MG MG B 703 O HOH B 828 1555 1555 2.60
LINK MG MG H 702 O HOH H 856 1555 1555 2.60
LINK MG MG H 702 O HOH H 802 1555 1555 2.61
LINK MG MG H 703 O HOH H 808 1555 1555 2.62
LINK MG MG F 706 O HOH F 955 1555 1555 2.62
LINK MG MG G 702 O HOH I 808 1555 1555 2.62
LINK MG MG L 703 O HOH J 706 1555 1555 2.62
LINK MG MG E 706 O HOH E 896 1555 1555 2.63
LINK MG MG E 705 O HOH F 873 1555 1555 2.63
LINK MG MG F 706 O HOH E 979 1555 1555 2.63
LINK MG MG C 703 O HOH C 857 1555 1555 2.65
LINK MG MG L 702 O HOH L 820 1555 1555 2.65
LINK MG MG E 704 O HOH E 842 1555 1555 2.67
LINK MG MG D 709 O HOH D 936 1555 1555 2.67
LINK MG MG G 702 O HOH G 875 1555 1555 2.67
LINK MG MG E 706 O HOH D 915 1555 1555 2.69
LINK MG MG E 706 O HOH D1006 1555 1555 2.69
LINK MG MG I 704 O HOH I 803 1555 1555 2.71
LINK MG MG I 704 O HOH I 876 1555 1555 2.72
LINK MG MG H 702 O HOH H 818 1555 1555 2.73
LINK MG MG G 703 O HOH G 804 1555 1555 2.74
LINK MG MG D 709 O HOH D 935 1555 1555 2.75
LINK MG MG G 703 O BHOH G 810 1555 1555 2.77
LINK MG MG I 704 O HOH I 877 1555 1555 2.81
LINK MG MG L 702 O HOH L 809 1555 1555 2.86
LINK MG MG E 704 O HOH E 801 1555 1555 2.92
LINK MG MG D 710 O HOH E 832 1555 1555 2.92
LINK MG MG F 706 O HOH E 840 1555 1555 2.94
CISPEP 1 VAL A 137 PRO A 138 0 -4.63
CISPEP 2 GLY A 387 PRO A 388 0 6.65
CISPEP 3 VAL B 137 PRO B 138 0 -5.93
CISPEP 4 GLY B 387 PRO B 388 0 4.67
CISPEP 5 VAL C 137 PRO C 138 0 -9.33
CISPEP 6 GLY C 387 PRO C 388 0 9.57
CISPEP 7 VAL D 137 PRO D 138 0 -8.48
CISPEP 8 GLY D 387 PRO D 388 0 5.80
CISPEP 9 VAL E 137 PRO E 138 0 -8.13
CISPEP 10 GLY E 387 PRO E 388 0 2.79
CISPEP 11 VAL F 137 PRO F 138 0 -3.96
CISPEP 12 GLY F 387 PRO F 388 0 8.66
CISPEP 13 VAL G 137 PRO G 138 0 -5.64
CISPEP 14 GLY G 387 PRO G 388 0 7.51
CISPEP 15 VAL H 137 PRO H 138 0 -6.01
CISPEP 16 GLY H 387 PRO H 388 0 4.65
CISPEP 17 VAL I 137 PRO I 138 0 -10.60
CISPEP 18 GLY I 387 PRO I 388 0 5.34
CISPEP 19 VAL J 137 PRO J 138 0 -8.16
CISPEP 20 GLY J 387 PRO J 388 0 6.18
CISPEP 21 VAL K 137 PRO K 138 0 -7.73
CISPEP 22 GLY K 387 PRO K 388 0 7.49
CISPEP 23 VAL L 137 PRO L 138 0 -2.69
CISPEP 24 GLY L 387 PRO L 388 0 5.40
SITE 1 AC1 8 GLY A 387 ALA A 466 TYR A 467 ILE A 491
SITE 2 AC1 8 SER A 497 SER A 501 ARG A 548 CYS A 549
