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HEADER HYDROLASE 25-MAY-17 5O3U
TITLE STRUCTURAL CHARACTERIZATION OF THE FAST AND PROMISCUOUS MACROCYCLASE
TITLE 2 FROM PLANT - PCY1-S562A BOUND TO PRESEGETALIN F1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDE CYCLASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PUTATIVE PRESEGETALIN F1;
COMPND 8 CHAIN: L, M, N, O;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VACCARIA HISPANICA;
SOURCE 3 ORGANISM_TAXID: 39387;
SOURCE 4 GENE: PCY1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: VACCARIA HISPANICA;
SOURCE 9 ORGANISM_TAXID: 39387;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS SEGETALIN BIOSYNTHESIS, PROLYL OLIGOPEPTIDASE, MACROCYCLASE,
KEYWDS 2 PEPTIDASE, BETA-PROPELLER, CLOSED FORM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LUDEWIG,C.M.CZEKSTER,A.F.BENT,J.H.NAISMITH
REVDAT 4 27-NOV-19 5O3U 1 REMARK
REVDAT 3 16-OCT-19 5O3U 1 REMARK
REVDAT 2 28-MAR-18 5O3U 1 JRNL
REVDAT 1 07-FEB-18 5O3U 0
JRNL AUTH H.LUDEWIG,C.M.CZEKSTER,E.OUEIS,E.S.MUNDAY,M.ARSHAD,
JRNL AUTH 2 S.A.SYNOWSKY,A.F.BENT,J.H.NAISMITH
JRNL TITL CHARACTERIZATION OF THE FAST AND PROMISCUOUS MACROCYCLASE
JRNL TITL 2 FROM PLANT PCY1 ENABLES THE USE OF SIMPLE SUBSTRATES.
JRNL REF ACS CHEM. BIOL. V. 13 801 2018
JRNL REFN ESSN 1554-8937
JRNL PMID 29377663
JRNL DOI 10.1021/ACSCHEMBIO.8B00050
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 222236
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11725
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 16211
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.44
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE SET COUNT : 851
REMARK 3 BIN FREE R VALUE : 0.3640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23233
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.58000
REMARK 3 B22 (A**2) : 0.27000
REMARK 3 B33 (A**2) : 0.48000
REMARK 3 B12 (A**2) : 0.79000
REMARK 3 B13 (A**2) : 0.63000
REMARK 3 B23 (A**2) : -0.75000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.163
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.142
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.108
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.593
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 23977 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 21720 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 32513 ; 1.441 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 50487 ; 0.938 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2920 ; 6.333 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1185 ;32.177 ;23.975
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3993 ;12.381 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 147 ;17.865 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3448 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 26843 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5128 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 11635 ; 1.889 ; 1.010
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 11634 ; 1.888 ; 1.010
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14522 ; 2.815 ; 1.502
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 14523 ; 2.815 ; 1.502
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 12342 ; 3.337 ; 1.386
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 12342 ; 3.337 ; 1.386
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 17975 ; 4.988 ; 1.937
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 26160 ; 6.678 ;12.531
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 26014 ; 6.682 ;12.394
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 12
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 5 724 B 5 724 46924 0.07 0.05
REMARK 3 2 A 5 723 C 5 723 46882 0.07 0.05
REMARK 3 3 A 2 724 D 2 724 47488 0.06 0.05
REMARK 3 4 B 5 724 C 5 724 47218 0.07 0.05
REMARK 3 5 B 5 724 D 5 724 46998 0.06 0.05
REMARK 3 6 C 5 723 D 5 723 47314 0.07 0.05
REMARK 3 7 L 1 25 M 1 25 658 0.05 0.05
REMARK 3 8 L 1 25 N 1 25 654 0.01 0.05
REMARK 3 9 L 1 25 O 1 25 658 0.04 0.05
REMARK 3 10 M 1 25 N 1 25 654 0.01 0.05
REMARK 3 11 M 1 25 O 1 25 702 0.05 0.05
REMARK 3 12 N 1 25 O 1 25 658 0.01 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 32
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 68
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7850 -43.1450 284.3140
REMARK 3 T TENSOR
REMARK 3 T11: 0.2500 T22: 0.1276
REMARK 3 T33: 0.0395 T12: -0.0861
REMARK 3 T13: -0.0564 T23: 0.0608
REMARK 3 L TENSOR
REMARK 3 L11: 2.0712 L22: 1.1615
REMARK 3 L33: 1.3410 L12: -0.4477
REMARK 3 L13: -0.7542 L23: 0.1609
REMARK 3 S TENSOR
REMARK 3 S11: -0.0031 S12: 0.2475 S13: 0.1256
REMARK 3 S21: -0.0742 S22: -0.0419 S23: -0.0772
REMARK 3 S31: -0.1027 S32: 0.1202 S33: 0.0450
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 69 A 152
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1920 -38.0100 321.3180
REMARK 3 T TENSOR
REMARK 3 T11: 0.1526 T22: 0.0323
REMARK 3 T33: 0.0515 T12: -0.0348
REMARK 3 T13: -0.0366 T23: 0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 2.2613 L22: 0.7805
REMARK 3 L33: 4.8500 L12: -0.7638
REMARK 3 L13: 2.5669 L23: -1.1334
REMARK 3 S TENSOR
REMARK 3 S11: 0.0270 S12: -0.0705 S13: 0.0745
REMARK 3 S21: 0.0217 S22: -0.0487 S23: -0.0065
REMARK 3 S31: -0.0737 S32: 0.0581 S33: 0.0218
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 153 A 296
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8900 -50.5260 325.7620
REMARK 3 T TENSOR
REMARK 3 T11: 0.1588 T22: 0.1134
REMARK 3 T33: 0.0676 T12: -0.0220
REMARK 3 T13: -0.0490 T23: 0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 1.1370 L22: 3.3263
REMARK 3 L33: 1.1788 L12: -0.0385
REMARK 3 L13: -0.3095 L23: 1.0563
REMARK 3 S TENSOR
REMARK 3 S11: 0.0346 S12: 0.0880 S13: -0.0531
REMARK 3 S21: -0.1038 S22: 0.0298 S23: -0.2302
REMARK 3 S31: -0.0070 S32: 0.1330 S33: -0.0644
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 297 A 436
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5740 -62.6360 325.3550
REMARK 3 T TENSOR
REMARK 3 T11: 0.2090 T22: 0.0925
REMARK 3 T33: 0.0713 T12: -0.0483
REMARK 3 T13: -0.0377 T23: 0.0735
REMARK 3 L TENSOR
REMARK 3 L11: 1.6924 L22: 1.3746
REMARK 3 L33: 1.1005 L12: -1.0013
REMARK 3 L13: 0.9882 L23: -0.4645
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: -0.2131 S13: -0.1050
REMARK 3 S21: 0.0718 S22: 0.1056 S23: 0.1269
REMARK 3 S31: 0.0427 S32: -0.1671 S33: -0.1022
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 437 A 676
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2340 -57.3360 294.5920
REMARK 3 T TENSOR
REMARK 3 T11: 0.1860 T22: 0.0281
REMARK 3 T33: 0.0307 T12: -0.0393
REMARK 3 T13: -0.0586 T23: 0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 1.0818 L22: 0.8101
REMARK 3 L33: 0.9945 L12: 0.0506
REMARK 3 L13: -0.1688 L23: -0.0610
REMARK 3 S TENSOR
REMARK 3 S11: 0.0022 S12: 0.0333 S13: 0.0120
REMARK 3 S21: -0.0120 S22: 0.0126 S23: 0.0369
REMARK 3 S31: 0.0013 S32: 0.0326 S33: -0.0148
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 677 A 724
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6560 -41.4430 292.5530
REMARK 3 T TENSOR
