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HEADER HORMONE 09-DEC-20 7B75
TITLE CRYO-EM STRUCTURE OF HUMAN THYROGLOBULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYROGLOBULIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TG
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: THYROID;
SOURCE 6 TISSUE: THYROID
KEYWDS THYROGLOBULIN, T3 AND T4 HORMONOGENESIS, CRYO-EM, HORMONE
EXPDTA ELECTRON MICROSCOPY
AUTHOR R.ADAIXO,R.RIGHETTO,E.M.STEINER,N.M.I.TAYLOR,H.STAHLBERG
REVDAT 1 29-DEC-21 7B75 0
JRNL AUTH R.ADAIXO,E.M.STEINER,R.D.RIGHETTO,A.SCHMIDT,N.M.I.TAYLOR,
JRNL AUTH 2 H.STAHLBERG
JRNL TITL CRYO-EM STRUCTURE OF NATIVE HUMAN THYROGLOBULIN
JRNL REF NAT COMMUN 2021
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-021-27693-8
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : SERIALEM, FOCUS, CTFFIND, COOT, RELION,
REMARK 3 RELION, RELION, RELION
REMARK 3 RECONSTRUCTION SCHEMA : BACK PROJECTION
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : AB INITIO MODEL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.200
REMARK 3 NUMBER OF PARTICLES : 37619
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 7B75 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1292111988.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : HUMAN THYROGLOBULIN
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : HUMAN THYROGLOBULIN PURIFIED
REMARK 245 FROM THYROID GLAND TISSUE AND NON IN VITRO IODINATED
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 8119
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : TFS KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 215000
REMARK 245 CALIBRATED MAGNIFICATION : 78125
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 30340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 236890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 56.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, 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 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 LEU A 3
REMARK 465 VAL A 4
REMARK 465 LEU A 5
REMARK 465 GLU A 6
REMARK 465 ILE A 7
REMARK 465 PHE A 8
REMARK 465 THR A 9
REMARK 465 LEU A 10
REMARK 465 LEU A 11
REMARK 465 ALA A 12
REMARK 465 SER A 13
REMARK 465 ILE A 14
REMARK 465 CYS A 15
REMARK 465 TRP A 16
REMARK 465 VAL A 17
REMARK 465 SER A 18
REMARK 465 ALA A 19
REMARK 465 ASN A 20
REMARK 465 ILE A 21
REMARK 465 PHE A 22
REMARK 465 GLU A 23
REMARK 465 TYR A 24
REMARK 465 GLN A 25
REMARK 465 VAL A 26
REMARK 465 ASP A 27
REMARK 465 ALA A 28
REMARK 465 GLN A 29
REMARK 465 SER A 106
REMARK 465 GLY A 107
REMARK 465 TYR A 108
REMARK 465 ILE A 109
REMARK 465 ASN A 110
REMARK 465 SER A 111
REMARK 465 THR A 112
REMARK 465 ASP A 113
REMARK 465 THR A 114
REMARK 465 GLY A 381
REMARK 465 TYR A 382
REMARK 465 PHE A 383
REMARK 465 SER A 384
REMARK 465 GLN A 385
REMARK 465 HIS A 386
REMARK 465 ASP A 387
REMARK 465 LEU A 388
REMARK 465 PHE A 389
REMARK 465 SER A 390
REMARK 465 SER A 391
REMARK 465 PRO A 392
REMARK 465 GLU A 393
REMARK 465 LYS A 394
REMARK 465 ARG A 395
REMARK 465 TRP A 396
REMARK 465 ALA A 397
REMARK 465 SER A 398
REMARK 465 PRO A 399
REMARK 465 ARG A 400
REMARK 465 VAL A 401
REMARK 465 ALA A 402
REMARK 465 ARG A 403
REMARK 465 PHE A 404
REMARK 465 PHE A 497
REMARK 465 SER A 498
REMARK 465 GLN A 499
REMARK 465 PHE A 500
REMARK 465 PHE A 501
REMARK 465 GLN A 502
REMARK 465 GLN A 503
REMARK 465 LEU A 504
REMARK 465 GLY A 505
REMARK 465 LEU A 506
REMARK 465 ALA A 507
REMARK 465 SER A 508
REMARK 465 PHE A 509
REMARK 465 LEU A 510
REMARK 465 ASN A 511
REMARK 465 GLY A 512
REMARK 465 GLY A 513
REMARK 465 ARG A 514
REMARK 465 GLN A 515
REMARK 465 GLU A 516
REMARK 465 ASP A 517
REMARK 465 LEU A 518
REMARK 465 ALA A 519
REMARK 465 LYS A 520
REMARK 465 PRO A 521
REMARK 465 LEU A 522
REMARK 465 SER A 523
REMARK 465 VAL A 524
REMARK 465 GLY A 525
REMARK 465 LEU A 526
REMARK 465 ASP A 527
REMARK 465 SER A 528
REMARK 465 ASN A 529
REMARK 465 SER A 530
REMARK 465 SER A 531
REMARK 465 THR A 532
REMARK 465 GLY A 533
REMARK 465 THR A 534
REMARK 465 PRO A 535
REMARK 465 GLU A 536
REMARK 465 ALA A 537
REMARK 465 ALA A 538
REMARK 465 LYS A 539
REMARK 465 LYS A 540
REMARK 465 ASP A 541
REMARK 465 GLY A 542
REMARK 465 THR A 543
REMARK 465 MET A 544
REMARK 465 ASN A 545
REMARK 465 LYS A 546
REMARK 465 ALA A 812
REMARK 465 ALA A 813
REMARK 465 SER A 814
REMARK 465 GLY A 815
REMARK 465 ASN A 816
REMARK 465 PHE A 817
REMARK 465 SER A 818
REMARK 465 LEU A 819
REMARK 465 PHE A 820
REMARK 465 ILE A 821
REMARK 465 GLN A 822
REMARK 465 SER A 823
REMARK 465 LEU A 824
REMARK 465 TYR A 825
REMARK 465 GLU A 826
REMARK 465 ALA A 827
REMARK 465 GLY A 828
REMARK 465 GLN A 829
REMARK 465 GLN A 830
REMARK 465 ASP A 831
REMARK 465 VAL A 832
REMARK 465 PHE A 833
REMARK 465 PRO A 834
REMARK 465 VAL A 835
REMARK 465 LEU A 836
REMARK 465 SER A 837
REMARK 465 GLN A 838
REMARK 465 TYR A 839
REMARK 465 PRO A 840
REMARK 465 SER A 841
REMARK 465 GLU A 1232
REMARK 465 THR A 1233
REMARK 465 ILE A 1234
REMARK 465 SER A 1235
REMARK 465 GLY A 1236
REMARK 465 PRO A 1237
REMARK 465 THR A 1238
REMARK 465 GLY A 1239
REMARK 465 SER A 1240
REMARK 465 ALA A 1241
REMARK 465 MET A 1242
REMARK 465 PRO A 1261
REMARK 465 LEU A 1262
REMARK 465 ILE A 1263
REMARK 465 CYS A 1264
REMARK 465 SER A 1265
REMARK 465 LEU A 1266
REMARK 465 GLU A 1267
REMARK 465 SER A 1268
REMARK 465 GLY A 1269
REMARK 465 ARG A 1270
REMARK 465 TRP A 1271
REMARK 465 GLU A 1272
REMARK 465 SER A 1273
REMARK 465 GLN A 1353
REMARK 465 VAL A 1354
REMARK 465 GLY A 1355
REMARK 465 CYS A 1356
REMARK 465 LEU A 1357
REMARK 465 THR A 1358
REMARK 465 ARG A 1359
REMARK 465 GLU A 1360
REMARK 465 ARG A 1361
REMARK 465 LEU A 1362
REMARK 465 GLY A 1363
REMARK 465 LYS A 1415
REMARK 465 THR A 1416
REMARK 465 PHE A 1417
REMARK 465 PRO A 1418
REMARK 465 ALA A 1419
REMARK 465 GLU A 1420
REMARK 465 THR A 1421
REMARK 465 ILE A 1422
REMARK 465 ARG A 1423
REMARK 465 PHE A 1424
REMARK 465 LEU A 1425
REMARK 465 ASN A 1636
REMARK 465 VAL A 1637
REMARK 465 ALA A 1638
REMARK 465 CYS A 1639
REMARK 465 MET A 1640
REMARK 465 THR A 1641
REMARK 465 SER A 1642
REMARK 465 ASP A 1643
REMARK 465 GLN A 1644
REMARK 465 LYS A 1645
REMARK 465 ARG A 1646
REMARK 465 ASP A 1647
REMARK 465 ALA A 1648
REMARK 465 LEU A 1649
REMARK 465 GLY A 1650
REMARK 465 ASN A 1651
REMARK 465 SER A 1652
REMARK 465 LYS A 1653
REMARK 465 ALA A 1654
REMARK 465 THR A 1655
REMARK 465 SER A 1656
REMARK 465 PHE A 1657
REMARK 465 GLY A 1658
REMARK 465 SER A 1659
REMARK 465 TYR A 1782
REMARK 465 ASP A 1783
REMARK 465 GLN A 1784
REMARK 465 GLU A 1785
REMARK 465 SER A 1786
REMARK 465 HIS A 1787
REMARK 465 GLN A 1788
REMARK 465 VAL A 1789
REMARK 465 ILE A 1790
REMARK 465 LEU A 1791
REMARK 465 ARG A 1792
REMARK 465 LEU A 1793
REMARK 465 GLY A 1794
REMARK 465 ASP A 1795
REMARK 465 GLN A 1796
REMARK 465 GLU A 1797
REMARK 465 PHE A 1798
REMARK 465 ILE A 1799
REMARK 465 LYS A 1800
REMARK 465 SER A 1801
REMARK 465 LEU A 1802
REMARK 465 THR A 1803
REMARK 465 PRO A 1804
REMARK 465 LEU A 1805
REMARK 465 GLU A 1806
REMARK 465 GLY A 1807
REMARK 465 THR A 1808
REMARK 465 GLN A 1809
REMARK 465 ASP A 1810
REMARK 465 THR A 1811
REMARK 465 PHE A 1812
REMARK 465 THR A 1813
REMARK 465 SER A 2728
REMARK 465 ALA A 2729
REMARK 465 ASP A 2730
REMARK 465 GLY A 2731
REMARK 465 ALA A 2732
REMARK 465 LYS A 2733
REMARK 465 GLY A 2734
REMARK 465 GLY A 2735
REMARK 465 GLN A 2736
REMARK 465 SER A 2737
REMARK 465 ALA A 2738
REMARK 465 GLU A 2739
REMARK 465 SER A 2740
REMARK 465 GLU A 2741
REMARK 465 GLU A 2742
REMARK 465 GLU A 2743
REMARK 465 GLU A 2744
REMARK 465 LEU A 2745
REMARK 465 THR A 2746
REMARK 465 ALA A 2747
REMARK 465 GLY A 2748
REMARK 465 SER A 2749
REMARK 465 GLY A 2750
REMARK 465 LEU A 2751
REMARK 465 ARG A 2752
REMARK 465 GLU A 2753
REMARK 465 ASP A 2754
REMARK 465 LEU A 2755
REMARK 465 LEU A 2756
REMARK 465 SER A 2757
REMARK 465 LEU A 2758
REMARK 465 GLN A 2759
REMARK 465 GLU A 2760
REMARK 465 PRO A 2761
REMARK 465 GLY A 2762
REMARK 465 SER A 2763
REMARK 465 LYS A 2764
REMARK 465 THR A 2765
REMARK 465 TYR A 2766
REMARK 465 SER A 2767
REMARK 465 LYS A 2768
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 LEU B 3
REMARK 465 VAL B 4
REMARK 465 LEU B 5
REMARK 465 GLU B 6
REMARK 465 ILE B 7
REMARK 465 PHE B 8
REMARK 465 THR B 9
REMARK 465 LEU B 10
REMARK 465 LEU B 11
REMARK 465 ALA B 12
REMARK 465 SER B 13
REMARK 465 ILE B 14
REMARK 465 CYS B 15
REMARK 465 TRP B 16
REMARK 465 VAL B 17
REMARK 465 SER B 18
REMARK 465 ALA B 19
REMARK 465 ASN B 20
REMARK 465 ILE B 21
REMARK 465 PHE B 22
REMARK 465 GLU B 23
REMARK 465 TYR B 24
REMARK 465 GLN B 25
REMARK 465 VAL B 26
REMARK 465 ASP B 27
REMARK 465 ALA B 28
REMARK 465 GLN B 29
REMARK 465 SER B 106
REMARK 465 GLY B 107
REMARK 465 TYR B 108
REMARK 465 ILE B 109
REMARK 465 ASN B 110
REMARK 465 SER B 111
REMARK 465 THR B 112
REMARK 465 ASP B 113
REMARK 465 THR B 114
REMARK 465 GLY B 381
REMARK 465 TYR B 382
