HEADER CELL ADHESION 16-NOV-15 5ES4
TITLE RE-REFINEMENT OF INTEGRIN ALPHAXBETA2 ECTODOMAIN IN THE CLOSED/BENT
TITLE 2 CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-X;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: UNP RESIDUES 20-1103;
COMPND 5 SYNONYM: CD11 ANTIGEN-LIKE FAMILY MEMBER C,LEU M5,LEUKOCYTE ADHESION
COMPND 6 GLYCOPROTEIN P150,95 ALPHA CHAIN,LEUKOCYTE ADHESION RECEPTOR P150,95;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTEGRIN BETA-2;
COMPND 10 CHAIN: B, D, F, H;
COMPND 11 FRAGMENT: UNP RESIDUES 23-696;
COMPND 12 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA-1/CR3/P150,95
COMPND 13 SUBUNIT BETA,COMPLEMENT RECEPTOR C3 SUBUNIT BETA;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ITGAX, CD11C;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: ITGB2, CD18, MFI7;
SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS COMPLEMENT RECEPTOR-4 ALPHAXBETA2, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SEN,T.A.SPRINGER
REVDAT 5 23-MAR-22 5ES4 1 HETSYN
REVDAT 4 29-JUL-20 5ES4 1 COMPND JRNL REMARK HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 11-MAY-16 5ES4 1 JRNL
REVDAT 2 13-APR-16 5ES4 1 JRNL
REVDAT 1 02-MAR-16 5ES4 0
JRNL AUTH M.SEN,T.A.SPRINGER
JRNL TITL LEUKOCYTE INTEGRIN ALPHA L BETA 2 HEADPIECE STRUCTURES: THE
JRNL TITL 2 ALPHA I DOMAIN, THE POCKET FOR THE INTERNAL LIGAND, AND
JRNL TITL 3 CONCERTED MOVEMENTS OF ITS LOOPS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 2940 2016
JRNL REFN ESSN 1091-6490
JRNL PMID 26936951
JRNL DOI 10.1073/PNAS.1601379113
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 174325
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.258
REMARK 3 R VALUE (WORKING SET) : 0.257
REMARK 3 FREE R VALUE : 0.307
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1819
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.5123 - 7.7502 1.00 13892 136 0.2144 0.2548
REMARK 3 2 7.7502 - 6.1553 1.00 13539 157 0.2721 0.3119
REMARK 3 3 6.1553 - 5.3783 1.00 13411 126 0.2474 0.3122
REMARK 3 4 5.3783 - 4.8870 1.00 13305 139 0.2242 0.2983
REMARK 3 5 4.8870 - 4.5370 1.00 13264 148 0.2152 0.2764
REMARK 3 6 4.5370 - 4.2697 1.00 13235 156 0.2366 0.2852
REMARK 3 7 4.2697 - 4.0560 1.00 13243 140 0.2744 0.3089
REMARK 3 8 4.0560 - 3.8795 0.99 13120 135 0.2929 0.3470
REMARK 3 9 3.8795 - 3.7302 0.99 13187 133 0.3154 0.3710
REMARK 3 10 3.7302 - 3.6015 1.00 13152 129 0.3412 0.3978
REMARK 3 11 3.6015 - 3.4889 1.00 13110 144 0.3748 0.4323
REMARK 3 12 3.4889 - 3.3892 0.99 13054 139 0.4038 0.4333
REMARK 3 13 3.3892 - 3.3000 0.98 12994 137 0.4497 0.4375
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.660
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 52369
REMARK 3 ANGLE : 1.183 71193
REMARK 3 CHIRALITY : 0.068 8134
REMARK 3 PLANARITY : 0.006 9200
REMARK 3 DIHEDRAL : 10.662 31783
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 31
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 356 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8475 19.0553 -13.0643
REMARK 3 T TENSOR
REMARK 3 T11: 1.0907 T22: 0.8894
REMARK 3 T33: 1.0174 T12: 0.1686
REMARK 3 T13: -0.1897 T23: 0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 0.5350 L22: -0.0194
REMARK 3 L33: 1.9736 L12: -0.0281
REMARK 3 L13: 0.4240 L23: -0.0136
REMARK 3 S TENSOR
REMARK 3 S11: 0.0710 S12: 0.2877 S13: 0.1536
REMARK 3 S21: 0.5312 S22: 0.0820 S23: -0.1148
REMARK 3 S31: 0.2526 S32: -0.2792 S33: -0.0007
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 357 THROUGH 639 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8387 13.1322 33.4337
REMARK 3 T TENSOR
REMARK 3 T11: 1.1710 T22: 0.9972
REMARK 3 T33: 0.9151 T12: 0.0772
REMARK 3 T13: -0.0584 T23: 0.0620
REMARK 3 L TENSOR
REMARK 3 L11: 0.0742 L22: 0.6161
REMARK 3 L33: 1.3861 L12: -0.2979
REMARK 3 L13: 0.4379 L23: -0.3662
REMARK 3 S TENSOR
REMARK 3 S11: 0.2080 S12: 0.1018 S13: -0.0881
REMARK 3 S21: -0.5670 S22: -0.3229 S23: -0.0015
REMARK 3 S31: 0.6908 S32: 0.6632 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 640 THROUGH 1080 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9024 24.3481 49.6324
REMARK 3 T TENSOR
REMARK 3 T11: 0.8846 T22: 0.6125
REMARK 3 T33: 0.9151 T12: -0.0850
REMARK 3 T13: -0.0063 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 1.8000 L22: 0.7717
REMARK 3 L33: 1.0714 L12: 0.9671
REMARK 3 L13: -1.4503 L23: -0.8556
REMARK 3 S TENSOR
REMARK 3 S11: -0.2447 S12: 0.2449 S13: -0.0668
REMARK 3 S21: -0.2238 S22: 0.1569 S23: -0.0796
REMARK 3 S31: 0.1134 S32: -0.1145 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1912 -17.4612 19.7820
REMARK 3 T TENSOR
REMARK 3 T11: 3.0612 T22: 0.7163
REMARK 3 T33: 1.4059 T12: 0.9727
REMARK 3 T13: 0.3294 T23: -0.2149
REMARK 3 L TENSOR
REMARK 3 L11: 1.2029 L22: 2.4227
REMARK 3 L33: -0.2099 L12: 0.4320
REMARK 3 L13: 0.0939 L23: 0.3704
REMARK 3 S TENSOR
REMARK 3 S11: 0.5014 S12: 0.2700 S13: -0.3386
REMARK 3 S21: -1.2947 S22: -0.2348 S23: -0.3760
REMARK 3 S31: 0.7022 S32: 0.7436 S33: -0.0334
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 214 THROUGH 360 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.7293 -10.0144 9.5107
REMARK 3 T TENSOR
REMARK 3 T11: 3.1564 T22: 1.0246
REMARK 3 T33: 0.9320 T12: 0.5109
REMARK 3 T13: 0.3806 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.8752 L22: 0.0473
REMARK 3 L33: 0.7341 L12: 1.2470
REMARK 3 L13: 1.0325 L23: 0.2268
REMARK 3 S TENSOR
REMARK 3 S11: -0.3774 S12: -0.0308 S13: -0.1027
REMARK 3 S21: -1.2514 S22: 0.3798 S23: 0.1059
REMARK 3 S31: 1.4433 S32: -0.0808 S33: 0.0589
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 361 THROUGH 431 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1412 -22.6481 33.4044
REMARK 3 T TENSOR
REMARK 3 T11: 3.0961 T22: 1.7495
REMARK 3 T33: 1.9777 T12: 0.5934
REMARK 3 T13: 0.3271 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.7494 L22: 0.3835
REMARK 3 L33: 0.1826 L12: 0.3679
REMARK 3 L13: 0.2502 L23: 0.4006
REMARK 3 S TENSOR
REMARK 3 S11: 0.4171 S12: 0.1674 S13: -0.6883
REMARK 3 S21: -0.1816 S22: 0.2605 S23: -0.2681
REMARK 3 S31: 1.2230 S32: 0.1080 S33: 0.0001
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 432 THROUGH 482 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3511 -20.8730 75.9306
REMARK 3 T TENSOR
REMARK 3 T11: 2.4039 T22: 1.0923
REMARK 3 T33: 1.5191 T12: 0.0771
REMARK 3 T13: 0.0755 T23: 0.2545
REMARK 3 L TENSOR
REMARK 3 L11: 0.2008 L22: 0.0402
REMARK 3 L33: -0.0507 L12: -0.0336
REMARK 3 L13: -0.0496 L23: 0.0939
REMARK 3 S TENSOR
REMARK 3 S11: -0.1815 S12: -0.9226 S13: -0.0523
REMARK 3 S21: 1.2020 S22: 0.1714 S23: -0.6247
REMARK 3 S31: 0.4945 S32: 0.2607 S33: -0.0067
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 483 THROUGH 674 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5625 8.5697 31.4036
REMARK 3 T TENSOR
REMARK 3 T11: 1.6011 T22: 1.3644
REMARK 3 T33: 1.2366 T12: 0.1252
REMARK 3 T13: 0.1033 T23: 0.1948
REMARK 3 L TENSOR
REMARK 3 L11: 0.0168 L22: 0.3744
REMARK 3 L33: 1.0413 L12: 0.3339
REMARK 3 L13: -0.2293 L23: 0.0267
REMARK 3 S TENSOR
REMARK 3 S11: 0.1618 S12: 0.0115 S13: -0.0533
REMARK 3 S21: -0.1410 S22: 0.0330 S23: -0.0297
REMARK 3 S31: -0.0560 S32: 0.3744 S33: 0.0001
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 691 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.2543 52.2123 103.5674
REMARK 3 T TENSOR
REMARK 3 T11: 1.0714 T22: 1.6971
REMARK 3 T33: 1.0304 T12: -0.2065
REMARK 3 T13: -0.3427 T23: 0.1277
REMARK 3 L TENSOR
REMARK 3 L11: 0.2791 L22: -0.0443
REMARK 3 L33: 2.1045 L12: 0.0177
REMARK 3 L13: 0.1562 L23: 0.3331
REMARK 3 S TENSOR
REMARK 3 S11: 0.1392 S12: -0.5806 S13: -0.0572
REMARK 3 S21: 0.3325 S22: 0.0623 S23: -0.2993
REMARK 3 S31: 0.4669 S32: -0.4254 S33: 0.0013
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 692 THROUGH 1080 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6626 26.9297 84.6488
REMARK 3 T TENSOR
REMARK 3 T11: 0.9046 T22: 1.1136
REMARK 3 T33: 0.9701 T12: -0.1400
REMARK 3 T13: -0.0608 T23: 0.1525
REMARK 3 L TENSOR
REMARK 3 L11: 1.2728 L22: 1.1934
REMARK 3 L33: -0.7676 L12: 1.2282
REMARK 3 L13: -0.6990 L23: -0.4859
REMARK 3 S TENSOR
REMARK 3 S11: 0.2280 S12: -0.7463 S13: -0.2308
REMARK 3 S21: 0.4537 S22: -0.4739 S23: -0.2659
REMARK 3 S31: -0.1466 S32: 0.4522 S33: -0.0001
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.0168 19.1363 84.0506
REMARK 3 T TENSOR
REMARK 3 T11: 2.2710 T22: 1.5064
REMARK 3 T33: 2.5413 T12: 0.5055
REMARK 3 T13: -0.7395 T23: 0.1006
REMARK 3 L TENSOR
REMARK 3 L11: 1.8622 L22: 0.8054
REMARK 3 L33: 0.2355 L12: -0.2240
REMARK 3 L13: 0.8319 L23: 0.3244
REMARK 3 S TENSOR
REMARK 3 S11: 0.0515 S12: -0.4489 S13: -0.3119
REMARK 3 S21: 0.8712 S22: 0.2873 S23: -1.9268
REMARK 3 S31: 0.5190 S32: 0.2002 S33: 0.4020
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 115 THROUGH 464 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.3557 28.0030 113.6542
REMARK 3 T TENSOR
REMARK 3 T11: 2.6140 T22: 2.4190
REMARK 3 T33: 1.9485 T12: 0.2874
REMARK 3 T13: -0.7390 T23: 0.2978
REMARK 3 L TENSOR
REMARK 3 L11: 0.5375 L22: 0.5466
REMARK 3 L33: 0.8805 L12: 0.4454
REMARK 3 L13: 0.1902 L23: 0.8263
REMARK 3 S TENSOR
REMARK 3 S11: 0.2875 S12: -0.5803 S13: -0.1037
REMARK 3 S21: 0.9077 S22: 0.1172 S23: -0.6085
REMARK 3 S31: 0.5389 S32: -0.0545 S33: -0.0001
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 465 THROUGH 552 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1466 37.3821 65.5840
REMARK 3 T TENSOR
REMARK 3 T11: 1.3118 T22: 1.8725
REMARK 3 T33: 1.6731 T12: -0.1358
REMARK 3 T13: 0.0436 T23: 0.3005
REMARK 3 L TENSOR
REMARK 3 L11: 0.0651 L22: 0.3716
REMARK 3 L33: 0.0550 L12: 0.3442
REMARK 3 L13: 0.1643 L23: 0.2556
REMARK 3 S TENSOR
REMARK 3 S11: 0.2933 S12: -1.0831 S13: -1.3964
REMARK 3 S21: 0.6804 S22: -0.4022 S23: 0.3491
REMARK 3 S31: -0.3445 S32: -0.2646 S33: 0.0001
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 553 THROUGH 674 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7896 10.3725 111.4364
REMARK 3 T TENSOR
REMARK 3 T11: 2.4834 T22: 2.3111
REMARK 3 T33: 1.8081 T12: -0.2761
REMARK 3 T13: -0.3243 T23: 0.3956
REMARK 3 L TENSOR
REMARK 3 L11: 0.9561 L22: 0.1425
REMARK 3 L33: 0.6229 L12: -0.3400
REMARK 3 L13: 0.4030 L23: 0.1446
REMARK 3 S TENSOR
REMARK 3 S11: 0.0236 S12: 0.7308 S13: -0.6598
REMARK 3 S21: -0.0915 S22: 0.9432 S23: -0.0275
REMARK 3 S31: 1.2925 S32: -1.8916 S33: 0.0002
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 662 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.9778 33.6309 114.0189
REMARK 3 T TENSOR
REMARK 3 T11: 0.8609 T22: 1.4674
REMARK 3 T33: 0.8845 T12: -0.0844
REMARK 3 T13: -0.0870 T23: 0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 1.6397 L22: 0.3888
REMARK 3 L33: 3.2576 L12: 0.2250
REMARK 3 L13: 0.9517 L23: 1.1692
REMARK 3 S TENSOR
REMARK 3 S11: -0.0589 S12: -0.9337 S13: 0.0294
REMARK 3 S21: 0.3804 S22: -0.0145 S23: 0.0239
REMARK 3 S31: 0.4358 S32: -0.2393 S33: -0.0003
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 663 THROUGH 1080 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.2323 57.0371 87.2665
REMARK 3 T TENSOR
REMARK 3 T11: 0.7691 T22: 0.9888
REMARK 3 T33: 0.9558 T12: -0.1658
REMARK 3 T13: -0.1993 T23: -0.0565
REMARK 3 L TENSOR
REMARK 3 L11: 0.2492 L22: 0.2142
REMARK 3 L33: 0.3393 L12: 0.2898
REMARK 3 L13: -0.1391 L23: 0.1106
REMARK 3 S TENSOR
REMARK 3 S11: 0.1475 S12: -0.2997 S13: -0.0202
REMARK 3 S21: 0.2743 S22: -0.1453 S23: 0.0107
REMARK 3 S31: -0.0142 S32: 0.0843 S33: 0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): -68.3457 60.3004 109.9680
REMARK 3 T TENSOR
REMARK 3 T11: 1.5041 T22: 1.8722
REMARK 3 T33: 1.6818 T12: 0.6585
REMARK 3 T13: 0.0796 T23: -0.5674
REMARK 3 L TENSOR
REMARK 3 L11: 1.3326 L22: 1.8915
REMARK 3 L33: 0.5562 L12: -0.2167
REMARK 3 L13: -0.2469 L23: 0.8752
REMARK 3 S TENSOR
REMARK 3 S11: -0.0904 S12: -0.8106 S13: 0.0466
REMARK 3 S21: 0.0497 S22: 0.0363 S23: 0.8037
REMARK 3 S31: 0.1534 S32: -1.1558 S33: 0.0201
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 139 THROUGH 329 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.6236 47.4628 142.2594
REMARK 3 T TENSOR
REMARK 3 T11: 1.4349 T22: 3.1606
REMARK 3 T33: 1.1526 T12: 0.1980
REMARK 3 T13: -0.1088 T23: -0.4680
REMARK 3 L TENSOR
REMARK 3 L11: 0.1143 L22: 1.4565
REMARK 3 L33: -0.0402 L12: 0.2355
REMARK 3 L13: -0.2830 L23: -0.5176
REMARK 3 S TENSOR
REMARK 3 S11: -0.1709 S12: -1.1006 S13: -0.0944
REMARK 3 S21: 0.1576 S22: -0.0144 S23: -0.0098
REMARK 3 S31: -0.0501 S32: -0.3321 S33: 0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 330 THROUGH 482 )
REMARK 3 ORIGIN FOR THE GROUP (A): -68.2545 56.4141 100.2052
REMARK 3 T TENSOR
REMARK 3 T11: 0.7418 T22: 1.6206
REMARK 3 T33: 1.1040 T12: 0.0958
REMARK 3 T13: -0.1781 T23: -0.3731
REMARK 3 L TENSOR
REMARK 3 L11: 1.0604 L22: 1.4876
REMARK 3 L33: 0.4418 L12: -1.4932
REMARK 3 L13: -0.8512 L23: 0.6118
REMARK 3 S TENSOR
REMARK 3 S11: -0.2156 S12: -0.2259 S13: 0.2636
REMARK 3 S21: 0.0659 S22: 0.1740 S23: -0.0708
REMARK 3 S31: -1.3949 S32: -0.3270 S33: 0.0246
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 483 THROUGH 674 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.6508 66.5325 106.0644
REMARK 3 T TENSOR
REMARK 3 T11: 1.1586 T22: 1.4360
REMARK 3 T33: 1.1849 T12: -0.1830
REMARK 3 T13: -0.0556 T23: -0.3506
REMARK 3 L TENSOR
REMARK 3 L11: 1.6607 L22: 0.1483
REMARK 3 L33: -0.0455 L12: 0.9404
REMARK 3 L13: -0.2852 L23: -0.3347
REMARK 3 S TENSOR
REMARK 3 S11: 0.2429 S12: -0.5480 S13: 0.3130
REMARK 3 S21: 0.2832 S22: -0.2751 S23: 0.2845
REMARK 3 S31: -0.1578 S32: -0.4788 S33: -0.0000
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1 THROUGH 595 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5575 71.4845 16.2816
REMARK 3 T TENSOR
REMARK 3 T11: 1.4847 T22: 0.7402
REMARK 3 T33: 1.0635 T12: 0.1494
