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HEADER IMMUNE SYSTEM 20-OCT-22 8EVD
TITLE CRYSTAL STRUCTURE OF NANOBODY VHH101 BOUND TO ITS ANTIGEN PA14 CIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NANOBODY VHH101;
COMPND 3 CHAIN: A, B, E, F, I, J;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CFTR INHIBITORY FACTOR;
COMPND 7 CHAIN: C, D, G, H, K, L;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VICUGNA PACOS;
SOURCE 3 ORGANISM_TAXID: 30538;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: DE3 RIL;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCOMB3X;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PA14;
SOURCE 11 ORGANISM_TAXID: 652611;
SOURCE 12 GENE: PA2394;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PDPM73
KEYWDS PSEUDOMONAS AERUGINOSA, NANOBODY VHH, IMMUNOGLOBULIN DOMAIN, CFTR
KEYWDS 2 INHIBITORY FACTOR (CIF), IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.SIMARD,N.M.TAHER,K.S.BEAUCHEMIN,D.R.MADDEN
REVDAT 1 13-MAR-24 8EVD 0
JRNL AUTH A.R.SIMARD,D.R.MADDEN
JRNL TITL CRYSTAL STRUCTURE OF NANOBODY VHH101 BOUND TO ITS ANTIGEN
JRNL TITL 2 PA14 CIF
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.VASYLIEVA,S.KITAMURA,J.DONG,B.BARNYCH,K.L.HVORECNY,
REMARK 1 AUTH 2 D.R.MADDEN,S.J.GEE,D.W.WOLAN,C.MORISSEAU,B.D.HAMMOCK
REMARK 1 TITL NANOBODY-BASED BINDING ASSAY FOR THE DISCOVERY OF POTENT
REMARK 1 TITL 2 INHIBITORS OF CFTR INHIBITORY FACTOR (CIF).
REMARK 1 REF ANAL CHIM ACTA V.1057 106 2019
REMARK 1 REFN ISSN 1873-4324
REMARK 1 PMID 30832908
REMARK 1 DOI 10.1016/J.ACA.2018.12.060
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 165132
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 8270
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 47.1900 - 6.2100 0.88 4871 396 0.1680 0.1927
REMARK 3 2 6.2100 - 4.9300 0.87 5146 0 0.1706 0.0000
REMARK 3 3 4.9300 - 4.3100 0.87 4726 390 0.1430 0.1552
REMARK 3 4 4.3100 - 3.9100 0.88 4788 390 0.1523 0.1749
REMARK 3 5 3.9100 - 3.6300 0.90 5240 33 0.1547 0.2190
REMARK 3 6 3.6300 - 3.4200 0.91 4959 388 0.1636 0.1684
REMARK 3 7 3.4200 - 3.2500 0.93 5113 324 0.1710 0.1962
REMARK 3 8 3.2500 - 3.1100 0.93 5261 145 0.1720 0.1860
REMARK 3 9 3.1100 - 2.9900 0.95 5145 371 0.1937 0.2119
REMARK 3 10 2.9900 - 2.8800 0.95 5265 283 0.1955 0.2261
REMARK 3 11 2.8800 - 2.7900 0.95 5330 201 0.1947 0.2207
REMARK 3 12 2.7900 - 2.7100 0.96 5252 340 0.1987 0.2082
REMARK 3 13 2.7100 - 2.6400 0.95 5225 266 0.2016 0.2547
REMARK 3 14 2.6400 - 2.5800 0.94 5234 268 0.2107 0.2566
REMARK 3 15 2.5800 - 2.5200 0.96 5277 269 0.2079 0.2318
REMARK 3 16 2.5200 - 2.4700 0.96 5260 301 0.2155 0.2504
REMARK 3 17 2.4700 - 2.4200 0.96 5240 286 0.2189 0.2539
REMARK 3 18 2.4200 - 2.3700 0.96 5322 245 0.2102 0.2312
REMARK 3 19 2.3700 - 2.3300 0.96 5272 281 0.2146 0.2453
REMARK 3 20 2.3300 - 2.2900 0.97 5315 273 0.2207 0.2549
REMARK 3 21 2.2900 - 2.2500 0.97 5362 298 0.2199 0.2395
REMARK 3 22 2.2500 - 2.2200 0.97 5318 280 0.2232 0.2577
REMARK 3 23 2.2200 - 2.1900 0.97 5330 267 0.2308 0.2661
REMARK 3 24 2.1900 - 2.1500 0.97 5340 305 0.2273 0.2534
REMARK 3 25 2.1500 - 2.1300 0.97 5375 258 0.2348 0.2498
REMARK 3 26 2.1300 - 2.1000 0.97 5348 276 0.2379 0.2654
REMARK 3 27 2.1000 - 2.0700 0.98 5384 339 0.2498 0.2685
REMARK 3 28 2.0700 - 2.0500 0.97 5379 244 0.2567 0.3021
REMARK 3 29 2.0500 - 2.0200 0.98 5339 305 0.2638 0.2992
REMARK 3 30 2.0200 - 2.0000 0.98 5446 248 0.2792 0.3024
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.223
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.309
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 20184
REMARK 3 ANGLE : 0.966 27376
REMARK 3 CHIRALITY : 0.062 2868
REMARK 3 PLANARITY : 0.007 3580
REMARK 3 DIHEDRAL : 13.803 7218
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A'
REMARK 3 ORIGIN FOR THE GROUP (A): -56.3886 19.9454 50.4021
REMARK 3 T TENSOR
REMARK 3 T11: 0.2794 T22: 0.2466
REMARK 3 T33: 0.1720 T12: -0.0152
REMARK 3 T13: -0.0026 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.8188 L22: 2.0142
REMARK 3 L33: 2.1232 L12: 0.0456
REMARK 3 L13: -0.5476 L23: -0.1759
REMARK 3 S TENSOR
REMARK 3 S11: -0.0219 S12: -0.2478 S13: -0.1149
REMARK 3 S21: 0.3249 S22: 0.0564 S23: 0.0335
REMARK 3 S31: 0.2988 S32: -0.1318 S33: -0.0283
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B'
REMARK 3 ORIGIN FOR THE GROUP (A): -24.3544 23.0303 7.6967
REMARK 3 T TENSOR
REMARK 3 T11: 0.2832 T22: 0.2544
REMARK 3 T33: 0.3708 T12: 0.0045
REMARK 3 T13: 0.1054 T23: 0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 1.8787 L22: 2.6270
REMARK 3 L33: 2.2250 L12: 0.0052
REMARK 3 L13: 0.0990 L23: -0.1982
REMARK 3 S TENSOR
REMARK 3 S11: 0.1016 S12: 0.2041 S13: 0.3632
REMARK 3 S21: -0.3421 S22: -0.0190 S23: -0.5738
REMARK 3 S31: -0.2488 S32: 0.3233 S33: -0.0799
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C'
REMARK 3 ORIGIN FOR THE GROUP (A): -50.3617 42.6473 21.7162
REMARK 3 T TENSOR
REMARK 3 T11: 0.2484 T22: 0.2423
REMARK 3 T33: 0.2195 T12: 0.0020
REMARK 3 T13: -0.0062 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 1.0560 L22: 1.8519
REMARK 3 L33: 1.2715 L12: -0.1320
REMARK 3 L13: -0.0379 L23: 0.0323
REMARK 3 S TENSOR
REMARK 3 S11: 0.0217 S12: 0.0296 S13: 0.1602
REMARK 3 S21: -0.0296 S22: -0.0250 S23: -0.0428
REMARK 3 S31: -0.1819 S32: 0.0154 S33: 0.0010
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'D'
REMARK 3 ORIGIN FOR THE GROUP (A): -50.5779 0.6419 20.8614
REMARK 3 T TENSOR
REMARK 3 T11: 0.2535 T22: 0.2294
REMARK 3 T33: 0.2524 T12: -0.0146
REMARK 3 T13: 0.0212 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.3607 L22: 1.9106
REMARK 3 L33: 0.8404 L12: -0.2066
REMARK 3 L13: -0.0514 L23: 0.0787
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: -0.0506 S13: -0.2293