REMARK 465 PHE B 383
REMARK 465 SER B 384
REMARK 465 GLN B 385
REMARK 465 HIS B 386
REMARK 465 ASP B 387
REMARK 465 LEU B 388
REMARK 465 PHE B 389
REMARK 465 SER B 390
REMARK 465 SER B 391
REMARK 465 PRO B 392
REMARK 465 GLU B 393
REMARK 465 LYS B 394
REMARK 465 ARG B 395
REMARK 465 TRP B 396
REMARK 465 ALA B 397
REMARK 465 SER B 398
REMARK 465 PRO B 399
REMARK 465 ARG B 400
REMARK 465 VAL B 401
REMARK 465 ALA B 402
REMARK 465 ARG B 403
REMARK 465 PHE B 404
REMARK 465 PHE B 497
REMARK 465 SER B 498
REMARK 465 GLN B 499
REMARK 465 PHE B 500
REMARK 465 PHE B 501
REMARK 465 GLN B 502
REMARK 465 GLN B 503
REMARK 465 LEU B 504
REMARK 465 GLY B 505
REMARK 465 LEU B 506
REMARK 465 ALA B 507
REMARK 465 SER B 508
REMARK 465 PHE B 509
REMARK 465 LEU B 510
REMARK 465 ASN B 511
REMARK 465 GLY B 512
REMARK 465 GLY B 513
REMARK 465 ARG B 514
REMARK 465 GLN B 515
REMARK 465 GLU B 516
REMARK 465 ASP B 517
REMARK 465 LEU B 518
REMARK 465 ALA B 519
REMARK 465 LYS B 520
REMARK 465 PRO B 521
REMARK 465 LEU B 522
REMARK 465 SER B 523
REMARK 465 VAL B 524
REMARK 465 GLY B 525
REMARK 465 LEU B 526
REMARK 465 ASP B 527
REMARK 465 SER B 528
REMARK 465 ASN B 529
REMARK 465 SER B 530
REMARK 465 SER B 531
REMARK 465 THR B 532
REMARK 465 GLY B 533
REMARK 465 THR B 534
REMARK 465 PRO B 535
REMARK 465 GLU B 536
REMARK 465 ALA B 537
REMARK 465 ALA B 538
REMARK 465 LYS B 539
REMARK 465 LYS B 540
REMARK 465 ASP B 541
REMARK 465 GLY B 542
REMARK 465 THR B 543
REMARK 465 MET B 544
REMARK 465 ASN B 545
REMARK 465 LYS B 546
REMARK 465 ALA B 812
REMARK 465 ALA B 813
REMARK 465 SER B 814
REMARK 465 GLY B 815
REMARK 465 ASN B 816
REMARK 465 PHE B 817
REMARK 465 SER B 818
REMARK 465 LEU B 819
REMARK 465 PHE B 820
REMARK 465 ILE B 821
REMARK 465 GLN B 822
REMARK 465 SER B 823
REMARK 465 LEU B 824
REMARK 465 TYR B 825
REMARK 465 GLU B 826
REMARK 465 ALA B 827
REMARK 465 GLY B 828
REMARK 465 GLN B 829
REMARK 465 GLN B 830
REMARK 465 ASP B 831
REMARK 465 VAL B 832
REMARK 465 PHE B 833
REMARK 465 PRO B 834
REMARK 465 VAL B 835
REMARK 465 LEU B 836
REMARK 465 SER B 837
REMARK 465 GLN B 838
REMARK 465 TYR B 839
REMARK 465 PRO B 840
REMARK 465 SER B 841
REMARK 465 GLU B 1232
REMARK 465 THR B 1233
REMARK 465 ILE B 1234
REMARK 465 SER B 1235
REMARK 465 GLY B 1236
REMARK 465 PRO B 1237
REMARK 465 THR B 1238
REMARK 465 GLY B 1239
REMARK 465 SER B 1240
REMARK 465 ALA B 1241
REMARK 465 MET B 1242
REMARK 465 PRO B 1261
REMARK 465 LEU B 1262
REMARK 465 ILE B 1263
REMARK 465 CYS B 1264
REMARK 465 SER B 1265
REMARK 465 LEU B 1266
REMARK 465 GLU B 1267
REMARK 465 SER B 1268
REMARK 465 GLY B 1269
REMARK 465 ARG B 1270
REMARK 465 TRP B 1271
REMARK 465 GLU B 1272
REMARK 465 SER B 1273
REMARK 465 GLN B 1353
REMARK 465 VAL B 1354
REMARK 465 GLY B 1355
REMARK 465 CYS B 1356
REMARK 465 LEU B 1357
REMARK 465 THR B 1358
REMARK 465 ARG B 1359
REMARK 465 GLU B 1360
REMARK 465 ARG B 1361
REMARK 465 LEU B 1362
REMARK 465 GLY B 1363
REMARK 465 LYS B 1415
REMARK 465 THR B 1416
REMARK 465 PHE B 1417
REMARK 465 PRO B 1418
REMARK 465 ALA B 1419
REMARK 465 GLU B 1420
REMARK 465 THR B 1421
REMARK 465 ILE B 1422
REMARK 465 ARG B 1423
REMARK 465 PHE B 1424
REMARK 465 LEU B 1425
REMARK 465 ASN B 1636
REMARK 465 VAL B 1637
REMARK 465 ALA B 1638
REMARK 465 CYS B 1639
REMARK 465 MET B 1640
REMARK 465 THR B 1641
REMARK 465 SER B 1642
REMARK 465 ASP B 1643
REMARK 465 GLN B 1644
REMARK 465 LYS B 1645
REMARK 465 ARG B 1646
REMARK 465 ASP B 1647
REMARK 465 ALA B 1648
REMARK 465 LEU B 1649
REMARK 465 GLY B 1650
REMARK 465 ASN B 1651
REMARK 465 SER B 1652
REMARK 465 LYS B 1653
REMARK 465 ALA B 1654
REMARK 465 THR B 1655
REMARK 465 SER B 1656
REMARK 465 PHE B 1657
REMARK 465 GLY B 1658
REMARK 465 SER B 1659
REMARK 465 TYR B 1782
REMARK 465 ASP B 1783
REMARK 465 GLN B 1784
REMARK 465 GLU B 1785
REMARK 465 SER B 1786
REMARK 465 HIS B 1787
REMARK 465 GLN B 1788
REMARK 465 VAL B 1789
REMARK 465 ILE B 1790
REMARK 465 LEU B 1791
REMARK 465 ARG B 1792
REMARK 465 LEU B 1793
REMARK 465 GLY B 1794
REMARK 465 ASP B 1795
REMARK 465 GLN B 1796
REMARK 465 GLU B 1797
REMARK 465 PHE B 1798
REMARK 465 ILE B 1799
REMARK 465 LYS B 1800
REMARK 465 SER B 1801
REMARK 465 LEU B 1802
REMARK 465 THR B 1803
REMARK 465 PRO B 1804
REMARK 465 LEU B 1805
REMARK 465 GLU B 1806
REMARK 465 GLY B 1807
REMARK 465 THR B 1808
REMARK 465 GLN B 1809
REMARK 465 ASP B 1810
REMARK 465 THR B 1811
REMARK 465 PHE B 1812
REMARK 465 THR B 1813
REMARK 465 SER B 2728
REMARK 465 ALA B 2729
REMARK 465 ASP B 2730
REMARK 465 GLY B 2731
REMARK 465 ALA B 2732
REMARK 465 LYS B 2733
REMARK 465 GLY B 2734
REMARK 465 GLY B 2735
REMARK 465 GLN B 2736
REMARK 465 SER B 2737
REMARK 465 ALA B 2738
REMARK 465 GLU B 2739
REMARK 465 SER B 2740
REMARK 465 GLU B 2741
REMARK 465 GLU B 2742
REMARK 465 GLU B 2743
REMARK 465 GLU B 2744
REMARK 465 LEU B 2745
REMARK 465 THR B 2746
REMARK 465 ALA B 2747
REMARK 465 GLY B 2748
REMARK 465 SER B 2749
REMARK 465 GLY B 2750
REMARK 465 LEU B 2751
REMARK 465 ARG B 2752
REMARK 465 GLU B 2753
REMARK 465 ASP B 2754
REMARK 465 LEU B 2755
REMARK 465 LEU B 2756
REMARK 465 SER B 2757
REMARK 465 LEU B 2758
REMARK 465 GLN B 2759
REMARK 465 GLU B 2760
REMARK 465 PRO B 2761
REMARK 465 GLY B 2762
REMARK 465 SER B 2763
REMARK 465 LYS B 2764
REMARK 465 THR B 2765
REMARK 465 TYR B 2766
REMARK 465 SER B 2767
REMARK 465 LYS B 2768
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 ND2 ASN B 484 O5 NAG I 1 1.92
REMARK 500 ND2 ASN B 2122 O5 NAG L 1 1.94
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 A 324 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 CYS A 705 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 LEU A1022 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 CYS A1728 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 CYS A1760 CA - CB - SG ANGL. DEV. = 11.0 DEGREES
REMARK 500 LEU A2566 CA - CB - CG ANGL. DEV. = 16.0 DEGREES
REMARK 500 ASP B 324 CB - CG - OD2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 CYS B 705 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 LEU B1022 CA - CB - CG ANGL. DEV. = 16.0 DEGREES
REMARK 500 CYS B1728 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 CYS B1760 CA - CB - SG ANGL. DEV. = 10.9 DEGREES
REMARK 500 LEU B2566 CA - CB - CG ANGL. DEV. = 15.8 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 GLU A 79 -169.92 -104.50
REMARK 500 PHE A 196 -11.00 75.47
REMARK 500 MET A 202 -3.56 76.50
REMARK 500 SER A 269 -7.57 70.78
REMARK 500 SER A 292 -1.77 64.48
REMARK 500 PHE A 295 55.03 -98.67
REMARK 500 GLU A 333 -60.61 -120.88
REMARK 500 GLN A 655 70.49 51.77
REMARK 500 PHE A 699 -167.36 -126.19
REMARK 500 ASP A 707 -61.11 -94.81
REMARK 500 GLU A 709 29.52 44.49
REMARK 500 ILE A 760 80.94 52.90
REMARK 500 ASP A 844 -167.48 -79.23
REMARK 500 PRO A 846 -168.53 -75.96
REMARK 500 LEU A 872 -53.13 -120.20
REMARK 500 SER A 877 -1.30 68.89
REMARK 500 ASP A 885 -8.98 73.91
REMARK 500 SER A 887 49.84 -90.98
REMARK 500 ALA A 904 48.67 -92.89
REMARK 500 LEU A 975 32.14 -140.72
REMARK 500 PHE A1010 45.49 -84.93
REMARK 500 SER A1011 76.75 45.58
REMARK 500 PRO A1012 -163.95 -74.31
REMARK 500 SER A1015 -159.93 -141.68
REMARK 500 ALA A1018 -3.30 68.16
REMARK 500 PHE A1058 72.72 59.86
REMARK 500 ASN A1097 77.56 -162.97
REMARK 500 SER A1120 -168.95 -117.83
REMARK 500 GLU A1197 77.00 62.52
REMARK 500 GLN A1207 77.61 53.01
REMARK 500 GLN A1297 42.99 -109.11
REMARK 500 MET A1305 47.95 -80.59
REMARK 500 ARG A1328 51.76 -90.40
REMARK 500 PHE A1330 -3.50 63.55
REMARK 500 PHE A1338 28.46 44.52
REMARK 500 THR A1432 -3.80 66.55
REMARK 500 SER A1433 68.16 -159.96
REMARK 500 LEU A1488 -9.19 72.17
REMARK 500 THR A1498 73.87 59.86
REMARK 500 SER A1501 -167.98 -100.81
REMARK 500 THR A1556 46.27 -141.29
REMARK 500 GLN A1564 69.25 61.33
REMARK 500 LEU A1566 47.58 -86.53
REMARK 500 ASN A1584 49.27 -85.44
REMARK 500 ALA A1585 58.96 -156.30
REMARK 500 CYS A1607 40.03 -104.49
REMARK 500 CYS A1613 -62.32 -109.77
REMARK 500 SER A1614 -31.77 65.07
REMARK 500 PHE A1615 161.06 178.20
REMARK 500 TYR A1630 -165.09 -122.95
REMARK 500
REMARK 500 THIS ENTRY HAS 167 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 THR A 2057 TYR A 2058 -148.98
REMARK 500 SER B 2121 ASN B 2122 137.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-12073 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF HUMAN THYROGLOBULIN
DBREF 7B75 A 1 2768 UNP P01266 THYG_HUMAN 1 2768
DBREF 7B75 B 1 2768 UNP P01266 THYG_HUMAN 1 2768
SEQRES 1 A 2768 MET ALA LEU VAL LEU GLU ILE PHE THR LEU LEU ALA SER
SEQRES 2 A 2768 ILE CYS TRP VAL SER ALA ASN ILE PHE GLU TYR GLN VAL
SEQRES 3 A 2768 ASP ALA GLN PRO LEU ARG PRO CYS GLU LEU GLN ARG GLU
SEQRES 4 A 2768 THR ALA PHE LEU LYS GLN ALA ASP TYR VAL PRO GLN CYS
SEQRES 5 A 2768 ALA GLU ASP GLY SER PHE GLN THR VAL GLN CYS GLN ASN
SEQRES 6 A 2768 ASP GLY ARG SER CYS TRP CYS VAL GLY ALA ASN GLY SER
SEQRES 7 A 2768 GLU VAL LEU GLY SER ARG GLN PRO GLY ARG PRO VAL ALA