REMARK 3 T13: -0.1690 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 1.6784 L22: 1.0807
REMARK 3 L33: 1.4591 L12: 0.3457
REMARK 3 L13: 0.4159 L23: 0.9257
REMARK 3 S TENSOR
REMARK 3 S11: 0.0963 S12: 0.2738 S13: 0.0629
REMARK 3 S21: -1.0693 S22: -0.1938 S23: 0.1216
REMARK 3 S31: -0.6160 S32: 0.2550 S33: -0.0000
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 596 THROUGH 805 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0874 74.9653 66.7027
REMARK 3 T TENSOR
REMARK 3 T11: 0.6675 T22: 0.5679
REMARK 3 T33: 0.8916 T12: -0.0137
REMARK 3 T13: -0.0620 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 1.9784 L22: 1.0632
REMARK 3 L33: 0.3539 L12: 0.2474
REMARK 3 L13: 1.5811 L23: 1.0393
REMARK 3 S TENSOR
REMARK 3 S11: 0.0148 S12: -0.0485 S13: 0.1488
REMARK 3 S21: 0.0034 S22: -0.1111 S23: -0.0742
REMARK 3 S31: -0.0987 S32: -0.4240 S33: 0.0002
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 806 THROUGH 1080 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.0730 53.8071 44.2472
REMARK 3 T TENSOR
REMARK 3 T11: 0.7835 T22: 0.9442
REMARK 3 T33: 1.0062 T12: -0.0169
REMARK 3 T13: -0.1188 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.9706 L22: 0.7727
REMARK 3 L33: 2.3246 L12: 0.5957
REMARK 3 L13: 0.5162 L23: 1.4744
REMARK 3 S TENSOR
REMARK 3 S11: -0.1092 S12: 0.4143 S13: -0.0448
REMARK 3 S21: -0.2586 S22: 0.1849 S23: -0.1019
REMARK 3 S31: -0.2487 S32: -0.0071 S33: -0.0000
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5760 108.4226 64.3220
REMARK 3 T TENSOR
REMARK 3 T11: 2.2734 T22: 1.3884
REMARK 3 T33: 1.8285 T12: 0.2301
REMARK 3 T13: -0.3036 T23: -0.2511
REMARK 3 L TENSOR
REMARK 3 L11: 0.1702 L22: 0.3981
REMARK 3 L33: 0.1983 L12: 0.0333
REMARK 3 L13: 0.1681 L23: -0.2580
REMARK 3 S TENSOR
REMARK 3 S11: 0.2828 S12: -0.4666 S13: 0.3192
REMARK 3 S21: -0.4477 S22: -0.0498 S23: 0.2422
REMARK 3 S31: 0.1035 S32: -0.2548 S33: -0.0000
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 56 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9773 104.0076 4.3038
REMARK 3 T TENSOR
REMARK 3 T11: 3.0905 T22: 1.4228
REMARK 3 T33: 1.8870 T12: 0.5616
REMARK 3 T13: -0.5342 T23: 0.1643
REMARK 3 L TENSOR
REMARK 3 L11: 1.2741 L22: 0.8021
REMARK 3 L33: 0.5041 L12: -0.0348
REMARK 3 L13: -1.1657 L23: -0.9343
REMARK 3 S TENSOR
REMARK 3 S11: 0.2330 S12: 0.7484 S13: 0.2900
REMARK 3 S21: -0.8764 S22: 0.2901 S23: 0.3229
REMARK 3 S31: 0.1891 S32: 0.0376 S33: 0.0001
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 214 THROUGH 363 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7739 98.1485 9.1884
REMARK 3 T TENSOR
REMARK 3 T11: 3.2111 T22: 1.3136
REMARK 3 T33: 1.3701 T12: 0.5228
REMARK 3 T13: -1.0467 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.1534 L22: 0.0345
REMARK 3 L33: 0.3869 L12: 0.4307
REMARK 3 L13: -0.4171 L23: 0.2500
REMARK 3 S TENSOR
REMARK 3 S11: -0.3587 S12: -0.2886 S13: -0.2148
REMARK 3 S21: -2.5386 S22: -0.0111 S23: 0.0209
REMARK 3 S31: -1.4447 S32: -0.1086 S33: 0.0058
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 364 THROUGH 413 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.3730 107.8770 29.2268
REMARK 3 T TENSOR
REMARK 3 T11: 2.6134 T22: 1.7754
REMARK 3 T33: 2.5923 T12: 0.8671
REMARK 3 T13: -0.3576 T23: -0.4484
REMARK 3 L TENSOR
REMARK 3 L11: 0.4494 L22: 0.1504
REMARK 3 L33: 0.4770 L12: 0.1389
REMARK 3 L13: -0.1509 L23: -0.3885
REMARK 3 S TENSOR
REMARK 3 S11: -0.1498 S12: -1.2560 S13: -0.0922
REMARK 3 S21: 1.1145 S22: 0.0411 S23: 1.2840
REMARK 3 S31: -2.2460 S32: 0.4997 S33: -0.0205
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 414 THROUGH 452 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8792 116.5890 59.0051
REMARK 3 T TENSOR
REMARK 3 T11: 3.1130 T22: 1.4163
REMARK 3 T33: 2.3566 T12: -0.3613
REMARK 3 T13: -0.4336 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 0.0949 L22: 0.2749
REMARK 3 L33: 0.0503 L12: 0.2947
REMARK 3 L13: -0.0151 L23: -0.1671
REMARK 3 S TENSOR
REMARK 3 S11: -0.1503 S12: 0.0608 S13: 0.5736
REMARK 3 S21: -0.1630 S22: -0.2782 S23: -0.5553
REMARK 3 S31: -1.0971 S32: -0.5152 S33: 0.0002
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 453 THROUGH 497 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6654 99.4284 77.1453
REMARK 3 T TENSOR
REMARK 3 T11: 1.9555 T22: 1.0582
REMARK 3 T33: 1.0899 T12: -0.3163
REMARK 3 T13: -0.0717 T23: -0.2419
REMARK 3 L TENSOR
REMARK 3 L11: 0.7893 L22: 0.3130
REMARK 3 L33: 0.1212 L12: -0.4264
REMARK 3 L13: 0.1760 L23: -0.2825
REMARK 3 S TENSOR
REMARK 3 S11: -0.0216 S12: -0.4311 S13: -0.7657
REMARK 3 S21: 0.2648 S22: 0.5813 S23: -0.2499
REMARK 3 S31: -1.3844 S32: 0.2747 S33: 0.0390
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 498 THROUGH 637 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.3029 79.2381 37.6724
REMARK 3 T TENSOR
REMARK 3 T11: 1.4919 T22: 0.9855
REMARK 3 T33: 1.3437 T12: -0.0186
REMARK 3 T13: -0.2150 T23: 0.0377
REMARK 3 L TENSOR
REMARK 3 L11: 0.6602 L22: 0.1200
REMARK 3 L33: 0.6020 L12: -0.1488
REMARK 3 L13: -0.4682 L23: -0.1256
REMARK 3 S TENSOR
REMARK 3 S11: 0.3969 S12: 0.3452 S13: -0.0067
REMARK 3 S21: 0.4741 S22: -0.0094 S23: -0.0542
REMARK 3 S31: 0.4028 S32: -0.3233 S33: 0.0000
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 638 THROUGH 674 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.7688 63.5464 15.9661
REMARK 3 T TENSOR
REMARK 3 T11: 1.5622 T22: 1.0187
REMARK 3 T33: 1.3418 T12: 0.0051
REMARK 3 T13: -0.1839 T23: -0.0572
REMARK 3 L TENSOR
REMARK 3 L11: -0.0784 L22: 0.0976
REMARK 3 L33: 0.1637 L12: -0.0442
REMARK 3 L13: -0.0373 L23: -0.1413
REMARK 3 S TENSOR
REMARK 3 S11: 0.3058 S12: 0.9430 S13: -0.2164
REMARK 3 S21: 0.3379 S22: 0.6075 S23: -0.2494
REMARK 3 S31: -0.0703 S32: 0.6374 S33: -0.0002
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5ES4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215429.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-06
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 : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97926
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 198644
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.20500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.55M TRI-SODIUM CITRATE, 0.1M
REMARK 280 IMIDAZOLE, PH 6.5, EVAPORATION, TEMPERATURE 277K, VAPOR
REMARK 280 DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 66.01500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 268.32500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 81.74000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 268.32500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.01500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 81.74000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 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 APPLY THE FOLLOWING TO CHAINS: A, B, I, J, K, L, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, N, O, P, Q
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 APPLY THE FOLLOWING TO CHAINS: E, F, R, S, T, U
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 APPLY THE FOLLOWING TO CHAINS: G, H, V, W, X, Y
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 TYR A 1081
REMARK 465 LYS A 1082
REMARK 465 VAL A 1083
REMARK 465 HIS A 1084
REMARK 465 GLY A 1085
REMARK 465 CYS A 1086
REMARK 465 GLY A 1087
REMARK 465 GLY A 1088
REMARK 465 LEU A 1089
REMARK 465 GLU A 1090
REMARK 465 ASN A 1091
REMARK 465 LEU A 1092
REMARK 465 TYR A 1093
REMARK 465 PHE A 1094
REMARK 465 GLN A 1095
REMARK 465 GLY A 1096
REMARK 465 GLY A 1097
REMARK 465 GLU A 1098
REMARK 465 ASN A 1099
REMARK 465 ALA A 1100
REMARK 465 GLN A 1101
REMARK 465 CYS A 1102
REMARK 465 GLU A 1103
REMARK 465 LYS A 1104
REMARK 465 GLU A 1105
REMARK 465 LEU A 1106
REMARK 465 GLN A 1107
REMARK 465 ALA A 1108
REMARK 465 LEU A 1109
REMARK 465 GLU A 1110
REMARK 465 LYS A 1111
REMARK 465 GLU A 1112
REMARK 465 ASN A 1113
REMARK 465 ALA A 1114
REMARK 465 GLN A 1115
REMARK 465 LEU A 1116
REMARK 465 GLU A 1117
REMARK 465 TRP A 1118
REMARK 465 GLU A 1119
REMARK 465 LEU A 1120
REMARK 465 GLN A 1121
REMARK 465 ALA A 1122
REMARK 465 LEU A 1123
REMARK 465 GLU A 1124
REMARK 465 LYS A 1125
REMARK 465 GLU A 1126
REMARK 465 LEU A 1127
REMARK 465 ALA A 1128
REMARK 465 GLN A 1129
REMARK 465 TRP A 1130
REMARK 465 SER A 1131
REMARK 465 HIS A 1132
REMARK 465 PRO A 1133
REMARK 465 GLN A 1134
REMARK 465 PHE A 1135
REMARK 465 GLU A 1136
REMARK 465 LYS A 1137
REMARK 465 ASP B 675
REMARK 465 GLY B 676
REMARK 465 CYS B 677
REMARK 465 GLY B 678
REMARK 465 LEU B 679
REMARK 465 GLU B 680
REMARK 465 ASN B 681
REMARK 465 LEU B 682
REMARK 465 TYR B 683
REMARK 465 PHE B 684
REMARK 465 GLN B 685
REMARK 465 GLY B 686
REMARK 465 GLY B 687
REMARK 465 LYS B 688
REMARK 465 ASN B 689
REMARK 465 ALA B 690
REMARK 465 GLN B 691
REMARK 465 CYS B 692
REMARK 465 LYS B 693
REMARK 465 LYS B 694
REMARK 465 LYS B 695
REMARK 465 LEU B 696
REMARK 465 GLN B 697
REMARK 465 ALA B 698
REMARK 465 LEU B 699
REMARK 465 LYS B 700
REMARK 465 LYS B 701
REMARK 465 LYS B 702
REMARK 465 ASN B 703
REMARK 465 ALA B 704
REMARK 465 GLN B 705
REMARK 465 LEU B 706
REMARK 465 LYS B 707
REMARK 465 TRP B 708
REMARK 465 LYS B 709
REMARK 465 LEU B 710
REMARK 465 GLN B 711
REMARK 465 ALA B 712
REMARK 465 LEU B 713
REMARK 465 LYS B 714
REMARK 465 LYS B 715
REMARK 465 LYS B 716
REMARK 465 LEU B 717
REMARK 465 ALA B 718
REMARK 465 GLN B 719
REMARK 465 GLY B 720
REMARK 465 GLY B 721
REMARK 465 HIS B 722
REMARK 465 HIS B 723
REMARK 465 HIS B 724
REMARK 465 HIS B 725
REMARK 465 HIS B 726
REMARK 465 HIS B 727
REMARK 465 GLU C 130
REMARK 465 GLN C 131
REMARK 465 ASP C 132
REMARK 465 ILE C 133
REMARK 465 VAL C 134
REMARK 465 PHE C 135
REMARK 465 LEU C 136
REMARK 465 ILE C 137
REMARK 465 ASP C 138
REMARK 465 GLY C 139
REMARK 465 SER C 140
REMARK 465 GLY C 141
REMARK 465 SER C 142
REMARK 465 ILE C 143
REMARK 465 SER C 144
REMARK 465 SER C 145
REMARK 465 ARG C 146
REMARK 465 ASN C 147
REMARK 465 PHE C 148
REMARK 465 ALA C 149
REMARK 465 THR C 150
REMARK 465 MET C 151
REMARK 465 MET C 152
REMARK 465 ASN C 153
REMARK 465 PHE C 154
REMARK 465 VAL C 155
REMARK 465 ARG C 156
REMARK 465 ALA C 157
REMARK 465 VAL C 158
REMARK 465 ILE C 159
REMARK 465 SER C 160
REMARK 465 GLN C 161
REMARK 465 PHE C 162
REMARK 465 GLN C 163
REMARK 465 ARG C 164
REMARK 465 PRO C 165
REMARK 465 SER C 166
REMARK 465 THR C 167
REMARK 465 GLN C 168
REMARK 465 PHE C 169
REMARK 465 SER C 170
REMARK 465 LEU C 171
REMARK 465 MET C 172
REMARK 465 GLN C 173
REMARK 465 PHE C 174
REMARK 465 SER C 175
REMARK 465 ASN C 176
REMARK 465 LYS C 177
REMARK 465 PHE C 178
REMARK 465 GLN C 179
REMARK 465 THR C 180
REMARK 465 HIS C 181
REMARK 465 PHE C 182
REMARK 465 THR C 183
REMARK 465 PHE C 184
REMARK 465 GLU C 185
REMARK 465 GLU C 186
REMARK 465 PHE C 187
REMARK 465 ARG C 188
REMARK 465 ARG C 189
REMARK 465 SER C 190
REMARK 465 SER C 191
REMARK 465 ASN C 192
REMARK 465 PRO C 193
REMARK 465 LEU C 194
REMARK 465 SER C 195
REMARK 465 LEU C 196
REMARK 465 LEU C 197
REMARK 465 ALA C 198
REMARK 465 SER C 199
REMARK 465 VAL C 200
REMARK 465 HIS C 201
REMARK 465 GLN C 202
REMARK 465 LEU C 203
REMARK 465 GLN C 204
REMARK 465 GLY C 205
REMARK 465 PHE C 206
REMARK 465 THR C 207
REMARK 465 TYR C 208
REMARK 465 THR C 209
REMARK 465 ALA C 210
REMARK 465 THR C 211
REMARK 465 ALA C 212
REMARK 465 ILE C 213
REMARK 465 GLN C 214
REMARK 465 ASN C 215
REMARK 465 VAL C 216
REMARK 465 VAL C 217
REMARK 465 HIS C 218
REMARK 465 ARG C 219
REMARK 465 LEU C 220
REMARK 465 PHE C 221
REMARK 465 HIS C 222
REMARK 465 ALA C 223
REMARK 465 SER C 224
REMARK 465 TYR C 225
REMARK 465 GLY C 226
REMARK 465 ALA C 227
REMARK 465 ARG C 228
REMARK 465 ARG C 229
REMARK 465 ASP C 230
REMARK 465 ALA C 231
REMARK 465 ALA C 232
REMARK 465 LYS C 233
REMARK 465 ILE C 234
REMARK 465 LEU C 235
REMARK 465 ILE C 236
REMARK 465 VAL C 237
REMARK 465 ILE C 238
REMARK 465 THR C 239
REMARK 465 ASP C 240
REMARK 465 GLY C 241
REMARK 465 LYS C 242
REMARK 465 LYS C 243
REMARK 465 GLU C 244
REMARK 465 GLY C 245
REMARK 465 ASP C 246
REMARK 465 SER C 247
REMARK 465 LEU C 248
REMARK 465 ASP C 249
REMARK 465 TYR C 250
REMARK 465 LYS C 251
REMARK 465 ASP C 252
REMARK 465 VAL C 253
REMARK 465 ILE C 254
REMARK 465 PRO C 255
REMARK 465 MET C 256
REMARK 465 ALA C 257
REMARK 465 ASP C 258
REMARK 465 ALA C 259
REMARK 465 ALA C 260
REMARK 465 GLY C 261
REMARK 465 ILE C 262
REMARK 465 ILE C 263
REMARK 465 ARG C 264
REMARK 465 TYR C 265
REMARK 465 ALA C 266
REMARK 465 ILE C 267
REMARK 465 GLY C 268
REMARK 465 VAL C 269
REMARK 465 GLY C 270
REMARK 465 LEU C 271
REMARK 465 ALA C 272
REMARK 465 PHE C 273
REMARK 465 GLN C 274
REMARK 465 ASN C 275
REMARK 465 ARG C 276
REMARK 465 ASN C 277
REMARK 465 SER C 278
REMARK 465 TRP C 279
REMARK 465 LYS C 280
REMARK 465 GLU C 281
REMARK 465 LEU C 282
REMARK 465 ASN C 283
REMARK 465 ASP C 284
REMARK 465 ILE C 285
REMARK 465 ALA C 286
REMARK 465 SER C 287
REMARK 465 LYS C 288
REMARK 465 PRO C 289
REMARK 465 SER C 290
REMARK 465 GLN C 291
REMARK 465 GLU C 292
REMARK 465 HIS C 293
REMARK 465 ILE C 294
REMARK 465 PHE C 295
REMARK 465 LYS C 296
REMARK 465 VAL C 297
REMARK 465 GLU C 298
REMARK 465 ASP C 299
REMARK 465 PHE C 300
REMARK 465 ASP C 301
REMARK 465 ALA C 302
REMARK 465 LEU C 303
REMARK 465 LYS C 304
REMARK 465 ASP C 305
REMARK 465 ILE C 306
REMARK 465 GLN C 307
REMARK 465 ASN C 308
REMARK 465 GLN C 309
REMARK 465 LEU C 310
REMARK 465 LYS C 311
REMARK 465 GLU C 312
REMARK 465 LYS C 313
REMARK 465 ILE C 314
REMARK 465 PHE C 315
REMARK 465 ALA C 316
REMARK 465 ILE C 317
REMARK 465 GLU C 318
REMARK 465 GLY C 319
REMARK 465 THR C 320
REMARK 465 GLU C 321
REMARK 465 THR C 322
REMARK 465 THR C 323
REMARK 465 SER C 324
REMARK 465 SER C 325
REMARK 465 TYR C 1081
REMARK 465 LYS C 1082
REMARK 465 VAL C 1083
REMARK 465 HIS C 1084