REMARK 3 T11: 0.2091 T22: 0.0514
REMARK 3 T33: 0.0672 T12: -0.0293
REMARK 3 T13: -0.0490 T23: 0.0501
REMARK 3 L TENSOR
REMARK 3 L11: 1.1602 L22: 1.9238
REMARK 3 L33: 3.1477 L12: -0.1629
REMARK 3 L13: -0.2506 L23: 1.5946
REMARK 3 S TENSOR
REMARK 3 S11: -0.0431 S12: 0.0609 S13: 0.0407
REMARK 3 S21: 0.0245 S22: 0.0782 S23: -0.0327
REMARK 3 S31: -0.0745 S32: 0.1614 S33: -0.0351
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 8 B 68
REMARK 3 ORIGIN FOR THE GROUP (A): -26.7350 -16.7470 285.6160
REMARK 3 T TENSOR
REMARK 3 T11: 0.2802 T22: 0.2376
REMARK 3 T33: 0.1405 T12: 0.0158
REMARK 3 T13: -0.1187 T23: -0.0927
REMARK 3 L TENSOR
REMARK 3 L11: 1.8927 L22: 2.1443
REMARK 3 L33: 1.6695 L12: -0.5937
REMARK 3 L13: 1.0430 L23: 0.3798
REMARK 3 S TENSOR
REMARK 3 S11: 0.2090 S12: 0.4145 S13: -0.2876
REMARK 3 S21: -0.2525 S22: -0.2928 S23: 0.2535
REMARK 3 S31: -0.0549 S32: -0.1012 S33: 0.0839
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 69 B 152
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1830 -25.0220 321.8880
REMARK 3 T TENSOR
REMARK 3 T11: 0.1579 T22: 0.0515
REMARK 3 T33: 0.0819 T12: -0.0312
REMARK 3 T13: -0.0296 T23: 0.0590
REMARK 3 L TENSOR
REMARK 3 L11: 2.1737 L22: 0.7624
REMARK 3 L33: 4.7265 L12: -0.7597
REMARK 3 L13: -2.6265 L23: 0.6596
REMARK 3 S TENSOR
REMARK 3 S11: -0.0279 S12: -0.0713 S13: -0.1501
REMARK 3 S21: 0.0955 S22: -0.0035 S23: 0.0773
REMARK 3 S31: 0.0510 S32: -0.0591 S33: 0.0315
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 153 B 277
REMARK 3 ORIGIN FOR THE GROUP (A): -35.6880 -15.0660 326.9390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1402 T22: 0.1117
REMARK 3 T33: 0.0740 T12: -0.0300
REMARK 3 T13: -0.0090 T23: 0.0397
REMARK 3 L TENSOR
REMARK 3 L11: 1.1962 L22: 3.7389
REMARK 3 L33: 0.8222 L12: -0.1759
REMARK 3 L13: 0.2723 L23: -0.4963
REMARK 3 S TENSOR
REMARK 3 S11: -0.0569 S12: 0.0216 S13: -0.0622
REMARK 3 S21: -0.0936 S22: 0.0067 S23: 0.1607
REMARK 3 S31: 0.0490 S32: -0.0665 S33: 0.0502
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 278 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): -20.4100 2.3940 329.4730
REMARK 3 T TENSOR
REMARK 3 T11: 0.1863 T22: 0.0599
REMARK 3 T33: 0.0281 T12: -0.0374
REMARK 3 T13: -0.0655 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 2.3111 L22: 1.3505
REMARK 3 L33: 1.8659 L12: -0.6981
REMARK 3 L13: -1.0092 L23: 0.0390
REMARK 3 S TENSOR
REMARK 3 S11: -0.0424 S12: -0.2215 S13: 0.1134
REMARK 3 S21: 0.0827 S22: 0.0989 S23: -0.0505
REMARK 3 S31: -0.0106 S32: 0.1587 S33: -0.0565
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 402 B 465
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2380 -6.1100 316.1510
REMARK 3 T TENSOR
REMARK 3 T11: 0.1931 T22: 0.1212
REMARK 3 T33: 0.0933 T12: -0.0453
REMARK 3 T13: -0.0500 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 1.0420 L22: 2.1927
REMARK 3 L33: 1.6428 L12: -0.2508
REMARK 3 L13: 0.1253 L23: -1.0889
REMARK 3 S TENSOR
REMARK 3 S11: -0.0284 S12: -0.2260 S13: 0.0137
REMARK 3 S21: 0.1849 S22: 0.0686 S23: -0.1739
REMARK 3 S31: -0.0631 S32: 0.1427 S33: -0.0402
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 466 B 724
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8250 -6.3030 295.5660
REMARK 3 T TENSOR
REMARK 3 T11: 0.1916 T22: 0.0441
REMARK 3 T33: 0.0333 T12: -0.0332
REMARK 3 T13: -0.0462 T23: 0.0323
REMARK 3 L TENSOR
REMARK 3 L11: 1.1654 L22: 1.0594
REMARK 3 L33: 0.6464 L12: -0.2306
REMARK 3 L13: 0.0206 L23: 0.2230
REMARK 3 S TENSOR
REMARK 3 S11: 0.0407 S12: 0.0713 S13: -0.0381
REMARK 3 S21: -0.0910 S22: -0.0448 S23: -0.0244
REMARK 3 S31: -0.0104 S32: -0.0099 S33: 0.0040
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 5 C 68
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9390 -27.9850 400.7990
REMARK 3 T TENSOR
REMARK 3 T11: 0.3220 T22: 0.2111
REMARK 3 T33: 0.0779 T12: 0.0376
REMARK 3 T13: -0.0304 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 3.0219 L22: 1.6509
REMARK 3 L33: 1.6545 L12: 0.2223
REMARK 3 L13: -1.1828 L23: 0.2331
REMARK 3 S TENSOR
REMARK 3 S11: 0.0391 S12: -0.4482 S13: 0.2448
REMARK 3 S21: 0.1703 S22: -0.0565 S23: 0.0996
REMARK 3 S31: -0.1614 S32: -0.1565 S33: 0.0174
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 69 C 152
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4840 -20.4630 363.8900
REMARK 3 T TENSOR
REMARK 3 T11: 0.1790 T22: 0.0464
REMARK 3 T33: 0.1018 T12: -0.0220
REMARK 3 T13: -0.0169 T23: 0.0624
REMARK 3 L TENSOR
REMARK 3 L11: 2.4695 L22: 0.6240
REMARK 3 L33: 4.0545 L12: 0.5765
REMARK 3 L13: 2.4711 L23: 0.6496
REMARK 3 S TENSOR
REMARK 3 S11: 0.0083 S12: 0.0826 S13: 0.1222
REMARK 3 S21: 0.0089 S22: 0.0005 S23: 0.0859
REMARK 3 S31: -0.0945 S32: -0.0447 S33: -0.0088
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 153 C 297
REMARK 3 ORIGIN FOR THE GROUP (A): -8.8790 -31.8120 358.7620
REMARK 3 T TENSOR
REMARK 3 T11: 0.1529 T22: 0.1163
REMARK 3 T33: 0.1226 T12: -0.0232
REMARK 3 T13: -0.0238 T23: 0.0464
REMARK 3 L TENSOR
REMARK 3 L11: 0.7585 L22: 3.9191
REMARK 3 L33: 0.8585 L12: -0.3309
REMARK 3 L13: -0.1213 L23: -0.4196
REMARK 3 S TENSOR
REMARK 3 S11: -0.0043 S12: -0.0420 S13: -0.0032
REMARK 3 S21: 0.1378 S22: -0.0014 S23: 0.2411
REMARK 3 S31: -0.0527 S32: -0.1252 S33: 0.0058
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 298 C 551
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5480 -44.9430 368.9570
REMARK 3 T TENSOR
REMARK 3 T11: 0.1901 T22: 0.0763
REMARK 3 T33: 0.0465 T12: -0.0297
REMARK 3 T13: -0.0348 T23: 0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 0.4614 L22: 0.2407
REMARK 3 L33: 0.9181 L12: 0.0011
REMARK 3 L13: 0.4203 L23: 0.0248
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: 0.1236 S13: 0.0028
REMARK 3 S21: -0.0002 S22: 0.0193 S23: -0.0436
REMARK 3 S31: -0.0222 S32: 0.1477 S33: -0.0213
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 552 C 697
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6390 -37.9160 394.8380
REMARK 3 T TENSOR
REMARK 3 T11: 0.2380 T22: 0.0648
REMARK 3 T33: 0.0219 T12: 0.0023
REMARK 3 T13: -0.0115 T23: 0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 1.9244 L22: 1.5485
REMARK 3 L33: 1.6279 L12: 0.2960
REMARK 3 L13: 0.3217 L23: 0.3252
REMARK 3 S TENSOR
REMARK 3 S11: -0.0407 S12: -0.0936 S13: 0.0463
REMARK 3 S21: 0.1372 S22: 0.0159 S23: 0.0720
REMARK 3 S31: -0.1287 S32: -0.1445 S33: 0.0248
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 698 C 724
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8290 -26.3480 389.1040
REMARK 3 T TENSOR
REMARK 3 T11: 0.2718 T22: 0.0183
REMARK 3 T33: 0.1020 T12: -0.0435
REMARK 3 T13: -0.0003 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 2.3111 L22: 2.7285
REMARK 3 L33: 5.2837 L12: -1.5864
REMARK 3 L13: 1.3045 L23: -2.9956
REMARK 3 S TENSOR
REMARK 3 S11: 0.0532 S12: -0.0651 S13: -0.0460
REMARK 3 S21: -0.0147 S22: 0.1310 S23: 0.0264
REMARK 3 S31: 0.0812 S32: -0.0650 S33: -0.1842
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 4 D 68
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8600 -2.6060 401.7700
REMARK 3 T TENSOR
REMARK 3 T11: 0.4318 T22: 0.2981
REMARK 3 T33: 0.0705 T12: 0.1269
REMARK 3 T13: -0.0193 T23: 0.0719
REMARK 3 L TENSOR
REMARK 3 L11: 2.3987 L22: 1.4028