REMARK 3 S21: 0.0918 S22: -0.0527 S23: 0.1403
REMARK 3 S31: 0.1894 S32: -0.0600 S33: 0.0650
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'E'
REMARK 3 ORIGIN FOR THE GROUP (A): -1.6914 51.9122 60.5753
REMARK 3 T TENSOR
REMARK 3 T11: 0.2528 T22: 0.3690
REMARK 3 T33: 0.3502 T12: 0.0168
REMARK 3 T13: 0.0534 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 3.0881 L22: 2.8983
REMARK 3 L33: 2.7680 L12: -0.7184
REMARK 3 L13: 0.2221 L23: -0.0045
REMARK 3 S TENSOR
REMARK 3 S11: 0.0588 S12: 0.2926 S13: -0.3760
REMARK 3 S21: -0.2985 S22: -0.1208 S23: -0.4388
REMARK 3 S31: 0.2340 S32: 0.4685 S33: 0.0299
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'F'
REMARK 3 ORIGIN FOR THE GROUP (A): -55.2641 54.6661 52.8342
REMARK 3 T TENSOR
REMARK 3 T11: 0.3221 T22: 0.3229
REMARK 3 T33: 0.3014 T12: 0.0479
REMARK 3 T13: -0.0748 T23: -0.0770
REMARK 3 L TENSOR
REMARK 3 L11: 2.9456 L22: 3.1728
REMARK 3 L33: 2.6718 L12: -0.0216
REMARK 3 L13: -0.1085 L23: -0.1787
REMARK 3 S TENSOR
REMARK 3 S11: -0.0818 S12: 0.1022 S13: 0.3205
REMARK 3 S21: -0.2781 S22: -0.0700 S23: 0.5443
REMARK 3 S31: -0.3968 S32: -0.4892 S33: 0.1343
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'G'
REMARK 3 ORIGIN FOR THE GROUP (A): -29.9746 74.0578 68.3414
REMARK 3 T TENSOR
REMARK 3 T11: 0.2569 T22: 0.2617
REMARK 3 T33: 0.3501 T12: 0.0011
REMARK 3 T13: 0.0060 T23: -0.0465
REMARK 3 L TENSOR
REMARK 3 L11: 2.6168 L22: 2.7815
REMARK 3 L33: 1.4110 L12: 0.0049
REMARK 3 L13: -0.3238 L23: -0.0256
REMARK 3 S TENSOR
REMARK 3 S11: 0.0614 S12: -0.1155 S13: 0.6907
REMARK 3 S21: 0.1050 S22: -0.0441 S23: -0.0414
REMARK 3 S31: -0.3115 S32: -0.0124 S33: -0.0202
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'H'
REMARK 3 ORIGIN FOR THE GROUP (A): -30.5339 32.1535 68.9734
REMARK 3 T TENSOR
REMARK 3 T11: 0.2636 T22: 0.2747
REMARK 3 T33: 0.3007 T12: 0.0039
REMARK 3 T13: -0.0284 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.2658 L22: 2.4333
REMARK 3 L33: 1.2590 L12: 0.4059
REMARK 3 L13: 0.2588 L23: 0.1933
REMARK 3 S TENSOR
REMARK 3 S11: 0.0524 S12: -0.1206 S13: -0.2749
REMARK 3 S21: 0.1584 S22: -0.0325 S23: -0.3062
REMARK 3 S31: 0.2034 S32: 0.1074 S33: -0.0174
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'I'
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5575 80.1521 53.0455
REMARK 3 T TENSOR
REMARK 3 T11: 0.5290 T22: 0.5429
REMARK 3 T33: 0.3068 T12: -0.0879
REMARK 3 T13: -0.0200 T23: 0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 2.4648 L22: 3.0667
REMARK 3 L33: 1.7841 L12: 0.1085
REMARK 3 L13: 0.3104 L23: -0.3485
REMARK 3 S TENSOR
REMARK 3 S11: 0.1036 S12: -0.5979 S13: 0.1701
REMARK 3 S21: 0.8787 S22: -0.1977 S23: -0.0985
REMARK 3 S31: -0.4727 S32: 0.0927 S33: 0.1152
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'J'
REMARK 3 ORIGIN FOR THE GROUP (A): -22.6060 80.2335 6.1470
REMARK 3 T TENSOR
REMARK 3 T11: 0.1550 T22: 0.2266
REMARK 3 T33: 0.1684 T12: 0.0064
REMARK 3 T13: 0.0086 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 1.7870 L22: 2.6297
REMARK 3 L33: 2.3271 L12: 0.6376
REMARK 3 L13: 0.8147 L23: 0.3862
REMARK 3 S TENSOR
REMARK 3 S11: 0.0434 S12: -0.0147 S13: -0.1031
REMARK 3 S21: -0.0376 S22: 0.0588 S23: -0.0274
REMARK 3 S31: 0.0899 S32: -0.0992 S33: -0.0838
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'K'
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4939 60.0984 22.3180
REMARK 3 T TENSOR
REMARK 3 T11: 0.2901 T22: 0.2988
REMARK 3 T33: 0.3479 T12: 0.0082
REMARK 3 T13: 0.0293 T23: 0.0539
REMARK 3 L TENSOR
REMARK 3 L11: 1.5544 L22: 2.1199
REMARK 3 L33: 1.8836 L12: -0.3114
REMARK 3 L13: -0.0106 L23: 0.2408
REMARK 3 S TENSOR
REMARK 3 S11: -0.0452 S12: -0.0998 S13: -0.4179
REMARK 3 S21: 0.0825 S22: -0.0549 S23: -0.0087
REMARK 3 S31: 0.4120 S32: 0.0114 S33: 0.0953
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'L'
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2941 101.8308 24.7573
REMARK 3 T TENSOR
REMARK 3 T11: 0.2665 T22: 0.3213
REMARK 3 T33: 0.3324 T12: -0.0687
REMARK 3 T13: -0.0265 T23: -0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 1.5290 L22: 2.4473
REMARK 3 L33: 1.2363 L12: -0.5766
REMARK 3 L13: -0.0581 L23: -0.2347
REMARK 3 S TENSOR
REMARK 3 S11: 0.0558 S12: -0.2661 S13: 0.4022
REMARK 3 S21: 0.3006 S22: -0.0600 S23: -0.3427
REMARK 3 S31: -0.2623 S32: 0.2397 S33: -0.0037
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "A" and resid 4 through 127)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : chain "B"
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "E" and resid 4 through 127)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "F" and resid 4 through 127)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : chain "I"
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 6
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "J" and resid 4 through 127)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : ens_2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "C" and resid 26 through 317)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "D" and resid 26 through 317)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : chain "G"
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "H" and resid 26 through 317)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : chain "K"
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 6
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "L" and resid 26 through 317)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ATOMS MODELED WITH ZERO OCCUPANCY COULD
REMARK 3 NOT BE PLACED WITH CONFIDENCE AND WERE SELECTED FOR ZERO-
REMARK 3 OCCUPANCY FLAGGING AFTER MANUAL INSPECTION OF THE 2FO-FC MAP AT
REMARK 3 A 0.5-SIGMA CUTOFF.