REMARK 465 GLY C 1085
REMARK 465 CYS C 1086
REMARK 465 GLY C 1087
REMARK 465 GLY C 1088
REMARK 465 LEU C 1089
REMARK 465 GLU C 1090
REMARK 465 ASN C 1091
REMARK 465 LEU C 1092
REMARK 465 TYR C 1093
REMARK 465 PHE C 1094
REMARK 465 GLN C 1095
REMARK 465 GLY C 1096
REMARK 465 GLY C 1097
REMARK 465 GLU C 1098
REMARK 465 ASN C 1099
REMARK 465 ALA C 1100
REMARK 465 GLN C 1101
REMARK 465 CYS C 1102
REMARK 465 GLU C 1103
REMARK 465 LYS C 1104
REMARK 465 GLU C 1105
REMARK 465 LEU C 1106
REMARK 465 GLN C 1107
REMARK 465 ALA C 1108
REMARK 465 LEU C 1109
REMARK 465 GLU C 1110
REMARK 465 LYS C 1111
REMARK 465 GLU C 1112
REMARK 465 ASN C 1113
REMARK 465 ALA C 1114
REMARK 465 GLN C 1115
REMARK 465 LEU C 1116
REMARK 465 GLU C 1117
REMARK 465 TRP C 1118
REMARK 465 GLU C 1119
REMARK 465 LEU C 1120
REMARK 465 GLN C 1121
REMARK 465 ALA C 1122
REMARK 465 LEU C 1123
REMARK 465 GLU C 1124
REMARK 465 LYS C 1125
REMARK 465 GLU C 1126
REMARK 465 LEU C 1127
REMARK 465 ALA C 1128
REMARK 465 GLN C 1129
REMARK 465 TRP C 1130
REMARK 465 SER C 1131
REMARK 465 HIS C 1132
REMARK 465 PRO C 1133
REMARK 465 GLN C 1134
REMARK 465 PHE C 1135
REMARK 465 GLU C 1136
REMARK 465 LYS C 1137
REMARK 465 ASP D 675
REMARK 465 GLY D 676
REMARK 465 CYS D 677
REMARK 465 GLY D 678
REMARK 465 LEU D 679
REMARK 465 GLU D 680
REMARK 465 ASN D 681
REMARK 465 LEU D 682
REMARK 465 TYR D 683
REMARK 465 PHE D 684
REMARK 465 GLN D 685
REMARK 465 GLY D 686
REMARK 465 GLY D 687
REMARK 465 LYS D 688
REMARK 465 ASN D 689
REMARK 465 ALA D 690
REMARK 465 GLN D 691
REMARK 465 CYS D 692
REMARK 465 LYS D 693
REMARK 465 LYS D 694
REMARK 465 LYS D 695
REMARK 465 LEU D 696
REMARK 465 GLN D 697
REMARK 465 ALA D 698
REMARK 465 LEU D 699
REMARK 465 LYS D 700
REMARK 465 LYS D 701
REMARK 465 LYS D 702
REMARK 465 ASN D 703
REMARK 465 ALA D 704
REMARK 465 GLN D 705
REMARK 465 LEU D 706
REMARK 465 LYS D 707
REMARK 465 TRP D 708
REMARK 465 LYS D 709
REMARK 465 LEU D 710
REMARK 465 GLN D 711
REMARK 465 ALA D 712
REMARK 465 LEU D 713
REMARK 465 LYS D 714
REMARK 465 LYS D 715
REMARK 465 LYS D 716
REMARK 465 LEU D 717
REMARK 465 ALA D 718
REMARK 465 GLN D 719
REMARK 465 GLY D 720
REMARK 465 GLY D 721
REMARK 465 HIS D 722
REMARK 465 HIS D 723
REMARK 465 HIS D 724
REMARK 465 HIS D 725
REMARK 465 HIS D 726
REMARK 465 HIS D 727
REMARK 465 GLU E 130
REMARK 465 GLN E 131
REMARK 465 ASP E 132
REMARK 465 ILE E 133
REMARK 465 VAL E 134
REMARK 465 PHE E 135
REMARK 465 LEU E 136
REMARK 465 ILE E 137
REMARK 465 ASP E 138
REMARK 465 GLY E 139
REMARK 465 SER E 140
REMARK 465 GLY E 141
REMARK 465 SER E 142
REMARK 465 ILE E 143
REMARK 465 SER E 144
REMARK 465 SER E 145
REMARK 465 ARG E 146
REMARK 465 ASN E 147
REMARK 465 PHE E 148
REMARK 465 ALA E 149
REMARK 465 THR E 150
REMARK 465 MET E 151
REMARK 465 MET E 152
REMARK 465 ASN E 153
REMARK 465 PHE E 154
REMARK 465 VAL E 155
REMARK 465 ARG E 156
REMARK 465 ALA E 157
REMARK 465 VAL E 158
REMARK 465 ILE E 159
REMARK 465 SER E 160
REMARK 465 GLN E 161
REMARK 465 PHE E 162
REMARK 465 GLN E 163
REMARK 465 ARG E 164
REMARK 465 PRO E 165
REMARK 465 SER E 166
REMARK 465 THR E 167
REMARK 465 GLN E 168
REMARK 465 PHE E 169
REMARK 465 SER E 170
REMARK 465 LEU E 171
REMARK 465 MET E 172
REMARK 465 GLN E 173
REMARK 465 PHE E 174
REMARK 465 SER E 175
REMARK 465 ASN E 176
REMARK 465 LYS E 177
REMARK 465 PHE E 178
REMARK 465 GLN E 179
REMARK 465 THR E 180
REMARK 465 HIS E 181
REMARK 465 PHE E 182
REMARK 465 THR E 183
REMARK 465 PHE E 184
REMARK 465 GLU E 185
REMARK 465 GLU E 186
REMARK 465 PHE E 187
REMARK 465 ARG E 188
REMARK 465 ARG E 189
REMARK 465 SER E 190
REMARK 465 SER E 191
REMARK 465 ASN E 192
REMARK 465 PRO E 193
REMARK 465 LEU E 194
REMARK 465 SER E 195
REMARK 465 LEU E 196
REMARK 465 LEU E 197
REMARK 465 ALA E 198
REMARK 465 SER E 199
REMARK 465 VAL E 200
REMARK 465 HIS E 201
REMARK 465 GLN E 202
REMARK 465 LEU E 203
REMARK 465 GLN E 204
REMARK 465 GLY E 205
REMARK 465 PHE E 206
REMARK 465 THR E 207
REMARK 465 TYR E 208
REMARK 465 THR E 209
REMARK 465 ALA E 210
REMARK 465 THR E 211
REMARK 465 ALA E 212
REMARK 465 ILE E 213
REMARK 465 GLN E 214
REMARK 465 ASN E 215
REMARK 465 VAL E 216
REMARK 465 VAL E 217
REMARK 465 HIS E 218
REMARK 465 ARG E 219
REMARK 465 LEU E 220
REMARK 465 PHE E 221
REMARK 465 HIS E 222
REMARK 465 ALA E 223
REMARK 465 SER E 224
REMARK 465 TYR E 225
REMARK 465 GLY E 226
REMARK 465 ALA E 227
REMARK 465 ARG E 228
REMARK 465 ARG E 229
REMARK 465 ASP E 230
REMARK 465 ALA E 231
REMARK 465 ALA E 232
REMARK 465 LYS E 233
REMARK 465 ILE E 234
REMARK 465 LEU E 235
REMARK 465 ILE E 236
REMARK 465 VAL E 237
REMARK 465 ILE E 238
REMARK 465 THR E 239
REMARK 465 ASP E 240
REMARK 465 GLY E 241
REMARK 465 LYS E 242
REMARK 465 LYS E 243
REMARK 465 GLU E 244
REMARK 465 GLY E 245
REMARK 465 ASP E 246
REMARK 465 SER E 247
REMARK 465 LEU E 248
REMARK 465 ASP E 249
REMARK 465 TYR E 250
REMARK 465 LYS E 251
REMARK 465 ASP E 252
REMARK 465 VAL E 253
REMARK 465 ILE E 254
REMARK 465 PRO E 255
REMARK 465 MET E 256
REMARK 465 ALA E 257
REMARK 465 ASP E 258
REMARK 465 ALA E 259
REMARK 465 ALA E 260
REMARK 465 GLY E 261
REMARK 465 ILE E 262
REMARK 465 ILE E 263
REMARK 465 ARG E 264
REMARK 465 TYR E 265
REMARK 465 ALA E 266
REMARK 465 ILE E 267
REMARK 465 GLY E 268
REMARK 465 VAL E 269
REMARK 465 GLY E 270
REMARK 465 LEU E 271
REMARK 465 ALA E 272
REMARK 465 PHE E 273
REMARK 465 GLN E 274
REMARK 465 ASN E 275
REMARK 465 ARG E 276
REMARK 465 ASN E 277
REMARK 465 SER E 278
REMARK 465 TRP E 279
REMARK 465 LYS E 280
REMARK 465 GLU E 281
REMARK 465 LEU E 282
REMARK 465 ASN E 283
REMARK 465 ASP E 284
REMARK 465 ILE E 285
REMARK 465 ALA E 286
REMARK 465 SER E 287
REMARK 465 LYS E 288
REMARK 465 PRO E 289
REMARK 465 SER E 290
REMARK 465 GLN E 291
REMARK 465 GLU E 292
REMARK 465 HIS E 293
REMARK 465 ILE E 294
REMARK 465 PHE E 295
REMARK 465 LYS E 296
REMARK 465 VAL E 297
REMARK 465 GLU E 298
REMARK 465 ASP E 299
REMARK 465 PHE E 300
REMARK 465 ASP E 301
REMARK 465 ALA E 302
REMARK 465 LEU E 303
REMARK 465 LYS E 304
REMARK 465 ASP E 305
REMARK 465 ILE E 306
REMARK 465 GLN E 307
REMARK 465 ASN E 308
REMARK 465 GLN E 309
REMARK 465 LEU E 310
REMARK 465 LYS E 311
REMARK 465 GLU E 312
REMARK 465 LYS E 313
REMARK 465 ILE E 314
REMARK 465 PHE E 315
REMARK 465 ALA E 316
REMARK 465 ILE E 317
REMARK 465 GLU E 318
REMARK 465 GLY E 319
REMARK 465 THR E 320
REMARK 465 GLU E 321
REMARK 465 THR E 322
REMARK 465 THR E 323
REMARK 465 SER E 324
REMARK 465 SER E 325
REMARK 465 TYR E 1081
REMARK 465 LYS E 1082
REMARK 465 VAL E 1083
REMARK 465 HIS E 1084
REMARK 465 GLY E 1085
REMARK 465 CYS E 1086
REMARK 465 GLY E 1087
REMARK 465 GLY E 1088
REMARK 465 LEU E 1089
REMARK 465 GLU E 1090
REMARK 465 ASN E 1091
REMARK 465 LEU E 1092
REMARK 465 TYR E 1093
REMARK 465 PHE E 1094
REMARK 465 GLN E 1095
REMARK 465 GLY E 1096
REMARK 465 GLY E 1097
REMARK 465 GLU E 1098
REMARK 465 ASN E 1099
REMARK 465 ALA E 1100
REMARK 465 GLN E 1101
REMARK 465 CYS E 1102
REMARK 465 GLU E 1103
REMARK 465 LYS E 1104
REMARK 465 GLU E 1105
REMARK 465 LEU E 1106
REMARK 465 GLN E 1107
REMARK 465 ALA E 1108
REMARK 465 LEU E 1109
REMARK 465 GLU E 1110
REMARK 465 LYS E 1111
REMARK 465 GLU E 1112
REMARK 465 ASN E 1113
REMARK 465 ALA E 1114
REMARK 465 GLN E 1115
REMARK 465 LEU E 1116
REMARK 465 GLU E 1117
REMARK 465 TRP E 1118
REMARK 465 GLU E 1119
REMARK 465 LEU E 1120
REMARK 465 GLN E 1121
REMARK 465 ALA E 1122
REMARK 465 LEU E 1123
REMARK 465 GLU E 1124
REMARK 465 LYS E 1125
REMARK 465 GLU E 1126
REMARK 465 LEU E 1127
REMARK 465 ALA E 1128
REMARK 465 GLN E 1129
REMARK 465 TRP E 1130
REMARK 465 SER E 1131
REMARK 465 HIS E 1132
REMARK 465 PRO E 1133
REMARK 465 GLN E 1134
REMARK 465 PHE E 1135
REMARK 465 GLU E 1136
REMARK 465 LYS E 1137
REMARK 465 ASP F 675
REMARK 465 GLY F 676
REMARK 465 CYS F 677
REMARK 465 GLY F 678
REMARK 465 LEU F 679
REMARK 465 GLU F 680
REMARK 465 ASN F 681
REMARK 465 LEU F 682
REMARK 465 TYR F 683
REMARK 465 PHE F 684
REMARK 465 GLN F 685
REMARK 465 GLY F 686
REMARK 465 GLY F 687
REMARK 465 LYS F 688
REMARK 465 ASN F 689
REMARK 465 ALA F 690
REMARK 465 GLN F 691
REMARK 465 CYS F 692
REMARK 465 LYS F 693
REMARK 465 LYS F 694
REMARK 465 LYS F 695
REMARK 465 LEU F 696
REMARK 465 GLN F 697
REMARK 465 ALA F 698
REMARK 465 LEU F 699
REMARK 465 LYS F 700
REMARK 465 LYS F 701
REMARK 465 LYS F 702
REMARK 465 ASN F 703
REMARK 465 ALA F 704
REMARK 465 GLN F 705
REMARK 465 LEU F 706
REMARK 465 LYS F 707
REMARK 465 TRP F 708
REMARK 465 LYS F 709
REMARK 465 LEU F 710
REMARK 465 GLN F 711
REMARK 465 ALA F 712
REMARK 465 LEU F 713
REMARK 465 LYS F 714
REMARK 465 LYS F 715
REMARK 465 LYS F 716
REMARK 465 LEU F 717
REMARK 465 ALA F 718
REMARK 465 GLN F 719
REMARK 465 GLY F 720
REMARK 465 GLY F 721
REMARK 465 HIS F 722
REMARK 465 HIS F 723
REMARK 465 HIS F 724
REMARK 465 HIS F 725
REMARK 465 HIS F 726
REMARK 465 HIS F 727
REMARK 465 GLN G 129
REMARK 465 GLU G 130
REMARK 465 GLN G 131
REMARK 465 ASP G 132
REMARK 465 ILE G 133
REMARK 465 VAL G 134
REMARK 465 PHE G 135
REMARK 465 LEU G 136
REMARK 465 ILE G 137
REMARK 465 ASP G 138
REMARK 465 GLY G 139
REMARK 465 SER G 140
REMARK 465 GLY G 141
REMARK 465 SER G 142
REMARK 465 ILE G 143
REMARK 465 SER G 144
REMARK 465 SER G 145
REMARK 465 ARG G 146
REMARK 465 ASN G 147
REMARK 465 PHE G 148
REMARK 465 ALA G 149
REMARK 465 THR G 150
REMARK 465 MET G 151
REMARK 465 MET G 152
REMARK 465 ASN G 153
REMARK 465 PHE G 154
REMARK 465 VAL G 155
REMARK 465 ARG G 156
REMARK 465 ALA G 157
REMARK 465 VAL G 158
REMARK 465 ILE G 159
REMARK 465 SER G 160
REMARK 465 GLN G 161
REMARK 465 PHE G 162
REMARK 465 GLN G 163
REMARK 465 ARG G 164
REMARK 465 PRO G 165
REMARK 465 SER G 166
REMARK 465 THR G 167
REMARK 465 GLN G 168
REMARK 465 PHE G 169
REMARK 465 SER G 170
REMARK 465 LEU G 171
REMARK 465 MET G 172
REMARK 465 GLN G 173
REMARK 465 PHE G 174
REMARK 465 SER G 175
REMARK 465 ASN G 176
REMARK 465 LYS G 177
REMARK 465 PHE G 178
REMARK 465 GLN G 179
REMARK 465 THR G 180
REMARK 465 HIS G 181
REMARK 465 PHE G 182
REMARK 465 THR G 183
REMARK 465 PHE G 184
REMARK 465 GLU G 185
REMARK 465 GLU G 186
REMARK 465 PHE G 187
REMARK 465 ARG G 188
REMARK 465 ARG G 189
REMARK 465 SER G 190
REMARK 465 SER G 191
REMARK 465 ASN G 192
REMARK 465 PRO G 193
REMARK 465 LEU G 194
REMARK 465 SER G 195
REMARK 465 LEU G 196
REMARK 465 LEU G 197
REMARK 465 ALA G 198
REMARK 465 SER G 199
REMARK 465 VAL G 200
REMARK 465 HIS G 201
REMARK 465 GLN G 202
REMARK 465 LEU G 203
REMARK 465 GLN G 204
REMARK 465 GLY G 205
REMARK 465 PHE G 206
REMARK 465 THR G 207
REMARK 465 TYR G 208
REMARK 465 THR G 209
REMARK 465 ALA G 210
REMARK 465 THR G 211
REMARK 465 ALA G 212
REMARK 465 ILE G 213
REMARK 465 GLN G 214
REMARK 465 ASN G 215
REMARK 465 VAL G 216
REMARK 465 VAL G 217
REMARK 465 HIS G 218
REMARK 465 ARG G 219
REMARK 465 LEU G 220
REMARK 465 PHE G 221
REMARK 465 HIS G 222
REMARK 465 ALA G 223
REMARK 465 SER G 224
REMARK 465 TYR G 225
REMARK 465 GLY G 226
REMARK 465 ALA G 227
REMARK 465 ARG G 228
REMARK 465 ARG G 229
REMARK 465 ASP G 230
REMARK 465 ALA G 231
REMARK 465 ALA G 232
REMARK 465 LYS G 233
REMARK 465 ILE G 234
REMARK 465 LEU G 235
REMARK 465 ILE G 236
REMARK 465 VAL G 237
REMARK 465 ILE G 238
REMARK 465 THR G 239
REMARK 465 ASP G 240
REMARK 465 GLY G 241
REMARK 465 LYS G 242
REMARK 465 LYS G 243
REMARK 465 GLU G 244
REMARK 465 GLY G 245
REMARK 465 ASP G 246
REMARK 465 SER G 247
REMARK 465 LEU G 248
REMARK 465 ASP G 249
REMARK 465 TYR G 250
REMARK 465 LYS G 251
REMARK 465 ASP G 252
REMARK 465 VAL G 253
REMARK 465 ILE G 254
REMARK 465 PRO G 255
REMARK 465 MET G 256
REMARK 465 ALA G 257
REMARK 465 ASP G 258
REMARK 465 ALA G 259
REMARK 465 ALA G 260
REMARK 465 GLY G 261
REMARK 465 ILE G 262
REMARK 465 ILE G 263
REMARK 465 ARG G 264
REMARK 465 TYR G 265
REMARK 465 ALA G 266
REMARK 465 ILE G 267
REMARK 465 GLY G 268
REMARK 465 VAL G 269
REMARK 465 GLY G 270
REMARK 465 LEU G 271
REMARK 465 ALA G 272
REMARK 465 PHE G 273
REMARK 465 GLN G 274
REMARK 465 ASN G 275
REMARK 465 ARG G 276
REMARK 465 ASN G 277
REMARK 465 SER G 278
REMARK 465 TRP G 279
REMARK 465 LYS G 280
REMARK 465 GLU G 281
REMARK 465 LEU G 282
REMARK 465 ASN G 283
REMARK 465 ASP G 284
REMARK 465 ILE G 285
REMARK 465 ALA G 286
REMARK 465 SER G 287
REMARK 465 LYS G 288
REMARK 465 PRO G 289
REMARK 465 SER G 290
REMARK 465 GLN G 291
REMARK 465 GLU G 292
REMARK 465 HIS G 293
REMARK 465 ILE G 294
REMARK 465 PHE G 295
REMARK 465 LYS G 296
REMARK 465 VAL G 297
REMARK 465 GLU G 298
REMARK 465 ASP G 299
REMARK 465 PHE G 300
REMARK 465 ASP G 301
REMARK 465 ALA G 302
REMARK 465 LEU G 303
REMARK 465 LYS G 304
REMARK 465 ASP G 305
REMARK 465 ILE G 306
REMARK 465 GLN G 307
REMARK 465 ASN G 308
REMARK 465 GLN G 309
REMARK 465 LEU G 310
REMARK 465 LYS G 311
REMARK 465 GLU G 312
REMARK 465 LYS G 313
REMARK 465 ILE G 314
REMARK 465 PHE G 315
REMARK 465 ALA G 316
REMARK 465 ILE G 317
REMARK 465 GLU G 318
REMARK 465 GLY G 319
REMARK 465 THR G 320
REMARK 465 GLU G 321
REMARK 465 THR G 322
REMARK 465 THR G 323
REMARK 465 SER G 324
REMARK 465 SER G 325
REMARK 465 TYR G 1081
REMARK 465 LYS G 1082
REMARK 465 VAL G 1083
REMARK 465 HIS G 1084
REMARK 465 GLY G 1085
REMARK 465 CYS G 1086
REMARK 465 GLY G 1087
REMARK 465 GLY G 1088
REMARK 465 LEU G 1089
REMARK 465 GLU G 1090
REMARK 465 ASN G 1091
REMARK 465 LEU G 1092
REMARK 465 TYR G 1093
REMARK 465 PHE G 1094
REMARK 465 GLN G 1095
REMARK 465 GLY G 1096
REMARK 465 GLY G 1097
REMARK 465 GLU G 1098
REMARK 465 ASN G 1099
REMARK 465 ALA G 1100
REMARK 465 GLN G 1101
REMARK 465 CYS G 1102
REMARK 465 GLU G 1103
REMARK 465 LYS G 1104
REMARK 465 GLU G 1105
REMARK 465 LEU G 1106
REMARK 465 GLN G 1107
REMARK 465 ALA G 1108
REMARK 465 LEU G 1109
REMARK 465 GLU G 1110
REMARK 465 LYS G 1111
REMARK 465 GLU G 1112
REMARK 465 ASN G 1113
REMARK 465 ALA G 1114
REMARK 465 GLN G 1115