SEQRES 8 A 2768 CYS LEU SER PHE CYS GLN LEU GLN LYS GLN GLN ILE LEU
SEQRES 9 A 2768 LEU SER GLY TYR ILE ASN SER THR ASP THR SER TYR LEU
SEQRES 10 A 2768 PRO GLN CYS GLN ASP SER GLY ASP TYR ALA PRO VAL GLN
SEQRES 11 A 2768 CYS ASP VAL GLN GLN VAL GLN CYS TRP CYS VAL ASP ALA
SEQRES 12 A 2768 GLU GLY MET GLU VAL TYR GLY THR ARG GLN LEU GLY ARG
SEQRES 13 A 2768 PRO LYS ARG CYS PRO ARG SER CYS GLU ILE ARG ASN ARG
SEQRES 14 A 2768 ARG LEU LEU HIS GLY VAL GLY ASP LYS SER PRO PRO GLN
SEQRES 15 A 2768 CYS SER ALA GLU GLY GLU PHE MET PRO VAL GLN CYS LYS
SEQRES 16 A 2768 PHE VAL ASN THR THR ASP MET MET ILE PHE ASP LEU VAL
SEQRES 17 A 2768 HIS SER TYR ASN ARG PHE PRO ASP ALA PHE VAL THR PHE
SEQRES 18 A 2768 SER SER PHE GLN ARG ARG PHE PRO GLU VAL SER GLY TYR
SEQRES 19 A 2768 CYS HIS CYS ALA ASP SER GLN GLY ARG GLU LEU ALA GLU
SEQRES 20 A 2768 THR GLY LEU GLU LEU LEU LEU ASP GLU ILE TYR ASP THR
SEQRES 21 A 2768 ILE PHE ALA GLY LEU ASP LEU PRO SER THR PHE THR GLU
SEQRES 22 A 2768 THR THR LEU TYR ARG ILE LEU GLN ARG ARG PHE LEU ALA
SEQRES 23 A 2768 VAL GLN SER VAL ILE SER GLY ARG PHE ARG CYS PRO THR
SEQRES 24 A 2768 LYS CYS GLU VAL GLU ARG PHE THR ALA THR SER PHE GLY
SEQRES 25 A 2768 HIS PRO TYR VAL PRO SER CYS ARG ARG ASN GLY ASP TYR
SEQRES 26 A 2768 GLN ALA VAL GLN CYS GLN THR GLU GLY PRO CYS TRP CYS
SEQRES 27 A 2768 VAL ASP ALA GLN GLY LYS GLU MET HIS GLY THR ARG GLN
SEQRES 28 A 2768 GLN GLY GLU PRO PRO SER CYS ALA GLU GLY GLN SER CYS
SEQRES 29 A 2768 ALA SER GLU ARG GLN GLN ALA LEU SER ARG LEU TYR PHE
SEQRES 30 A 2768 GLY THR SER GLY TYR PHE SER GLN HIS ASP LEU PHE SER
SEQRES 31 A 2768 SER PRO GLU LYS ARG TRP ALA SER PRO ARG VAL ALA ARG
SEQRES 32 A 2768 PHE ALA THR SER CYS PRO PRO THR ILE LYS GLU LEU PHE
SEQRES 33 A 2768 VAL ASP SER GLY LEU LEU ARG PRO MET VAL GLU GLY GLN
SEQRES 34 A 2768 SER GLN GLN PHE SER VAL SER GLU ASN LEU LEU LYS GLU
SEQRES 35 A 2768 ALA ILE ARG ALA ILE PHE PRO SER ARG GLY LEU ALA ARG
SEQRES 36 A 2768 LEU ALA LEU GLN PHE THR THR ASN PRO LYS ARG LEU GLN
SEQRES 37 A 2768 GLN ASN LEU PHE GLY GLY LYS PHE LEU VAL ASN VAL GLY
SEQRES 38 A 2768 GLN PHE ASN LEU SER GLY ALA LEU GLY THR ARG GLY THR
SEQRES 39 A 2768 PHE ASN PHE SER GLN PHE PHE GLN GLN LEU GLY LEU ALA
SEQRES 40 A 2768 SER PHE LEU ASN GLY GLY ARG GLN GLU ASP LEU ALA LYS
SEQRES 41 A 2768 PRO LEU SER VAL GLY LEU ASP SER ASN SER SER THR GLY
SEQRES 42 A 2768 THR PRO GLU ALA ALA LYS LYS ASP GLY THR MET ASN LYS
SEQRES 43 A 2768 PRO THR VAL GLY SER PHE GLY PHE GLU ILE ASN LEU GLN
SEQRES 44 A 2768 GLU ASN GLN ASN ALA LEU LYS PHE LEU ALA SER LEU LEU
SEQRES 45 A 2768 GLU LEU PRO GLU PHE LEU LEU PHE LEU GLN HIS ALA ILE
SEQRES 46 A 2768 SER VAL PRO GLU ASP VAL ALA ARG ASP LEU GLY ASP VAL
SEQRES 47 A 2768 MET GLU THR VAL LEU SER SER GLN THR CYS GLU GLN THR
SEQRES 48 A 2768 PRO GLU ARG LEU PHE VAL PRO SER CYS THR THR GLU GLY
SEQRES 49 A 2768 SER TYR GLU ASP VAL GLN CYS PHE SER GLY GLU CYS TRP
SEQRES 50 A 2768 CYS VAL ASN SER TRP GLY LYS GLU LEU PRO GLY SER ARG
SEQRES 51 A 2768 VAL ARG GLY GLY GLN PRO ARG CYS PRO THR ASP CYS GLU
SEQRES 52 A 2768 LYS GLN ARG ALA ARG MET GLN SER LEU MET GLY SER GLN
SEQRES 53 A 2768 PRO ALA GLY SER THR LEU PHE VAL PRO ALA CYS THR SER
SEQRES 54 A 2768 GLU GLY HIS PHE LEU PRO VAL GLN CYS PHE ASN SER GLU
SEQRES 55 A 2768 CYS TYR CYS VAL ASP ALA GLU GLY GLN ALA ILE PRO GLY
SEQRES 56 A 2768 THR ARG SER ALA ILE GLY LYS PRO LYS LYS CYS PRO THR
SEQRES 57 A 2768 PRO CYS GLN LEU GLN SER GLU GLN ALA PHE LEU ARG THR
SEQRES 58 A 2768 VAL GLN ALA LEU LEU SER ASN SER SER MET LEU PRO THR
SEQRES 59 A 2768 LEU SER ASP THR TYR ILE PRO GLN CYS SER THR ASP GLY
SEQRES 60 A 2768 GLN TRP ARG GLN VAL GLN CYS ASN GLY PRO PRO GLU GLN
SEQRES 61 A 2768 VAL PHE GLU LEU TYR GLN ARG TRP GLU ALA GLN ASN LYS
SEQRES 62 A 2768 GLY GLN ASP LEU THR PRO ALA LYS LEU LEU VAL LYS ILE
SEQRES 63 A 2768 MET SER TYR ARG GLU ALA ALA SER GLY ASN PHE SER LEU
SEQRES 64 A 2768 PHE ILE GLN SER LEU TYR GLU ALA GLY GLN GLN ASP VAL
SEQRES 65 A 2768 PHE PRO VAL LEU SER GLN TYR PRO SER LEU GLN ASP VAL
SEQRES 66 A 2768 PRO LEU ALA ALA LEU GLU GLY LYS ARG PRO GLN PRO ARG
SEQRES 67 A 2768 GLU ASN ILE LEU LEU GLU PRO TYR LEU PHE TRP GLN ILE
SEQRES 68 A 2768 LEU ASN GLY GLN LEU SER GLN TYR PRO GLY SER TYR SER
SEQRES 69 A 2768 ASP PHE SER THR PRO LEU ALA HIS PHE ASP LEU ARG ASN
SEQRES 70 A 2768 CYS TRP CYS VAL ASP GLU ALA GLY GLN GLU LEU GLU GLY
SEQRES 71 A 2768 MET ARG SER GLU PRO SER LYS LEU PRO THR CYS PRO GLY
SEQRES 72 A 2768 SER CYS GLU GLU ALA LYS LEU ARG VAL LEU GLN PHE ILE
SEQRES 73 A 2768 ARG GLU THR GLU GLU ILE VAL SER ALA SER ASN SER SER
SEQRES 74 A 2768 ARG PHE PRO LEU GLY GLU SER PHE LEU VAL ALA LYS GLY
SEQRES 75 A 2768 ILE ARG LEU ARG ASN GLU ASP LEU GLY LEU PRO PRO LEU
SEQRES 76 A 2768 PHE PRO PRO ARG GLU ALA PHE ALA GLU GLN PHE LEU ARG
SEQRES 77 A 2768 GLY SER ASP TYR ALA ILE ARG LEU ALA ALA GLN SER THR
SEQRES 78 A 2768 LEU SER PHE TYR GLN ARG ARG ARG PHE SER PRO ASP ASP
SEQRES 79 A 2768 SER ALA GLY ALA SER ALA LEU LEU ARG SER GLY PRO TYR
SEQRES 80 A 2768 MET PRO GLN CYS ASP ALA PHE GLY SER TRP GLU PRO VAL
SEQRES 81 A 2768 GLN CYS HIS ALA GLY THR GLY HIS CYS TRP CYS VAL ASP
SEQRES 82 A 2768 GLU LYS GLY GLY PHE ILE PRO GLY SER LEU THR ALA ARG
SEQRES 83 A 2768 SER LEU GLN ILE PRO GLN CYS PRO THR THR CYS GLU LYS
SEQRES 84 A 2768 SER ARG THR SER GLY LEU LEU SER SER TRP LYS GLN ALA
SEQRES 85 A 2768 ARG SER GLN GLU ASN PRO SER PRO LYS ASP LEU PHE VAL
SEQRES 86 A 2768 PRO ALA CYS LEU GLU THR GLY GLU TYR ALA ARG LEU GLN
SEQRES 87 A 2768 ALA SER GLY ALA GLY THR TRP CYS VAL ASP PRO ALA SER
SEQRES 88 A 2768 GLY GLU GLU LEU ARG PRO GLY SER SER SER SER ALA GLN
SEQRES 89 A 2768 CYS PRO SER LEU CYS ASN VAL LEU LYS SER GLY VAL LEU
SEQRES 90 A 2768 SER ARG ARG VAL SER PRO GLY TYR VAL PRO ALA CYS ARG
SEQRES 91 A 2768 ALA GLU ASP GLY GLY PHE SER PRO VAL GLN CYS ASP GLN
SEQRES 92 A 2768 ALA GLN GLY SER CYS TRP CYS VAL MET ASP SER GLY GLU
SEQRES 93 A 2768 GLU VAL PRO GLY THR ARG VAL THR GLY GLY GLN PRO ALA
SEQRES 94 A 2768 CYS GLU SER PRO ARG CYS PRO LEU PRO PHE ASN ALA SER
SEQRES 95 A 2768 GLU VAL VAL GLY GLY THR ILE LEU CYS GLU THR ILE SER
SEQRES 96 A 2768 GLY PRO THR GLY SER ALA MET GLN GLN CYS GLN LEU LEU
SEQRES 97 A 2768 CYS ARG GLN GLY SER TRP SER VAL PHE PRO PRO GLY PRO
SEQRES 98 A 2768 LEU ILE CYS SER LEU GLU SER GLY ARG TRP GLU SER GLN
SEQRES 99 A 2768 LEU PRO GLN PRO ARG ALA CYS GLN ARG PRO GLN LEU TRP
SEQRES 100 A 2768 GLN THR ILE GLN THR GLN GLY HIS PHE GLN LEU GLN LEU
SEQRES 101 A 2768 PRO PRO GLY LYS MET CYS SER ALA ASP TYR ALA ASP LEU
SEQRES 102 A 2768 LEU GLN THR PHE GLN VAL PHE ILE LEU ASP GLU LEU THR
SEQRES 103 A 2768 ALA ARG GLY PHE CYS GLN ILE GLN VAL LYS THR PHE GLY
SEQRES 104 A 2768 THR LEU VAL SER ILE PRO VAL CYS ASN ASN SER SER VAL
SEQRES 105 A 2768 GLN VAL GLY CYS LEU THR ARG GLU ARG LEU GLY VAL ASN
SEQRES 106 A 2768 VAL THR TRP LYS SER ARG LEU GLU ASP ILE PRO VAL ALA
SEQRES 107 A 2768 SER LEU PRO ASP LEU HIS ASP ILE GLU ARG ALA LEU VAL
SEQRES 108 A 2768 GLY LYS ASP LEU LEU GLY ARG PHE THR ASP LEU ILE GLN
SEQRES 109 A 2768 SER GLY SER PHE GLN LEU HIS LEU ASP SER LYS THR PHE
SEQRES 110 A 2768 PRO ALA GLU THR ILE ARG PHE LEU GLN GLY ASP HIS PHE
SEQRES 111 A 2768 GLY THR SER PRO ARG THR TRP PHE GLY CYS SER GLU GLY
SEQRES 112 A 2768 PHE TYR GLN VAL LEU THR SER GLU ALA SER GLN ASP GLY
SEQRES 113 A 2768 LEU GLY CYS VAL LYS CYS PRO GLU GLY SER TYR SER GLN
SEQRES 114 A 2768 ASP GLU GLU CYS ILE PRO CYS PRO VAL GLY PHE TYR GLN
SEQRES 115 A 2768 GLU GLN ALA GLY SER LEU ALA CYS VAL PRO CYS PRO VAL
SEQRES 116 A 2768 GLY ARG THR THR ILE SER ALA GLY ALA PHE SER GLN THR
SEQRES 117 A 2768 HIS CYS VAL THR ASP CYS GLN ARG ASN GLU ALA GLY LEU
SEQRES 118 A 2768 GLN CYS ASP GLN ASN GLY GLN TYR ARG ALA SER GLN LYS
SEQRES 119 A 2768 ASP ARG GLY SER GLY LYS ALA PHE CYS VAL ASP GLY GLU
SEQRES 120 A 2768 GLY ARG ARG LEU PRO TRP TRP GLU THR GLU ALA PRO LEU
SEQRES 121 A 2768 GLU ASP SER GLN CYS LEU MET MET GLN LYS PHE GLU LYS
SEQRES 122 A 2768 VAL PRO GLU SER LYS VAL ILE PHE ASP ALA ASN ALA PRO
SEQRES 123 A 2768 VAL ALA VAL ARG SER LYS VAL PRO ASP SER GLU PHE PRO
SEQRES 124 A 2768 VAL MET GLN CYS LEU THR ASP CYS THR GLU ASP GLU ALA
SEQRES 125 A 2768 CYS SER PHE PHE THR VAL SER THR THR GLU PRO GLU ILE
SEQRES 126 A 2768 SER CYS ASP PHE TYR ALA TRP THR SER ASP ASN VAL ALA
SEQRES 127 A 2768 CYS MET THR SER ASP GLN LYS ARG ASP ALA LEU GLY ASN
SEQRES 128 A 2768 SER LYS ALA THR SER PHE GLY SER LEU ARG CYS GLN VAL
SEQRES 129 A 2768 LYS VAL ARG SER HIS GLY GLN ASP SER PRO ALA VAL TYR
SEQRES 130 A 2768 LEU LYS LYS GLY GLN GLY SER THR THR THR LEU GLN LYS
SEQRES 131 A 2768 ARG PHE GLU PRO THR GLY PHE GLN ASN MET LEU SER GLY
SEQRES 132 A 2768 LEU TYR ASN PRO ILE VAL PHE SER ALA SER GLY ALA ASN
SEQRES 133 A 2768 LEU THR ASP ALA HIS LEU PHE CYS LEU LEU ALA CYS ASP
SEQRES 134 A 2768 ARG ASP LEU CYS CYS ASP GLY PHE VAL LEU THR GLN VAL
SEQRES 135 A 2768 GLN GLY GLY ALA ILE ILE CYS GLY LEU LEU SER SER PRO