SITE 1 AC2 2 LYS A 397 HOH A 807
SITE 1 AC3 2 GLN A 266 TRP A 302
SITE 1 AC4 7 LYS A 99 GLU A 162 HOH A 938 HOH A 949
SITE 2 AC4 7 GLU C 42 HOH C 841 HOH C 858
SITE 1 AC5 4 ASP A 244 GLU A 263 HOH A 812 HOH A 947
SITE 1 AC6 7 GLY B 386 GLY B 387 ALA B 466 TYR B 467
SITE 2 AC6 7 SER B 497 SER B 501 ARG B 548
SITE 1 AC7 7 LEU B 544 ASP B 546 LEU B 551 LEU E 544
SITE 2 AC7 7 ASP E 546 PRO E 550 LEU E 551
SITE 1 AC8 6 GLU A 42 HOH A 853 HOH A 854 LYS B 99
SITE 2 AC8 6 GLU B 162 HOH B 828
SITE 1 AC9 9 GLY C 387 ALA C 466 TYR C 467 SER C 497
SITE 2 AC9 9 SER C 501 ILE C 503 PHE C 507 ASP C 508
SITE 3 AC9 9 ARG C 548
SITE 1 BC1 5 GLU B 42 HOH B 829 LYS C 99 GLU C 162
SITE 2 BC1 5 HOH C 801
SITE 1 BC2 6 ASP C 244 GLU C 263 HOH C 802 HOH C 810
SITE 2 BC2 6 HOH C 857 HOH C 859
SITE 1 BC3 10 GLY D 387 ALA D 466 TYR D 467 ILE D 491
SITE 2 BC3 10 SER D 497 SER D 501 ARG D 548 HIS D 578
SITE 3 BC3 10 HEZ D 707 HOH D1013
SITE 1 BC4 7 LEU A 544 ASP A 546 PRO A 550 LEU A 551
SITE 2 BC4 7 LEU D 544 ASP D 546 LEU D 551
SITE 1 BC5 6 TYR D 239 ASP D 424 LEU D 427 ARG D 428
SITE 2 BC5 6 HOH D 869 HOH D 900
SITE 1 BC6 4 TYR D 16 TYR D 41 ARG D 583 ARG D 589
SITE 1 BC7 2 LYS D 535 TYR D 607
SITE 1 BC8 6 TYR D 220 ALA D 265 GLN D 266 ALA D 267
SITE 2 BC8 6 HOH D 826 HOH D 920
SITE 1 BC9 4 ALA D 466 HIS D 578 SER D 581 HEZ D 701
SITE 1 CC1 6 SER D 241 PRO D 388 LYS D 389 PHE D 507
SITE 2 CC1 6 VAL D 511 HOH D 938
SITE 1 CC2 5 ASP D 244 GLU D 263 HOH D 802 HOH D 935
SITE 2 CC2 5 HOH D 936
SITE 1 CC3 6 LYS D 99 GLU D 162 HOH D1021 GLU E 42
SITE 2 CC3 6 HOH E 832 HOH E 902
SITE 1 CC4 2 ARG D 55 GLU F 160
SITE 1 CC5 8 GLY E 386 GLY E 387 ALA E 466 TYR E 467
SITE 2 CC5 8 ILE E 491 SER E 497 SER E 501 ARG E 548
SITE 1 CC6 7 LYS E 316 GLU E 317 ARG E 321 PRO E 322
SITE 2 CC6 7 GLU E 324 TYR E 326 GLN E 334
SITE 1 CC7 2 TYR E 16 ARG E 589
SITE 1 CC8 6 TYR E 232 ASP E 244 GLU E 263 HOH E 801
SITE 2 CC8 6 HOH E 842 HOH E 987
SITE 1 CC9 7 LYS E 99 GLU E 162 HOH E 919 GLU F 42
SITE 2 CC9 7 HOH F 871 HOH F 872 HOH F 873
SITE 1 DC1 5 HOH D 915 HOH D1006 HOH E 896 HOH E 901
SITE 2 DC1 5 HOH E 946
SITE 1 DC2 9 GLY F 387 ALA F 466 TYR F 467 ILE F 491
SITE 2 DC2 9 SER F 497 SER F 501 PHE F 507 ASP F 508
SITE 3 DC2 9 ARG F 548