REMARK 4
REMARK 4 8EVD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1000269373.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS-II
REMARK 200 BEAMLINE : 17-ID-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979339
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 165194
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 47.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.08194
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.90250
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.020
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3KD2, 8E2N
REMARK 200
REMARK 200 REMARK: TWO CRYSTALS GROWING TOGETHER
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% (V/V) ISOPROPANOL, 1 M AMMONIUM
REMARK 280 CITRATE/AMMONIUM HYDROXIDE PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 292.8K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 94.48000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.99500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 94.48000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.99500
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, 3
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH E 208 LIES ON A SPECIAL POSITION.
REMARK 375 HOH E 240 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 SER A 129
REMARK 465 GLY A 130
REMARK 465 GLN A 131
REMARK 465 ALA A 132
REMARK 465 GLY A 133
REMARK 465 GLN A 134
REMARK 465 HIS A 135
REMARK 465 HIS A 136
REMARK 465 HIS A 137
REMARK 465 HIS A 138
REMARK 465 HIS A 139
REMARK 465 HIS A 140
REMARK 465 GLY A 141
REMARK 465 ALA A 142
REMARK 465 TYR A 143
REMARK 465 PRO A 144
REMARK 465 TYR A 145
REMARK 465 ASP A 146
REMARK 465 VAL A 147
REMARK 465 PRO A 148
REMARK 465 ASP A 149
REMARK 465 TYR A 150
REMARK 465 ALA A 151
REMARK 465 SER A 152
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 SER B 128
REMARK 465 SER B 129
REMARK 465 GLY B 130
REMARK 465 GLN B 131
REMARK 465 ALA B 132
REMARK 465 GLY B 133
REMARK 465 GLN B 134
REMARK 465 HIS B 135
REMARK 465 HIS B 136
REMARK 465 HIS B 137
REMARK 465 HIS B 138
REMARK 465 HIS B 139
REMARK 465 HIS B 140
REMARK 465 GLY B 141
REMARK 465 ALA B 142
REMARK 465 TYR B 143
REMARK 465 PRO B 144
REMARK 465 TYR B 145
REMARK 465 ASP B 146
REMARK 465 VAL B 147
REMARK 465 PRO B 148
REMARK 465 ASP B 149
REMARK 465 TYR B 150
REMARK 465 ALA B 151
REMARK 465 SER B 152
REMARK 465 ALA C 25
REMARK 465 HIS C 320
REMARK 465 HIS C 321
REMARK 465 HIS C 322
REMARK 465 HIS C 323
REMARK 465 HIS C 324
REMARK 465 HIS C 325
REMARK 465 ALA D 25
REMARK 465 HIS D 320
REMARK 465 HIS D 321
REMARK 465 HIS D 322
REMARK 465 HIS D 323
REMARK 465 HIS D 324
REMARK 465 HIS D 325
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 SER E 129
REMARK 465 GLY E 130
REMARK 465 GLN E 131
REMARK 465 ALA E 132
REMARK 465 GLY E 133
REMARK 465 GLN E 134
REMARK 465 HIS E 135
REMARK 465 HIS E 136
REMARK 465 HIS E 137
REMARK 465 HIS E 138
REMARK 465 HIS E 139
REMARK 465 HIS E 140
REMARK 465 GLY E 141
REMARK 465 ALA E 142
REMARK 465 TYR E 143
REMARK 465 PRO E 144
REMARK 465 TYR E 145
REMARK 465 ASP E 146
REMARK 465 VAL E 147
REMARK 465 PRO E 148
REMARK 465 ASP E 149
REMARK 465 TYR E 150
REMARK 465 ALA E 151
REMARK 465 SER E 152
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 GLY F 130
REMARK 465 GLN F 131
REMARK 465 ALA F 132
REMARK 465 GLY F 133
REMARK 465 GLN F 134
REMARK 465 HIS F 135
REMARK 465 HIS F 136
REMARK 465 HIS F 137
REMARK 465 HIS F 138
REMARK 465 HIS F 139
REMARK 465 HIS F 140
REMARK 465 GLY F 141
REMARK 465 ALA F 142
REMARK 465 TYR F 143
REMARK 465 PRO F 144
REMARK 465 TYR F 145
REMARK 465 ASP F 146
REMARK 465 VAL F 147
REMARK 465 PRO F 148
REMARK 465 ASP F 149
REMARK 465 TYR F 150
REMARK 465 ALA F 151
REMARK 465 SER F 152
REMARK 465 ALA G 25
REMARK 465 GLY G 318
REMARK 465 ARG G 319
REMARK 465 HIS G 320
REMARK 465 HIS G 321
REMARK 465 HIS G 322
REMARK 465 HIS G 323
REMARK 465 HIS G 324
REMARK 465 HIS G 325
REMARK 465 ALA H 25
REMARK 465 HIS H 320
REMARK 465 HIS H 321
REMARK 465 HIS H 322
REMARK 465 HIS H 323
REMARK 465 HIS H 324
REMARK 465 HIS H 325
REMARK 465 MET I 1
REMARK 465 ALA I 2
REMARK 465 GLU I 3
REMARK 465 SER I 128
REMARK 465 SER I 129
REMARK 465 GLY I 130
REMARK 465 GLN I 131
REMARK 465 ALA I 132
REMARK 465 GLY I 133
REMARK 465 GLN I 134
REMARK 465 HIS I 135
REMARK 465 HIS I 136
REMARK 465 HIS I 137
REMARK 465 HIS I 138
REMARK 465 HIS I 139
REMARK 465 HIS I 140
REMARK 465 GLY I 141
REMARK 465 ALA I 142
REMARK 465 TYR I 143
REMARK 465 PRO I 144
REMARK 465 TYR I 145
REMARK 465 ASP I 146
REMARK 465 VAL I 147
REMARK 465 PRO I 148
REMARK 465 ASP I 149
REMARK 465 TYR I 150
REMARK 465 ALA I 151
REMARK 465 SER I 152
REMARK 465 MET J 1
REMARK 465 ALA J 2
REMARK 465 GLU J 3
REMARK 465 GLY J 130
REMARK 465 GLN J 131
REMARK 465 ALA J 132
REMARK 465 GLY J 133
REMARK 465 GLN J 134
REMARK 465 HIS J 135
REMARK 465 HIS J 136
REMARK 465 HIS J 137
REMARK 465 HIS J 138
REMARK 465 HIS J 139
REMARK 465 HIS J 140
REMARK 465 GLY J 141
REMARK 465 ALA J 142
REMARK 465 TYR J 143
REMARK 465 PRO J 144
REMARK 465 TYR J 145
REMARK 465 ASP J 146
REMARK 465 VAL J 147
REMARK 465 PRO J 148
REMARK 465 ASP J 149
REMARK 465 TYR J 150
REMARK 465 ALA J 151
REMARK 465 SER J 152
REMARK 465 ALA K 25
REMARK 465 GLY K 318
REMARK 465 ARG K 319
REMARK 465 HIS K 320
REMARK 465 HIS K 321
REMARK 465 HIS K 322
REMARK 465 HIS K 323
REMARK 465 HIS K 324
REMARK 465 HIS K 325
REMARK 465 ALA L 25
REMARK 465 HIS L 320
REMARK 465 HIS L 321
REMARK 465 HIS L 322
REMARK 465 HIS L 323
REMARK 465 HIS L 324
REMARK 465 HIS L 325
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 45 CE NZ
REMARK 480 LYS B 45 CG CD CE NZ
REMARK 480 ARG C 121 CG CD NE CZ NH1 NH2
REMARK 480 GLU C 212 CD OE1 OE2
REMARK 480 ARG D 80 CD NE CZ NH1 NH2
REMARK 480 ARG D 186 NE CZ NH1 NH2
REMARK 480 GLN E 15 CG CD OE1 NE2