SEQRES 136 A 2768 SER VAL LEU LEU CYS ASN VAL LYS ASP TRP MET ASP PRO
SEQRES 137 A 2768 SER GLU ALA TRP ALA ASN ALA THR CYS PRO GLY VAL THR
SEQRES 138 A 2768 TYR ASP GLN GLU SER HIS GLN VAL ILE LEU ARG LEU GLY
SEQRES 139 A 2768 ASP GLN GLU PHE ILE LYS SER LEU THR PRO LEU GLU GLY
SEQRES 140 A 2768 THR GLN ASP THR PHE THR ASN PHE GLN GLN VAL TYR LEU
SEQRES 141 A 2768 TRP LYS ASP SER ASP MET GLY SER ARG PRO GLU SER MET
SEQRES 142 A 2768 GLY CYS ARG LYS ASP THR VAL PRO ARG PRO ALA SER PRO
SEQRES 143 A 2768 THR GLU ALA GLY LEU THR THR GLU LEU PHE SER PRO VAL
SEQRES 144 A 2768 ASP LEU ASN GLN VAL ILE VAL ASN GLY ASN GLN SER LEU
SEQRES 145 A 2768 SER SER GLN LYS HIS TRP LEU PHE LYS HIS LEU PHE SER
SEQRES 146 A 2768 ALA GLN GLN ALA ASN LEU TRP CYS LEU SER ARG CYS VAL
SEQRES 147 A 2768 GLN GLU HIS SER PHE CYS GLN LEU ALA GLU ILE THR GLU
SEQRES 148 A 2768 SER ALA SER LEU TYR PHE THR CYS THR LEU TYR PRO GLU
SEQRES 149 A 2768 ALA GLN VAL CYS ASP ASP ILE MET GLU SER ASN ALA GLN
SEQRES 150 A 2768 GLY CYS ARG LEU ILE LEU PRO GLN MET PRO LYS ALA LEU
SEQRES 151 A 2768 PHE ARG LYS LYS VAL ILE LEU GLU ASP LYS VAL LYS ASN
SEQRES 152 A 2768 PHE TYR THR ARG LEU PRO PHE GLN LYS LEU MET GLY ILE
SEQRES 153 A 2768 SER ILE ARG ASN LYS VAL PRO MET SER GLU LYS SER ILE
SEQRES 154 A 2768 SER ASN GLY PHE PHE GLU CYS GLU ARG ARG CYS ASP ALA
SEQRES 155 A 2768 ASP PRO CYS CYS THR GLY PHE GLY PHE LEU ASN VAL SER
SEQRES 156 A 2768 GLN LEU LYS GLY GLY GLU VAL THR CYS LEU THR LEU ASN
SEQRES 157 A 2768 SER LEU GLY ILE GLN MET CYS SER GLU GLU ASN GLY GLY
SEQRES 158 A 2768 ALA TRP ARG ILE LEU ASP CYS GLY SER PRO ASP ILE GLU
SEQRES 159 A 2768 VAL HIS THR TYR PRO PHE GLY TRP TYR GLN LYS PRO ILE
SEQRES 160 A 2768 ALA GLN ASN ASN ALA PRO SER PHE CYS PRO LEU VAL VAL
SEQRES 161 A 2768 LEU PRO SER LEU THR GLU LYS VAL SER LEU ASP SER TRP
SEQRES 162 A 2768 GLN SER LEU ALA LEU SER SER VAL VAL VAL ASP PRO SER
SEQRES 163 A 2768 ILE ARG HIS PHE ASP VAL ALA HIS VAL SER THR ALA ALA
SEQRES 164 A 2768 THR SER ASN PHE SER ALA VAL ARG ASP LEU CYS LEU SER
SEQRES 165 A 2768 GLU CYS SER GLN HIS GLU ALA CYS LEU ILE THR THR LEU
SEQRES 166 A 2768 GLN THR GLN PRO GLY ALA VAL ARG CYS MET PHE TYR ALA
SEQRES 167 A 2768 ASP THR GLN SER CYS THR HIS SER LEU GLN GLY GLN ASN
SEQRES 168 A 2768 CYS ARG LEU LEU LEU ARG GLU GLU ALA THR HIS ILE TYR
SEQRES 169 A 2768 ARG LYS PRO GLY ILE SER LEU LEU SER TYR GLU ALA SER
SEQRES 170 A 2768 VAL PRO SER VAL PRO ILE SER THR HIS GLY ARG LEU LEU
SEQRES 171 A 2768 GLY ARG SER GLN ALA ILE GLN VAL GLY THR SER TRP LYS
SEQRES 172 A 2768 GLN VAL ASP GLN PHE LEU GLY VAL PRO TYR ALA ALA PRO
SEQRES 173 A 2768 PRO LEU ALA GLU ARG ARG PHE GLN ALA PRO GLU PRO LEU
SEQRES 174 A 2768 ASN TRP THR GLY SER TRP ASP ALA SER LYS PRO ARG ALA
SEQRES 175 A 2768 SER CYS TRP GLN PRO GLY THR ARG THR SER THR SER PRO
SEQRES 176 A 2768 GLY VAL SER GLU ASP CYS LEU TYR LEU ASN VAL PHE ILE
SEQRES 177 A 2768 PRO GLN ASN VAL ALA PRO ASN ALA SER VAL LEU VAL PHE
SEQRES 178 A 2768 PHE HIS ASN THR MET ASP ARG GLU GLU SER GLU GLY TRP
SEQRES 179 A 2768 PRO ALA ILE ASP GLY SER PHE LEU ALA ALA VAL GLY ASN
SEQRES 180 A 2768 LEU ILE VAL VAL THR ALA SER TYR ARG VAL GLY VAL PHE
SEQRES 181 A 2768 GLY PHE LEU SER SER GLY SER GLY GLU VAL SER GLY ASN
SEQRES 182 A 2768 TRP GLY LEU LEU ASP GLN VAL ALA ALA LEU THR TRP VAL
SEQRES 183 A 2768 GLN THR HIS ILE ARG GLY PHE GLY GLY ASP PRO ARG ARG
SEQRES 184 A 2768 VAL SER LEU ALA ALA ASP ARG GLY GLY ALA ASP VAL ALA
SEQRES 185 A 2768 SER ILE HIS LEU LEU THR ALA ARG ALA THR ASN SER GLN
SEQRES 186 A 2768 LEU PHE ARG ARG ALA VAL LEU MET GLY GLY SER ALA LEU
SEQRES 187 A 2768 SER PRO ALA ALA VAL ILE SER HIS GLU ARG ALA GLN GLN
SEQRES 188 A 2768 GLN ALA ILE ALA LEU ALA LYS GLU VAL SER CYS PRO MET
SEQRES 189 A 2768 SER SER SER GLN GLU VAL VAL SER CYS LEU ARG GLN LYS
SEQRES 190 A 2768 PRO ALA ASN VAL LEU ASN ASP ALA GLN THR LYS LEU LEU
SEQRES 191 A 2768 ALA VAL SER GLY PRO PHE HIS TYR TRP GLY PRO VAL ILE
SEQRES 192 A 2768 ASP GLY HIS PHE LEU ARG GLU PRO PRO ALA ARG ALA LEU
SEQRES 193 A 2768 LYS ARG SER LEU TRP VAL GLU VAL ASP LEU LEU ILE GLY
SEQRES 194 A 2768 SER SER GLN ASP ASP GLY LEU ILE ASN ARG ALA LYS ALA
SEQRES 195 A 2768 VAL LYS GLN PHE GLU GLU SER ARG GLY ARG THR SER SER
SEQRES 196 A 2768 LYS THR ALA PHE TYR GLN ALA LEU GLN ASN SER LEU GLY
SEQRES 197 A 2768 GLY GLU ASP SER ASP ALA ARG VAL GLU ALA ALA ALA THR
SEQRES 198 A 2768 TRP TYR TYR SER LEU GLU HIS SER THR ASP ASP TYR ALA
SEQRES 199 A 2768 SER PHE SER ARG ALA LEU GLU ASN ALA THR ARG ASP TYR
SEQRES 200 A 2768 PHE ILE ILE CYS PRO ILE ILE ASP MET ALA SER ALA TRP
SEQRES 201 A 2768 ALA LYS ARG ALA ARG GLY ASN VAL PHE MET TYR HIS ALA
SEQRES 202 A 2768 PRO GLU ASN TYR GLY HIS GLY SER LEU GLU LEU LEU ALA
SEQRES 203 A 2768 ASP VAL GLN PHE ALA LEU GLY LEU PRO PHE TYR PRO ALA
SEQRES 204 A 2768 TYR GLU GLY GLN PHE SER LEU GLU GLU LYS SER LEU SER
SEQRES 205 A 2768 LEU LYS ILE MET GLN TYR PHE SER HIS PHE ILE ARG SER
SEQRES 206 A 2768 GLY ASN PRO ASN TYR PRO TYR GLU PHE SER ARG LYS VAL
SEQRES 207 A 2768 PRO THR PHE ALA THR PRO TRP PRO ASP PHE VAL PRO ARG
SEQRES 208 A 2768 ALA GLY GLY GLU ASN TYR LYS GLU PHE SER GLU LEU LEU
SEQRES 209 A 2768 PRO ASN ARG GLN GLY LEU LYS LYS ALA ASP CYS SER PHE
SEQRES 210 A 2768 TRP SER LYS TYR ILE SER SER LEU LYS THR SER ALA ASP
SEQRES 211 A 2768 GLY ALA LYS GLY GLY GLN SER ALA GLU SER GLU GLU GLU
SEQRES 212 A 2768 GLU LEU THR ALA GLY SER GLY LEU ARG GLU ASP LEU LEU
SEQRES 213 A 2768 SER LEU GLN GLU PRO GLY SER LYS THR TYR SER LYS
SEQRES 1 B 2768 MET ALA LEU VAL LEU GLU ILE PHE THR LEU LEU ALA SER
SEQRES 2 B 2768 ILE CYS TRP VAL SER ALA ASN ILE PHE GLU TYR GLN VAL
SEQRES 3 B 2768 ASP ALA GLN PRO LEU ARG PRO CYS GLU LEU GLN ARG GLU
SEQRES 4 B 2768 THR ALA PHE LEU LYS GLN ALA ASP TYR VAL PRO GLN CYS
SEQRES 5 B 2768 ALA GLU ASP GLY SER PHE GLN THR VAL GLN CYS GLN ASN
SEQRES 6 B 2768 ASP GLY ARG SER CYS TRP CYS VAL GLY ALA ASN GLY SER
SEQRES 7 B 2768 GLU VAL LEU GLY SER ARG GLN PRO GLY ARG PRO VAL ALA
SEQRES 8 B 2768 CYS LEU SER PHE CYS GLN LEU GLN LYS GLN GLN ILE LEU
SEQRES 9 B 2768 LEU SER GLY TYR ILE ASN SER THR ASP THR SER TYR LEU
SEQRES 10 B 2768 PRO GLN CYS GLN ASP SER GLY ASP TYR ALA PRO VAL GLN
SEQRES 11 B 2768 CYS ASP VAL GLN GLN VAL GLN CYS TRP CYS VAL ASP ALA
SEQRES 12 B 2768 GLU GLY MET GLU VAL TYR GLY THR ARG GLN LEU GLY ARG
SEQRES 13 B 2768 PRO LYS ARG CYS PRO ARG SER CYS GLU ILE ARG ASN ARG
SEQRES 14 B 2768 ARG LEU LEU HIS GLY VAL GLY ASP LYS SER PRO PRO GLN
SEQRES 15 B 2768 CYS SER ALA GLU GLY GLU PHE MET PRO VAL GLN CYS LYS
SEQRES 16 B 2768 PHE VAL ASN THR THR ASP MET MET ILE PHE ASP LEU VAL
SEQRES 17 B 2768 HIS SER TYR ASN ARG PHE PRO ASP ALA PHE VAL THR PHE
SEQRES 18 B 2768 SER SER PHE GLN ARG ARG PHE PRO GLU VAL SER GLY TYR
SEQRES 19 B 2768 CYS HIS CYS ALA ASP SER GLN GLY ARG GLU LEU ALA GLU
SEQRES 20 B 2768 THR GLY LEU GLU LEU LEU LEU ASP GLU ILE TYR ASP THR
SEQRES 21 B 2768 ILE PHE ALA GLY LEU ASP LEU PRO SER THR PHE THR GLU
SEQRES 22 B 2768 THR THR LEU TYR ARG ILE LEU GLN ARG ARG PHE LEU ALA
SEQRES 23 B 2768 VAL GLN SER VAL ILE SER GLY ARG PHE ARG CYS PRO THR
SEQRES 24 B 2768 LYS CYS GLU VAL GLU ARG PHE THR ALA THR SER PHE GLY
SEQRES 25 B 2768 HIS PRO TYR VAL PRO SER CYS ARG ARG ASN GLY ASP TYR
SEQRES 26 B 2768 GLN ALA VAL GLN CYS GLN THR GLU GLY PRO CYS TRP CYS
SEQRES 27 B 2768 VAL ASP ALA GLN GLY LYS GLU MET HIS GLY THR ARG GLN
SEQRES 28 B 2768 GLN GLY GLU PRO PRO SER CYS ALA GLU GLY GLN SER CYS
SEQRES 29 B 2768 ALA SER GLU ARG GLN GLN ALA LEU SER ARG LEU TYR PHE
SEQRES 30 B 2768 GLY THR SER GLY TYR PHE SER GLN HIS ASP LEU PHE SER
SEQRES 31 B 2768 SER PRO GLU LYS ARG TRP ALA SER PRO ARG VAL ALA ARG
SEQRES 32 B 2768 PHE ALA THR SER CYS PRO PRO THR ILE LYS GLU LEU PHE
SEQRES 33 B 2768 VAL ASP SER GLY LEU LEU ARG PRO MET VAL GLU GLY GLN
SEQRES 34 B 2768 SER GLN GLN PHE SER VAL SER GLU ASN LEU LEU LYS GLU
SEQRES 35 B 2768 ALA ILE ARG ALA ILE PHE PRO SER ARG GLY LEU ALA ARG
SEQRES 36 B 2768 LEU ALA LEU GLN PHE THR THR ASN PRO LYS ARG LEU GLN
SEQRES 37 B 2768 GLN ASN LEU PHE GLY GLY LYS PHE LEU VAL ASN VAL GLY
SEQRES 38 B 2768 GLN PHE ASN LEU SER GLY ALA LEU GLY THR ARG GLY THR
SEQRES 39 B 2768 PHE ASN PHE SER GLN PHE PHE GLN GLN LEU GLY LEU ALA
SEQRES 40 B 2768 SER PHE LEU ASN GLY GLY ARG GLN GLU ASP LEU ALA LYS
SEQRES 41 B 2768 PRO LEU SER VAL GLY LEU ASP SER ASN SER SER THR GLY
SEQRES 42 B 2768 THR PRO GLU ALA ALA LYS LYS ASP GLY THR MET ASN LYS
SEQRES 43 B 2768 PRO THR VAL GLY SER PHE GLY PHE GLU ILE ASN LEU GLN
SEQRES 44 B 2768 GLU ASN GLN ASN ALA LEU LYS PHE LEU ALA SER LEU LEU
SEQRES 45 B 2768 GLU LEU PRO GLU PHE LEU LEU PHE LEU GLN HIS ALA ILE
SEQRES 46 B 2768 SER VAL PRO GLU ASP VAL ALA ARG ASP LEU GLY ASP VAL
SEQRES 47 B 2768 MET GLU THR VAL LEU SER SER GLN THR CYS GLU GLN THR
SEQRES 48 B 2768 PRO GLU ARG LEU PHE VAL PRO SER CYS THR THR GLU GLY
SEQRES 49 B 2768 SER TYR GLU ASP VAL GLN CYS PHE SER GLY GLU CYS TRP