SITE 1 DC3 5 LEU C 544 LEU F 544 ASP F 546 PRO F 550
SITE 2 DC3 5 LEU F 551
SITE 1 DC4 5 TYR F 220 TYR F 232 ALA F 265 GLN F 266
SITE 2 DC4 5 ALA F 267
SITE 1 DC5 5 ASP F 244 GLU F 263 HOH F 802 HOH F 878
SITE 2 DC5 5 HOH F 954
SITE 1 DC6 7 GLU D 42 HOH D 856 HOH D 939 HOH D 940
SITE 2 DC6 7 LYS F 99 GLU F 162 HOH F 879
SITE 1 DC7 7 GLU E 163 HOH E 840 HOH E 841 HOH E 979
SITE 2 DC7 7 HOH E 988 GLU F 37 HOH F 955
SITE 1 DC8 2 LYS E 98 ARG F 55
SITE 1 DC9 8 GLY G 387 ALA G 466 TYR G 467 ILE G 491
SITE 2 DC9 8 SER G 497 SER G 501 PHE G 507 ARG G 548
SITE 1 EC1 7 LYS G 99 GLU G 162 HOH G 827 HOH G 875
SITE 2 EC1 7 GLU I 42 HOH I 808 HOH I 875
SITE 1 EC2 4 ASP G 244 GLU G 263 HOH G 804 HOH G 810
SITE 1 EC3 9 GLY H 386 GLY H 387 ALA H 466 TYR H 467
SITE 2 EC3 9 SER H 497 SER H 501 PHE H 507 ASP H 508
SITE 3 EC3 9 ARG H 548
SITE 1 EC4 6 ASP H 244 GLU H 263 HOH H 802 HOH H 818
SITE 2 EC4 6 HOH H 856 HOH H 857
SITE 1 EC5 7 GLU G 42 HOH G 828 HOH G 876 LYS H 99
SITE 2 EC5 7 GLU H 162 HOH H 801 HOH H 808
SITE 1 EC6 8 GLY I 387 ALA I 466 TYR I 467 ILE I 491
SITE 2 EC6 8 SER I 497 SER I 501 PHE I 507 ARG I 548
SITE 1 EC7 4 ASP I 480 LYS I 483 LYS I 535 TYR I 607
SITE 1 EC8 6 GLU H 42 HOH H 858 LYS I 99 GLU I 162
SITE 2 EC8 6 HOH I 833 HOH I 834
SITE 1 EC9 6 ASP I 244 GLU I 263 HOH I 803 HOH I 871
SITE 2 EC9 6 HOH I 876 HOH I 877
SITE 1 FC1 7 GLY K 386 GLY K 387 ALA K 466 TYR K 467
SITE 2 FC1 7 SER K 497 SER K 501 ARG K 548
SITE 1 FC2 7 GLY L 387 ALA L 466 TYR L 467 SER L 497
SITE 2 FC2 7 SER L 501 PHE L 507 ARG L 548
SITE 1 FC3 5 ASP L 244 GLU L 263 HOH L 809 HOH L 820
SITE 2 FC3 5 HOH L 851
SITE 1 FC4 6 THR J 44 GLU J 59 HOH J 706 HOH J 707
SITE 2 FC4 6 LYS L 99 GLU L 162
CRYST1 183.310 183.800 275.740 90.00 90.00 90.00 P 21 21 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 0.005455 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005441 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003627 0.00000
TER 4941 LYS A 618
TER 9868 LYS B 618
TER 14752 LYS C 618
TER 19742 LYS D 618
TER 24748 LYS E 618
TER 29724 LYS F 618
TER 34611 LYS G 618
TER 39478 LYS H 618
TER 44389 LYS I 618
TER 49007 LYS J 618
TER 53667 LYS K 618
TER 58530 LYS L 618
MASTER 2053 0 49 168 470 0 91 659755 12 359 576
END |