REMARK 480 LYS E 45 CG CD CE NZ
REMARK 480 GLU E 46 CG CD OE1 OE2
REMARK 480 LYS E 70 CD CE NZ
REMARK 480 LYS E 81 NZ
REMARK 480 LYS E 92 CE NZ
REMARK 480 GLU E 94 CG CD OE1 OE2
REMARK 480 GLU E 106 CD OE1 OE2
REMARK 480 LYS F 45 CE NZ
REMARK 480 GLU G 35 CD OE1 OE2
REMARK 480 ARG G 39 CG CD NE CZ NH1 NH2
REMARK 480 GLN G 53 CG CD OE1 NE2
REMARK 480 ARG G 80 CG CD NE CZ NH1 NH2
REMARK 480 GLU G 212 CD OE1 OE2
REMARK 480 GLU G 285 CG CD OE1 OE2
REMARK 480 ARG G 309 CG CD NE CZ NH1 NH2
REMARK 480 ASN H 32 CG OD1 ND2
REMARK 480 LYS H 45 CE NZ
REMARK 480 ARG H 80 CG CD NE CZ NH1 NH2
REMARK 480 LYS H 98 CE NZ
REMARK 480 ARG H 121 CG CD NE CZ NH1 NH2
REMARK 480 ARG H 163 CD NE CZ NH1 NH2
REMARK 480 GLU H 285 CG CD OE1 OE2
REMARK 480 GLU H 301 CD OE1 OE2
REMARK 480 LYS I 45 CD CE NZ
REMARK 480 GLU I 46 CG CD OE1 OE2
REMARK 480 GLU I 48 CG CD OE1 OE2
REMARK 480 LYS I 70 CE NZ
REMARK 480 LYS I 81 CE NZ
REMARK 480 GLN I 121 CD OE1 NE2
REMARK 480 GLN I 124 CG CD OE1 NE2
REMARK 480 LYS J 92 CE NZ
REMARK 480 ARG K 163 NE CZ NH1 NH2
REMARK 480 GLU K 212 CD OE1 OE2
REMARK 480 ARG K 217 NE CZ NH1 NH2
REMARK 480 ARG K 224 CD NE CZ NH1 NH2
REMARK 480 LYS K 254 CE NZ
REMARK 480 ARG K 317 NE CZ NH1 NH2
REMARK 480 LYS L 45 NZ
REMARK 480 LYS L 50 CD CE NZ
REMARK 480 ARG L 80 CD NE CZ NH1 NH2
REMARK 480 ASP L 120 CG OD1 OD2
REMARK 480 GLU L 212 CG CD OE1 OE2
REMARK 480 ARG L 224 CZ NH1 NH2
REMARK 480 LYS L 254 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 ALA A 97 170.60 176.87
REMARK 500 ALA B 97 168.80 179.02
REMARK 500 ASP C 129 -130.99 59.48
REMARK 500 ALA C 154 151.51 176.97
REMARK 500 ASP D 129 -129.43 51.59
REMARK 500 ALA D 154 151.21 179.41
REMARK 500 ALA E 97 171.11 178.45
REMARK 500 ALA F 97 169.30 179.53
REMARK 500 ASP G 129 -130.47 58.98
REMARK 500 ALA G 154 151.56 179.71
REMARK 500 ASP H 129 -131.29 60.14
REMARK 500 ALA H 154 149.61 179.48
REMARK 500 ALA I 97 169.81 178.53
REMARK 500 ALA J 97 168.47 179.45
REMARK 500 ASP K 129 -131.39 59.59
REMARK 500 ALA K 154 152.00 178.01
REMARK 500 ASP L 129 -130.40 58.61
REMARK 500 ALA L 154 149.76 177.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KD2 RELATED DB: PDB
REMARK 900 3KD2 CONTAINS CIF
REMARK 900 RELATED ID: 8EE2 RELATED DB: PDB
REMARK 900 3EE2 CONTAINS CIF COMPLEXED TO RELATED NANOBODY VHH219
REMARK 900 RELATED ID: 8ELN RELATED DB: PDB
REMARK 900 3ELN CONTAINS CIF COMPLEXED TO RELATED NANOBODY VHH222
DBREF 8EVD A 1 152 PDB 8EVD 8EVD 1 152
DBREF 8EVD B 1 152 PDB 8EVD 8EVD 1 152
DBREF1 8EVD C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 8EVD C A0A0M3KL26 1 301
DBREF1 8EVD D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 8EVD D A0A0M3KL26 1 301
DBREF 8EVD E 1 152 PDB 8EVD 8EVD 1 152
DBREF 8EVD F 1 152 PDB 8EVD 8EVD 1 152
DBREF1 8EVD G 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 8EVD G A0A0M3KL26 1 301
DBREF1 8EVD H 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 8EVD H A0A0M3KL26 1 301
DBREF 8EVD I 1 152 PDB 8EVD 8EVD 1 152
DBREF 8EVD J 1 152 PDB 8EVD 8EVD 1 152
DBREF1 8EVD K 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 8EVD K A0A0M3KL26 1 301
DBREF1 8EVD L 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 8EVD L A0A0M3KL26 1 301
SEQRES 1 A 152 MET ALA GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU
SEQRES 2 A 152 VAL GLN ALA GLY GLY SER LEU ARG LEU THR CYS ALA ALA
SEQRES 3 A 152 SER ALA GLY SER PHE ARG GLY TYR ALA MET GLY TRP PHE
SEQRES 4 A 152 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA
SEQRES 5 A 152 VAL SER VAL LEU THR TRP SER GLY ASP SER THR ASN ILE
SEQRES 6 A 152 ALA ASP SER VAL LYS GLY ARG PHE THR ILE PHE ARG ASP
SEQRES 7 A 152 THR ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU
SEQRES 8 A 152 LYS PRO GLU ASP THR ALA VAL TYR TYR CYS ASN GLY ALA
SEQRES 9 A 152 SER GLU ILE GLY ALA LEU GLN SER GLY ALA SER LEU TRP
SEQRES 10 A 152 SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY
SEQRES 11 A 152 GLN ALA GLY GLN HIS HIS HIS HIS HIS HIS GLY ALA TYR
SEQRES 12 A 152 PRO TYR ASP VAL PRO ASP TYR ALA SER
SEQRES 1 B 152 MET ALA GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU
SEQRES 2 B 152 VAL GLN ALA GLY GLY SER LEU ARG LEU THR CYS ALA ALA
SEQRES 3 B 152 SER ALA GLY SER PHE ARG GLY TYR ALA MET GLY TRP PHE
SEQRES 4 B 152 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA
SEQRES 5 B 152 VAL SER VAL LEU THR TRP SER GLY ASP SER THR ASN ILE
SEQRES 6 B 152 ALA ASP SER VAL LYS GLY ARG PHE THR ILE PHE ARG ASP
SEQRES 7 B 152 THR ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU
SEQRES 8 B 152 LYS PRO GLU ASP THR ALA VAL TYR TYR CYS ASN GLY ALA
SEQRES 9 B 152 SER GLU ILE GLY ALA LEU GLN SER GLY ALA SER LEU TRP
SEQRES 10 B 152 SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY
SEQRES 11 B 152 GLN ALA GLY GLN HIS HIS HIS HIS HIS HIS GLY ALA TYR
SEQRES 12 B 152 PRO TYR ASP VAL PRO ASP TYR ALA SER
SEQRES 1 C 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 C 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 C 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 C 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 C 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 C 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 C 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 C 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 C 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 C 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 C 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 C 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 C 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 C 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 C 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 C 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 C 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 C 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 C 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 C 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 C 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 C 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 C 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 C 301 HIS HIS