SEQRES 50 B 2768 CYS VAL ASN SER TRP GLY LYS GLU LEU PRO GLY SER ARG
SEQRES 51 B 2768 VAL ARG GLY GLY GLN PRO ARG CYS PRO THR ASP CYS GLU
SEQRES 52 B 2768 LYS GLN ARG ALA ARG MET GLN SER LEU MET GLY SER GLN
SEQRES 53 B 2768 PRO ALA GLY SER THR LEU PHE VAL PRO ALA CYS THR SER
SEQRES 54 B 2768 GLU GLY HIS PHE LEU PRO VAL GLN CYS PHE ASN SER GLU
SEQRES 55 B 2768 CYS TYR CYS VAL ASP ALA GLU GLY GLN ALA ILE PRO GLY
SEQRES 56 B 2768 THR ARG SER ALA ILE GLY LYS PRO LYS LYS CYS PRO THR
SEQRES 57 B 2768 PRO CYS GLN LEU GLN SER GLU GLN ALA PHE LEU ARG THR
SEQRES 58 B 2768 VAL GLN ALA LEU LEU SER ASN SER SER MET LEU PRO THR
SEQRES 59 B 2768 LEU SER ASP THR TYR ILE PRO GLN CYS SER THR ASP GLY
SEQRES 60 B 2768 GLN TRP ARG GLN VAL GLN CYS ASN GLY PRO PRO GLU GLN
SEQRES 61 B 2768 VAL PHE GLU LEU TYR GLN ARG TRP GLU ALA GLN ASN LYS
SEQRES 62 B 2768 GLY GLN ASP LEU THR PRO ALA LYS LEU LEU VAL LYS ILE
SEQRES 63 B 2768 MET SER TYR ARG GLU ALA ALA SER GLY ASN PHE SER LEU
SEQRES 64 B 2768 PHE ILE GLN SER LEU TYR GLU ALA GLY GLN GLN ASP VAL
SEQRES 65 B 2768 PHE PRO VAL LEU SER GLN TYR PRO SER LEU GLN ASP VAL
SEQRES 66 B 2768 PRO LEU ALA ALA LEU GLU GLY LYS ARG PRO GLN PRO ARG
SEQRES 67 B 2768 GLU ASN ILE LEU LEU GLU PRO TYR LEU PHE TRP GLN ILE
SEQRES 68 B 2768 LEU ASN GLY GLN LEU SER GLN TYR PRO GLY SER TYR SER
SEQRES 69 B 2768 ASP PHE SER THR PRO LEU ALA HIS PHE ASP LEU ARG ASN
SEQRES 70 B 2768 CYS TRP CYS VAL ASP GLU ALA GLY GLN GLU LEU GLU GLY
SEQRES 71 B 2768 MET ARG SER GLU PRO SER LYS LEU PRO THR CYS PRO GLY
SEQRES 72 B 2768 SER CYS GLU GLU ALA LYS LEU ARG VAL LEU GLN PHE ILE
SEQRES 73 B 2768 ARG GLU THR GLU GLU ILE VAL SER ALA SER ASN SER SER
SEQRES 74 B 2768 ARG PHE PRO LEU GLY GLU SER PHE LEU VAL ALA LYS GLY
SEQRES 75 B 2768 ILE ARG LEU ARG ASN GLU ASP LEU GLY LEU PRO PRO LEU
SEQRES 76 B 2768 PHE PRO PRO ARG GLU ALA PHE ALA GLU GLN PHE LEU ARG
SEQRES 77 B 2768 GLY SER ASP TYR ALA ILE ARG LEU ALA ALA GLN SER THR
SEQRES 78 B 2768 LEU SER PHE TYR GLN ARG ARG ARG PHE SER PRO ASP ASP
SEQRES 79 B 2768 SER ALA GLY ALA SER ALA LEU LEU ARG SER GLY PRO TYR
SEQRES 80 B 2768 MET PRO GLN CYS ASP ALA PHE GLY SER TRP GLU PRO VAL
SEQRES 81 B 2768 GLN CYS HIS ALA GLY THR GLY HIS CYS TRP CYS VAL ASP
SEQRES 82 B 2768 GLU LYS GLY GLY PHE ILE PRO GLY SER LEU THR ALA ARG
SEQRES 83 B 2768 SER LEU GLN ILE PRO GLN CYS PRO THR THR CYS GLU LYS
SEQRES 84 B 2768 SER ARG THR SER GLY LEU LEU SER SER TRP LYS GLN ALA
SEQRES 85 B 2768 ARG SER GLN GLU ASN PRO SER PRO LYS ASP LEU PHE VAL
SEQRES 86 B 2768 PRO ALA CYS LEU GLU THR GLY GLU TYR ALA ARG LEU GLN
SEQRES 87 B 2768 ALA SER GLY ALA GLY THR TRP CYS VAL ASP PRO ALA SER
SEQRES 88 B 2768 GLY GLU GLU LEU ARG PRO GLY SER SER SER SER ALA GLN
SEQRES 89 B 2768 CYS PRO SER LEU CYS ASN VAL LEU LYS SER GLY VAL LEU
SEQRES 90 B 2768 SER ARG ARG VAL SER PRO GLY TYR VAL PRO ALA CYS ARG
SEQRES 91 B 2768 ALA GLU ASP GLY GLY PHE SER PRO VAL GLN CYS ASP GLN
SEQRES 92 B 2768 ALA GLN GLY SER CYS TRP CYS VAL MET ASP SER GLY GLU
SEQRES 93 B 2768 GLU VAL PRO GLY THR ARG VAL THR GLY GLY GLN PRO ALA
SEQRES 94 B 2768 CYS GLU SER PRO ARG CYS PRO LEU PRO PHE ASN ALA SER
SEQRES 95 B 2768 GLU VAL VAL GLY GLY THR ILE LEU CYS GLU THR ILE SER
SEQRES 96 B 2768 GLY PRO THR GLY SER ALA MET GLN GLN CYS GLN LEU LEU
SEQRES 97 B 2768 CYS ARG GLN GLY SER TRP SER VAL PHE PRO PRO GLY PRO
SEQRES 98 B 2768 LEU ILE CYS SER LEU GLU SER GLY ARG TRP GLU SER GLN
SEQRES 99 B 2768 LEU PRO GLN PRO ARG ALA CYS GLN ARG PRO GLN LEU TRP
SEQRES 100 B 2768 GLN THR ILE GLN THR GLN GLY HIS PHE GLN LEU GLN LEU
SEQRES 101 B 2768 PRO PRO GLY LYS MET CYS SER ALA ASP TYR ALA ASP LEU
SEQRES 102 B 2768 LEU GLN THR PHE GLN VAL PHE ILE LEU ASP GLU LEU THR
SEQRES 103 B 2768 ALA ARG GLY PHE CYS GLN ILE GLN VAL LYS THR PHE GLY
SEQRES 104 B 2768 THR LEU VAL SER ILE PRO VAL CYS ASN ASN SER SER VAL
SEQRES 105 B 2768 GLN VAL GLY CYS LEU THR ARG GLU ARG LEU GLY VAL ASN
SEQRES 106 B 2768 VAL THR TRP LYS SER ARG LEU GLU ASP ILE PRO VAL ALA
SEQRES 107 B 2768 SER LEU PRO ASP LEU HIS ASP ILE GLU ARG ALA LEU VAL
SEQRES 108 B 2768 GLY LYS ASP LEU LEU GLY ARG PHE THR ASP LEU ILE GLN
SEQRES 109 B 2768 SER GLY SER PHE GLN LEU HIS LEU ASP SER LYS THR PHE
SEQRES 110 B 2768 PRO ALA GLU THR ILE ARG PHE LEU GLN GLY ASP HIS PHE
SEQRES 111 B 2768 GLY THR SER PRO ARG THR TRP PHE GLY CYS SER GLU GLY
SEQRES 112 B 2768 PHE TYR GLN VAL LEU THR SER GLU ALA SER GLN ASP GLY
SEQRES 113 B 2768 LEU GLY CYS VAL LYS CYS PRO GLU GLY SER TYR SER GLN
SEQRES 114 B 2768 ASP GLU GLU CYS ILE PRO CYS PRO VAL GLY PHE TYR GLN
SEQRES 115 B 2768 GLU GLN ALA GLY SER LEU ALA CYS VAL PRO CYS PRO VAL
SEQRES 116 B 2768 GLY ARG THR THR ILE SER ALA GLY ALA PHE SER GLN THR
SEQRES 117 B 2768 HIS CYS VAL THR ASP CYS GLN ARG ASN GLU ALA GLY LEU
SEQRES 118 B 2768 GLN CYS ASP GLN ASN GLY GLN TYR ARG ALA SER GLN LYS
SEQRES 119 B 2768 ASP ARG GLY SER GLY LYS ALA PHE CYS VAL ASP GLY GLU
SEQRES 120 B 2768 GLY ARG ARG LEU PRO TRP TRP GLU THR GLU ALA PRO LEU
SEQRES 121 B 2768 GLU ASP SER GLN CYS LEU MET MET GLN LYS PHE GLU LYS
SEQRES 122 B 2768 VAL PRO GLU SER LYS VAL ILE PHE ASP ALA ASN ALA PRO
SEQRES 123 B 2768 VAL ALA VAL ARG SER LYS VAL PRO ASP SER GLU PHE PRO
SEQRES 124 B 2768 VAL MET GLN CYS LEU THR ASP CYS THR GLU ASP GLU ALA
SEQRES 125 B 2768 CYS SER PHE PHE THR VAL SER THR THR GLU PRO GLU ILE
SEQRES 126 B 2768 SER CYS ASP PHE TYR ALA TRP THR SER ASP ASN VAL ALA
SEQRES 127 B 2768 CYS MET THR SER ASP GLN LYS ARG ASP ALA LEU GLY ASN
SEQRES 128 B 2768 SER LYS ALA THR SER PHE GLY SER LEU ARG CYS GLN VAL
SEQRES 129 B 2768 LYS VAL ARG SER HIS GLY GLN ASP SER PRO ALA VAL TYR
SEQRES 130 B 2768 LEU LYS LYS GLY GLN GLY SER THR THR THR LEU GLN LYS
SEQRES 131 B 2768 ARG PHE GLU PRO THR GLY PHE GLN ASN MET LEU SER GLY
SEQRES 132 B 2768 LEU TYR ASN PRO ILE VAL PHE SER ALA SER GLY ALA ASN
SEQRES 133 B 2768 LEU THR ASP ALA HIS LEU PHE CYS LEU LEU ALA CYS ASP
SEQRES 134 B 2768 ARG ASP LEU CYS CYS ASP GLY PHE VAL LEU THR GLN VAL
SEQRES 135 B 2768 GLN GLY GLY ALA ILE ILE CYS GLY LEU LEU SER SER PRO
SEQRES 136 B 2768 SER VAL LEU LEU CYS ASN VAL LYS ASP TRP MET ASP PRO
SEQRES 137 B 2768 SER GLU ALA TRP ALA ASN ALA THR CYS PRO GLY VAL THR
SEQRES 138 B 2768 TYR ASP GLN GLU SER HIS GLN VAL ILE LEU ARG LEU GLY
SEQRES 139 B 2768 ASP GLN GLU PHE ILE LYS SER LEU THR PRO LEU GLU GLY
SEQRES 140 B 2768 THR GLN ASP THR PHE THR ASN PHE GLN GLN VAL TYR LEU
SEQRES 141 B 2768 TRP LYS ASP SER ASP MET GLY SER ARG PRO GLU SER MET
SEQRES 142 B 2768 GLY CYS ARG LYS ASP THR VAL PRO ARG PRO ALA SER PRO
SEQRES 143 B 2768 THR GLU ALA GLY LEU THR THR GLU LEU PHE SER PRO VAL
SEQRES 144 B 2768 ASP LEU ASN GLN VAL ILE VAL ASN GLY ASN GLN SER LEU
SEQRES 145 B 2768 SER SER GLN LYS HIS TRP LEU PHE LYS HIS LEU PHE SER
SEQRES 146 B 2768 ALA GLN GLN ALA ASN LEU TRP CYS LEU SER ARG CYS VAL
SEQRES 147 B 2768 GLN GLU HIS SER PHE CYS GLN LEU ALA GLU ILE THR GLU
SEQRES 148 B 2768 SER ALA SER LEU TYR PHE THR CYS THR LEU TYR PRO GLU
SEQRES 149 B 2768 ALA GLN VAL CYS ASP ASP ILE MET GLU SER ASN ALA GLN
SEQRES 150 B 2768 GLY CYS ARG LEU ILE LEU PRO GLN MET PRO LYS ALA LEU
SEQRES 151 B 2768 PHE ARG LYS LYS VAL ILE LEU GLU ASP LYS VAL LYS ASN
SEQRES 152 B 2768 PHE TYR THR ARG LEU PRO PHE GLN LYS LEU MET GLY ILE
SEQRES 153 B 2768 SER ILE ARG ASN LYS VAL PRO MET SER GLU LYS SER ILE
SEQRES 154 B 2768 SER ASN GLY PHE PHE GLU CYS GLU ARG ARG CYS ASP ALA
SEQRES 155 B 2768 ASP PRO CYS CYS THR GLY PHE GLY PHE LEU ASN VAL SER
SEQRES 156 B 2768 GLN LEU LYS GLY GLY GLU VAL THR CYS LEU THR LEU ASN
SEQRES 157 B 2768 SER LEU GLY ILE GLN MET CYS SER GLU GLU ASN GLY GLY
SEQRES 158 B 2768 ALA TRP ARG ILE LEU ASP CYS GLY SER PRO ASP ILE GLU
SEQRES 159 B 2768 VAL HIS THR TYR PRO PHE GLY TRP TYR GLN LYS PRO ILE
SEQRES 160 B 2768 ALA GLN ASN ASN ALA PRO SER PHE CYS PRO LEU VAL VAL
SEQRES 161 B 2768 LEU PRO SER LEU THR GLU LYS VAL SER LEU ASP SER TRP
SEQRES 162 B 2768 GLN SER LEU ALA LEU SER SER VAL VAL VAL ASP PRO SER
SEQRES 163 B 2768 ILE ARG HIS PHE ASP VAL ALA HIS VAL SER THR ALA ALA
SEQRES 164 B 2768 THR SER ASN PHE SER ALA VAL ARG ASP LEU CYS LEU SER
SEQRES 165 B 2768 GLU CYS SER GLN HIS GLU ALA CYS LEU ILE THR THR LEU
SEQRES 166 B 2768 GLN THR GLN PRO GLY ALA VAL ARG CYS MET PHE TYR ALA
SEQRES 167 B 2768 ASP THR GLN SER CYS THR HIS SER LEU GLN GLY GLN ASN
SEQRES 168 B 2768 CYS ARG LEU LEU LEU ARG GLU GLU ALA THR HIS ILE TYR
SEQRES 169 B 2768 ARG LYS PRO GLY ILE SER LEU LEU SER TYR GLU ALA SER
SEQRES 170 B 2768 VAL PRO SER VAL PRO ILE SER THR HIS GLY ARG LEU LEU
SEQRES 171 B 2768 GLY ARG SER GLN ALA ILE GLN VAL GLY THR SER TRP LYS
SEQRES 172 B 2768 GLN VAL ASP GLN PHE LEU GLY VAL PRO TYR ALA ALA PRO
SEQRES 173 B 2768 PRO LEU ALA GLU ARG ARG PHE GLN ALA PRO GLU PRO LEU
SEQRES 174 B 2768 ASN TRP THR GLY SER TRP ASP ALA SER LYS PRO ARG ALA
SEQRES 175 B 2768 SER CYS TRP GLN PRO GLY THR ARG THR SER THR SER PRO
SEQRES 176 B 2768 GLY VAL SER GLU ASP CYS LEU TYR LEU ASN VAL PHE ILE