REMARK 3 L33: 1.7539 L12: 0.2665
REMARK 3 L13: 0.8583 L23: 0.3509
REMARK 3 S TENSOR
REMARK 3 S11: -0.0092 S12: -0.4122 S13: -0.1855
REMARK 3 S21: 0.1479 S22: -0.0004 S23: -0.1638
REMARK 3 S31: 0.2935 S32: 0.3705 S33: 0.0096
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 69 D 152
REMARK 3 ORIGIN FOR THE GROUP (A): -32.8120 -7.0620 364.7240
REMARK 3 T TENSOR
REMARK 3 T11: 0.1682 T22: 0.0236
REMARK 3 T33: 0.0462 T12: -0.0273
REMARK 3 T13: -0.0292 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 2.3232 L22: 1.1258
REMARK 3 L33: 4.5399 L12: 0.5471
REMARK 3 L13: -2.5642 L23: -0.6477
REMARK 3 S TENSOR
REMARK 3 S11: -0.0386 S12: 0.0808 S13: -0.0575
REMARK 3 S21: 0.0509 S22: 0.0091 S23: 0.0513
REMARK 3 S31: 0.0955 S32: 0.0020 S33: 0.0295
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 153 D 296
REMARK 3 ORIGIN FOR THE GROUP (A): -11.7710 5.2880 360.4120
REMARK 3 T TENSOR
REMARK 3 T11: 0.1425 T22: 0.1387
REMARK 3 T33: 0.1170 T12: -0.0432
REMARK 3 T13: -0.0310 T23: -0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 1.3170 L22: 3.6849
REMARK 3 L33: 1.2752 L12: -0.0529
REMARK 3 L13: -0.2794 L23: 0.5465
REMARK 3 S TENSOR
REMARK 3 S11: 0.0185 S12: -0.1701 S13: 0.1680
REMARK 3 S21: 0.1202 S22: 0.1092 S23: -0.2901
REMARK 3 S31: 0.0149 S32: 0.2277 S33: -0.1277
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 297 D 397
REMARK 3 ORIGIN FOR THE GROUP (A): -31.1590 22.1850 361.1330
REMARK 3 T TENSOR
REMARK 3 T11: 0.2211 T22: 0.0641
REMARK 3 T33: 0.1703 T12: 0.0006
REMARK 3 T13: 0.0323 T23: 0.0874
REMARK 3 L TENSOR
REMARK 3 L11: 2.5232 L22: 0.6918
REMARK 3 L33: 3.0423 L12: 0.4170
REMARK 3 L13: -1.7263 L23: 0.1790
REMARK 3 S TENSOR
REMARK 3 S11: 0.2856 S12: 0.1646 S13: 0.3661
REMARK 3 S21: -0.0501 S22: 0.0906 S23: 0.0767
REMARK 3 S31: -0.2952 S32: -0.2749 S33: -0.3762
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 398 D 436
REMARK 3 ORIGIN FOR THE GROUP (A): -44.4220 6.8240 361.0480
REMARK 3 T TENSOR
REMARK 3 T11: 0.2041 T22: 0.1883
REMARK 3 T33: 0.1358 T12: -0.0252
REMARK 3 T13: -0.0416 T23: 0.0549
REMARK 3 L TENSOR
REMARK 3 L11: 4.1534 L22: 2.2350
REMARK 3 L33: 7.3326 L12: 1.5086
REMARK 3 L13: -3.5419 L23: -1.9997
REMARK 3 S TENSOR
REMARK 3 S11: 0.0394 S12: 0.6154 S13: 0.3483
REMARK 3 S21: -0.2993 S22: 0.1787 S23: 0.3481
REMARK 3 S31: -0.1007 S32: -0.3788 S33: -0.2181
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 437 D 724
REMARK 3 ORIGIN FOR THE GROUP (A): -32.8620 9.2040 392.0110
REMARK 3 T TENSOR
REMARK 3 T11: 0.2431 T22: 0.1103
REMARK 3 T33: 0.0302 T12: 0.0043
REMARK 3 T13: -0.0449 T23: 0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 0.7096 L22: 1.1074
REMARK 3 L33: 1.3756 L12: -0.1953
REMARK 3 L13: -0.3687 L23: 0.2879
REMARK 3 S TENSOR
REMARK 3 S11: -0.0817 S12: -0.1592 S13: 0.0180
REMARK 3 S21: 0.1139 S22: 0.1336 S23: -0.0669
REMARK 3 S31: 0.1649 S32: 0.2301 S33: -0.0519
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 12
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9310 -52.2120 311.5760
REMARK 3 T TENSOR
REMARK 3 T11: 0.2944 T22: 0.2197
REMARK 3 T33: 0.2732 T12: -0.0300
REMARK 3 T13: 0.0438 T23: 0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.0102 L22: 0.7653
REMARK 3 L33: 11.8917 L12: -0.0603
REMARK 3 L13: -0.1908 L23: 2.8412
REMARK 3 S TENSOR
REMARK 3 S11: -0.0403 S12: 0.0093 S13: 0.0013
REMARK 3 S21: 0.0485 S22: -0.0236 S23: 0.1271
REMARK 3 S31: -0.2439 S32: 0.1596 S33: 0.0640
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 20 L 25
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5550 -42.0560 310.9120
REMARK 3 T TENSOR
REMARK 3 T11: 0.1932 T22: 0.0859
REMARK 3 T33: 0.1214 T12: -0.0037
REMARK 3 T13: -0.0170 T23: 0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 14.2459 L22: 4.8726
REMARK 3 L33: 7.5426 L12: 3.5506
REMARK 3 L13: 6.8550 L23: 3.2457
REMARK 3 S TENSOR
REMARK 3 S11: 0.0704 S12: 0.2482 S13: 0.0285
REMARK 3 S21: -0.0740 S22: -0.1018 S23: 0.2546
REMARK 3 S31: 0.4047 S32: 0.2435 S33: 0.0314
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 1 M 11
REMARK 3 ORIGIN FOR THE GROUP (A): -23.9340 -9.9780 313.6460
REMARK 3 T TENSOR
REMARK 3 T11: 0.2780 T22: 0.2477
REMARK 3 T33: 0.2371 T12: -0.0395
REMARK 3 T13: -0.0502 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 0.0489 L22: 0.9046
REMARK 3 L33: 10.2938 L12: 0.2050
REMARK 3 L13: -0.6509 L23: -2.8791
REMARK 3 S TENSOR
REMARK 3 S11: 0.0105 S12: -0.0274 S13: -0.0316
REMARK 3 S21: -0.0342 S22: -0.0414 S23: -0.1585
REMARK 3 S31: 0.3318 S32: 0.0305 S33: 0.0309
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 19 M 25
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5620 -18.9680 312.6630
REMARK 3 T TENSOR
REMARK 3 T11: 0.1972 T22: 0.0994
REMARK 3 T33: 0.1805 T12: -0.0120
REMARK 3 T13: -0.0260 T23: 0.0320
REMARK 3 L TENSOR
REMARK 3 L11: 9.1557 L22: 3.7423
REMARK 3 L33: 5.1689 L12: -0.2167
REMARK 3 L13: -4.0311 L23: 0.7793
REMARK 3 S TENSOR
REMARK 3 S11: 0.1345 S12: 0.2628 S13: 0.3275
REMARK 3 S21: 0.0273 S22: -0.1334 S23: 0.0409
REMARK 3 S31: -0.2880 S32: -0.3611 S33: -0.0011
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 11
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6070 -35.3660 372.5420
REMARK 3 T TENSOR
REMARK 3 T11: 0.3897 T22: 0.3335
REMARK 3 T33: 0.3367 T12: 0.0173
REMARK 3 T13: 0.0677 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.2024 L22: 2.5799
REMARK 3 L33: 19.7719 L12: -0.7040
REMARK 3 L13: 1.8548 L23: -6.4572
REMARK 3 S TENSOR
REMARK 3 S11: 0.0410 S12: 0.0246 S13: 0.0512
REMARK 3 S21: -0.0226 S22: 0.0514 S23: -0.1678
REMARK 3 S31: -0.2940 S32: 0.1466 S33: -0.0924
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 20 N 25
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1050 -25.8210 373.8980
REMARK 3 T TENSOR
REMARK 3 T11: 0.2247 T22: 0.0749
REMARK 3 T33: 0.1573 T12: -0.0340
REMARK 3 T13: 0.0188 T23: 0.0550
REMARK 3 L TENSOR
REMARK 3 L11: 10.1221 L22: 3.9014
REMARK 3 L33: 15.8058 L12: -3.4680
REMARK 3 L13: 8.7221 L23: -3.0821
REMARK 3 S TENSOR
REMARK 3 S11: 0.0411 S12: -0.2314 S13: -0.3772
REMARK 3 S21: 0.2468 S22: 0.0236 S23: -0.0134
REMARK 3 S31: 0.0848 S32: -0.2096 S33: -0.0647
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 11
REMARK 3 ORIGIN FOR THE GROUP (A): -24.2970 7.1530 374.5650
REMARK 3 T TENSOR
REMARK 3 T11: 0.2866 T22: 0.2202
REMARK 3 T33: 0.2150 T12: 0.0255
REMARK 3 T13: -0.0547 T23: 0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.4533 L22: 1.7988
REMARK 3 L33: 11.1992 L12: -0.0480
REMARK 3 L13: -1.2069 L23: 3.9034
REMARK 3 S TENSOR
REMARK 3 S11: -0.0225 S12: -0.0185 S13: 0.0404
REMARK 3 S21: -0.0599 S22: 0.0296 S23: 0.0661
REMARK 3 S31: 0.0240 S32: 0.0862 S33: -0.0072
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 19 O 25
REMARK 3 ORIGIN FOR THE GROUP (A): -35.2220 -2.1540 374.6550
REMARK 3 T TENSOR
REMARK 3 T11: 0.4017 T22: 0.1985
REMARK 3 T33: 0.1365 T12: -0.1128
REMARK 3 T13: 0.0360 T23: -0.0633
REMARK 3 L TENSOR
REMARK 3 L11: 12.2719 L22: 8.9971
REMARK 3 L33: 4.2175 L12: -3.0190
REMARK 3 L13: 0.4343 L23: 2.6239
REMARK 3 S TENSOR
REMARK 3 S11: -0.0195 S12: -0.3012 S13: 0.8016
REMARK 3 S21: 0.3646 S22: 0.1193 S23: -0.1085
REMARK 3 S31: -0.2549 S32: 0.2392 S33: -0.0998