SEQRES 1 D 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 D 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 D 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 D 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 D 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 D 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 D 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 D 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 D 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 D 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 D 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 D 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 D 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 D 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 D 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 D 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 D 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 D 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 D 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 D 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 D 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 D 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 D 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 D 301 HIS HIS
SEQRES 1 E 152 MET ALA GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU
SEQRES 2 E 152 VAL GLN ALA GLY GLY SER LEU ARG LEU THR CYS ALA ALA
SEQRES 3 E 152 SER ALA GLY SER PHE ARG GLY TYR ALA MET GLY TRP PHE
SEQRES 4 E 152 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA
SEQRES 5 E 152 VAL SER VAL LEU THR TRP SER GLY ASP SER THR ASN ILE
SEQRES 6 E 152 ALA ASP SER VAL LYS GLY ARG PHE THR ILE PHE ARG ASP
SEQRES 7 E 152 THR ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU
SEQRES 8 E 152 LYS PRO GLU ASP THR ALA VAL TYR TYR CYS ASN GLY ALA
SEQRES 9 E 152 SER GLU ILE GLY ALA LEU GLN SER GLY ALA SER LEU TRP
SEQRES 10 E 152 SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY
SEQRES 11 E 152 GLN ALA GLY GLN HIS HIS HIS HIS HIS HIS GLY ALA TYR
SEQRES 12 E 152 PRO TYR ASP VAL PRO ASP TYR ALA SER
SEQRES 1 F 152 MET ALA GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU
SEQRES 2 F 152 VAL GLN ALA GLY GLY SER LEU ARG LEU THR CYS ALA ALA
SEQRES 3 F 152 SER ALA GLY SER PHE ARG GLY TYR ALA MET GLY TRP PHE
SEQRES 4 F 152 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA
SEQRES 5 F 152 VAL SER VAL LEU THR TRP SER GLY ASP SER THR ASN ILE
SEQRES 6 F 152 ALA ASP SER VAL LYS GLY ARG PHE THR ILE PHE ARG ASP
SEQRES 7 F 152 THR ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU
SEQRES 8 F 152 LYS PRO GLU ASP THR ALA VAL TYR TYR CYS ASN GLY ALA
SEQRES 9 F 152 SER GLU ILE GLY ALA LEU GLN SER GLY ALA SER LEU TRP
SEQRES 10 F 152 SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY
SEQRES 11 F 152 GLN ALA GLY GLN HIS HIS HIS HIS HIS HIS GLY ALA TYR
SEQRES 12 F 152 PRO TYR ASP VAL PRO ASP TYR ALA SER
SEQRES 1 G 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 G 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 G 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 G 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 G 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 G 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 G 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 G 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 G 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 G 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 G 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 G 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 G 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 G 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 G 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 G 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 G 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 G 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 G 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 G 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 G 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 G 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 G 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 G 301 HIS HIS
SEQRES 1 H 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 H 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 H 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 H 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 H 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 H 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 H 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 H 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 H 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 H 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 H 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 H 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 H 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 H 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 H 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 H 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 H 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 H 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 H 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 H 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 H 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 H 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 H 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 H 301 HIS HIS