SEQRES 177 B 2768 PRO GLN ASN VAL ALA PRO ASN ALA SER VAL LEU VAL PHE
SEQRES 178 B 2768 PHE HIS ASN THR MET ASP ARG GLU GLU SER GLU GLY TRP
SEQRES 179 B 2768 PRO ALA ILE ASP GLY SER PHE LEU ALA ALA VAL GLY ASN
SEQRES 180 B 2768 LEU ILE VAL VAL THR ALA SER TYR ARG VAL GLY VAL PHE
SEQRES 181 B 2768 GLY PHE LEU SER SER GLY SER GLY GLU VAL SER GLY ASN
SEQRES 182 B 2768 TRP GLY LEU LEU ASP GLN VAL ALA ALA LEU THR TRP VAL
SEQRES 183 B 2768 GLN THR HIS ILE ARG GLY PHE GLY GLY ASP PRO ARG ARG
SEQRES 184 B 2768 VAL SER LEU ALA ALA ASP ARG GLY GLY ALA ASP VAL ALA
SEQRES 185 B 2768 SER ILE HIS LEU LEU THR ALA ARG ALA THR ASN SER GLN
SEQRES 186 B 2768 LEU PHE ARG ARG ALA VAL LEU MET GLY GLY SER ALA LEU
SEQRES 187 B 2768 SER PRO ALA ALA VAL ILE SER HIS GLU ARG ALA GLN GLN
SEQRES 188 B 2768 GLN ALA ILE ALA LEU ALA LYS GLU VAL SER CYS PRO MET
SEQRES 189 B 2768 SER SER SER GLN GLU VAL VAL SER CYS LEU ARG GLN LYS
SEQRES 190 B 2768 PRO ALA ASN VAL LEU ASN ASP ALA GLN THR LYS LEU LEU
SEQRES 191 B 2768 ALA VAL SER GLY PRO PHE HIS TYR TRP GLY PRO VAL ILE
SEQRES 192 B 2768 ASP GLY HIS PHE LEU ARG GLU PRO PRO ALA ARG ALA LEU
SEQRES 193 B 2768 LYS ARG SER LEU TRP VAL GLU VAL ASP LEU LEU ILE GLY
SEQRES 194 B 2768 SER SER GLN ASP ASP GLY LEU ILE ASN ARG ALA LYS ALA
SEQRES 195 B 2768 VAL LYS GLN PHE GLU GLU SER ARG GLY ARG THR SER SER
SEQRES 196 B 2768 LYS THR ALA PHE TYR GLN ALA LEU GLN ASN SER LEU GLY
SEQRES 197 B 2768 GLY GLU ASP SER ASP ALA ARG VAL GLU ALA ALA ALA THR
SEQRES 198 B 2768 TRP TYR TYR SER LEU GLU HIS SER THR ASP ASP TYR ALA
SEQRES 199 B 2768 SER PHE SER ARG ALA LEU GLU ASN ALA THR ARG ASP TYR
SEQRES 200 B 2768 PHE ILE ILE CYS PRO ILE ILE ASP MET ALA SER ALA TRP
SEQRES 201 B 2768 ALA LYS ARG ALA ARG GLY ASN VAL PHE MET TYR HIS ALA
SEQRES 202 B 2768 PRO GLU ASN TYR GLY HIS GLY SER LEU GLU LEU LEU ALA
SEQRES 203 B 2768 ASP VAL GLN PHE ALA LEU GLY LEU PRO PHE TYR PRO ALA
SEQRES 204 B 2768 TYR GLU GLY GLN PHE SER LEU GLU GLU LYS SER LEU SER
SEQRES 205 B 2768 LEU LYS ILE MET GLN TYR PHE SER HIS PHE ILE ARG SER
SEQRES 206 B 2768 GLY ASN PRO ASN TYR PRO TYR GLU PHE SER ARG LYS VAL
SEQRES 207 B 2768 PRO THR PHE ALA THR PRO TRP PRO ASP PHE VAL PRO ARG
SEQRES 208 B 2768 ALA GLY GLY GLU ASN TYR LYS GLU PHE SER GLU LEU LEU
SEQRES 209 B 2768 PRO ASN ARG GLN GLY LEU LYS LYS ALA ASP CYS SER PHE
SEQRES 210 B 2768 TRP SER LYS TYR ILE SER SER LEU LYS THR SER ALA ASP
SEQRES 211 B 2768 GLY ALA LYS GLY GLY GLN SER ALA GLU SER GLU GLU GLU
SEQRES 212 B 2768 GLU LEU THR ALA GLY SER GLY LEU ARG GLU ASP LEU LEU
SEQRES 213 B 2768 SER LEU GLN GLU PRO GLY SER LYS THR TYR SER LYS
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET MAN G 4 11
HET NAG H 1 14
HET NAG H 2 14
HET BMA H 3 11
HET MAN H 4 11
HET MAN H 5 11
HET MAN H 6 11
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET NAG K 1 14
HET NAG K 2 14
HET BMA K 3 11
HET NAG L 1 14
HET NAG L 2 14
HET NAG M 1 14
HET NAG M 2 14
HET BMA M 3 11
HET MAN M 4 11
HET NAG N 1 14
HET NAG N 2 14
HET BMA N 3 11
HET MAN N 4 11
HET MAN N 5 11
HET MAN N 6 11
HET NAG A2801 14
HET NAG A2802 14
HET NAG A2803 14
HET NAG A2804 14
HET NAG A2805 14
HET NAG A2806 14
HET NAG A2807 14
HET NAG A2808 14
HET NAG B2801 14
HET NAG B2802 14
HET NAG B2803 14
HET NAG B2804 14
HET NAG B2805 14
HET NAG B2806 14
HET NAG B2807 14
HET NAG B2808 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 3 NAG 40(C8 H15 N O6)
FORMUL 5 BMA 6(C6 H12 O6)
FORMUL 7 MAN 8(C6 H12 O6)
HELIX 1 AA1 ARG A 32 LYS A 44 1 13
HELIX 2 AA2 SER A 94 LEU A 105 1 12
HELIX 3 AA3 VAL A 148 ARG A 152 5 5
HELIX 4 AA4 ARG A 162 LEU A 171 1 10
HELIX 5 AA5 VAL A 208 ARG A 213 1 6
HELIX 6 AA6 THR A 220 PHE A 228 1 9
HELIX 7 AA7 THR A 270 GLU A 273 5 4
HELIX 8 AA8 THR A 274 ILE A 291 1 18
HELIX 9 AA9 THR A 299 GLY A 312 1 14
HELIX 10 AB1 MET A 346 ARG A 350 5 5
HELIX 11 AB2 CYS A 364 TYR A 376 1 13
HELIX 12 AB3 LEU A 421 GLU A 427 1 7
HELIX 13 AB4 VAL A 435 PHE A 448 1 14
HELIX 14 AB5 SER A 450 THR A 461 1 12
HELIX 15 AB6 ARG A 466 PHE A 472 1 7
HELIX 16 AB7 LYS A 475 GLN A 482 1 8
HELIX 17 AB8 ASN A 557 GLU A 573 1 17
HELIX 18 AB9 LEU A 574 SER A 586 1 13
HELIX 19 AC1 ASP A 594 SER A 605 1 12
HELIX 20 AC2 GLN A 606 CYS A 608 5 3
HELIX 21 AC3 THR A 660 GLY A 674 1 15
HELIX 22 AC4 THR A 728 LEU A 746 1 19
HELIX 23 AC5 PRO A 778 ASN A 792 1 15
HELIX 24 AC6 ASP A 796 ILE A 806 1 11
HELIX 25 AC7 GLY A 923 SER A 949 1 27
HELIX 26 AC8 GLY A 954 GLY A 962 1 9
HELIX 27 AC9 ASN A 967 GLY A 971 5 5
HELIX 28 AD1 PRO A 978 PHE A 986 1 9
HELIX 29 AD2 SER A 990 ARG A 1009 1 20
HELIX 30 AD3 THR A 1075 SER A 1087 1 13
HELIX 31 AD4 SER A 1147 SER A 1158 1 12
HELIX 32 AD5 LEU A 1300 LYS A 1304 5 5
HELIX 33 AD6 LEU A 1314 ARG A 1328 1 15
HELIX 34 AD7 ASP A 1382 GLY A 1392 1 11
HELIX 35 AD8 LEU A 1395 SER A 1405 1 11
HELIX 36 AD9 SER A 1453 LEU A 1457 5 5
HELIX 37 AE1 SER A 1506 CYS A 1510 5 5
HELIX 38 AE2 THR A 1512 ASN A 1517 1 6
HELIX 39 AE3 PRO A 1552 GLU A 1557 1 6
HELIX 40 AE4 PRO A 1575 VAL A 1579 5 5
HELIX 41 AE5 PHE A 1598 CYS A 1607 1 10
HELIX 42 AE6 THR A 1718 ASP A 1731 1 14
HELIX 43 AE7 GLN A 1888 GLU A 1900 1 13
HELIX 44 AE8 SER A 1988 ASP A 2003 1 16
HELIX 45 AE9 ALA A 2097 SER A 2099 5 3
HELIX 46 AF1 ASN A 2122 HIS A 2137 1 16
HELIX 47 AF2 GLY A 2319 ASN A 2327 1 9
HELIX 48 AF3 ASN A 2353 HIS A 2369 1 17
HELIX 49 AF4 ILE A 2370 PHE A 2373 5 4
HELIX 50 AF5 SER A 2393 THR A 2398 1 6
HELIX 51 AF6 SER A 2425 SER A 2441 1 17
HELIX 52 AF7 SER A 2446 ARG A 2455 1 10
HELIX 53 AF8 PRO A 2458 VAL A 2472 1 15
HELIX 54 AF9 SER A 2473 TYR A 2478 5 6
HELIX 55 AG1 PRO A 2491 LEU A 2496 1 6
HELIX 56 AG2 LYS A 2497 SER A 2499 5 3
HELIX 57 AG3 ILE A 2517 ARG A 2519 5 3
HELIX 58 AG4 ALA A 2520 GLY A 2531 1 12
HELIX 59 AG5 LYS A 2536 GLY A 2548 1 13
HELIX 60 AG6 ASP A 2553 TYR A 2564 1 12
HELIX 61 AG7 ASP A 2572 ILE A 2589 1 18
HELIX 62 AG8 ILE A 2589 ARG A 2603 1 15
HELIX 63 AG9 LEU A 2625 LEU A 2632 1 8
HELIX 64 AH1 GLY A 2633 TYR A 2637 5 5
HELIX 65 AH2 SER A 2645 SER A 2665 1 21
HELIX 66 AH3 LYS A 2711 LYS A 2720 1 10
HELIX 67 AH4 LYS A 2720 THR A 2727 1 8
HELIX 68 AH5 ARG B 32 LYS B 44 1 13
HELIX 69 AH6 SER B 94 LEU B 105 1 12
HELIX 70 AH7 VAL B 148 ARG B 152 5 5
HELIX 71 AH8 ARG B 162 LEU B 171 1 10
HELIX 72 AH9 VAL B 208 ARG B 213 1 6
HELIX 73 AI1 THR B 220 PHE B 228 1 9
HELIX 74 AI2 THR B 270 GLU B 273 5 4
HELIX 75 AI3 THR B 274 ILE B 291 1 18
HELIX 76 AI4 THR B 299 PHE B 311 1 13
HELIX 77 AI5 MET B 346 ARG B 350 5 5
HELIX 78 AI6 CYS B 364 TYR B 376 1 13
HELIX 79 AI7 LEU B 421 GLU B 427 1 7
HELIX 80 AI8 VAL B 435 PHE B 448 1 14
HELIX 81 AI9 SER B 450 THR B 461 1 12
HELIX 82 AJ1 ARG B 466 PHE B 472 1 7
HELIX 83 AJ2 LYS B 475 GLN B 482 1 8
HELIX 84 AJ3 ASN B 557 GLU B 573 1 17
HELIX 85 AJ4 LEU B 574 SER B 586 1 13
HELIX 86 AJ5 ASP B 594 SER B 605 1 12
HELIX 87 AJ6 GLN B 606 CYS B 608 5 3
HELIX 88 AJ7 THR B 660 GLY B 674 1 15
HELIX 89 AJ8 THR B 728 LEU B 746 1 19
HELIX 90 AJ9 PRO B 778 ASN B 792 1 15
HELIX 91 AK1 ASP B 796 ILE B 806 1 11
HELIX 92 AK2 GLY B 923 SER B 949 1 27
HELIX 93 AK3 GLY B 954 GLY B 962 1 9
HELIX 94 AK4 ASN B 967 GLY B 971 5 5
HELIX 95 AK5 PRO B 978 PHE B 986 1 9
HELIX 96 AK6 SER B 990 ARG B 1009 1 20
HELIX 97 AK7 THR B 1075 SER B 1088 1 14
HELIX 98 AK8 SER B 1147 SER B 1158 1 12
HELIX 99 AK9 LEU B 1300 LYS B 1304 5 5
HELIX 100 AL1 LEU B 1314 ARG B 1328 1 15
HELIX 101 AL2 ASP B 1382 GLY B 1392 1 11
HELIX 102 AL3 LEU B 1395 SER B 1405 1 11
HELIX 103 AL4 SER B 1453 LEU B 1457 5 5
HELIX 104 AL5 SER B 1506 CYS B 1510 5 5
HELIX 105 AL6 THR B 1512 ASN B 1517 1 6
HELIX 106 AL7 PRO B 1552 GLU B 1557 1 6
HELIX 107 AL8 PRO B 1575 VAL B 1579 5 5
HELIX 108 AL9 PHE B 1598 CYS B 1607 1 10
HELIX 109 AM1 THR B 1718 ASP B 1731 1 14
HELIX 110 AM2 GLN B 1888 GLU B 1900 1 13
HELIX 111 AM3 SER B 1988 ASP B 2003 1 16
HELIX 112 AM4 ALA B 2097 SER B 2099 5 3
HELIX 113 AM5 ASN B 2122 HIS B 2137 1 16
HELIX 114 AM6 GLY B 2319 ASN B 2327 1 9
HELIX 115 AM7 ASN B 2353 HIS B 2369 1 17
HELIX 116 AM8 ILE B 2370 PHE B 2373 5 4
HELIX 117 AM9 SER B 2393 THR B 2398 1 6
HELIX 118 AN1 SER B 2425 SER B 2441 1 17
HELIX 119 AN2 SER B 2446 ARG B 2455 1 10
HELIX 120 AN3 PRO B 2458 VAL B 2472 1 15
HELIX 121 AN4 SER B 2473 TYR B 2478 5 6
HELIX 122 AN5 PRO B 2491 LEU B 2496 1 6
HELIX 123 AN6 LYS B 2497 SER B 2499 5 3
HELIX 124 AN7 ILE B 2517 ARG B 2519 5 3
HELIX 125 AN8 ALA B 2520 GLY B 2531 1 12
HELIX 126 AN9 LYS B 2536 GLY B 2548 1 13
HELIX 127 AO1 ASP B 2553 TYR B 2564 1 12
HELIX 128 AO2 ASP B 2572 ILE B 2589 1 18
HELIX 129 AO3 ILE B 2589 ARG B 2603 1 15
HELIX 130 AO4 LEU B 2625 LEU B 2632 1 8
HELIX 131 AO5 GLY B 2633 TYR B 2637 5 5
HELIX 132 AO6 SER B 2645 SER B 2665 1 21
HELIX 133 AO7 LYS B 2711 LYS B 2720 1 10
HELIX 134 AO8 LYS B 2720 THR B 2727 1 8
SHEET 1 AA1 2 CYS A 52 ALA A 53 0
SHEET 2 AA1 2 SER A 57 PHE A 58 -1 O SER A 57 N ALA A 53
SHEET 1 AA2 3 VAL A 61 GLN A 62 0
SHEET 2 AA2 3 SER A 69 CYS A 72 -1 O TRP A 71 N GLN A 62
SHEET 3 AA2 3 GLN A 85 PRO A 86 -1 N GLN A 85 O CYS A 70