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5O3U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1200005112.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9785
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 222236
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 73.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: APO PCY1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PCY1-S562A COMPLEX WITH PRESEGF1 WAS
REMARK 280 CRYSTALLIZED AT 13.0 MG/ML WITH 0.161.3 MM PRESEGB1 IN 27% (W/V)
REMARK 280 PEG 3350, 100 MM CA CHLORIDE AND 0.1 M BIS-TRIS AT PH 6.5. FOR
REMARK 280 CRYO PROTECTION 10 % (V/V) GLYCEROL WERE ADDED TO RESERVOIR
REMARK 280 SOLUTION., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, M
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, N
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, O
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 LYS A 199
REMARK 465 GLU A 200
REMARK 465 GLY A 201
REMARK 465 GLU A 202
REMARK 465 ASP A 203
REMARK 465 HIS A 204
REMARK 465 MET A 205
REMARK 465 THR A 206
REMARK 465 ARG A 207
REMARK 465 GLY A 282
REMARK 465 ARG A 283
REMARK 465 GLU A 284
REMARK 465 ASP A 285
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 SER B 4
REMARK 465 LEU B 198
REMARK 465 LYS B 199
REMARK 465 GLU B 200
REMARK 465 GLY B 201
REMARK 465 GLU B 202
REMARK 465 ASP B 203
REMARK 465 HIS B 204
REMARK 465 MET B 205
REMARK 465 THR B 206
REMARK 465 ARG B 207
REMARK 465 SER B 208
REMARK 465 ARG B 281
REMARK 465 GLY B 282
REMARK 465 ARG B 283
REMARK 465 GLU B 284
REMARK 465 ASP B 285
REMARK 465 LYS B 421
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 THR C 3
REMARK 465 SER C 4
REMARK 465 LEU C 198
REMARK 465 LYS C 199
REMARK 465 GLU C 200
REMARK 465 GLY C 201
REMARK 465 GLU C 202
REMARK 465 ASP C 203
REMARK 465 HIS C 204
REMARK 465 MET C 205
REMARK 465 THR C 206
REMARK 465 ARG C 207
REMARK 465 SER C 208
REMARK 465 GLY C 282
REMARK 465 ARG C 283
REMARK 465 GLU C 284
REMARK 465 MET D 1
REMARK 465 LEU D 198
REMARK 465 LYS D 199
REMARK 465 GLU D 200
REMARK 465 GLY D 201
REMARK 465 GLU D 202
REMARK 465 ASP D 203
REMARK 465 HIS D 204
REMARK 465 MET D 205
REMARK 465 THR D 206
REMARK 465 ARG D 207
REMARK 465 SER D 208
REMARK 465 ARG D 283
REMARK 465 GLU D 284
REMARK 465 MET L -12
REMARK 465 ALA L -11
REMARK 465 THR L -10
REMARK 465 SER L -9
REMARK 465 PHE L -8
REMARK 465 GLN L -7
REMARK 465 PHE L -6
REMARK 465 ASP L -5
REMARK 465 GLY L -4
REMARK 465 LEU L -3
REMARK 465 LYS L -2
REMARK 465 PRO L -1
REMARK 465 SER L 0
REMARK 465 GLN L 13
REMARK 465 VAL L 14
REMARK 465 SER L 15
REMARK 465 ASN L 16
REMARK 465 GLY L 17
REMARK 465 MET L 18
REMARK 465 ASP L 19
REMARK 465 MET M -12
REMARK 465 ALA M -11
REMARK 465 THR M -10
REMARK 465 SER M -9
REMARK 465 PHE M -8
REMARK 465 GLN M -7
REMARK 465 PHE M -6
REMARK 465 ASP M -5
REMARK 465 GLY M -4
REMARK 465 LEU M -3
REMARK 465 LYS M -2
REMARK 465 PRO M -1
REMARK 465 SER M 0
REMARK 465 THR M 12
REMARK 465 GLN M 13
REMARK 465 VAL M 14
REMARK 465 SER M 15
REMARK 465 ASN M 16
REMARK 465 GLY M 17
REMARK 465 MET M 18
REMARK 465 MET N -12
REMARK 465 ALA N -11
REMARK 465 THR N -10
REMARK 465 SER N -9
REMARK 465 PHE N -8
REMARK 465 GLN N -7
REMARK 465 PHE N -6
REMARK 465 ASP N -5
REMARK 465 GLY N -4
REMARK 465 LEU N -3
REMARK 465 LYS N -2
REMARK 465 PRO N -1
REMARK 465 SER N 0
REMARK 465 THR N 12
REMARK 465 GLN N 13
REMARK 465 VAL N 14
REMARK 465 SER N 15
REMARK 465 ASN N 16
REMARK 465 GLY N 17
REMARK 465 MET N 18
REMARK 465 ASP N 19
REMARK 465 MET O -12
REMARK 465 ALA O -11
REMARK 465 THR O -10
REMARK 465 SER O -9
REMARK 465 PHE O -8
REMARK 465 GLN O -7
REMARK 465 PHE O -6
REMARK 465 ASP O -5
REMARK 465 GLY O -4
REMARK 465 LEU O -3
REMARK 465 LYS O -2
REMARK 465 PRO O -1
REMARK 465 SER O 0
REMARK 465 THR O 12
REMARK 465 GLN O 13
REMARK 465 VAL O 14
REMARK 465 SER O 15
REMARK 465 ASN O 16
REMARK 465 GLY O 17
REMARK 465 MET O 18
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS B 8 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU B 139 O HOH B 801 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY C 697 C GLY C 697 O -0.115
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP C 399 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG D 231 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG D 231 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 89 -122.53 49.70
REMARK 500 LYS A 177 -84.22 -118.07
REMARK 500 ALA A 318 77.48 -158.11
REMARK 500 LYS A 321 162.10 71.32
REMARK 500 GLU A 354 -47.94 69.75
REMARK 500 ASP A 423 64.98 -152.01
REMARK 500 TYR A 481 -72.39 -132.57
REMARK 500 ARG A 528 -122.47 56.53
REMARK 500 ARG A 554 -19.42 90.14
REMARK 500 ALA A 562 -111.83 64.92
REMARK 500 CYS A 586 52.27 36.99
REMARK 500 CYS A 586 51.77 37.68
REMARK 500 THR A 598 -115.03 37.55
REMARK 500 CYS A 673 -65.81 -124.86
REMARK 500 SER B 7 -30.10 -136.25
REMARK 500 ALA B 89 -121.53 49.27
REMARK 500 LYS B 177 -84.49 -116.78
REMARK 500 ALA B 318 78.00 -157.20
REMARK 500 LYS B 321 159.84 70.74
REMARK 500 GLU B 354 -45.27 68.97
REMARK 500 ASP B 423 65.45 -150.80
REMARK 500 THR B 425 -11.77 95.10
REMARK 500 TYR B 481 -72.19 -132.40
REMARK 500 ARG B 528 -122.52 56.17
REMARK 500 ARG B 554 -16.54 87.83
REMARK 500 ALA B 562 -111.26 65.05
REMARK 500 CYS B 586 51.63 37.67
REMARK 500 THR B 598 -114.48 36.96
REMARK 500 CYS B 673 -65.57 -124.68
REMARK 500 ALA C 89 -120.85 48.48
REMARK 500 LYS C 177 -83.84 -117.52
REMARK 500 ALA C 318 77.81 -158.89
REMARK 500 LYS C 321 162.20 71.59
REMARK 500 GLU C 354 -50.20 66.82
REMARK 500 ALA C 395 148.22 -172.17
REMARK 500 ASP C 423 65.49 -151.84
REMARK 500 TYR C 481 -72.67 -132.34
REMARK 500 ARG C 528 -122.33 56.29
REMARK 500 ARG C 554 -19.91 90.46
REMARK 500 ALA C 562 -111.25 65.07
REMARK 500 CYS C 586 51.22 37.71
REMARK 500 THR C 598 -114.91 37.39
REMARK 500 CYS C 673 -64.91 -124.79
REMARK 500 ALA D 89 -121.53 47.25
REMARK 500 LYS D 177 -84.55 -116.73
REMARK 500 ALA D 318 77.81 -158.10
REMARK 500 LYS D 321 161.98 71.31
REMARK 500 GLU D 354 -50.38 69.48
REMARK 500 ASP D 423 64.82 -151.47
REMARK 500 THR D 425 -9.71 93.74
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR C 696 GLY C 697 149.38
REMARK 500 GLY C 697 ARG C 698 -131.63
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5O3U A 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5O3U B 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5O3U C 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5O3U D 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5O3U L -12 25 UNP F6LNM3 F6LNM3_9CARY 1 38
DBREF 5O3U M -12 25 UNP F6LNM3 F6LNM3_9CARY 1 38
DBREF 5O3U N -12 25 UNP F6LNM3 F6LNM3_9CARY 1 38
DBREF 5O3U O -12 25 UNP F6LNM3 F6LNM3_9CARY 1 38
SEQADV 5O3U ALA A 562 UNP R4P353 SER 562 ENGINEERED MUTATION
SEQADV 5O3U ALA B 562 UNP R4P353 SER 562 ENGINEERED MUTATION
SEQADV 5O3U ALA C 562 UNP R4P353 SER 562 ENGINEERED MUTATION
SEQADV 5O3U ALA D 562 UNP R4P353 SER 562 ENGINEERED MUTATION
SEQRES 1 A 724 MET ALA THR SER GLY PHE SER LYS PRO LEU HIS TYR PRO
SEQRES 2 A 724 PRO VAL ARG ARG ASP GLU THR VAL VAL ASP ASP TYR PHE
SEQRES 3 A 724 GLY VAL LYS VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP
SEQRES 4 A 724 PRO ASN SER GLU GLU THR LYS GLU PHE VAL ASP ASN GLN
SEQRES 5 A 724 GLU LYS LEU ALA ASN SER VAL LEU GLU GLU CYS GLU LEU
SEQRES 6 A 724 ILE ASP LYS PHE LYS GLN LYS ILE ILE ASP PHE VAL ASN
SEQRES 7 A 724 PHE PRO ARG CYS GLY VAL PRO PHE ARG ARG ALA ASN LYS
SEQRES 8 A 724 TYR PHE HIS PHE TYR ASN SER GLY LEU GLN ALA GLN ASN
SEQRES 9 A 724 VAL PHE GLN MET GLN ASP ASP LEU ASP GLY LYS PRO GLU
SEQRES 10 A 724 VAL LEU TYR ASP PRO ASN LEU ARG GLU GLY GLY ARG SER
SEQRES 11 A 724 GLY LEU SER LEU TYR SER VAL SER GLU ASP ALA LYS TYR
SEQRES 12 A 724 PHE ALA PHE GLY ILE HIS SER GLY LEU THR GLU TRP VAL
SEQRES 13 A 724 THR ILE LYS ILE LEU LYS THR GLU ASP ARG SER TYR LEU
SEQRES 14 A 724 PRO ASP THR LEU GLU TRP VAL LYS PHE SER PRO ALA ILE
SEQRES 15 A 724 TRP THR HIS ASP ASN LYS GLY PHE PHE TYR CYS PRO TYR
SEQRES 16 A 724 PRO PRO LEU LYS GLU GLY GLU ASP HIS MET THR ARG SER
SEQRES 17 A 724 ALA VAL ASN GLN GLU ALA ARG TYR HIS PHE LEU GLY THR
SEQRES 18 A 724 ASP GLN SER GLU ASP ILE LEU LEU TRP ARG ASP LEU GLU
SEQRES 19 A 724 ASN PRO ALA HIS HIS LEU LYS CYS GLN ILE THR ASP ASP
SEQRES 20 A 724 GLY LYS TYR PHE LEU LEU TYR ILE LEU ASP GLY CYS ASP
SEQRES 21 A 724 ASP ALA ASN LYS VAL TYR CYS LEU ASP LEU THR LYS LEU
SEQRES 22 A 724 PRO ASN GLY LEU GLU SER PHE ARG GLY ARG GLU ASP SER
SEQRES 23 A 724 ALA PRO PHE MET LYS LEU ILE ASP SER PHE ASP ALA SER
SEQRES 24 A 724 TYR THR ALA ILE ALA ASN ASP GLY SER VAL PHE THR PHE
SEQRES 25 A 724 GLN THR ASN LYS ASP ALA PRO ARG LYS LYS LEU VAL ARG
SEQRES 26 A 724 VAL ASP LEU ASN ASN PRO SER VAL TRP THR ASP LEU VAL
SEQRES 27 A 724 PRO GLU SER LYS LYS ASP LEU LEU GLU SER ALA HIS ALA
SEQRES 28 A 724 VAL ASN GLU ASN GLN LEU ILE LEU ARG TYR LEU SER ASP
SEQRES 29 A 724 VAL LYS HIS VAL LEU GLU ILE ARG ASP LEU GLU SER GLY
SEQRES 30 A 724 ALA LEU GLN HIS ARG LEU PRO ILE ASP ILE GLY SER VAL
SEQRES 31 A 724 ASP GLY ILE THR ALA ARG ARG ARG ASP SER VAL VAL PHE
SEQRES 32 A 724 PHE LYS PHE THR SER ILE LEU THR PRO GLY ILE VAL TYR
SEQRES 33 A 724 GLN CYS ASP LEU LYS ASN ASP PRO THR GLN LEU LYS ILE
SEQRES 34 A 724 PHE ARG GLU SER VAL VAL PRO ASP PHE ASP ARG SER GLU
SEQRES 35 A 724 PHE GLU VAL LYS GLN VAL PHE VAL PRO SER LYS ASP GLY
SEQRES 36 A 724 THR LYS ILE PRO ILE PHE ILE ALA ALA ARG LYS GLY ILE
SEQRES 37 A 724 SER LEU ASP GLY SER HIS PRO CYS GLU MET HIS GLY TYR
SEQRES 38 A 724 GLY GLY PHE GLY ILE ASN MET MET PRO THR PHE SER ALA
SEQRES 39 A 724 SER ARG ILE VAL PHE LEU LYS HIS LEU GLY GLY VAL PHE
SEQRES 40 A 724 CYS LEU ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY GLU
SEQRES 41 A 724 GLU TRP HIS LYS ALA GLY PHE ARG ASP LYS LYS GLN ASN
SEQRES 42 A 724 VAL PHE ASP ASP PHE ILE SER ALA ALA GLU TYR LEU ILE
SEQRES 43 A 724 SER SER GLY TYR THR LYS ALA ARG ARG VAL ALA ILE GLU
SEQRES 44 A 724 GLY GLY ALA ASN GLY GLY LEU LEU VAL ALA ALA CYS ILE
SEQRES 45 A 724 ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA GLU ALA ASN
SEQRES 46 A 724 CYS GLY VAL MET ASP MET LEU ARG PHE HIS LYS PHE THR
SEQRES 47 A 724 LEU GLY TYR LEU TRP THR GLY ASP TYR GLY CYS SER ASP
SEQRES 48 A 724 LYS GLU GLU GLU PHE LYS TRP LEU ILE LYS TYR SER PRO
SEQRES 49 A 724 ILE HIS ASN VAL ARG ARG PRO TRP GLU GLN PRO GLY ASN
SEQRES 50 A 724 GLU GLU THR GLN TYR PRO ALA THR MET ILE LEU THR ALA
SEQRES 51 A 724 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER PHE LYS
SEQRES 52 A 724 LEU LEU ALA THR MET GLN HIS VAL LEU CYS THR SER LEU
SEQRES 53 A 724 GLU ASP SER PRO GLN LYS ASN PRO ILE ILE ALA ARG ILE
SEQRES 54 A 724 GLN ARG LYS ALA ALA HIS TYR GLY ARG ALA THR MET THR
SEQRES 55 A 724 GLN ILE ALA GLU VAL ALA ASP ARG TYR GLY PHE MET ALA
SEQRES 56 A 724 LYS ALA LEU GLU ALA PRO TRP ILE ASP
SEQRES 1 B 724 MET ALA THR SER GLY PHE SER LYS PRO LEU HIS TYR PRO
SEQRES 2 B 724 PRO VAL ARG ARG ASP GLU THR VAL VAL ASP ASP TYR PHE
SEQRES 3 B 724 GLY VAL LYS VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP
SEQRES 4 B 724 PRO ASN SER GLU GLU THR LYS GLU PHE VAL ASP ASN GLN
SEQRES 5 B 724 GLU LYS LEU ALA ASN SER VAL LEU GLU GLU CYS GLU LEU
SEQRES 6 B 724 ILE ASP LYS PHE LYS GLN LYS ILE ILE ASP PHE VAL ASN
SEQRES 7 B 724 PHE PRO ARG CYS GLY VAL PRO PHE ARG ARG ALA ASN LYS
SEQRES 8 B 724 TYR PHE HIS PHE TYR ASN SER GLY LEU GLN ALA GLN ASN
SEQRES 9 B 724 VAL PHE GLN MET GLN ASP ASP LEU ASP GLY LYS PRO GLU
SEQRES 10 B 724 VAL LEU TYR ASP PRO ASN LEU ARG GLU GLY GLY ARG SER
SEQRES 11 B 724 GLY LEU SER LEU TYR SER VAL SER GLU ASP ALA LYS TYR
SEQRES 12 B 724 PHE ALA PHE GLY ILE HIS SER GLY LEU THR GLU TRP VAL
SEQRES 13 B 724 THR ILE LYS ILE LEU LYS THR GLU ASP ARG SER TYR LEU
SEQRES 14 B 724 PRO ASP THR LEU GLU TRP VAL LYS PHE SER PRO ALA ILE
SEQRES 15 B 724 TRP THR HIS ASP ASN LYS GLY PHE PHE TYR CYS PRO TYR
SEQRES 16 B 724 PRO PRO LEU LYS GLU GLY GLU ASP HIS MET THR ARG SER
SEQRES 17 B 724 ALA VAL ASN GLN GLU ALA ARG TYR HIS PHE LEU GLY THR
SEQRES 18 B 724 ASP GLN SER GLU ASP ILE LEU LEU TRP ARG ASP LEU GLU
SEQRES 19 B 724 ASN PRO ALA HIS HIS LEU LYS CYS GLN ILE THR ASP ASP
SEQRES 20 B 724 GLY LYS TYR PHE LEU LEU TYR ILE LEU ASP GLY CYS ASP
SEQRES 21 B 724 ASP ALA ASN LYS VAL TYR CYS LEU ASP LEU THR LYS LEU
SEQRES 22 B 724 PRO ASN GLY LEU GLU SER PHE ARG GLY ARG GLU ASP SER
SEQRES 23 B 724 ALA PRO PHE MET LYS LEU ILE ASP SER PHE ASP ALA SER
SEQRES 24 B 724 TYR THR ALA ILE ALA ASN ASP GLY SER VAL PHE THR PHE
SEQRES 25 B 724 GLN THR ASN LYS ASP ALA PRO ARG LYS LYS LEU VAL ARG
SEQRES 26 B 724 VAL ASP LEU ASN ASN PRO SER VAL TRP THR ASP LEU VAL
SEQRES 27 B 724 PRO GLU SER LYS LYS ASP LEU LEU GLU SER ALA HIS ALA
SEQRES 28 B 724 VAL ASN GLU ASN GLN LEU ILE LEU ARG TYR LEU SER ASP
SEQRES 29 B 724 VAL LYS HIS VAL LEU GLU ILE ARG ASP LEU GLU SER GLY
SEQRES 30 B 724 ALA LEU GLN HIS ARG LEU PRO ILE ASP ILE GLY SER VAL
SEQRES 31 B 724 ASP GLY ILE THR ALA ARG ARG ARG ASP SER VAL VAL PHE
SEQRES 32 B 724 PHE LYS PHE THR SER ILE LEU THR PRO GLY ILE VAL TYR
SEQRES 33 B 724 GLN CYS ASP LEU LYS ASN ASP PRO THR GLN LEU LYS ILE
SEQRES 34 B 724 PHE ARG GLU SER VAL VAL PRO ASP PHE ASP ARG SER GLU
SEQRES 35 B 724 PHE GLU VAL LYS GLN VAL PHE VAL PRO SER LYS ASP GLY
SEQRES 36 B 724 THR LYS ILE PRO ILE PHE ILE ALA ALA ARG LYS GLY ILE
SEQRES 37 B 724 SER LEU ASP GLY SER HIS PRO CYS GLU MET HIS GLY TYR
SEQRES 38 B 724 GLY GLY PHE GLY ILE ASN MET MET PRO THR PHE SER ALA
SEQRES 39 B 724 SER ARG ILE VAL PHE LEU LYS HIS LEU GLY GLY VAL PHE
SEQRES 40 B 724 CYS LEU ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY GLU
SEQRES 41 B 724 GLU TRP HIS LYS ALA GLY PHE ARG ASP LYS LYS GLN ASN
SEQRES 42 B 724 VAL PHE ASP ASP PHE ILE SER ALA ALA GLU TYR LEU ILE
SEQRES 43 B 724 SER SER GLY TYR THR LYS ALA ARG ARG VAL ALA ILE GLU
SEQRES 44 B 724 GLY GLY ALA ASN GLY GLY LEU LEU VAL ALA ALA CYS ILE
SEQRES 45 B 724 ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA GLU ALA ASN
SEQRES 46 B 724 CYS GLY VAL MET ASP MET LEU ARG PHE HIS LYS PHE THR
SEQRES 47 B 724 LEU GLY TYR LEU TRP THR GLY ASP TYR GLY CYS SER ASP
SEQRES 48 B 724 LYS GLU GLU GLU PHE LYS TRP LEU ILE LYS TYR SER PRO
SEQRES 49 B 724 ILE HIS ASN VAL ARG ARG PRO TRP GLU GLN PRO GLY ASN
SEQRES 50 B 724 GLU GLU THR GLN TYR PRO ALA THR MET ILE LEU THR ALA
SEQRES 51 B 724 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER PHE LYS