SEQRES 1 I 152 MET ALA GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU
SEQRES 2 I 152 VAL GLN ALA GLY GLY SER LEU ARG LEU THR CYS ALA ALA
SEQRES 3 I 152 SER ALA GLY SER PHE ARG GLY TYR ALA MET GLY TRP PHE
SEQRES 4 I 152 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA
SEQRES 5 I 152 VAL SER VAL LEU THR TRP SER GLY ASP SER THR ASN ILE
SEQRES 6 I 152 ALA ASP SER VAL LYS GLY ARG PHE THR ILE PHE ARG ASP
SEQRES 7 I 152 THR ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU
SEQRES 8 I 152 LYS PRO GLU ASP THR ALA VAL TYR TYR CYS ASN GLY ALA
SEQRES 9 I 152 SER GLU ILE GLY ALA LEU GLN SER GLY ALA SER LEU TRP
SEQRES 10 I 152 SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY
SEQRES 11 I 152 GLN ALA GLY GLN HIS HIS HIS HIS HIS HIS GLY ALA TYR
SEQRES 12 I 152 PRO TYR ASP VAL PRO ASP TYR ALA SER
SEQRES 1 J 152 MET ALA GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU
SEQRES 2 J 152 VAL GLN ALA GLY GLY SER LEU ARG LEU THR CYS ALA ALA
SEQRES 3 J 152 SER ALA GLY SER PHE ARG GLY TYR ALA MET GLY TRP PHE
SEQRES 4 J 152 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA
SEQRES 5 J 152 VAL SER VAL LEU THR TRP SER GLY ASP SER THR ASN ILE
SEQRES 6 J 152 ALA ASP SER VAL LYS GLY ARG PHE THR ILE PHE ARG ASP
SEQRES 7 J 152 THR ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU
SEQRES 8 J 152 LYS PRO GLU ASP THR ALA VAL TYR TYR CYS ASN GLY ALA
SEQRES 9 J 152 SER GLU ILE GLY ALA LEU GLN SER GLY ALA SER LEU TRP
SEQRES 10 J 152 SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY
SEQRES 11 J 152 GLN ALA GLY GLN HIS HIS HIS HIS HIS HIS GLY ALA TYR
SEQRES 12 J 152 PRO TYR ASP VAL PRO ASP TYR ALA SER
SEQRES 1 K 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 K 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 K 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 K 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 K 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 K 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 K 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 K 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 K 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 K 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 K 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 K 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 K 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 K 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 K 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 K 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 K 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 K 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 K 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 K 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 K 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 K 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 K 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 K 301 HIS HIS
SEQRES 1 L 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 L 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 L 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 L 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 L 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 L 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 L 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 L 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 L 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 L 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 L 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 L 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 L 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 L 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 L 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 L 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 L 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 L 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 L 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 L 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 L 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 L 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 L 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 L 301 HIS HIS
FORMUL 13 HOH *922(H2 O)
HELIX 1 AA1 LYS A 92 THR A 96 5 5
HELIX 2 AA2 GLU A 106 SER A 112 1 7
HELIX 3 AA3 LYS B 92 THR B 96 5 5
HELIX 4 AA4 GLU B 106 SER B 112 1 7
HELIX 5 AA5 THR C 66 HIS C 71 5 6
HELIX 6 AA6 LEU C 73 ALA C 78 1 6
HELIX 7 AA7 SER C 102 SER C 118 1 17
HELIX 8 AA8 ASP C 129 ASN C 134 1 6
HELIX 9 AA9 THR C 135 ASN C 142 1 8
HELIX 10 AB1 ASP C 158 PHE C 164 5 7
HELIX 11 AB2 TRP C 176 ALA C 183 1 8
HELIX 12 AB3 ARG C 186 ALA C 193 1 8
HELIX 13 AB4 LYS C 195 HIS C 207 1 13
HELIX 14 AB5 ASN C 210 PHE C 214 5 5
HELIX 15 AB6 SER C 215 ALA C 227 1 13
HELIX 16 AB7 LYS C 228 ALA C 241 1 14
HELIX 17 AB8 ALA C 241 ALA C 253 1 13
HELIX 18 AB9 THR C 274 ALA C 284 1 11
HELIX 19 AC1 TRP C 298 CYS C 303 1 6
HELIX 20 AC2 CYS C 303 ARG C 317 1 15
HELIX 21 AC3 THR D 66 HIS D 71 5 6
HELIX 22 AC4 LEU D 73 ALA D 78 1 6
HELIX 23 AC5 SER D 102 SER D 118 1 17
HELIX 24 AC6 ASP D 129 ASN D 134 1 6
HELIX 25 AC7 THR D 135 ASN D 142 1 8
HELIX 26 AC8 ASP D 158 PHE D 164 5 7
HELIX 27 AC9 TRP D 176 ALA D 183 1 8
HELIX 28 AD1 ARG D 186 ALA D 193 1 8
HELIX 29 AD2 LYS D 195 HIS D 207 1 13
HELIX 30 AD3 ASN D 210 PHE D 214 5 5
HELIX 31 AD4 SER D 215 ALA D 227 1 13
HELIX 32 AD5 LYS D 228 ALA D 241 1 14
HELIX 33 AD6 ALA D 241 ALA D 253 1 13
HELIX 34 AD7 THR D 274 ALA D 284 1 11
HELIX 35 AD8 TRP D 298 CYS D 303 1 6
HELIX 36 AD9 CYS D 303 ARG D 317 1 15
HELIX 37 AE1 ASP E 67 LYS E 70 5 4
HELIX 38 AE2 LYS E 92 THR E 96 5 5