SHEET 1 AA3 3 GLN A 130 CYS A 131 0
SHEET 2 AA3 3 GLN A 137 TRP A 139 -1 O TRP A 139 N GLN A 130
SHEET 3 AA3 3 GLN A 153 LEU A 154 -1 O GLN A 153 N CYS A 138
SHEET 1 AA4 3 VAL A 192 CYS A 194 0
SHEET 2 AA4 3 GLY A 233 CYS A 237 -1 O HIS A 236 N GLN A 193
SHEET 3 AA4 3 GLU A 251 LEU A 253 -1 O LEU A 253 N GLY A 233
SHEET 1 AA5 2 VAL A 328 CYS A 330 0
SHEET 2 AA5 2 CYS A 336 CYS A 338 -1 O TRP A 337 N GLN A 329
SHEET 1 AA6 2 VAL A 629 PHE A 632 0
SHEET 2 AA6 2 GLU A 635 CYS A 638 -1 O TRP A 637 N GLN A 630
SHEET 1 AA7 3 GLN A 697 CYS A 698 0
SHEET 2 AA7 3 GLU A 702 TYR A 704 -1 O TYR A 704 N GLN A 697
SHEET 3 AA7 3 SER A 718 ALA A 719 -1 O SER A 718 N CYS A 703
SHEET 1 AA8 2 VAL A 772 GLN A 773 0
SHEET 2 AA8 2 TRP A 899 CYS A 900 -1 O TRP A 899 N GLN A 773
SHEET 1 AA9 2 VAL A1040 CYS A1042 0
SHEET 2 AA9 2 CYS A1049 CYS A1051 -1 O TRP A1050 N GLN A1041
SHEET 1 AB1 2 GLN A1091 ALA A1092 0
SHEET 2 AB1 2 LEU A1103 PHE A1104 -1 O PHE A1104 N GLN A1091
SHEET 1 AB2 2 LEU A1117 ALA A1119 0
SHEET 2 AB2 2 THR A1124 CYS A1126 -1 O TRP A1125 N GLN A1118
SHEET 1 AB3 2 GLY A1227 LEU A1230 0
SHEET 2 AB3 2 GLN A1246 CYS A1249 -1 O GLN A1246 N LEU A1230
SHEET 1 AB4 2 TRP A1254 SER A1255 0
SHEET 2 AB4 2 CYS A1281 GLN A1282 -1 O GLN A1282 N TRP A1254
SHEET 1 AB5 3 PRO A1284 GLN A1285 0
SHEET 2 AB5 3 CYS A1459 LYS A1461 -1 O CYS A1459 N GLN A1285
SHEET 3 AB5 3 PHE A1444 GLN A1446 -1 N TYR A1445 O VAL A1460
SHEET 1 AB6 3 ASN A1365 ARG A1371 0
SHEET 2 AB6 3 THR A1289 HIS A1295 -1 N ILE A1290 O SER A1370
SHEET 3 AB6 3 TRP A1437 GLY A1439 -1 O TRP A1437 N GLN A1291
SHEET 1 AB7 2 GLN A1332 THR A1337 0
SHEET 2 AB7 2 THR A1340 PRO A1345 -1 O VAL A1342 N VAL A1335
SHEET 1 AB8 2 SER A1466 SER A1468 0
SHEET 2 AB8 2 CYS A1473 PRO A1475 -1 O ILE A1474 N TYR A1467
SHEET 1 AB9 2 PHE A1480 TYR A1481 0
SHEET 2 AB9 2 VAL A1491 PRO A1492 -1 O VAL A1491 N TYR A1481
SHEET 1 AC1 2 SER A1532 LYS A1534 0
SHEET 2 AC1 2 ALA A1541 CYS A1543 -1 O PHE A1542 N GLN A1533
SHEET 1 AC2 6 THR A1685 THR A1686 0
SHEET 2 AC2 6 ARG A1691 GLU A1693 -1 O PHE A1692 N THR A1685
SHEET 3 AC2 6 PHE A1815 TRP A1821 -1 O LEU A1820 N GLU A1693
SHEET 4 AC2 6 GLY A1736 GLN A1741 -1 N PHE A1737 O TYR A1819
SHEET 5 AC2 6 ILE A1747 LEU A1752 -1 O ILE A1748 N THR A1740
SHEET 6 AC2 6 ILE A1708 PHE A1710 -1 N ILE A1708 O CYS A1749
SHEET 1 AC3 7 PHE A1697 MET A1700 0
SHEET 2 AC3 7 VAL A1757 ASN A1761 -1 O CYS A1760 N GLN A1698
SHEET 3 AC3 7 LYS A1876 PHE A1880 -1 O LEU A1879 N LEU A1758
SHEET 4 AC3 7 PHE A1917 TYR A1922 -1 O PHE A1917 N PHE A1880
SHEET 5 AC3 7 LEU A1906 THR A1910 -1 N LEU A1906 O TYR A1922
SHEET 6 AC3 7 ALA A1949 LYS A1953 -1 O PHE A1951 N ALA A1907
SHEET 7 AC3 7 PHE A1856 PRO A1858 -1 N SER A1857 O ARG A1952
SHEET 1 AC4 3 ILE A1865 VAL A1866 0
SHEET 2 AC4 3 ARG A1940 LEU A1943 1 O LEU A1943 N ILE A1865
SHEET 3 AC4 3 GLN A1926 VAL A1927 -1 N VAL A1927 O ARG A1940
SHEET 1 AC5 5 THR A1966 ARG A1967 0
SHEET 2 AC5 5 TYR A2063 GLN A2064 -1 O GLN A2064 N THR A1966
SHEET 3 AC5 5 GLY A2008 ASN A2013 -1 N PHE A2009 O TYR A2063
SHEET 4 AC5 5 VAL A2022 SER A2029 -1 O LEU A2025 N GLY A2010
SHEET 5 AC5 5 SER A1977 ILE A1978 -1 N SER A1977 O ASN A2028
SHEET 1 AC6 5 THR A1966 ARG A1967 0
SHEET 2 AC6 5 TYR A2063 GLN A2064 -1 O GLN A2064 N THR A1966
SHEET 3 AC6 5 GLY A2008 ASN A2013 -1 N PHE A2009 O TYR A2063
SHEET 4 AC6 5 VAL A2022 SER A2029 -1 O LEU A2025 N GLY A2010
SHEET 5 AC6 5 VAL A1982 PRO A1983 -1 N VAL A1982 O CYS A2024
SHEET 1 AC7 7 LYS A1972 LEU A1973 0
SHEET 2 AC7 7 ILE A2032 MET A2034 -1 O MET A2034 N LYS A1972
SHEET 3 AC7 7 PHE A2110 SER A2116 -1 O HIS A2114 N GLN A2033
SHEET 4 AC7 7 ALA A2151 TYR A2157 -1 O CYS A2154 N ALA A2113
SHEET 5 AC7 7 ILE A2142 THR A2147 -1 N ILE A2142 O TYR A2157
SHEET 6 AC7 7 HIS A2182 ARG A2185 -1 O HIS A2182 N LEU A2145
SHEET 7 AC7 7 GLN A2094 LEU A2096 -1 N GLN A2094 O ARG A2185
SHEET 1 AC8 3 VAL A2101 VAL A2103 0
SHEET 2 AC8 3 ASN A2171 LEU A2176 1 O LEU A2174 N VAL A2102
SHEET 3 AC8 3 GLN A2161 THR A2164 -1 N THR A2164 O ASN A2171
SHEET 1 AC9 4 SER A2193 GLU A2195 0
SHEET 2 AC9 4 VAL A2198 ILE A2203 -1 O SER A2200 N SER A2193
SHEET 3 AC9 4 GLY A2207 LEU A2210 -1 O GLY A2207 N ILE A2203
SHEET 4 AC9 4 GLY A2253 ASP A2256 1 O GLY A2253 N ARG A2208
SHEET 1 AD111 ARG A2212 VAL A2218 0
SHEET 2 AD111 SER A2221 GLN A2227 -1 O LYS A2223 N ILE A2216
SHEET 3 AD111 VAL A2286 PRO A2289 -1 O ILE A2288 N ASP A2226
SHEET 4 AD111 ILE A2329 ALA A2333 -1 O VAL A2330 N PHE A2287
SHEET 5 AD111 ALA A2296 PHE A2302 1 N PHE A2301 O VAL A2331
SHEET 6 AD111 GLY A2375 ASP A2385 1 O SER A2381 N VAL A2300
SHEET 7 AD111 ARG A2409 MET A2413 1 O VAL A2411 N LEU A2382
SHEET 8 AD111 LEU A2506 GLY A2509 1 O LEU A2507 N ALA A2410
SHEET 9 AD111 VAL A2608 HIS A2612 1 O PHE A2609 N ILE A2508
SHEET 10 AD111 TYR A2697 GLU A2699 1 O LYS A2698 N MET A2610
SHEET 11 AD111 ASN A2706 ARG A2707 -1 O ARG A2707 N TYR A2697
SHEET 1 AD2 2 VAL A2231 PRO A2232 0
SHEET 2 AD2 2 TYR A2283 LEU A2284 -1 O LEU A2284 N VAL A2231
SHEET 1 AD3 2 CYS B 52 ALA B 53 0
SHEET 2 AD3 2 SER B 57 PHE B 58 -1 O SER B 57 N ALA B 53
SHEET 1 AD4 3 VAL B 61 GLN B 62 0
SHEET 2 AD4 3 SER B 69 CYS B 72 -1 O TRP B 71 N GLN B 62
SHEET 3 AD4 3 GLN B 85 PRO B 86 -1 O GLN B 85 N CYS B 70
SHEET 1 AD5 3 GLN B 130 CYS B 131 0
SHEET 2 AD5 3 GLN B 137 TRP B 139 -1 O TRP B 139 N GLN B 130
SHEET 3 AD5 3 GLN B 153 LEU B 154 -1 O GLN B 153 N CYS B 138
SHEET 1 AD6 3 VAL B 192 CYS B 194 0
SHEET 2 AD6 3 GLY B 233 CYS B 237 -1 O HIS B 236 N GLN B 193
SHEET 3 AD6 3 GLU B 251 LEU B 253 -1 O LEU B 253 N GLY B 233
SHEET 1 AD7 2 VAL B 328 CYS B 330 0
SHEET 2 AD7 2 CYS B 336 CYS B 338 -1 O TRP B 337 N GLN B 329
SHEET 1 AD8 2 VAL B 629 PHE B 632 0
SHEET 2 AD8 2 GLU B 635 CYS B 638 -1 O TRP B 637 N GLN B 630
SHEET 1 AD9 3 GLN B 697 CYS B 698 0
SHEET 2 AD9 3 GLU B 702 TYR B 704 -1 O TYR B 704 N GLN B 697
SHEET 3 AD9 3 SER B 718 ALA B 719 -1 O SER B 718 N CYS B 703
SHEET 1 AE1 2 VAL B 772 GLN B 773 0
SHEET 2 AE1 2 TRP B 899 CYS B 900 -1 O TRP B 899 N GLN B 773
SHEET 1 AE2 2 VAL B1040 CYS B1042 0
SHEET 2 AE2 2 CYS B1049 CYS B1051 -1 O TRP B1050 N GLN B1041
SHEET 1 AE3 2 GLN B1091 ALA B1092 0
SHEET 2 AE3 2 LEU B1103 PHE B1104 -1 O PHE B1104 N GLN B1091
SHEET 1 AE4 2 LEU B1117 ALA B1119 0
SHEET 2 AE4 2 THR B1124 CYS B1126 -1 O TRP B1125 N GLN B1118
SHEET 1 AE5 2 GLY B1227 LEU B1230 0
SHEET 2 AE5 2 GLN B1246 CYS B1249 -1 O GLN B1246 N LEU B1230
SHEET 1 AE6 2 TRP B1254 SER B1255 0
SHEET 2 AE6 2 CYS B1281 GLN B1282 -1 O GLN B1282 N TRP B1254
SHEET 1 AE7 3 PRO B1284 GLN B1285 0
SHEET 2 AE7 3 CYS B1459 LYS B1461 -1 O CYS B1459 N GLN B1285
SHEET 3 AE7 3 PHE B1444 GLN B1446 -1 N TYR B1445 O VAL B1460
SHEET 1 AE8 3 ASN B1365 ARG B1371 0
SHEET 2 AE8 3 THR B1289 HIS B1295 -1 N ILE B1290 O SER B1370
SHEET 3 AE8 3 TRP B1437 GLY B1439 -1 O TRP B1437 N GLN B1291
SHEET 1 AE9 2 GLN B1332 THR B1337 0
SHEET 2 AE9 2 THR B1340 PRO B1345 -1 O VAL B1342 N VAL B1335
SHEET 1 AF1 2 SER B1466 SER B1468 0
SHEET 2 AF1 2 CYS B1473 PRO B1475 -1 O ILE B1474 N TYR B1467
SHEET 1 AF2 2 PHE B1480 TYR B1481 0
SHEET 2 AF2 2 VAL B1491 PRO B1492 -1 O VAL B1491 N TYR B1481
SHEET 1 AF3 2 SER B1532 LYS B1534 0
SHEET 2 AF3 2 ALA B1541 CYS B1543 -1 O PHE B1542 N GLN B1533
SHEET 1 AF4 6 THR B1685 THR B1686 0
SHEET 2 AF4 6 ARG B1691 GLU B1693 -1 O PHE B1692 N THR B1685
SHEET 3 AF4 6 PHE B1815 TRP B1821 -1 O LEU B1820 N GLU B1693
SHEET 4 AF4 6 GLY B1736 GLN B1741 -1 N PHE B1737 O TYR B1819
SHEET 5 AF4 6 ILE B1747 LEU B1752 -1 O ILE B1748 N THR B1740
SHEET 6 AF4 6 ILE B1708 PHE B1710 -1 N ILE B1708 O CYS B1749
SHEET 1 AF5 7 PHE B1697 MET B1700 0
SHEET 2 AF5 7 VAL B1757 ASN B1761 -1 O CYS B1760 N GLN B1698
SHEET 3 AF5 7 LYS B1876 PHE B1880 -1 O LEU B1879 N LEU B1758
SHEET 4 AF5 7 PHE B1917 TYR B1922 -1 O PHE B1917 N PHE B1880
SHEET 5 AF5 7 LEU B1906 THR B1910 -1 N LEU B1906 O TYR B1922
SHEET 6 AF5 7 ALA B1949 LYS B1953 -1 O PHE B1951 N ALA B1907
SHEET 7 AF5 7 PHE B1856 PRO B1858 -1 N SER B1857 O ARG B1952
SHEET 1 AF6 3 ILE B1865 VAL B1866 0
SHEET 2 AF6 3 ARG B1940 LEU B1943 1 O LEU B1943 N ILE B1865
SHEET 3 AF6 3 GLN B1926 VAL B1927 -1 N VAL B1927 O ARG B1940
SHEET 1 AF7 5 THR B1966 ARG B1967 0
SHEET 2 AF7 5 TYR B2063 GLN B2064 -1 O GLN B2064 N THR B1966
SHEET 3 AF7 5 GLY B2008 ASN B2013 -1 N PHE B2009 O TYR B2063
SHEET 4 AF7 5 VAL B2022 SER B2029 -1 O LEU B2025 N GLY B2010
SHEET 5 AF7 5 SER B1977 ILE B1978 -1 N SER B1977 O ASN B2028
SHEET 1 AF8 5 THR B1966 ARG B1967 0
SHEET 2 AF8 5 TYR B2063 GLN B2064 -1 O GLN B2064 N THR B1966
SHEET 3 AF8 5 GLY B2008 ASN B2013 -1 N PHE B2009 O TYR B2063
SHEET 4 AF8 5 VAL B2022 SER B2029 -1 O LEU B2025 N GLY B2010
SHEET 5 AF8 5 VAL B1982 PRO B1983 -1 N VAL B1982 O CYS B2024
SHEET 1 AF9 7 LYS B1972 LEU B1973 0
SHEET 2 AF9 7 ILE B2032 MET B2034 -1 O MET B2034 N LYS B1972
SHEET 3 AF9 7 PHE B2110 SER B2116 -1 O HIS B2114 N GLN B2033
SHEET 4 AF9 7 ALA B2151 TYR B2157 -1 O CYS B2154 N ALA B2113
SHEET 5 AF9 7 ILE B2142 THR B2147 -1 N ILE B2142 O TYR B2157