SEQRES 52 B 724 LEU LEU ALA THR MET GLN HIS VAL LEU CYS THR SER LEU
SEQRES 53 B 724 GLU ASP SER PRO GLN LYS ASN PRO ILE ILE ALA ARG ILE
SEQRES 54 B 724 GLN ARG LYS ALA ALA HIS TYR GLY ARG ALA THR MET THR
SEQRES 55 B 724 GLN ILE ALA GLU VAL ALA ASP ARG TYR GLY PHE MET ALA
SEQRES 56 B 724 LYS ALA LEU GLU ALA PRO TRP ILE ASP
SEQRES 1 C 724 MET ALA THR SER GLY PHE SER LYS PRO LEU HIS TYR PRO
SEQRES 2 C 724 PRO VAL ARG ARG ASP GLU THR VAL VAL ASP ASP TYR PHE
SEQRES 3 C 724 GLY VAL LYS VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP
SEQRES 4 C 724 PRO ASN SER GLU GLU THR LYS GLU PHE VAL ASP ASN GLN
SEQRES 5 C 724 GLU LYS LEU ALA ASN SER VAL LEU GLU GLU CYS GLU LEU
SEQRES 6 C 724 ILE ASP LYS PHE LYS GLN LYS ILE ILE ASP PHE VAL ASN
SEQRES 7 C 724 PHE PRO ARG CYS GLY VAL PRO PHE ARG ARG ALA ASN LYS
SEQRES 8 C 724 TYR PHE HIS PHE TYR ASN SER GLY LEU GLN ALA GLN ASN
SEQRES 9 C 724 VAL PHE GLN MET GLN ASP ASP LEU ASP GLY LYS PRO GLU
SEQRES 10 C 724 VAL LEU TYR ASP PRO ASN LEU ARG GLU GLY GLY ARG SER
SEQRES 11 C 724 GLY LEU SER LEU TYR SER VAL SER GLU ASP ALA LYS TYR
SEQRES 12 C 724 PHE ALA PHE GLY ILE HIS SER GLY LEU THR GLU TRP VAL
SEQRES 13 C 724 THR ILE LYS ILE LEU LYS THR GLU ASP ARG SER TYR LEU
SEQRES 14 C 724 PRO ASP THR LEU GLU TRP VAL LYS PHE SER PRO ALA ILE
SEQRES 15 C 724 TRP THR HIS ASP ASN LYS GLY PHE PHE TYR CYS PRO TYR
SEQRES 16 C 724 PRO PRO LEU LYS GLU GLY GLU ASP HIS MET THR ARG SER
SEQRES 17 C 724 ALA VAL ASN GLN GLU ALA ARG TYR HIS PHE LEU GLY THR
SEQRES 18 C 724 ASP GLN SER GLU ASP ILE LEU LEU TRP ARG ASP LEU GLU
SEQRES 19 C 724 ASN PRO ALA HIS HIS LEU LYS CYS GLN ILE THR ASP ASP
SEQRES 20 C 724 GLY LYS TYR PHE LEU LEU TYR ILE LEU ASP GLY CYS ASP
SEQRES 21 C 724 ASP ALA ASN LYS VAL TYR CYS LEU ASP LEU THR LYS LEU
SEQRES 22 C 724 PRO ASN GLY LEU GLU SER PHE ARG GLY ARG GLU ASP SER
SEQRES 23 C 724 ALA PRO PHE MET LYS LEU ILE ASP SER PHE ASP ALA SER
SEQRES 24 C 724 TYR THR ALA ILE ALA ASN ASP GLY SER VAL PHE THR PHE
SEQRES 25 C 724 GLN THR ASN LYS ASP ALA PRO ARG LYS LYS LEU VAL ARG
SEQRES 26 C 724 VAL ASP LEU ASN ASN PRO SER VAL TRP THR ASP LEU VAL
SEQRES 27 C 724 PRO GLU SER LYS LYS ASP LEU LEU GLU SER ALA HIS ALA
SEQRES 28 C 724 VAL ASN GLU ASN GLN LEU ILE LEU ARG TYR LEU SER ASP
SEQRES 29 C 724 VAL LYS HIS VAL LEU GLU ILE ARG ASP LEU GLU SER GLY
SEQRES 30 C 724 ALA LEU GLN HIS ARG LEU PRO ILE ASP ILE GLY SER VAL
SEQRES 31 C 724 ASP GLY ILE THR ALA ARG ARG ARG ASP SER VAL VAL PHE
SEQRES 32 C 724 PHE LYS PHE THR SER ILE LEU THR PRO GLY ILE VAL TYR
SEQRES 33 C 724 GLN CYS ASP LEU LYS ASN ASP PRO THR GLN LEU LYS ILE
SEQRES 34 C 724 PHE ARG GLU SER VAL VAL PRO ASP PHE ASP ARG SER GLU
SEQRES 35 C 724 PHE GLU VAL LYS GLN VAL PHE VAL PRO SER LYS ASP GLY
SEQRES 36 C 724 THR LYS ILE PRO ILE PHE ILE ALA ALA ARG LYS GLY ILE
SEQRES 37 C 724 SER LEU ASP GLY SER HIS PRO CYS GLU MET HIS GLY TYR
SEQRES 38 C 724 GLY GLY PHE GLY ILE ASN MET MET PRO THR PHE SER ALA
SEQRES 39 C 724 SER ARG ILE VAL PHE LEU LYS HIS LEU GLY GLY VAL PHE
SEQRES 40 C 724 CYS LEU ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY GLU
SEQRES 41 C 724 GLU TRP HIS LYS ALA GLY PHE ARG ASP LYS LYS GLN ASN
SEQRES 42 C 724 VAL PHE ASP ASP PHE ILE SER ALA ALA GLU TYR LEU ILE
SEQRES 43 C 724 SER SER GLY TYR THR LYS ALA ARG ARG VAL ALA ILE GLU
SEQRES 44 C 724 GLY GLY ALA ASN GLY GLY LEU LEU VAL ALA ALA CYS ILE
SEQRES 45 C 724 ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA GLU ALA ASN
SEQRES 46 C 724 CYS GLY VAL MET ASP MET LEU ARG PHE HIS LYS PHE THR
SEQRES 47 C 724 LEU GLY TYR LEU TRP THR GLY ASP TYR GLY CYS SER ASP
SEQRES 48 C 724 LYS GLU GLU GLU PHE LYS TRP LEU ILE LYS TYR SER PRO
SEQRES 49 C 724 ILE HIS ASN VAL ARG ARG PRO TRP GLU GLN PRO GLY ASN
SEQRES 50 C 724 GLU GLU THR GLN TYR PRO ALA THR MET ILE LEU THR ALA
SEQRES 51 C 724 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER PHE LYS
SEQRES 52 C 724 LEU LEU ALA THR MET GLN HIS VAL LEU CYS THR SER LEU
SEQRES 53 C 724 GLU ASP SER PRO GLN LYS ASN PRO ILE ILE ALA ARG ILE
SEQRES 54 C 724 GLN ARG LYS ALA ALA HIS TYR GLY ARG ALA THR MET THR
SEQRES 55 C 724 GLN ILE ALA GLU VAL ALA ASP ARG TYR GLY PHE MET ALA
SEQRES 56 C 724 LYS ALA LEU GLU ALA PRO TRP ILE ASP
SEQRES 1 D 724 MET ALA THR SER GLY PHE SER LYS PRO LEU HIS TYR PRO
SEQRES 2 D 724 PRO VAL ARG ARG ASP GLU THR VAL VAL ASP ASP TYR PHE
SEQRES 3 D 724 GLY VAL LYS VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP
SEQRES 4 D 724 PRO ASN SER GLU GLU THR LYS GLU PHE VAL ASP ASN GLN
SEQRES 5 D 724 GLU LYS LEU ALA ASN SER VAL LEU GLU GLU CYS GLU LEU
SEQRES 6 D 724 ILE ASP LYS PHE LYS GLN LYS ILE ILE ASP PHE VAL ASN
SEQRES 7 D 724 PHE PRO ARG CYS GLY VAL PRO PHE ARG ARG ALA ASN LYS
SEQRES 8 D 724 TYR PHE HIS PHE TYR ASN SER GLY LEU GLN ALA GLN ASN
SEQRES 9 D 724 VAL PHE GLN MET GLN ASP ASP LEU ASP GLY LYS PRO GLU
SEQRES 10 D 724 VAL LEU TYR ASP PRO ASN LEU ARG GLU GLY GLY ARG SER
SEQRES 11 D 724 GLY LEU SER LEU TYR SER VAL SER GLU ASP ALA LYS TYR
SEQRES 12 D 724 PHE ALA PHE GLY ILE HIS SER GLY LEU THR GLU TRP VAL
SEQRES 13 D 724 THR ILE LYS ILE LEU LYS THR GLU ASP ARG SER TYR LEU
SEQRES 14 D 724 PRO ASP THR LEU GLU TRP VAL LYS PHE SER PRO ALA ILE
SEQRES 15 D 724 TRP THR HIS ASP ASN LYS GLY PHE PHE TYR CYS PRO TYR
SEQRES 16 D 724 PRO PRO LEU LYS GLU GLY GLU ASP HIS MET THR ARG SER
SEQRES 17 D 724 ALA VAL ASN GLN GLU ALA ARG TYR HIS PHE LEU GLY THR
SEQRES 18 D 724 ASP GLN SER GLU ASP ILE LEU LEU TRP ARG ASP LEU GLU
SEQRES 19 D 724 ASN PRO ALA HIS HIS LEU LYS CYS GLN ILE THR ASP ASP
SEQRES 20 D 724 GLY LYS TYR PHE LEU LEU TYR ILE LEU ASP GLY CYS ASP
SEQRES 21 D 724 ASP ALA ASN LYS VAL TYR CYS LEU ASP LEU THR LYS LEU
SEQRES 22 D 724 PRO ASN GLY LEU GLU SER PHE ARG GLY ARG GLU ASP SER
SEQRES 23 D 724 ALA PRO PHE MET LYS LEU ILE ASP SER PHE ASP ALA SER
SEQRES 24 D 724 TYR THR ALA ILE ALA ASN ASP GLY SER VAL PHE THR PHE
SEQRES 25 D 724 GLN THR ASN LYS ASP ALA PRO ARG LYS LYS LEU VAL ARG
SEQRES 26 D 724 VAL ASP LEU ASN ASN PRO SER VAL TRP THR ASP LEU VAL
SEQRES 27 D 724 PRO GLU SER LYS LYS ASP LEU LEU GLU SER ALA HIS ALA
SEQRES 28 D 724 VAL ASN GLU ASN GLN LEU ILE LEU ARG TYR LEU SER ASP
SEQRES 29 D 724 VAL LYS HIS VAL LEU GLU ILE ARG ASP LEU GLU SER GLY
SEQRES 30 D 724 ALA LEU GLN HIS ARG LEU PRO ILE ASP ILE GLY SER VAL
SEQRES 31 D 724 ASP GLY ILE THR ALA ARG ARG ARG ASP SER VAL VAL PHE
SEQRES 32 D 724 PHE LYS PHE THR SER ILE LEU THR PRO GLY ILE VAL TYR
SEQRES 33 D 724 GLN CYS ASP LEU LYS ASN ASP PRO THR GLN LEU LYS ILE
SEQRES 34 D 724 PHE ARG GLU SER VAL VAL PRO ASP PHE ASP ARG SER GLU
SEQRES 35 D 724 PHE GLU VAL LYS GLN VAL PHE VAL PRO SER LYS ASP GLY
SEQRES 36 D 724 THR LYS ILE PRO ILE PHE ILE ALA ALA ARG LYS GLY ILE
SEQRES 37 D 724 SER LEU ASP GLY SER HIS PRO CYS GLU MET HIS GLY TYR
SEQRES 38 D 724 GLY GLY PHE GLY ILE ASN MET MET PRO THR PHE SER ALA
SEQRES 39 D 724 SER ARG ILE VAL PHE LEU LYS HIS LEU GLY GLY VAL PHE
SEQRES 40 D 724 CYS LEU ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY GLU
SEQRES 41 D 724 GLU TRP HIS LYS ALA GLY PHE ARG ASP LYS LYS GLN ASN
SEQRES 42 D 724 VAL PHE ASP ASP PHE ILE SER ALA ALA GLU TYR LEU ILE
SEQRES 43 D 724 SER SER GLY TYR THR LYS ALA ARG ARG VAL ALA ILE GLU