HELIX 39 AE3 GLU E 106 SER E 112 1 7
HELIX 40 AE4 LYS F 92 THR F 96 5 5
HELIX 41 AE5 GLU F 106 SER F 112 1 7
HELIX 42 AE6 THR G 66 HIS G 71 5 6
HELIX 43 AE7 LEU G 73 ALA G 78 1 6
HELIX 44 AE8 SER G 102 SER G 118 1 17
HELIX 45 AE9 ASP G 129 ASN G 134 1 6
HELIX 46 AF1 THR G 135 ASN G 142 1 8
HELIX 47 AF2 ASP G 158 PHE G 164 5 7
HELIX 48 AF3 TRP G 176 ALA G 183 1 8
HELIX 49 AF4 ARG G 186 ALA G 193 1 8
HELIX 50 AF5 LYS G 195 HIS G 207 1 13
HELIX 51 AF6 ASN G 210 PHE G 214 5 5
HELIX 52 AF7 SER G 215 ALA G 227 1 13
HELIX 53 AF8 LYS G 228 ALA G 241 1 14
HELIX 54 AF9 ALA G 241 ALA G 253 1 13
HELIX 55 AG1 THR G 274 LYS G 281 1 8
HELIX 56 AG2 TRP G 298 CYS G 303 1 6
HELIX 57 AG3 CYS G 303 ARG G 317 1 15
HELIX 58 AG4 THR H 66 HIS H 71 5 6
HELIX 59 AG5 LEU H 73 ALA H 78 1 6
HELIX 60 AG6 SER H 102 SER H 118 1 17
HELIX 61 AG7 ASP H 129 ASN H 134 1 6
HELIX 62 AG8 THR H 135 ASN H 142 1 8
HELIX 63 AG9 ASP H 158 PHE H 164 5 7
HELIX 64 AH1 TRP H 176 ALA H 183 1 8
HELIX 65 AH2 ARG H 186 ALA H 193 1 8
HELIX 66 AH3 LYS H 195 HIS H 207 1 13
HELIX 67 AH4 ASN H 210 PHE H 214 5 5
HELIX 68 AH5 SER H 215 ALA H 227 1 13
HELIX 69 AH6 LYS H 228 ALA H 241 1 14
HELIX 70 AH7 ALA H 241 ALA H 253 1 13
HELIX 71 AH8 THR H 274 ALA H 284 1 11
HELIX 72 AH9 TRP H 298 CYS H 303 1 6
HELIX 73 AI1 CYS H 303 ARG H 317 1 15
HELIX 74 AI2 LYS I 92 THR I 96 5 5
HELIX 75 AI3 GLU I 106 SER I 112 1 7
HELIX 76 AI4 LYS J 92 THR J 96 5 5
HELIX 77 AI5 GLU J 106 SER J 112 1 7
HELIX 78 AI6 THR K 66 HIS K 71 5 6
HELIX 79 AI7 LEU K 73 ALA K 78 1 6
HELIX 80 AI8 SER K 102 SER K 118 1 17
HELIX 81 AI9 ASP K 129 ASN K 134 1 6
HELIX 82 AJ1 THR K 135 ASN K 142 1 8
HELIX 83 AJ2 ASP K 158 PHE K 164 5 7
HELIX 84 AJ3 TRP K 176 ALA K 183 1 8
HELIX 85 AJ4 ARG K 186 ALA K 193 1 8
HELIX 86 AJ5 LYS K 195 HIS K 207 1 13
HELIX 87 AJ6 ASN K 210 PHE K 214 5 5
HELIX 88 AJ7 SER K 215 ALA K 227 1 13
HELIX 89 AJ8 LYS K 228 ALA K 241 1 14
HELIX 90 AJ9 ALA K 241 ALA K 253 1 13
HELIX 91 AK1 THR K 274 ALA K 282 1 9
HELIX 92 AK2 TRP K 298 CYS K 303 1 6
HELIX 93 AK3 CYS K 303 ARG K 317 1 15
HELIX 94 AK4 THR L 66 HIS L 71 5 6
HELIX 95 AK5 LEU L 73 ALA L 78 1 6
HELIX 96 AK6 SER L 102 SER L 118 1 17
HELIX 97 AK7 ASP L 129 ASN L 134 1 6
HELIX 98 AK8 THR L 135 ASN L 142 1 8
HELIX 99 AK9 ASP L 158 PHE L 164 5 7
HELIX 100 AL1 TRP L 176 ALA L 183 1 8
HELIX 101 AL2 ARG L 186 ALA L 193 1 8
HELIX 102 AL3 LYS L 195 HIS L 207 1 13
HELIX 103 AL4 ASN L 210 PHE L 214 5 5
HELIX 104 AL5 SER L 215 ALA L 227 1 13
HELIX 105 AL6 LYS L 228 ALA L 241 1 14
HELIX 106 AL7 ALA L 241 ALA L 253 1 13
HELIX 107 AL8 THR L 274 ALA L 282 1 9
HELIX 108 AL9 TRP L 298 CYS L 303 1 6
HELIX 109 AM1 CYS L 303 ARG L 317 1 15
SHEET 1 AA1 4 GLN A 5 SER A 9 0
SHEET 2 AA1 4 LEU A 20 ALA A 28 -1 O ALA A 25 N VAL A 7
SHEET 3 AA1 4 THR A 83 MET A 88 -1 O MET A 88 N LEU A 20
SHEET 4 AA1 4 PHE A 73 ASP A 78 -1 N PHE A 76 O TYR A 85
SHEET 1 AA2 6 GLY A 12 GLN A 15 0
SHEET 2 AA2 6 THR A 123 SER A 128 1 O THR A 126 N GLY A 12
SHEET 3 AA2 6 ALA A 97 ALA A 104 -1 N ALA A 97 O VAL A 125
SHEET 4 AA2 6 ALA A 35 GLN A 41 -1 N PHE A 39 O TYR A 100
SHEET 5 AA2 6 GLU A 48 VAL A 53 -1 O ALA A 51 N TRP A 38
SHEET 6 AA2 6 THR A 63 ILE A 65 -1 O ASN A 64 N ALA A 52
SHEET 1 AA3 4 GLN B 5 SER B 9 0
SHEET 2 AA3 4 LEU B 20 ALA B 28 -1 O SER B 27 N GLN B 5
SHEET 3 AA3 4 THR B 83 MET B 88 -1 O VAL B 84 N CYS B 24
SHEET 4 AA3 4 PHE B 73 ASP B 78 -1 N THR B 74 O GLN B 87
SHEET 1 AA4 6 GLY B 12 LEU B 13 0
SHEET 2 AA4 6 THR B 123 THR B 126 1 O THR B 126 N GLY B 12
SHEET 3 AA4 6 ALA B 97 ALA B 104 -1 N TYR B 99 O THR B 123
SHEET 4 AA4 6 ALA B 35 GLN B 41 -1 N PHE B 39 O TYR B 100
SHEET 5 AA4 6 GLU B 48 VAL B 53 -1 O ALA B 51 N TRP B 38
SHEET 6 AA4 6 THR B 63 ILE B 65 -1 O ASN B 64 N ALA B 52
SHEET 1 AA5 8 PHE C 34 VAL C 41 0
SHEET 2 AA5 8 VAL C 44 GLY C 52 -1 O LYS C 50 N GLU C 35
SHEET 3 AA5 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 AA5 8 LEU C 56 VAL C 60 1 N VAL C 57 O THR C 82
SHEET 5 AA5 8 PHE C 123 HIS C 128 1 O VAL C 126 N MET C 58
SHEET 6 AA5 8 ILE C 146 MET C 152 1 O ALA C 147 N PHE C 123
SHEET 7 AA5 8 THR C 261 GLY C 266 1 O MET C 262 N TYR C 151
SHEET 8 AA5 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 AA6 2 PHE C 167 THR C 168 0
SHEET 2 AA6 2 GLY C 171 GLU C 172 -1 O GLY C 171 N THR C 168
SHEET 1 AA7 8 PHE D 34 VAL D 41 0
SHEET 2 AA7 8 VAL D 44 GLY D 52 -1 O LYS D 50 N GLU D 35
SHEET 3 AA7 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 AA7 8 LEU D 56 VAL D 60 1 N VAL D 57 O THR D 82
SHEET 5 AA7 8 PHE D 123 HIS D 128 1 O VAL D 126 N VAL D 60
SHEET 6 AA7 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 AA7 8 THR D 261 GLY D 266 1 O MET D 262 N TYR D 151
SHEET 8 AA7 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 AA8 2 PHE D 167 THR D 168 0
SHEET 2 AA8 2 GLY D 171 GLU D 172 -1 O GLY D 171 N THR D 168
SHEET 1 AA9 4 GLN E 5 SER E 9 0
SHEET 2 AA9 4 LEU E 20 ALA E 28 -1 O ALA E 25 N VAL E 7
SHEET 3 AA9 4 THR E 83 MET E 88 -1 O MET E 88 N LEU E 20
SHEET 4 AA9 4 PHE E 73 ASP E 78 -1 N PHE E 76 O TYR E 85
SHEET 1 AB1 6 LEU E 13 VAL E 14 0
SHEET 2 AB1 6 THR E 123 VAL E 127 1 O THR E 126 N VAL E 14
SHEET 3 AB1 6 ALA E 97 ALA E 104 -1 N TYR E 99 O THR E 123
SHEET 4 AB1 6 ALA E 35 GLN E 41 -1 N PHE E 39 O TYR E 100
SHEET 5 AB1 6 ARG E 47 VAL E 53 -1 O ALA E 51 N TRP E 38
SHEET 6 AB1 6 THR E 63 ILE E 65 -1 O ASN E 64 N ALA E 52
SHEET 1 AB2 4 GLN F 5 SER F 9 0
SHEET 2 AB2 4 LEU F 20 ALA F 28 -1 O ALA F 25 N VAL F 7
SHEET 3 AB2 4 THR F 83 MET F 88 -1 O MET F 88 N LEU F 20
SHEET 4 AB2 4 PHE F 73 ASP F 78 -1 N PHE F 76 O TYR F 85
SHEET 1 AB3 6 LEU F 13 GLN F 15 0
SHEET 2 AB3 6 THR F 123 SER F 128 1 O THR F 126 N VAL F 14
SHEET 3 AB3 6 ALA F 97 ALA F 104 -1 N ALA F 97 O VAL F 125
SHEET 4 AB3 6 ALA F 35 GLN F 41 -1 N PHE F 39 O TYR F 100
SHEET 5 AB3 6 GLU F 48 VAL F 53 -1 O VAL F 53 N MET F 36