SHEET 6 AF9 7 HIS B2182 ARG B2185 -1 O HIS B2182 N LEU B2145
SHEET 7 AF9 7 GLN B2094 LEU B2096 -1 N GLN B2094 O ARG B2185
SHEET 1 AG1 3 VAL B2101 VAL B2103 0
SHEET 2 AG1 3 ASN B2171 LEU B2176 1 O LEU B2174 N VAL B2102
SHEET 3 AG1 3 GLN B2161 THR B2164 -1 N THR B2164 O ASN B2171
SHEET 1 AG2 4 SER B2193 GLU B2195 0
SHEET 2 AG2 4 VAL B2198 ILE B2203 -1 O SER B2200 N SER B2193
SHEET 3 AG2 4 GLY B2207 LEU B2210 -1 O GLY B2207 N ILE B2203
SHEET 4 AG2 4 GLY B2253 ASP B2256 1 O GLY B2253 N ARG B2208
SHEET 1 AG311 ARG B2212 VAL B2218 0
SHEET 2 AG311 SER B2221 GLN B2227 -1 O LYS B2223 N ILE B2216
SHEET 3 AG311 VAL B2286 PRO B2289 -1 O ILE B2288 N ASP B2226
SHEET 4 AG311 ILE B2329 ALA B2333 -1 O VAL B2330 N PHE B2287
SHEET 5 AG311 ALA B2296 PHE B2302 1 N PHE B2301 O VAL B2331
SHEET 6 AG311 GLY B2375 ASP B2385 1 O SER B2381 N VAL B2300
SHEET 7 AG311 ARG B2409 MET B2413 1 O VAL B2411 N LEU B2382
SHEET 8 AG311 LEU B2506 GLY B2509 1 O LEU B2507 N ALA B2410
SHEET 9 AG311 VAL B2608 HIS B2612 1 O PHE B2609 N ILE B2508
SHEET 10 AG311 TYR B2697 GLU B2699 1 O LYS B2698 N MET B2610
SHEET 11 AG311 ASN B2706 ARG B2707 -1 O ARG B2707 N TYR B2697
SHEET 1 AG4 2 VAL B2231 PRO B2232 0
SHEET 2 AG4 2 TYR B2283 LEU B2284 -1 O LEU B2284 N VAL B2231
SSBOND 1 CYS A 34 CYS A 52 1555 1555 2.03
SSBOND 2 CYS A 63 CYS A 70 1555 1555 2.03
SSBOND 3 CYS A 72 CYS A 92 1555 1555 2.03
SSBOND 4 CYS A 96 CYS A 120 1555 1555 2.03
SSBOND 5 CYS A 131 CYS A 138 1555 1555 2.03
SSBOND 6 CYS A 140 CYS A 160 1555 1555 2.03
SSBOND 7 CYS A 164 CYS A 183 1555 1555 2.03
SSBOND 8 CYS A 194 CYS A 235 1555 1555 2.03
SSBOND 9 CYS A 237 CYS A 297 1555 1555 2.04
SSBOND 10 CYS A 301 CYS A 319 1555 1555 2.03
SSBOND 11 CYS A 330 CYS A 336 1555 1555 2.03
SSBOND 12 CYS A 338 CYS A 358 1555 1555 2.03
SSBOND 13 CYS A 364 CYS A 620 1555 1555 2.03
SSBOND 14 CYS A 408 CYS A 608 1555 1555 2.03
SSBOND 15 CYS A 631 CYS A 636 1555 1555 2.03
SSBOND 16 CYS A 638 CYS A 658 1555 1555 2.04
SSBOND 17 CYS A 662 CYS A 687 1555 1555 2.03
SSBOND 18 CYS A 698 CYS A 703 1555 1555 2.03
SSBOND 19 CYS A 705 CYS A 726 1555 1555 2.03
SSBOND 20 CYS A 730 CYS A 763 1555 1555 2.03
SSBOND 21 CYS A 774 CYS A 898 1555 1555 2.03
SSBOND 22 CYS A 900 CYS A 921 1555 1555 2.03
SSBOND 23 CYS A 925 CYS A 1031 1555 1555 2.03
SSBOND 24 CYS A 1042 CYS A 1049 1555 1555 2.03
SSBOND 25 CYS A 1051 CYS A 1073 1555 1555 2.03
SSBOND 26 CYS A 1077 CYS A 1108 1555 1555 2.03
SSBOND 27 CYS A 1126 CYS A 1145 1555 1555 2.04
SSBOND 28 CYS A 1149 CYS A 1169 1555 1555 2.03
SSBOND 29 CYS A 1181 CYS A 1188 1555 1555 2.04
SSBOND 30 CYS A 1190 CYS A 1210 1555 1555 2.03
SSBOND 31 CYS A 1231 CYS A 1245 1555 1555 2.03
SSBOND 32 CYS A 1249 CYS A 1281 1555 1555 2.04
SSBOND 33 CYS A 1331 CYS A 1347 1555 1555 2.03
SSBOND 34 CYS A 1440 CYS A 1459 1555 1555 2.03
SSBOND 35 CYS A 1462 CYS A 1473 1555 1555 2.03
SSBOND 36 CYS A 1476 CYS A 1490 1555 1555 2.03
SSBOND 37 CYS A 1493 CYS A 1510 1555 1555 2.04
SSBOND 38 CYS A 1514 CYS A 1523 1555 1555 2.04
SSBOND 39 CYS A 1543 CYS A 1565 1555 1555 2.03
SSBOND 40 CYS A 1603 CYS A 1627 1555 1555 2.03
SSBOND 41 CYS A 1607 CYS A 1613 1555 1555 2.03
SSBOND 42 CYS A 1724 CYS A 1749 1555 1555 2.02
SSBOND 43 CYS A 1728 CYS A 1734 1555 1555 2.03
SSBOND 44 CYS A 1760 CYS A 1777 1555 1555 2.04
SSBOND 45 CYS A 1893 CYS A 1919 1555 1555 2.03
SSBOND 46 CYS A 1897 CYS A 1904 1555 1555 2.02
SSBOND 47 CYS A 1928 CYS A 1939 1555 1555 2.03
SSBOND 48 CYS A 1996 CYS A 2024 1555 1555 2.02
SSBOND 49 CYS A 2000 CYS A 2006 1555 1555 2.03
SSBOND 50 CYS A 2005 CYS A 2076 1555 1555 2.04
SSBOND 51 CYS A 2035 CYS A 2048 1555 1555 2.03
SSBOND 52 CYS A 2130 CYS A 2154 1555 1555 2.03
SSBOND 53 CYS A 2134 CYS A 2140 1555 1555 2.04
SSBOND 54 CYS A 2163 CYS A 2172 1555 1555 2.03
SSBOND 55 CYS A 2264 CYS A 2281 1555 1555 2.03
SSBOND 56 CYS A 2442 CYS A 2453 1555 1555 2.03
SSBOND 57 CYS A 2591 CYS A 2715 1555 1555 2.03
SSBOND 58 CYS B 34 CYS B 52 1555 1555 2.03
SSBOND 59 CYS B 63 CYS B 70 1555 1555 2.03
SSBOND 60 CYS B 72 CYS B 92 1555 1555 2.03
SSBOND 61 CYS B 96 CYS B 120 1555 1555 2.03
SSBOND 62 CYS B 131 CYS B 138 1555 1555 2.03
SSBOND 63 CYS B 140 CYS B 160 1555 1555 2.03
SSBOND 64 CYS B 164 CYS B 183 1555 1555 2.03
SSBOND 65 CYS B 194 CYS B 235 1555 1555 2.03
SSBOND 66 CYS B 237 CYS B 297 1555 1555 2.04
SSBOND 67 CYS B 301 CYS B 319 1555 1555 2.03
SSBOND 68 CYS B 330 CYS B 336 1555 1555 2.03
SSBOND 69 CYS B 338 CYS B 358 1555 1555 2.03
SSBOND 70 CYS B 364 CYS B 620 1555 1555 2.03
SSBOND 71 CYS B 408 CYS B 608 1555 1555 2.03
SSBOND 72 CYS B 631 CYS B 636 1555 1555 2.03
SSBOND 73 CYS B 638 CYS B 658 1555 1555 2.04
SSBOND 74 CYS B 662 CYS B 687 1555 1555 2.03
SSBOND 75 CYS B 698 CYS B 703 1555 1555 2.03
SSBOND 76 CYS B 705 CYS B 726 1555 1555 2.02
SSBOND 77 CYS B 730 CYS B 763 1555 1555 2.03
SSBOND 78 CYS B 774 CYS B 898 1555 1555 2.03
SSBOND 79 CYS B 900 CYS B 921 1555 1555 2.03
SSBOND 80 CYS B 925 CYS B 1031 1555 1555 2.03
SSBOND 81 CYS B 1042 CYS B 1049 1555 1555 2.03
SSBOND 82 CYS B 1051 CYS B 1073 1555 1555 2.02
SSBOND 83 CYS B 1077 CYS B 1108 1555 1555 2.03
SSBOND 84 CYS B 1126 CYS B 1145 1555 1555 2.04
SSBOND 85 CYS B 1149 CYS B 1169 1555 1555 2.03
SSBOND 86 CYS B 1181 CYS B 1188 1555 1555 2.05
SSBOND 87 CYS B 1190 CYS B 1210 1555 1555 2.03
SSBOND 88 CYS B 1231 CYS B 1245 1555 1555 2.03
SSBOND 89 CYS B 1249 CYS B 1281 1555 1555 2.04
SSBOND 90 CYS B 1331 CYS B 1347 1555 1555 2.03
SSBOND 91 CYS B 1440 CYS B 1459 1555 1555 2.03
SSBOND 92 CYS B 1462 CYS B 1473 1555 1555 2.03
SSBOND 93 CYS B 1476 CYS B 1490 1555 1555 2.03
SSBOND 94 CYS B 1493 CYS B 1510 1555 1555 2.04
SSBOND 95 CYS B 1514 CYS B 1523 1555 1555 2.04
SSBOND 96 CYS B 1543 CYS B 1565 1555 1555 2.03
SSBOND 97 CYS B 1603 CYS B 1627 1555 1555 2.03
SSBOND 98 CYS B 1607 CYS B 1613 1555 1555 2.03
SSBOND 99 CYS B 1724 CYS B 1749 1555 1555 2.02
SSBOND 100 CYS B 1728 CYS B 1734 1555 1555 2.03
SSBOND 101 CYS B 1760 CYS B 1777 1555 1555 2.04
SSBOND 102 CYS B 1893 CYS B 1919 1555 1555 2.03
SSBOND 103 CYS B 1897 CYS B 1904 1555 1555 2.02
SSBOND 104 CYS B 1928 CYS B 1939 1555 1555 2.03
SSBOND 105 CYS B 1996 CYS B 2024 1555 1555 2.03
SSBOND 106 CYS B 2000 CYS B 2006 1555 1555 2.03
SSBOND 107 CYS B 2005 CYS B 2076 1555 1555 2.03
SSBOND 108 CYS B 2035 CYS B 2048 1555 1555 2.03
SSBOND 109 CYS B 2130 CYS B 2154 1555 1555 2.03
SSBOND 110 CYS B 2134 CYS B 2140 1555 1555 2.04
SSBOND 111 CYS B 2163 CYS B 2172 1555 1555 2.03
SSBOND 112 CYS B 2264 CYS B 2281 1555 1555 2.03
SSBOND 113 CYS B 2442 CYS B 2453 1555 1555 2.03
SSBOND 114 CYS B 2591 CYS B 2715 1555 1555 2.03
LINK ND2 ASN A 76 C1 NAG A2801 1555 1555 1.45
LINK ND2 ASN A 484 C1 NAG C 1 1555 1555 1.46
LINK ND2 ASN A 748 C1 NAG A2802 1555 1555 1.44
LINK ND2 ASN A 947 C1 NAG A2803 1555 1555 1.44
LINK ND2 ASN A1220 C1 NAG A2804 1555 1555 1.44
LINK ND2 ASN A1349 C1 NAG A2805 1555 1555 1.45
LINK ND2 ASN A1365 C1 NAG A2806 1555 1555 1.44
LINK ND2 ASN A1716 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A1774 C1 NAG A2807 1555 1555 1.44
LINK ND2 ASN A2013 C1 NAG E 1 1555 1555 1.50
LINK ND2 ASN A2122 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN A2250 C1 NAG A2808 1555 1555 1.44
LINK ND2 ASN A2295 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN A2582 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN B 76 C1 NAG B2801 1555 1555 1.44
LINK ND2 ASN B 484 C1 NAG I 1 1555 1555 1.42
LINK ND2 ASN B 748 C1 NAG B2802 1555 1555 1.44
LINK ND2 ASN B 947 C1 NAG B2803 1555 1555 1.44
LINK ND2 ASN B1220 C1 NAG B2804 1555 1555 1.44
LINK ND2 ASN B1349 C1 NAG B2805 1555 1555 1.45
LINK ND2 ASN B1365 C1 NAG B2806 1555 1555 1.44
LINK ND2 ASN B1716 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN B1774 C1 NAG B2807 1555 1555 1.46
LINK ND2 ASN B2013 C1 NAG K 1 1555 1555 1.46
LINK ND2 ASN B2122 C1 NAG L 1 1555 1555 1.43
LINK ND2 ASN B2250 C1 NAG B2808 1555 1555 1.44
LINK ND2 ASN B2295 C1 NAG M 1 1555 1555 1.44
LINK ND2 ASN B2582 C1 NAG N 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45
LINK O3 BMA G 3 C1 MAN G 4 1555 1555 1.45
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.44
LINK O3 BMA H 3 C1 MAN H 4 1555 1555 1.44
LINK O6 BMA H 3 C1 MAN H 6 1555 1555 1.46
LINK O3 MAN H 4 C1 MAN H 5 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.43
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45
LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.43
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45
LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.45
LINK O3 BMA M 3 C1 MAN M 4 1555 1555 1.45
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45
LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.44
LINK O3 BMA N 3 C1 MAN N 4 1555 1555 1.44
LINK O6 BMA N 3 C1 MAN N 6 1555 1555 1.46
LINK O3 MAN N 4 C1 MAN N 5 1555 1555 1.44
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
TER 19205 THR A2727
TER 38410 THR B2727
MASTER 805 0 54 134 194 0 0 639122 2 970 426
END |