SEQRES 44 D 724 GLY GLY ALA ASN GLY GLY LEU LEU VAL ALA ALA CYS ILE
SEQRES 45 D 724 ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA GLU ALA ASN
SEQRES 46 D 724 CYS GLY VAL MET ASP MET LEU ARG PHE HIS LYS PHE THR
SEQRES 47 D 724 LEU GLY TYR LEU TRP THR GLY ASP TYR GLY CYS SER ASP
SEQRES 48 D 724 LYS GLU GLU GLU PHE LYS TRP LEU ILE LYS TYR SER PRO
SEQRES 49 D 724 ILE HIS ASN VAL ARG ARG PRO TRP GLU GLN PRO GLY ASN
SEQRES 50 D 724 GLU GLU THR GLN TYR PRO ALA THR MET ILE LEU THR ALA
SEQRES 51 D 724 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER PHE LYS
SEQRES 52 D 724 LEU LEU ALA THR MET GLN HIS VAL LEU CYS THR SER LEU
SEQRES 53 D 724 GLU ASP SER PRO GLN LYS ASN PRO ILE ILE ALA ARG ILE
SEQRES 54 D 724 GLN ARG LYS ALA ALA HIS TYR GLY ARG ALA THR MET THR
SEQRES 55 D 724 GLN ILE ALA GLU VAL ALA ASP ARG TYR GLY PHE MET ALA
SEQRES 56 D 724 LYS ALA LEU GLU ALA PRO TRP ILE ASP
SEQRES 1 L 38 MET ALA THR SER PHE GLN PHE ASP GLY LEU LYS PRO SER
SEQRES 2 L 38 PHE SER ALA SER TYR SER SER LYS PRO ILE GLN THR GLN
SEQRES 3 L 38 VAL SER ASN GLY MET ASP ASN ALA SER ALA PRO VAL
SEQRES 1 M 38 MET ALA THR SER PHE GLN PHE ASP GLY LEU LYS PRO SER
SEQRES 2 M 38 PHE SER ALA SER TYR SER SER LYS PRO ILE GLN THR GLN
SEQRES 3 M 38 VAL SER ASN GLY MET ASP ASN ALA SER ALA PRO VAL
SEQRES 1 N 38 MET ALA THR SER PHE GLN PHE ASP GLY LEU LYS PRO SER
SEQRES 2 N 38 PHE SER ALA SER TYR SER SER LYS PRO ILE GLN THR GLN
SEQRES 3 N 38 VAL SER ASN GLY MET ASP ASN ALA SER ALA PRO VAL
SEQRES 1 O 38 MET ALA THR SER PHE GLN PHE ASP GLY LEU LYS PRO SER
SEQRES 2 O 38 PHE SER ALA SER TYR SER SER LYS PRO ILE GLN THR GLN
SEQRES 3 O 38 VAL SER ASN GLY MET ASP ASN ALA SER ALA PRO VAL
FORMUL 9 HOH *930(H2 O)
HELIX 1 AA1 TYR A 34 ASP A 39 5 6
HELIX 2 AA2 SER A 42 GLU A 61 1 20
HELIX 3 AA3 LEU A 65 ASN A 78 1 14
HELIX 4 AA4 ASP A 121 ARG A 129 5 9
HELIX 5 AA5 ASP A 222 ASP A 226 5 5
HELIX 6 AA6 THR A 271 LEU A 273 5 3
HELIX 7 AA7 ASN A 275 ARG A 281 5 7
HELIX 8 AA8 ASP A 439 SER A 441 5 3
HELIX 9 AA9 SER A 493 LEU A 503 1 11
HELIX 10 AB1 GLY A 519 ALA A 525 1 7
HELIX 11 AB2 GLY A 526 LYS A 530 5 5
HELIX 12 AB3 LYS A 531 SER A 548 1 18
HELIX 13 AB4 ALA A 562 ARG A 575 1 14
HELIX 14 AB5 PRO A 576 PHE A 579 5 4
HELIX 15 AB6 ARG A 593 PHE A 597 5 5
HELIX 16 AB7 LEU A 599 LEU A 602 5 4
HELIX 17 AB8 TRP A 603 GLY A 608 1 6
HELIX 18 AB9 LYS A 612 SER A 623 1 12
HELIX 19 AC1 PRO A 624 ASN A 627 5 4
HELIX 20 AC2 ARG A 630 GLN A 634 5 5
HELIX 21 AC3 PRO A 658 CYS A 673 1 16
HELIX 22 AC4 ALA A 699 GLU A 719 1 21
HELIX 23 AC5 TYR B 34 ASP B 39 5 6
HELIX 24 AC6 SER B 42 GLU B 61 1 20
HELIX 25 AC7 LEU B 65 ASN B 78 1 14
HELIX 26 AC8 ASP B 121 ARG B 129 5 9
HELIX 27 AC9 ASP B 222 ASP B 226 5 5
HELIX 28 AD1 THR B 271 LEU B 273 5 3
HELIX 29 AD2 ASN B 275 PHE B 280 5 6
HELIX 30 AD3 ASP B 439 SER B 441 5 3
HELIX 31 AD4 SER B 493 LEU B 503 1 11
HELIX 32 AD5 GLY B 519 ALA B 525 1 7
HELIX 33 AD6 GLY B 526 ASP B 529 5 4
HELIX 34 AD7 LYS B 530 SER B 548 1 19
HELIX 35 AD8 ALA B 562 ARG B 575 1 14
HELIX 36 AD9 PRO B 576 PHE B 579 5 4
HELIX 37 AE1 ARG B 593 PHE B 597 5 5
HELIX 38 AE2 LEU B 599 LEU B 602 5 4
HELIX 39 AE3 TRP B 603 GLY B 608 1 6
HELIX 40 AE4 LYS B 612 SER B 623 1 12
HELIX 41 AE5 PRO B 624 ASN B 627 5 4
HELIX 42 AE6 ARG B 630 GLN B 634 5 5
HELIX 43 AE7 PRO B 658 CYS B 673 1 16
HELIX 44 AE8 ALA B 699 GLU B 719 1 21
HELIX 45 AE9 TYR C 34 ASP C 39 5 6
HELIX 46 AF1 SER C 42 GLU C 61 1 20
HELIX 47 AF2 LEU C 65 ASN C 78 1 14
HELIX 48 AF3 ASP C 121 ARG C 129 5 9
HELIX 49 AF4 ASP C 222 ASP C 226 5 5
HELIX 50 AF5 THR C 271 LEU C 273 5 3
HELIX 51 AF6 ASN C 275 ARG C 281 5 7
HELIX 52 AF7 ASP C 439 SER C 441 5 3
HELIX 53 AF8 SER C 493 LEU C 503 1 11
HELIX 54 AF9 GLY C 519 ALA C 525 1 7
HELIX 55 AG1 GLY C 526 ASP C 529 5 4
HELIX 56 AG2 LYS C 530 SER C 548 1 19
HELIX 57 AG3 ALA C 562 ARG C 575 1 14
HELIX 58 AG4 PRO C 576 PHE C 579 5 4
HELIX 59 AG5 ARG C 593 PHE C 597 5 5
HELIX 60 AG6 LEU C 599 LEU C 602 5 4
HELIX 61 AG7 TRP C 603 GLY C 608 1 6
HELIX 62 AG8 LYS C 612 SER C 623 1 12
HELIX 63 AG9 PRO C 624 ASN C 627 5 4
HELIX 64 AH1 ARG C 630 GLN C 634 5 5
HELIX 65 AH2 PRO C 658 CYS C 673 1 16
HELIX 66 AH3 ALA C 699 GLU C 719 1 21
HELIX 67 AH4 TYR D 34 ASP D 39 5 6
HELIX 68 AH5 SER D 42 GLU D 61 1 20
HELIX 69 AH6 LEU D 65 ASN D 78 1 14
HELIX 70 AH7 ASP D 121 ARG D 129 5 9
HELIX 71 AH8 ASP D 222 ASP D 226 5 5
HELIX 72 AH9 THR D 271 LEU D 273 5 3
HELIX 73 AI1 ASN D 275 ARG D 281 5 7
HELIX 74 AI2 ASP D 439 SER D 441 5 3
HELIX 75 AI3 SER D 493 LEU D 503 1 11
HELIX 76 AI4 GLY D 519 ALA D 525 1 7
HELIX 77 AI5 GLY D 526 LYS D 530 5 5
HELIX 78 AI6 LYS D 531 SER D 548 1 18
HELIX 79 AI7 ALA D 562 ARG D 575 1 14
HELIX 80 AI8 PRO D 576 PHE D 579 5 4
HELIX 81 AI9 ARG D 593 PHE D 597 5 5
HELIX 82 AJ1 LEU D 599 LEU D 602 5 4
HELIX 83 AJ2 TRP D 603 GLY D 608 1 6
HELIX 84 AJ3 LYS D 612 SER D 623 1 12
HELIX 85 AJ4 PRO D 624 ASN D 627 5 4
HELIX 86 AJ5 ARG D 630 GLN D 634 5 5
HELIX 87 AJ6 PRO D 658 CYS D 673 1 16
HELIX 88 AJ7 ALA D 699 GLU D 719 1 21
SHEET 1 AA1 2 VAL A 22 TYR A 25 0
SHEET 2 AA1 2 VAL A 28 ALA A 31 -1 O VAL A 28 N TYR A 25
SHEET 1 AA2 3 ARG A 81 CYS A 82 0
SHEET 2 AA2 3 LYS A 91 ASN A 97 -1 O ASN A 97 N ARG A 81
SHEET 3 AA2 3 PHE A 86 ARG A 88 -1 N ARG A 88 O LYS A 91
SHEET 1 AA3 4 ARG A 81 CYS A 82 0
SHEET 2 AA3 4 LYS A 91 ASN A 97 -1 O ASN A 97 N ARG A 81
SHEET 3 AA3 4 VAL A 105 GLN A 109 -1 O VAL A 105 N TYR A 96
SHEET 4 AA3 4 GLU A 117 TYR A 120 -1 O LEU A 119 N PHE A 106
SHEET 1 AA4 4 TYR A 135 VAL A 137 0
SHEET 2 AA4 4 TYR A 143 HIS A 149 -1 O ALA A 145 N SER A 136
SHEET 3 AA4 4 VAL A 156 LYS A 162 -1 O LEU A 161 N PHE A 144
SHEET 4 AA4 4 LEU A 173 VAL A 176 -1 O VAL A 176 N VAL A 156
SHEET 1 AA5 4 ILE A 182 TRP A 183 0
SHEET 2 AA5 4 GLY A 189 TYR A 192 -1 O PHE A 191 N ILE A 182
SHEET 3 AA5 4 ALA A 214 PHE A 218 -1 O ARG A 215 N TYR A 192
SHEET 4 AA5 4 ILE A 227 TRP A 230 -1 O LEU A 229 N ALA A 214
SHEET 1 AA6 4 HIS A 239 ILE A 244 0
SHEET 2 AA6 4 TYR A 250 LEU A 256 -1 O LEU A 252 N GLN A 243
SHEET 3 AA6 4 ASN A 263 ASP A 269 -1 O LEU A 268 N PHE A 251
SHEET 4 AA6 4 MET A 290 ILE A 293 -1 O MET A 290 N CYS A 267
SHEET 1 AA7 4 TYR A 300 ASP A 306 0
SHEET 2 AA7 4 VAL A 309 THR A 314 -1 O THR A 311 N ALA A 304
SHEET 3 AA7 4 LYS A 322 ASP A 327 -1 O VAL A 326 N PHE A 310
SHEET 4 AA7 4 TRP A 334 VAL A 338 -1 O LEU A 337 N LEU A 323
SHEET 1 AA8 4 LEU A 345 VAL A 352 0
SHEET 2 AA8 4 GLN A 356 SER A 363 -1 O ILE A 358 N HIS A 350
SHEET 3 AA8 4 LYS A 366 ASP A 373 -1 O LYS A 366 N SER A 363
SHEET 4 AA8 4 LEU A 379 PRO A 384 -1 O LEU A 383 N LEU A 369
SHEET 1 AA9 4 SER A 389 ASP A 391 0
SHEET 2 AA9 4 VAL A 401 SER A 408 -1 O LYS A 405 N ASP A 391
SHEET 3 AA9 4 THR A 411 ASP A 419 -1 O ILE A 414 N PHE A 406
SHEET 4 AA9 4 LYS A 428 GLU A 432 -1 O PHE A 430 N VAL A 415
SHEET 1 AB1 8 PHE A 443 PRO A 451 0
SHEET 2 AB1 8 LYS A 457 ARG A 465 -1 O ILE A 458 N VAL A 450
SHEET 3 AB1 8 VAL A 506 ALA A 510 -1 O PHE A 507 N ALA A 463
SHEET 4 AB1 8 CYS A 476 HIS A 479 1 N GLU A 477 O CYS A 508
SHEET 5 AB1 8 VAL A 556 GLY A 561 1 O ALA A 557 N CYS A 476
SHEET 6 AB1 8 CYS A 581 ASN A 585 1 O ASN A 585 N GLY A 560
SHEET 7 AB1 8 ALA A 644 ALA A 650 1 O LEU A 648 N ALA A 584
SHEET 8 AB1 8 ILE A 685 GLN A 690 1 O GLN A 690 N THR A 649