SHEET 6 AB3 6 THR F 63 ILE F 65 -1 O ASN F 64 N ALA F 52
SHEET 1 AB4 8 GLU G 35 VAL G 41 0
SHEET 2 AB4 8 VAL G 44 GLY G 52 -1 O VAL G 44 N VAL G 41
SHEET 3 AB4 8 THR G 82 PRO G 86 -1 O VAL G 83 N GLY G 51
SHEET 4 AB4 8 LEU G 56 VAL G 60 1 N VAL G 57 O THR G 82
SHEET 5 AB4 8 PHE G 123 HIS G 128 1 O VAL G 126 N MET G 58
SHEET 6 AB4 8 ILE G 146 MET G 152 1 O ALA G 147 N PHE G 123
SHEET 7 AB4 8 THR G 261 GLY G 266 1 O LEU G 264 N TYR G 151
SHEET 8 AB4 8 VAL G 287 LEU G 292 1 O LEU G 292 N ALA G 265
SHEET 1 AB5 2 PHE G 167 THR G 168 0
SHEET 2 AB5 2 GLY G 171 GLU G 172 -1 O GLY G 171 N THR G 168
SHEET 1 AB6 8 GLU H 35 VAL H 41 0
SHEET 2 AB6 8 VAL H 44 GLY H 52 -1 O VAL H 44 N VAL H 41
SHEET 3 AB6 8 THR H 82 PRO H 86 -1 O VAL H 83 N GLY H 51
SHEET 4 AB6 8 LEU H 56 VAL H 60 1 N LEU H 59 O ILE H 84
SHEET 5 AB6 8 PHE H 123 HIS H 128 1 O VAL H 126 N VAL H 60
SHEET 6 AB6 8 ILE H 146 MET H 152 1 O ALA H 147 N PHE H 123
SHEET 7 AB6 8 THR H 261 GLY H 266 1 O MET H 262 N LEU H 149
SHEET 8 AB6 8 VAL H 287 LEU H 292 1 O LEU H 292 N ALA H 265
SHEET 1 AB7 2 PHE H 167 THR H 168 0
SHEET 2 AB7 2 GLY H 171 GLU H 172 -1 O GLY H 171 N THR H 168
SHEET 1 AB8 4 GLN I 5 SER I 9 0
SHEET 2 AB8 4 SER I 19 ALA I 28 -1 O ALA I 25 N VAL I 7
SHEET 3 AB8 4 THR I 83 ASN I 89 -1 O MET I 88 N LEU I 20
SHEET 4 AB8 4 PHE I 73 ASP I 78 -1 N PHE I 76 O TYR I 85
SHEET 1 AB9 6 GLY I 12 LEU I 13 0
SHEET 2 AB9 6 THR I 123 THR I 126 1 O THR I 126 N GLY I 12
SHEET 3 AB9 6 ALA I 97 ALA I 104 -1 N TYR I 99 O THR I 123
SHEET 4 AB9 6 ALA I 35 GLN I 41 -1 N PHE I 39 O TYR I 100
SHEET 5 AB9 6 GLU I 48 VAL I 53 -1 O ALA I 51 N TRP I 38
SHEET 6 AB9 6 THR I 63 ILE I 65 -1 O ASN I 64 N ALA I 52
SHEET 1 AC1 4 GLN J 5 SER J 9 0
SHEET 2 AC1 4 LEU J 20 ALA J 28 -1 O SER J 27 N GLN J 5
SHEET 3 AC1 4 THR J 83 MET J 88 -1 O MET J 88 N LEU J 20
SHEET 4 AC1 4 PHE J 73 ASP J 78 -1 N PHE J 76 O TYR J 85
SHEET 1 AC2 6 GLY J 12 GLN J 15 0
SHEET 2 AC2 6 THR J 123 SER J 128 1 O THR J 126 N GLY J 12
SHEET 3 AC2 6 ALA J 97 ALA J 104 -1 N TYR J 99 O THR J 123
SHEET 4 AC2 6 ALA J 35 GLN J 41 -1 N PHE J 39 O TYR J 100
SHEET 5 AC2 6 GLU J 48 VAL J 53 -1 O VAL J 50 N TRP J 38
SHEET 6 AC2 6 THR J 63 ILE J 65 -1 O ASN J 64 N ALA J 52
SHEET 1 AC3 8 GLU K 35 VAL K 41 0
SHEET 2 AC3 8 VAL K 44 GLY K 52 -1 O VAL K 44 N VAL K 41
SHEET 3 AC3 8 THR K 82 PRO K 86 -1 O VAL K 83 N GLY K 51
SHEET 4 AC3 8 LEU K 56 VAL K 60 1 N VAL K 57 O THR K 82
SHEET 5 AC3 8 PHE K 123 HIS K 128 1 O ASP K 124 N LEU K 56
SHEET 6 AC3 8 ILE K 146 MET K 152 1 O ALA K 147 N PHE K 123
SHEET 7 AC3 8 THR K 261 GLY K 266 1 O MET K 262 N LEU K 149
SHEET 8 AC3 8 VAL K 287 LEU K 292 1 O LEU K 292 N ALA K 265
SHEET 1 AC4 2 PHE K 167 THR K 168 0
SHEET 2 AC4 2 GLY K 171 GLU K 172 -1 O GLY K 171 N THR K 168
SHEET 1 AC5 8 PHE L 34 VAL L 41 0
SHEET 2 AC5 8 VAL L 44 GLY L 52 -1 O LYS L 50 N GLU L 35
SHEET 3 AC5 8 THR L 82 PRO L 86 -1 O VAL L 83 N GLY L 51
SHEET 4 AC5 8 LEU L 56 VAL L 60 1 N VAL L 57 O THR L 82
SHEET 5 AC5 8 PHE L 123 HIS L 128 1 O VAL L 126 N VAL L 60
SHEET 6 AC5 8 ILE L 146 MET L 152 1 O ALA L 147 N PHE L 123
SHEET 7 AC5 8 THR L 261 GLY L 266 1 O MET L 262 N LEU L 149
SHEET 8 AC5 8 VAL L 287 LEU L 292 1 O LEU L 292 N ALA L 265
SHEET 1 AC6 2 PHE L 167 THR L 168 0
SHEET 2 AC6 2 GLY L 171 GLU L 172 -1 O GLY L 171 N THR L 168
SSBOND 1 CYS A 24 CYS A 101 1555 1555 2.05
SSBOND 2 CYS B 24 CYS B 101 1555 1555 2.05
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.01
SSBOND 4 CYS D 295 CYS D 303 1555 1555 2.01
SSBOND 5 CYS E 24 CYS E 101 1555 1555 2.05
SSBOND 6 CYS F 24 CYS F 101 1555 1555 2.05
SSBOND 7 CYS G 295 CYS G 303 1555 1555 2.02
SSBOND 8 CYS H 295 CYS H 303 1555 1555 2.02
SSBOND 9 CYS I 24 CYS I 101 1555 1555 2.04
SSBOND 10 CYS J 24 CYS J 101 1555 1555 2.06
SSBOND 11 CYS K 295 CYS K 303 1555 1555 2.02
SSBOND 12 CYS L 295 CYS L 303 1555 1555 2.02
CRYST1 188.960 91.990 151.215 90.00 92.54 90.00 C 1 2 1 24
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 0.005292 0.000000 0.000235 0.00000
SCALE2 0.000000 0.010871 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006620 0.00000
MTRIX1 1 0.283714 -0.035834 0.958239 -55.87156 1
MTRIX2 1 -0.067503 -0.997569 -0.017318 40.11452 1
MTRIX3 1 0.956530 -0.059770 -0.285443 77.17412 1
MTRIX1 2 -0.455936 -0.019270 0.889804 -71.89500 1
MTRIX2 2 0.002411 0.999735 0.022886 30.79743 1
MTRIX3 2 -0.890009 0.012580 -0.455769 33.03208 1
MTRIX1 3 0.695210 -0.005523 -0.718786 20.39594 1
MTRIX2 3 -0.017317 -0.999809 -0.009066 74.10964 1
MTRIX3 3 -0.718599 0.018750 -0.695172 46.97146 1
MTRIX1 4 -0.992575 0.028654 -0.118213 -47.01345 1
MTRIX2 4 -0.018944 -0.996414 -0.082463 103.22834 1
MTRIX3 4 -0.120152 -0.079611 0.989558 -1.93145 1
MTRIX1 5 -0.422283 0.001008 -0.906463 -0.68110 1
MTRIX2 5 -0.027406 0.999528 0.013879 58.18623 1
MTRIX3 5 0.906050 0.030704 -0.422056 77.93901 1
MTRIX1 6 0.287714 -0.023909 0.957418 -55.86098 1
MTRIX2 6 -0.019641 -0.999625 -0.019061 42.69624 1
MTRIX3 6 0.957515 -0.013320 -0.288076 75.90692 1
MTRIX1 7 -0.482816 0.003755 0.875714 -73.42243 1
MTRIX2 7 -0.011773 0.999873 -0.010778 31.18347 1
MTRIX3 7 -0.875642 -0.015514 -0.482711 35.31489 1
MTRIX1 8 0.711517 0.001460 -0.702667 20.49603 1
MTRIX2 8 -0.011863 -0.999830 -0.014090 74.50097 1
MTRIX3 8 -0.702568 0.018361 -0.711379 48.25836 1
MTRIX1 9 -0.990908 0.005676 -0.134420 -45.78161 1
MTRIX2 9 0.004158 -0.997340 -0.072769 104.28904 1
MTRIX3 9 -0.134476 -0.072666 0.988249 -2.76024 1
MTRIX1 10 -0.401335 0.012733 -0.915843 0.42767 1
MTRIX2 10 -0.058331 0.997518 0.039430 55.49649 1
MTRIX3 10 0.914072 0.069246 -0.399597 76.51564 1
TER 930 SER A 128
TER 1854 VAL B 127
TER 4203 ARG C 319
TER 6552 ARG D 319
TER 7491 SER E 128
TER 8436 SER F 129
TER 10770 ARG G 317
TER 13119 ARG H 319
TER 14043 VAL I 127
TER 14979 SER J 129
TER 17313 ARG K 317
TER 19662 ARG L 319
MASTER 809 0 0 109 120 0 0 3620572 12 24 216
END |