SHEET 1 AB2 2 VAL B 22 TYR B 25 0
SHEET 2 AB2 2 VAL B 28 ALA B 31 -1 O VAL B 28 N TYR B 25
SHEET 1 AB3 3 ARG B 81 CYS B 82 0
SHEET 2 AB3 3 LYS B 91 ASN B 97 -1 O ASN B 97 N ARG B 81
SHEET 3 AB3 3 PHE B 86 ARG B 88 -1 N ARG B 88 O LYS B 91
SHEET 1 AB4 4 ARG B 81 CYS B 82 0
SHEET 2 AB4 4 LYS B 91 ASN B 97 -1 O ASN B 97 N ARG B 81
SHEET 3 AB4 4 VAL B 105 GLN B 109 -1 O VAL B 105 N TYR B 96
SHEET 4 AB4 4 GLU B 117 TYR B 120 -1 O LEU B 119 N PHE B 106
SHEET 1 AB5 4 TYR B 135 VAL B 137 0
SHEET 2 AB5 4 TYR B 143 HIS B 149 -1 O ALA B 145 N SER B 136
SHEET 3 AB5 4 VAL B 156 LYS B 162 -1 O LEU B 161 N PHE B 144
SHEET 4 AB5 4 TYR B 168 VAL B 176 -1 O VAL B 176 N VAL B 156
SHEET 1 AB6 4 ILE B 182 TRP B 183 0
SHEET 2 AB6 4 GLY B 189 TYR B 192 -1 O PHE B 191 N ILE B 182
SHEET 3 AB6 4 ALA B 214 PHE B 218 -1 O ARG B 215 N TYR B 192
SHEET 4 AB6 4 ILE B 227 TRP B 230 -1 O LEU B 229 N ALA B 214
SHEET 1 AB7 4 HIS B 238 ILE B 244 0
SHEET 2 AB7 4 TYR B 250 ASP B 257 -1 O LEU B 252 N GLN B 243
SHEET 3 AB7 4 ASN B 263 ASP B 269 -1 O LEU B 268 N PHE B 251
SHEET 4 AB7 4 MET B 290 ILE B 293 -1 O MET B 290 N CYS B 267
SHEET 1 AB8 4 TYR B 300 ASP B 306 0
SHEET 2 AB8 4 VAL B 309 THR B 314 -1 O THR B 311 N ILE B 303
SHEET 3 AB8 4 LYS B 322 ASP B 327 -1 O VAL B 326 N PHE B 310
SHEET 4 AB8 4 ASN B 330 VAL B 338 -1 O LEU B 337 N LEU B 323
SHEET 1 AB9 4 LEU B 345 VAL B 352 0
SHEET 2 AB9 4 GLN B 356 SER B 363 -1 O ARG B 360 N SER B 348
SHEET 3 AB9 4 LYS B 366 ASP B 373 -1 O LYS B 366 N SER B 363
SHEET 4 AB9 4 LEU B 379 PRO B 384 -1 O LEU B 383 N LEU B 369
SHEET 1 AC1 4 SER B 389 ASP B 391 0
SHEET 2 AC1 4 VAL B 401 SER B 408 -1 O LYS B 405 N ASP B 391
SHEET 3 AC1 4 THR B 411 ASP B 419 -1 O ILE B 414 N PHE B 406
SHEET 4 AC1 4 LYS B 428 GLU B 432 -1 O PHE B 430 N VAL B 415
SHEET 1 AC2 8 PHE B 443 PRO B 451 0
SHEET 2 AC2 8 LYS B 457 ARG B 465 -1 O ILE B 458 N VAL B 450
SHEET 3 AC2 8 VAL B 506 ALA B 510 -1 O PHE B 507 N ALA B 463
SHEET 4 AC2 8 CYS B 476 HIS B 479 1 N GLU B 477 O CYS B 508
SHEET 5 AC2 8 VAL B 556 GLY B 561 1 O ALA B 557 N CYS B 476
SHEET 6 AC2 8 CYS B 581 ASN B 585 1 O ASN B 585 N GLY B 560
SHEET 7 AC2 8 ALA B 644 ALA B 650 1 O LEU B 648 N ALA B 584
SHEET 8 AC2 8 ILE B 685 GLN B 690 1 O ILE B 686 N THR B 645
SHEET 1 AC3 2 VAL C 22 TYR C 25 0
SHEET 2 AC3 2 VAL C 28 ALA C 31 -1 O VAL C 28 N TYR C 25
SHEET 1 AC4 3 ARG C 81 CYS C 82 0
SHEET 2 AC4 3 LYS C 91 ASN C 97 -1 O ASN C 97 N ARG C 81
SHEET 3 AC4 3 PHE C 86 ARG C 88 -1 N ARG C 88 O LYS C 91
SHEET 1 AC5 4 ARG C 81 CYS C 82 0
SHEET 2 AC5 4 LYS C 91 ASN C 97 -1 O ASN C 97 N ARG C 81
SHEET 3 AC5 4 VAL C 105 GLN C 109 -1 O VAL C 105 N TYR C 96
SHEET 4 AC5 4 GLU C 117 TYR C 120 -1 O LEU C 119 N PHE C 106
SHEET 1 AC6 4 TYR C 135 VAL C 137 0
SHEET 2 AC6 4 TYR C 143 HIS C 149 -1 O ALA C 145 N SER C 136
SHEET 3 AC6 4 VAL C 156 LYS C 162 -1 O LEU C 161 N PHE C 144
SHEET 4 AC6 4 TYR C 168 VAL C 176 -1 O VAL C 176 N VAL C 156
SHEET 1 AC7 4 ILE C 182 TRP C 183 0
SHEET 2 AC7 4 GLY C 189 TYR C 192 -1 O PHE C 191 N ILE C 182
SHEET 3 AC7 4 ALA C 214 PHE C 218 -1 O ARG C 215 N TYR C 192
SHEET 4 AC7 4 ILE C 227 TRP C 230 -1 O LEU C 229 N ALA C 214
SHEET 1 AC8 4 HIS C 238 ILE C 244 0
SHEET 2 AC8 4 TYR C 250 ASP C 257 -1 O LEU C 252 N GLN C 243
SHEET 3 AC8 4 ASN C 263 ASP C 269 -1 O LEU C 268 N PHE C 251
SHEET 4 AC8 4 MET C 290 ILE C 293 -1 O MET C 290 N CYS C 267
SHEET 1 AC9 4 TYR C 300 ASP C 306 0
SHEET 2 AC9 4 VAL C 309 THR C 314 -1 O THR C 311 N ALA C 304
SHEET 3 AC9 4 LYS C 322 ASP C 327 -1 O VAL C 326 N PHE C 310
SHEET 4 AC9 4 ASN C 330 VAL C 338 -1 O LEU C 337 N LEU C 323
SHEET 1 AD1 4 LEU C 345 VAL C 352 0
SHEET 2 AD1 4 GLN C 356 SER C 363 -1 O ARG C 360 N SER C 348
SHEET 3 AD1 4 LYS C 366 ASP C 373 -1 O LYS C 366 N SER C 363
SHEET 4 AD1 4 LEU C 379 PRO C 384 -1 O LEU C 383 N LEU C 369
SHEET 1 AD2 4 SER C 389 THR C 394 0
SHEET 2 AD2 4 VAL C 401 SER C 408 -1 O LYS C 405 N ASP C 391
SHEET 3 AD2 4 THR C 411 ASP C 419 -1 O ILE C 414 N PHE C 406
SHEET 4 AD2 4 LYS C 428 GLU C 432 -1 O PHE C 430 N VAL C 415
SHEET 1 AD3 8 PHE C 443 PRO C 451 0
SHEET 2 AD3 8 LYS C 457 ARG C 465 -1 O ILE C 458 N VAL C 450
SHEET 3 AD3 8 VAL C 506 ALA C 510 -1 O PHE C 507 N ALA C 463
SHEET 4 AD3 8 CYS C 476 HIS C 479 1 N GLU C 477 O CYS C 508
SHEET 5 AD3 8 VAL C 556 GLY C 561 1 O ALA C 557 N CYS C 476
SHEET 6 AD3 8 CYS C 581 ASN C 585 1 O ASN C 585 N GLY C 560
SHEET 7 AD3 8 ALA C 644 ALA C 650 1 O LEU C 648 N ALA C 584
SHEET 8 AD3 8 ILE C 685 GLN C 690 1 O GLN C 690 N THR C 649
SHEET 1 AD4 2 VAL D 22 TYR D 25 0
SHEET 2 AD4 2 VAL D 28 ALA D 31 -1 O VAL D 28 N TYR D 25
SHEET 1 AD5 3 ARG D 81 CYS D 82 0
SHEET 2 AD5 3 LYS D 91 ASN D 97 -1 O ASN D 97 N ARG D 81
SHEET 3 AD5 3 PHE D 86 ARG D 88 -1 N ARG D 88 O LYS D 91
SHEET 1 AD6 4 ARG D 81 CYS D 82 0
SHEET 2 AD6 4 LYS D 91 ASN D 97 -1 O ASN D 97 N ARG D 81
SHEET 3 AD6 4 VAL D 105 GLN D 109 -1 O VAL D 105 N TYR D 96
SHEET 4 AD6 4 GLU D 117 TYR D 120 -1 O LEU D 119 N PHE D 106
SHEET 1 AD7 4 TYR D 135 VAL D 137 0
SHEET 2 AD7 4 TYR D 143 HIS D 149 -1 O ALA D 145 N SER D 136
SHEET 3 AD7 4 VAL D 156 LYS D 162 -1 O LEU D 161 N PHE D 144
SHEET 4 AD7 4 LEU D 173 VAL D 176 -1 O VAL D 176 N VAL D 156
SHEET 1 AD8 4 ILE D 182 TRP D 183 0
SHEET 2 AD8 4 GLY D 189 TYR D 192 -1 O PHE D 191 N ILE D 182
SHEET 3 AD8 4 ALA D 214 PHE D 218 -1 O ARG D 215 N TYR D 192
SHEET 4 AD8 4 ILE D 227 TRP D 230 -1 O LEU D 229 N ALA D 214
SHEET 1 AD9 4 HIS D 239 ILE D 244 0
SHEET 2 AD9 4 TYR D 250 LEU D 256 -1 O LEU D 252 N GLN D 243
SHEET 3 AD9 4 ASN D 263 ASP D 269 -1 O LEU D 268 N PHE D 251
SHEET 4 AD9 4 MET D 290 ILE D 293 -1 O MET D 290 N CYS D 267
SHEET 1 AE1 4 TYR D 300 ASP D 306 0
SHEET 2 AE1 4 VAL D 309 THR D 314 -1 O THR D 311 N ALA D 304
SHEET 3 AE1 4 LYS D 322 ASP D 327 -1 O VAL D 326 N PHE D 310
SHEET 4 AE1 4 TRP D 334 VAL D 338 -1 O LEU D 337 N LEU D 323
SHEET 1 AE2 4 LEU D 345 VAL D 352 0
SHEET 2 AE2 4 GLN D 356 SER D 363 -1 O ILE D 358 N HIS D 350
SHEET 3 AE2 4 LYS D 366 ASP D 373 -1 O LYS D 366 N SER D 363
SHEET 4 AE2 4 LEU D 379 PRO D 384 -1 O LEU D 383 N LEU D 369
SHEET 1 AE3 4 SER D 389 ASP D 391 0
SHEET 2 AE3 4 VAL D 401 SER D 408 -1 O LYS D 405 N ASP D 391
SHEET 3 AE3 4 THR D 411 ASP D 419 -1 O ILE D 414 N PHE D 406
SHEET 4 AE3 4 LYS D 428 GLU D 432 -1 O PHE D 430 N VAL D 415
SHEET 1 AE4 8 PHE D 443 PRO D 451 0
SHEET 2 AE4 8 LYS D 457 ARG D 465 -1 O ILE D 458 N VAL D 450
SHEET 3 AE4 8 VAL D 506 ALA D 510 -1 O PHE D 507 N ALA D 463
SHEET 4 AE4 8 CYS D 476 HIS D 479 1 N GLU D 477 O CYS D 508
SHEET 5 AE4 8 VAL D 556 GLY D 561 1 O ALA D 557 N CYS D 476
SHEET 6 AE4 8 CYS D 581 ASN D 585 1 O ASN D 585 N GLY D 560
SHEET 7 AE4 8 ALA D 644 ALA D 650 1 O LEU D 648 N ALA D 584
SHEET 8 AE4 8 ILE D 685 GLN D 690 1 O GLN D 690 N THR D 649
CRYST1 64.860 85.820 137.870 87.64 78.32 89.52 P 1 4
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 0.015418 -0.000129 -0.003185 0.00000
SCALE2 0.000000 0.011653 -0.000470 0.00000
SCALE3 0.000000 0.000000 0.007413 0.00000
TER 5730 ASP A 724
TER 11401 ASP B 724
TER 17116 ASP C 724
TER 22839 ASP D 724
TER 22971 VAL L 25
TER 23104 VAL M 25
TER 23229 VAL N 25
TER 23362 VAL O 25
MASTER 1149 0 0 88 164 0 0 624163 8 0 236
END |