REMARK 465 LEU G 1116
REMARK 465 GLU G 1117
REMARK 465 TRP G 1118
REMARK 465 GLU G 1119
REMARK 465 LEU G 1120
REMARK 465 GLN G 1121
REMARK 465 ALA G 1122
REMARK 465 LEU G 1123
REMARK 465 GLU G 1124
REMARK 465 LYS G 1125
REMARK 465 GLU G 1126
REMARK 465 LEU G 1127
REMARK 465 ALA G 1128
REMARK 465 GLN G 1129
REMARK 465 TRP G 1130
REMARK 465 SER G 1131
REMARK 465 HIS G 1132
REMARK 465 PRO G 1133
REMARK 465 GLN G 1134
REMARK 465 PHE G 1135
REMARK 465 GLU G 1136
REMARK 465 LYS G 1137
REMARK 465 ASP H 675
REMARK 465 GLY H 676
REMARK 465 CYS H 677
REMARK 465 GLY H 678
REMARK 465 LEU H 679
REMARK 465 GLU H 680
REMARK 465 ASN H 681
REMARK 465 LEU H 682
REMARK 465 TYR H 683
REMARK 465 PHE H 684
REMARK 465 GLN H 685
REMARK 465 GLY H 686
REMARK 465 GLY H 687
REMARK 465 LYS H 688
REMARK 465 ASN H 689
REMARK 465 ALA H 690
REMARK 465 GLN H 691
REMARK 465 CYS H 692
REMARK 465 LYS H 693
REMARK 465 LYS H 694
REMARK 465 LYS H 695
REMARK 465 LEU H 696
REMARK 465 GLN H 697
REMARK 465 ALA H 698
REMARK 465 LEU H 699
REMARK 465 LYS H 700
REMARK 465 LYS H 701
REMARK 465 LYS H 702
REMARK 465 ASN H 703
REMARK 465 ALA H 704
REMARK 465 GLN H 705
REMARK 465 LEU H 706
REMARK 465 LYS H 707
REMARK 465 TRP H 708
REMARK 465 LYS H 709
REMARK 465 LEU H 710
REMARK 465 GLN H 711
REMARK 465 ALA H 712
REMARK 465 LEU H 713
REMARK 465 LYS H 714
REMARK 465 LYS H 715
REMARK 465 LYS H 716
REMARK 465 LEU H 717
REMARK 465 ALA H 718
REMARK 465 GLN H 719
REMARK 465 GLY H 720
REMARK 465 GLY H 721
REMARK 465 HIS H 722
REMARK 465 HIS H 723
REMARK 465 HIS H 724
REMARK 465 HIS H 725
REMARK 465 HIS H 726
REMARK 465 HIS H 727
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 ARG D 143 CG CD NE CZ NH1 NH2
REMARK 470 SER E 326 OG
REMARK 470 ARG G 480 CG CD NE CZ NH1 NH2
REMARK 470 TRP G 482 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP G 482 CZ3 CH2
REMARK 470 ARG G 483 CG CD NE CZ NH1 NH2
REMARK 470 ARG G 484 CG CD NE CZ NH1 NH2
REMARK 470 LYS G1080 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 ND2 ASN E 920 O5 NAG E 3920 1.94
REMARK 500 ND2 ASN H 190 O5 NAG H 3190 1.98
REMARK 500 ND2 ASN E 678 O5 NAG E 3678 2.04
REMARK 500 ND2 ASN C 678 O5 NAG C 3678 2.05
REMARK 500 ND2 ASN F 190 O5 NAG F 3190 2.07
REMARK 500 O2 BMA W 3 O6 MAN W 7 2.11
REMARK 500 OH TYR C 741 O5 NAG P 1 2.11
REMARK 500 ND2 ASN E 678 C2 NAG E 3678 2.12
REMARK 500 ND2 ASN E 716 O5 NAG T 1 2.13
REMARK 500 OD2 ASP E 451 O HOH E 4001 2.15
REMARK 500 OG SER A 929 O7 NAG A 3031 2.15
REMARK 500 ND2 ASN G 678 O5 NAG G 3678 2.16
REMARK 500 ND2 ASN G 678 C2 NAG G 3678 2.17
REMARK 500 OG SER C 929 O7 NAG C 3031 2.17
REMARK 500 O THR C 411 O HOH C 4001 2.17
REMARK 500 O3 NAG N 2 O2 BMA N 3 2.17
REMARK 500 ND2 ASN C 920 C2 NAG C 3920 2.17
REMARK 500 ND2 ASN A 678 O5 NAG A 3678 2.17
REMARK 500 OE2 GLU E 335 OH TYR E 363 2.18
REMARK 500 O4 NAG R 1 C2 NAG R 2 2.18
REMARK 500 ND2 ASN C 880 C2 NAG Q 1 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU D 64 O4 MAN T 4 1655 2.02
REMARK 500 ND2 ASN A 192 O PRO A 986 4455 2.16
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 LYS C 722 C PRO C 723 N 0.213
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 663 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 663 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 LEU B 654 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 CYS C 703 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 LEU D 266 CA - CB - CG ANGL. DEV. = -15.4 DEGREES
REMARK 500 CYS D 448 CA - CB - SG ANGL. DEV. = 16.6 DEGREES
REMARK 500 LEU E 73 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 LEU E 115 CA - CB - CG ANGL. DEV. = 18.4 DEGREES
REMARK 500 LEU G 73 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG H 432 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 CYS H 609 CA - CB - SG ANGL. DEV. = 10.7 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 SER A 28 -38.86 -142.26
REMARK 500 ASN A 42 44.31 37.53
REMARK 500 ASN A 70 61.58 17.12
REMARK 500 CYS A 97 61.97 -105.98
REMARK 500 ARG A 128 170.14 64.67
REMARK 500 SER A 175 -105.93 -167.67
REMARK 500 ASN A 192 59.50 -142.52
REMARK 500 SER A 199 41.37 -76.51
REMARK 500 GLN A 204 -162.46 57.36
REMARK 500 PHE A 206 -152.72 -75.18
REMARK 500 TYR A 208 69.82 -112.94
REMARK 500 ARG A 219 -63.60 -122.27
REMARK 500 ARG A 229 -77.63 -45.79
REMARK 500 GLU A 298 -73.24 -66.47
REMARK 500 ASP A 299 -137.48 -110.40
REMARK 500 ALA A 316 65.57 -68.75
REMARK 500 THR A 323 68.87 21.28
REMARK 500 SER A 324 49.92 22.99
REMARK 500 SER A 326 65.72 -104.57
REMARK 500 GLU A 329 -126.72 -138.96
REMARK 500 VAL A 340 108.91 -161.48
REMARK 500 VAL A 351 -67.01 -107.60
REMARK 500 PRO A 365 95.41 -60.62
REMARK 500 TYR A 385 18.25 90.53
REMARK 500 LEU A 386 106.65 -49.25
REMARK 500 TRP A 395 -146.97 -94.62
REMARK 500 PRO A 406 -34.08 -38.75
REMARK 500 TYR A 408 107.24 -53.84
REMARK 500 HIS A 410 -3.76 67.21
REMARK 500 THR A 411 -74.10 -96.68
REMARK 500 SER A 421 -118.14 50.13
REMARK 500 THR A 433 -61.48 -130.80
REMARK 500 ALA A 461 58.43 -164.72
REMARK 500 GLN A 472 164.52 174.14
REMARK 500 ALA A 504 -76.43 -59.82
REMARK 500 THR A 507 146.90 -176.12
REMARK 500 PRO A 547 5.62 -67.20
REMARK 500 GLN A 551 134.78 -172.18
REMARK 500 ARG A 588 89.22 -64.18
REMARK 500 GLU A 622 -37.74 74.21
REMARK 500 LYS A 641 -26.46 86.99
REMARK 500 LYS A 644 -78.13 59.09
REMARK 500 ARG A 650 -39.60 80.10
REMARK 500 LEU A 652 -110.33 -67.20
REMARK 500 SER A 654 118.16 -160.24
REMARK 500 ASN A 678 152.49 142.40
REMARK 500 LEU A 689 -73.08 -63.53
REMARK 500 VAL A 708 -61.56 -108.80
REMARK 500 ARG A 731 109.59 -53.04
REMARK 500 CYS A 758 93.56 74.66
REMARK 500
REMARK 500 THIS ENTRY HAS 409 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 SER A 82 PRO A 83 136.87
REMARK 500 ARG A 480 GLY A 481 -146.95
REMARK 500 LEU A 724 LEU A 725 -149.68
REMARK 500 ASN A 885 ASN A 886 144.86
REMARK 500 GLU B 173 LYS B 174 144.44
REMARK 500 ARG B 231 ASN B 232 137.41
REMARK 500 SER C 82 PRO C 83 134.69
REMARK 500 LEU C 600 TRP C 601 -148.49
REMARK 500 TRP C 601 VAL C 602 -147.86
REMARK 500 GLU C 622 GLN C 623 144.20
REMARK 500 LYS C 690 ALA C 691 -148.02
REMARK 500 GLU C 884 ASN C 885 -148.42
REMARK 500 GLY D 102 TYR D 103 143.24
REMARK 500 ASP D 433 ARG D 434 137.64
REMARK 500 LEU D 436 CYS D 437 -144.82
REMARK 500 CYS D 437 HIS D 438 -145.65
REMARK 500 ASN D 620 CYS D 621 -147.49
REMARK 500 SER E 82 PRO E 83 139.46
REMARK 500 TYR E 465 GLU E 466 148.07
REMARK 500 ASP E 640 LYS E 641 138.89
REMARK 500 SER G 82 PRO G 83 139.60
REMARK 500 ARG G 642 SER G 643 144.59
REMARK 500 ASN G 729 LEU G 730 -147.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A2009 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 140 OG
REMARK 620 2 SER A 142 OG 101.2
REMARK 620 3 ASP A 240 OD1 118.9 96.6
REMARK 620 4 HOH A4008 O 156.8 96.2 73.8
REMARK 620 5 HOH A4011 O 84.6 106.6 143.2 75.6
REMARK 620 6 HOH A4012 O 86.7 167.3 88.1 73.7 63.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 447 OD1
REMARK 620 2 ASP A 449 OD1 83.1
REMARK 620 3 ASP A 451 OD1 80.9 79.8
REMARK 620 4 ASP A 451 OD2 125.0 77.6 45.4
REMARK 620 5 SER A 453 O 66.3 145.5 80.0 106.5
REMARK 620 6 ASP A 455 OD1 129.6 120.8 142.0 104.3 92.0
REMARK 620 7 ASP A 455 OD2 81.4 91.9 161.3 149.1 98.6 56.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 511 OD1
REMARK 620 2 ASN A 513 OD1 89.3
REMARK 620 3 ASP A 515 OD1 84.3 63.0
REMARK 620 4 LEU A 517 O 84.5 141.1 78.2
REMARK 620 5 ASP A 519 OD2 120.8 120.0 153.7 95.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 574 OD1
REMARK 620 2 THR A 576 OG1 100.3
REMARK 620 3 ASP A 578 OD1 98.2 86.1
REMARK 620 4 LEU A 580 O 77.7 175.5 98.1
REMARK 620 5 ASP A 582 OD1 137.3 85.4 124.5 93.4
REMARK 620 6 ASP A 582 OD2 89.8 87.0 170.3 89.0 47.9
REMARK 620 7 HOH A4020 O 151.2 100.9 64.0 82.4 64.0 110.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 116 O
REMARK 620 2 ASP B 120 OD2 120.7
REMARK 620 3 GLU B 325 OE2 83.7 115.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 447 OD1
REMARK 620 2 ASP C 449 OD1 59.9
REMARK 620 3 ASP C 449 OD2 104.5 47.1
REMARK 620 4 ASP C 451 OD1 77.1 80.8 104.7
REMARK 620 5 ASP C 451 OD2 119.2 80.2 67.5 51.2
REMARK 620 6 ASP C 455 OD1 115.2 134.4 103.6 144.8 125.4
REMARK 620 7 ASP C 455 OD2 69.9 91.5 93.8 145.2 160.4 51.1
REMARK 620 8 HOH C4003 O 171.3 116.5 74.5 94.7 52.3 73.2 118.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 511 OD1
REMARK 620 2 ASN C 513 OD1 79.6
REMARK 620 3 ASP C 515 OD1 94.1 69.7
REMARK 620 4 LEU C 517 O 87.6 149.0 83.4
REMARK 620 5 ASP C 519 OD2 97.9 103.8 165.1 105.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 574 OD1
REMARK 620 2 THR C 576 OG1 83.3
REMARK 620 3 ASP C 578 OD1 95.1 88.0
REMARK 620 4 LEU C 580 O 87.3 167.8 100.6
REMARK 620 5 ASP C 582 OD1 127.7 78.0 132.0 101.9
REMARK 620 6 ASP C 582 OD2 79.3 71.9 159.6 98.8 48.5
REMARK 620 7 HOH C4007 O 167.3 102.2 73.9 88.6 64.9 113.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER D 116 O
REMARK 620 2 GLU D 325 OE2 105.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 447 OD1
REMARK 620 2 ASP E 451 OD1 66.5
REMARK 620 3 ASP E 451 OD2 116.4 51.3
REMARK 620 4 SER E 453 O 61.2 76.2 109.4
REMARK 620 5 ASP E 455 OD1 123.4 169.4 119.8 104.3
REMARK 620 6 ASP E 455 OD2 73.2 138.9 159.1 91.5 51.6
REMARK 620 7 HOH E4001 O 167.8 102.3 51.6 122.3 68.3 117.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 511 OD1
REMARK 620 2 ASN E 513 OD1 73.6
REMARK 620 3 ASP E 515 OD1 82.4 68.0
REMARK 620 4 LEU E 517 O 87.1 146.8 83.1
REMARK 620 5 ASP E 519 OD1 153.6 121.5 122.4 87.4
REMARK 620 6 ASP E 519 OD2 111.1 116.8 166.3 95.2 43.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 574 OD1
REMARK 620 2 THR E 576 OG1 95.6
REMARK 620 3 ASP E 578 OD1 90.2 89.6
REMARK 620 4 LEU E 580 O 86.0 174.3 84.9
REMARK 620 5 ASP E 582 OD1 145.8 82.7 123.8 99.1
REMARK 620 6 ASP E 582 OD2 92.0 81.6 171.0 103.9 53.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER F 116 O
REMARK 620 2 ASP F 120 OD2 90.7
REMARK 620 3 GLU F 325 OE1 108.0 131.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 447 OD1
REMARK 620 2 ASP G 449 OD1 70.8
REMARK 620 3 ASP G 451 OD1 84.0 71.7
REMARK 620 4 SER G 453 O 78.8 140.1 80.2
REMARK 620 5 ASP G 455 OD1 128.5 125.3 145.5 93.7
REMARK 620 6 ASP G 455 OD2 79.2 93.7 160.7 105.3 53.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 511 OD1
REMARK 620 2 ASN G 513 OD1 79.2
REMARK 620 3 ASP G 515 OD1 98.2 80.4
REMARK 620 4 LEU G 517 O 91.5 157.8 81.0
REMARK 620 5 ASP G 519 OD1 138.1 117.6 121.5 82.8
REMARK 620 6 ASP G 519 OD2 95.3 108.7 165.0 92.1 43.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 576 OG1
REMARK 620 2 ASP G 578 OD1 86.1
REMARK 620 3 LEU G 580 O 120.2 95.1
REMARK 620 4 ASP G 582 OD1 72.4 157.3 101.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER H 116 O
REMARK 620 2 ASP H 120 OD2 101.6
REMARK 620 3 GLU H 325 O 170.5 69.9
REMARK 620 4 GLU H 325 OE2 103.7 154.4 84.6
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3K6S RELATED DB: PDB
REMARK 900 RE-REFINEMENT OF INTEGRIN ALPHAXBETA2 ECTODOMAIN IN THE CLOSED/BENT
REMARK 900 CONFORMATION
DBREF 5ES4 A 1 1084 UNP P20702 ITAX_HUMAN 20 1103
DBREF 5ES4 B 1 674 UNP P05107 ITB2_HUMAN 23 696
DBREF 5ES4 C 1 1084 UNP P20702 ITAX_HUMAN 20 1103
DBREF 5ES4 D 1 674 UNP P05107 ITB2_HUMAN 23 696
DBREF 5ES4 E 1 1084 UNP P20702 ITAX_HUMAN 20 1103
DBREF 5ES4 F 1 674 UNP P05107 ITB2_HUMAN 23 696
DBREF 5ES4 G 1 1084 UNP P20702 ITAX_HUMAN 20 1103
DBREF 5ES4 H 1 674 UNP P05107 ITB2_HUMAN 23 696
SEQADV 5ES4 GLY A 1085 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 CYS A 1086 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY A 1087 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY A 1088 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU A 1089 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU A 1090 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASN A 1091 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU A 1092 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 TYR A 1093 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 PHE A 1094 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN A 1095 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY A 1096 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY A 1097 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU A 1098 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASN A 1099 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA A 1100 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN A 1101 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 CYS A 1102 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU A 1103 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS A 1104 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU A 1105 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU A 1106 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN A 1107 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA A 1108 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU A 1109 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU A 1110 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS A 1111 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU A 1112 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASN A 1113 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA A 1114 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN A 1115 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU A 1116 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU A 1117 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 TRP A 1118 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU A 1119 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU A 1120 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN A 1121 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA A 1122 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU A 1123 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU A 1124 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS A 1125 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU A 1126 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU A 1127 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA A 1128 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN A 1129 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 TRP A 1130 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 SER A 1131 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 HIS A 1132 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 PRO A 1133 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN A 1134 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 PHE A 1135 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU A 1136 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS A 1137 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASP B 675 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY B 676 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 CYS B 677 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY B 678 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU B 679 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLU B 680 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ASN B 681 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU B 682 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 TYR B 683 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 PHE B 684 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN B 685 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY B 686 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY B 687 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS B 688 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ASN B 689 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA B 690 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN B 691 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 CYS B 692 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS B 693 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS B 694 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS B 695 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU B 696 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN B 697 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA B 698 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU B 699 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS B 700 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS B 701 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS B 702 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ASN B 703 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA B 704 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN B 705 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU B 706 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS B 707 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 TRP B 708 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS B 709 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU B 710 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN B 711 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA B 712 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU B 713 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS B 714 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS B 715 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS B 716 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU B 717 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA B 718 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN B 719 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY B 720 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY B 721 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS B 722 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS B 723 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS B 724 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS B 725 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS B 726 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS B 727 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY C 1085 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 CYS C 1086 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY C 1087 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY C 1088 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU C 1089 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU C 1090 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASN C 1091 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU C 1092 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 TYR C 1093 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 PHE C 1094 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN C 1095 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY C 1096 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY C 1097 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU C 1098 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASN C 1099 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA C 1100 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN C 1101 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 CYS C 1102 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU C 1103 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS C 1104 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU C 1105 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU C 1106 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN C 1107 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA C 1108 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU C 1109 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU C 1110 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS C 1111 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU C 1112 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASN C 1113 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA C 1114 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN C 1115 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU C 1116 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU C 1117 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 TRP C 1118 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU C 1119 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU C 1120 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN C 1121 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA C 1122 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU C 1123 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU C 1124 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS C 1125 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU C 1126 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU C 1127 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA C 1128 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN C 1129 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 TRP C 1130 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 SER C 1131 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 HIS C 1132 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 PRO C 1133 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN C 1134 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 PHE C 1135 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU C 1136 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS C 1137 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASP D 675 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY D 676 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 CYS D 677 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY D 678 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU D 679 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLU D 680 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ASN D 681 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU D 682 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 TYR D 683 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 PHE D 684 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN D 685 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY D 686 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY D 687 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS D 688 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ASN D 689 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA D 690 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN D 691 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 CYS D 692 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS D 693 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS D 694 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS D 695 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU D 696 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN D 697 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA D 698 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU D 699 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS D 700 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS D 701 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS D 702 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ASN D 703 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA D 704 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN D 705 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU D 706 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS D 707 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 TRP D 708 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS D 709 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU D 710 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN D 711 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA D 712 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU D 713 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS D 714 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS D 715 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS D 716 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU D 717 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA D 718 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN D 719 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY D 720 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY D 721 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS D 722 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS D 723 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS D 724 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS D 725 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS D 726 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS D 727 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY E 1085 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 CYS E 1086 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY E 1087 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY E 1088 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU E 1089 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU E 1090 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASN E 1091 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU E 1092 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 TYR E 1093 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 PHE E 1094 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN E 1095 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY E 1096 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY E 1097 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU E 1098 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASN E 1099 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA E 1100 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN E 1101 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 CYS E 1102 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU E 1103 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS E 1104 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU E 1105 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU E 1106 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN E 1107 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA E 1108 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU E 1109 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU E 1110 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS E 1111 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU E 1112 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASN E 1113 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA E 1114 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN E 1115 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU E 1116 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU E 1117 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 TRP E 1118 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU E 1119 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU E 1120 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN E 1121 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA E 1122 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU E 1123 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU E 1124 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS E 1125 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU E 1126 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU E 1127 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA E 1128 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN E 1129 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 TRP E 1130 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 SER E 1131 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 HIS E 1132 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 PRO E 1133 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN E 1134 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 PHE E 1135 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU E 1136 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS E 1137 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASP F 675 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY F 676 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 CYS F 677 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY F 678 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU F 679 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLU F 680 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ASN F 681 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU F 682 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 TYR F 683 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 PHE F 684 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN F 685 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY F 686 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY F 687 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS F 688 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ASN F 689 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA F 690 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN F 691 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 CYS F 692 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS F 693 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS F 694 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS F 695 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU F 696 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN F 697 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA F 698 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU F 699 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS F 700 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS F 701 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS F 702 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ASN F 703 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA F 704 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN F 705 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU F 706 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS F 707 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 TRP F 708 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS F 709 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU F 710 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN F 711 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA F 712 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU F 713 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS F 714 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS F 715 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS F 716 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU F 717 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA F 718 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN F 719 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY F 720 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY F 721 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS F 722 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS F 723 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS F 724 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS F 725 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS F 726 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS F 727 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY G 1085 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 CYS G 1086 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY G 1087 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY G 1088 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU G 1089 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU G 1090 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASN G 1091 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU G 1092 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 TYR G 1093 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 PHE G 1094 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN G 1095 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY G 1096 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLY G 1097 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU G 1098 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASN G 1099 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA G 1100 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN G 1101 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 CYS G 1102 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU G 1103 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS G 1104 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU G 1105 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU G 1106 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN G 1107 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA G 1108 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU G 1109 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU G 1110 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS G 1111 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU G 1112 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASN G 1113 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA G 1114 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN G 1115 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU G 1116 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU G 1117 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 TRP G 1118 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU G 1119 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU G 1120 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN G 1121 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA G 1122 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU G 1123 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU G 1124 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS G 1125 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU G 1126 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LEU G 1127 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ALA G 1128 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN G 1129 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 TRP G 1130 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 SER G 1131 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 HIS G 1132 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 PRO G 1133 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLN G 1134 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 PHE G 1135 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 GLU G 1136 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 LYS G 1137 UNP P20702 EXPRESSION TAG
SEQADV 5ES4 ASP H 675 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY H 676 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 CYS H 677 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY H 678 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU H 679 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLU H 680 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ASN H 681 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU H 682 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 TYR H 683 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 PHE H 684 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN H 685 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY H 686 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY H 687 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS H 688 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ASN H 689 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA H 690 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN H 691 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 CYS H 692 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS H 693 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS H 694 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS H 695 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU H 696 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN H 697 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA H 698 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU H 699 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS H 700 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS H 701 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS H 702 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ASN H 703 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA H 704 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN H 705 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU H 706 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS H 707 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 TRP H 708 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS H 709 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU H 710 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN H 711 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA H 712 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU H 713 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS H 714 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS H 715 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LYS H 716 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 LEU H 717 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 ALA H 718 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLN H 719 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY H 720 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 GLY H 721 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS H 722 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS H 723 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS H 724 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS H 725 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS H 726 UNP P05107 EXPRESSION TAG
SEQADV 5ES4 HIS H 727 UNP P05107 EXPRESSION TAG
SEQRES 1 A 1137 PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL
SEQRES 2 A 1137 ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA
SEQRES 3 A 1137 ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR
SEQRES 4 A 1137 ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR
SEQRES 5 A 1137 SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO
SEQRES 6 A 1137 PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA
SEQRES 7 A 1137 SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO
SEQRES 8 A 1137 THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR
SEQRES 9 A 1137 GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN
SEQRES 10 A 1137 ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU
SEQRES 11 A 1137 GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE
SEQRES 12 A 1137 SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG
SEQRES 13 A 1137 ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE
SEQRES 14 A 1137 SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE
SEQRES 15 A 1137 THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER
SEQRES 16 A 1137 LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR
SEQRES 17 A 1137 THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE
SEQRES 18 A 1137 HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE
SEQRES 19 A 1137 LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER
SEQRES 20 A 1137 LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA
SEQRES 21 A 1137 GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE
SEQRES 22 A 1137 GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA
SEQRES 23 A 1137 SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP
SEQRES 24 A 1137 PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU
SEQRES 25 A 1137 LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER
SEQRES 26 A 1137 SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER
SEQRES 27 A 1137 ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL
SEQRES 28 A 1137 GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO
SEQRES 29 A 1137 PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU
SEQRES 30 A 1137 ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR
SEQRES 31 A 1137 GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU
SEQRES 32 A 1137 GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE
SEQRES 33 A 1137 PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU
SEQRES 34 A 1137 VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER
SEQRES 35 A 1137 LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP
SEQRES 36 A 1137 LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR
SEQRES 37 A 1137 ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY
SEQRES 38 A 1137 TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU
SEQRES 39 A 1137 GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR
SEQRES 40 A 1137 VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL
SEQRES 41 A 1137 VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA
SEQRES 42 A 1137 VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER
SEQRES 43 A 1137 PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER
SEQRES 44 A 1137 SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY
SEQRES 45 A 1137 GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL
SEQRES 46 A 1137 GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO
SEQRES 47 A 1137 VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA
SEQRES 48 A 1137 GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL
SEQRES 49 A 1137 VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU
SEQRES 50 A 1137 TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG
SEQRES 51 A 1137 ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP
SEQRES 52 A 1137 PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR
SEQRES 53 A 1137 LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU
SEQRES 54 A 1137 LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER
SEQRES 55 A 1137 CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU
SEQRES 56 A 1137 ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG
SEQRES 57 A 1137 ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR
SEQRES 58 A 1137 PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA
SEQRES 59 A 1137 ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER
SEQRES 60 A 1137 PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU
SEQRES 61 A 1137 GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU
SEQRES 62 A 1137 ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA
SEQRES 63 A 1137 GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN
SEQRES 64 A 1137 GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA
SEQRES 65 A 1137 PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG
SEQRES 66 A 1137 ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR
SEQRES 67 A 1137 PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU
SEQRES 68 A 1137 GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU
SEQRES 69 A 1137 ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU
SEQRES 70 A 1137 GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER
SEQRES 71 A 1137 SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU
SEQRES 72 A 1137 SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR
SEQRES 73 A 1137 GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER
SEQRES 74 A 1137 ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA
SEQRES 75 A 1137 VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO
SEQRES 76 A 1137 SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA
SEQRES 77 A 1137 SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU
SEQRES 78 A 1137 ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP
SEQRES 79 A 1137 VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR
SEQRES 80 A 1137 LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE
SEQRES 81 A 1137 LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE
SEQRES 82 A 1137 THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN
SEQRES 83 A 1137 GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU
SEQRES 84 A 1137 LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU
SEQRES 85 A 1137 TYR PHE GLN GLY GLY GLU ASN ALA GLN CYS GLU LYS GLU
SEQRES 86 A 1137 LEU GLN ALA LEU GLU LYS GLU ASN ALA GLN LEU GLU TRP
SEQRES 87 A 1137 GLU LEU GLN ALA LEU GLU LYS GLU LEU ALA GLN TRP SER
SEQRES 88 A 1137 HIS PRO GLN PHE GLU LYS
SEQRES 1 B 727 GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU
SEQRES 2 B 727 CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS
SEQRES 3 B 727 LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG
SEQRES 4 B 727 CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA
SEQRES 5 B 727 ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR
SEQRES 6 B 727 GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO
SEQRES 7 B 727 GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA
SEQRES 8 B 727 ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO
SEQRES 9 B 727 ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET
SEQRES 10 B 727 LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP
SEQRES 11 B 727 LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG
SEQRES 12 B 727 ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO
SEQRES 13 B 727 PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS
SEQRES 14 B 727 PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE
SEQRES 15 B 727 ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE
SEQRES 16 B 727 GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU
SEQRES 17 B 727 ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL
SEQRES 18 B 727 ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR
SEQRES 19 B 727 ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE
SEQRES 20 B 727 ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN
SEQRES 21 B 727 ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG
SEQRES 22 B 727 SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA
SEQRES 23 B 727 HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA
SEQRES 24 B 727 VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR
SEQRES 25 B 727 GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU
SEQRES 26 B 727 ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR
SEQRES 27 B 727 ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA
SEQRES 28 B 727 LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS
SEQRES 29 B 727 SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP
SEQRES 30 B 727 CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN
SEQRES 31 B 727 VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER
SEQRES 32 B 727 PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR
SEQRES 33 B 727 VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP
SEQRES 34 B 727 GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE
SEQRES 35 B 727 LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE
SEQRES 36 B 727 GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER
SEQRES 37 B 727 GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER
SEQRES 38 B 727 ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN
SEQRES 39 B 727 CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE
SEQRES 40 B 727 TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU
SEQRES 41 B 727 ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY
SEQRES 42 B 727 LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE
SEQRES 43 B 727 GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY
SEQRES 44 B 727 CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY
SEQRES 45 B 727 ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR
SEQRES 46 B 727 GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER
SEQRES 47 B 727 PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS
SEQRES 48 B 727 PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA
SEQRES 49 B 727 CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY
SEQRES 50 B 727 ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL
SEQRES 51 B 727 ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR
SEQRES 52 B 727 LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ASP GLY
SEQRES 53 B 727 CYS GLY LEU GLU ASN LEU TYR PHE GLN GLY GLY LYS ASN
SEQRES 54 B 727 ALA GLN CYS LYS LYS LYS LEU GLN ALA LEU LYS LYS LYS
SEQRES 55 B 727 ASN ALA GLN LEU LYS TRP LYS LEU GLN ALA LEU LYS LYS
SEQRES 56 B 727 LYS LEU ALA GLN GLY GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 C 1137 PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL
SEQRES 2 C 1137 ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA
SEQRES 3 C 1137 ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR
SEQRES 4 C 1137 ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR
SEQRES 5 C 1137 SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO
SEQRES 6 C 1137 PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA
SEQRES 7 C 1137 SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO
SEQRES 8 C 1137 THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR
SEQRES 9 C 1137 GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN
SEQRES 10 C 1137 ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU
SEQRES 11 C 1137 GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE
SEQRES 12 C 1137 SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG
SEQRES 13 C 1137 ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE
SEQRES 14 C 1137 SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE
SEQRES 15 C 1137 THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER
SEQRES 16 C 1137 LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR
SEQRES 17 C 1137 THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE
SEQRES 18 C 1137 HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE
SEQRES 19 C 1137 LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER
SEQRES 20 C 1137 LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA
SEQRES 21 C 1137 GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE
SEQRES 22 C 1137 GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA
SEQRES 23 C 1137 SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP
SEQRES 24 C 1137 PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU
SEQRES 25 C 1137 LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER
SEQRES 26 C 1137 SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER
SEQRES 27 C 1137 ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL
SEQRES 28 C 1137 GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO
SEQRES 29 C 1137 PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU
SEQRES 30 C 1137 ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR
SEQRES 31 C 1137 GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU
SEQRES 32 C 1137 GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE
SEQRES 33 C 1137 PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU
SEQRES 34 C 1137 VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER
SEQRES 35 C 1137 LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP
SEQRES 36 C 1137 LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR
SEQRES 37 C 1137 ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY
SEQRES 38 C 1137 TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU
SEQRES 39 C 1137 GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR
SEQRES 40 C 1137 VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL
SEQRES 41 C 1137 VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA
SEQRES 42 C 1137 VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER
SEQRES 43 C 1137 PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER
SEQRES 44 C 1137 SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY
SEQRES 45 C 1137 GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL
SEQRES 46 C 1137 GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO
SEQRES 47 C 1137 VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA
SEQRES 48 C 1137 GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL
SEQRES 49 C 1137 VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU
SEQRES 50 C 1137 TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG
SEQRES 51 C 1137 ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP
SEQRES 52 C 1137 PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR
SEQRES 53 C 1137 LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU
SEQRES 54 C 1137 LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER
SEQRES 55 C 1137 CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU
SEQRES 56 C 1137 ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG
SEQRES 57 C 1137 ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR
SEQRES 58 C 1137 PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA
SEQRES 59 C 1137 ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER
SEQRES 60 C 1137 PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU
SEQRES 61 C 1137 GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU
SEQRES 62 C 1137 ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA
SEQRES 63 C 1137 GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN
SEQRES 64 C 1137 GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA
SEQRES 65 C 1137 PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG
SEQRES 66 C 1137 ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR
SEQRES 67 C 1137 PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU
SEQRES 68 C 1137 GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU
SEQRES 69 C 1137 ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU
SEQRES 70 C 1137 GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER
SEQRES 71 C 1137 SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU
SEQRES 72 C 1137 SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR
SEQRES 73 C 1137 GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER
SEQRES 74 C 1137 ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA
SEQRES 75 C 1137 VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO
SEQRES 76 C 1137 SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA
SEQRES 77 C 1137 SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU
SEQRES 78 C 1137 ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP
SEQRES 79 C 1137 VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR
SEQRES 80 C 1137 LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE
SEQRES 81 C 1137 LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE
SEQRES 82 C 1137 THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN
SEQRES 83 C 1137 GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU
SEQRES 84 C 1137 LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU
SEQRES 85 C 1137 TYR PHE GLN GLY GLY GLU ASN ALA GLN CYS GLU LYS GLU
SEQRES 86 C 1137 LEU GLN ALA LEU GLU LYS GLU ASN ALA GLN LEU GLU TRP
SEQRES 87 C 1137 GLU LEU GLN ALA LEU GLU LYS GLU LEU ALA GLN TRP SER
SEQRES 88 C 1137 HIS PRO GLN PHE GLU LYS
SEQRES 1 D 727 GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU
SEQRES 2 D 727 CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS
SEQRES 3 D 727 LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG
SEQRES 4 D 727 CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA
SEQRES 5 D 727 ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR
SEQRES 6 D 727 GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO
SEQRES 7 D 727 GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA
SEQRES 8 D 727 ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO
SEQRES 9 D 727 ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET
SEQRES 10 D 727 LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP
SEQRES 11 D 727 LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG
SEQRES 12 D 727 ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO
SEQRES 13 D 727 PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS
SEQRES 14 D 727 PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE
SEQRES 15 D 727 ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE
SEQRES 16 D 727 GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU
SEQRES 17 D 727 ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL
SEQRES 18 D 727 ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR
SEQRES 19 D 727 ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE
SEQRES 20 D 727 ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN
SEQRES 21 D 727 ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG
SEQRES 22 D 727 SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA
SEQRES 23 D 727 HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA
SEQRES 24 D 727 VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR
SEQRES 25 D 727 GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU
SEQRES 26 D 727 ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR
SEQRES 27 D 727 ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA
SEQRES 28 D 727 LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS
SEQRES 29 D 727 SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP
SEQRES 30 D 727 CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN
SEQRES 31 D 727 VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER
SEQRES 32 D 727 PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR
SEQRES 33 D 727 VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP
SEQRES 34 D 727 GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE
SEQRES 35 D 727 LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE
SEQRES 36 D 727 GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER
SEQRES 37 D 727 GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER
SEQRES 38 D 727 ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN
SEQRES 39 D 727 CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE
SEQRES 40 D 727 TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU
SEQRES 41 D 727 ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY
SEQRES 42 D 727 LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE
SEQRES 43 D 727 GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY
SEQRES 44 D 727 CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY
SEQRES 45 D 727 ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR
SEQRES 46 D 727 GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER
SEQRES 47 D 727 PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS
SEQRES 48 D 727 PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA
SEQRES 49 D 727 CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY
SEQRES 50 D 727 ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL
SEQRES 51 D 727 ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR
SEQRES 52 D 727 LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ASP GLY
SEQRES 53 D 727 CYS GLY LEU GLU ASN LEU TYR PHE GLN GLY GLY LYS ASN
SEQRES 54 D 727 ALA GLN CYS LYS LYS LYS LEU GLN ALA LEU LYS LYS LYS
SEQRES 55 D 727 ASN ALA GLN LEU LYS TRP LYS LEU GLN ALA LEU LYS LYS
SEQRES 56 D 727 LYS LEU ALA GLN GLY GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 E 1137 PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL
SEQRES 2 E 1137 ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA
SEQRES 3 E 1137 ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR
SEQRES 4 E 1137 ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR
SEQRES 5 E 1137 SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO
SEQRES 6 E 1137 PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA
SEQRES 7 E 1137 SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO
SEQRES 8 E 1137 THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR
SEQRES 9 E 1137 GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN
SEQRES 10 E 1137 ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU
SEQRES 11 E 1137 GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE
SEQRES 12 E 1137 SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG
SEQRES 13 E 1137 ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE
SEQRES 14 E 1137 SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE
SEQRES 15 E 1137 THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER
SEQRES 16 E 1137 LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR
SEQRES 17 E 1137 THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE
SEQRES 18 E 1137 HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE
SEQRES 19 E 1137 LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER
SEQRES 20 E 1137 LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA
SEQRES 21 E 1137 GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE
SEQRES 22 E 1137 GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA
SEQRES 23 E 1137 SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP
SEQRES 24 E 1137 PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU
SEQRES 25 E 1137 LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER
SEQRES 26 E 1137 SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER
SEQRES 27 E 1137 ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL
SEQRES 28 E 1137 GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO
SEQRES 29 E 1137 PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU
SEQRES 30 E 1137 ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR
SEQRES 31 E 1137 GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU
SEQRES 32 E 1137 GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE
SEQRES 33 E 1137 PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU
SEQRES 34 E 1137 VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER
SEQRES 35 E 1137 LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP
SEQRES 36 E 1137 LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR
SEQRES 37 E 1137 ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY
SEQRES 38 E 1137 TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU
SEQRES 39 E 1137 GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR
SEQRES 40 E 1137 VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL
SEQRES 41 E 1137 VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA
SEQRES 42 E 1137 VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER
SEQRES 43 E 1137 PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER
SEQRES 44 E 1137 SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY
SEQRES 45 E 1137 GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL
SEQRES 46 E 1137 GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO
SEQRES 47 E 1137 VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA
SEQRES 48 E 1137 GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL
SEQRES 49 E 1137 VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU
SEQRES 50 E 1137 TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG
SEQRES 51 E 1137 ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP
SEQRES 52 E 1137 PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR
SEQRES 53 E 1137 LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU
SEQRES 54 E 1137 LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER
SEQRES 55 E 1137 CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU
SEQRES 56 E 1137 ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG
SEQRES 57 E 1137 ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR
SEQRES 58 E 1137 PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA
SEQRES 59 E 1137 ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER
SEQRES 60 E 1137 PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU
SEQRES 61 E 1137 GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU
SEQRES 62 E 1137 ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA
SEQRES 63 E 1137 GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN
SEQRES 64 E 1137 GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA
SEQRES 65 E 1137 PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG
SEQRES 66 E 1137 ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR
SEQRES 67 E 1137 PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU
SEQRES 68 E 1137 GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU
SEQRES 69 E 1137 ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU
SEQRES 70 E 1137 GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER
SEQRES 71 E 1137 SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU
SEQRES 72 E 1137 SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR
SEQRES 73 E 1137 GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER
SEQRES 74 E 1137 ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA
SEQRES 75 E 1137 VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO
SEQRES 76 E 1137 SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA
SEQRES 77 E 1137 SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU
SEQRES 78 E 1137 ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP
SEQRES 79 E 1137 VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR
SEQRES 80 E 1137 LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE
SEQRES 81 E 1137 LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE
SEQRES 82 E 1137 THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN
SEQRES 83 E 1137 GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU
SEQRES 84 E 1137 LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU
SEQRES 85 E 1137 TYR PHE GLN GLY GLY GLU ASN ALA GLN CYS GLU LYS GLU
SEQRES 86 E 1137 LEU GLN ALA LEU GLU LYS GLU ASN ALA GLN LEU GLU TRP
SEQRES 87 E 1137 GLU LEU GLN ALA LEU GLU LYS GLU LEU ALA GLN TRP SER
SEQRES 88 E 1137 HIS PRO GLN PHE GLU LYS
SEQRES 1 F 727 GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU
SEQRES 2 F 727 CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS
SEQRES 3 F 727 LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG
SEQRES 4 F 727 CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA
SEQRES 5 F 727 ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR
SEQRES 6 F 727 GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO
SEQRES 7 F 727 GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA
SEQRES 8 F 727 ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO
SEQRES 9 F 727 ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET
SEQRES 10 F 727 LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP
SEQRES 11 F 727 LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG
SEQRES 12 F 727 ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO
SEQRES 13 F 727 PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS
SEQRES 14 F 727 PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE
SEQRES 15 F 727 ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE
SEQRES 16 F 727 GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU
SEQRES 17 F 727 ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL
SEQRES 18 F 727 ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR
SEQRES 19 F 727 ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE
SEQRES 20 F 727 ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN
SEQRES 21 F 727 ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG
SEQRES 22 F 727 SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA
SEQRES 23 F 727 HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA
SEQRES 24 F 727 VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR
SEQRES 25 F 727 GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU
SEQRES 26 F 727 ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR
SEQRES 27 F 727 ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA
SEQRES 28 F 727 LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS
SEQRES 29 F 727 SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP
SEQRES 30 F 727 CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN
SEQRES 31 F 727 VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER
SEQRES 32 F 727 PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR
SEQRES 33 F 727 VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP
SEQRES 34 F 727 GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE
SEQRES 35 F 727 LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE
SEQRES 36 F 727 GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER
SEQRES 37 F 727 GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER
SEQRES 38 F 727 ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN
SEQRES 39 F 727 CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE
SEQRES 40 F 727 TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU
SEQRES 41 F 727 ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY
SEQRES 42 F 727 LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE
SEQRES 43 F 727 GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY
SEQRES 44 F 727 CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY
SEQRES 45 F 727 ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR
SEQRES 46 F 727 GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER
SEQRES 47 F 727 PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS
SEQRES 48 F 727 PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA
SEQRES 49 F 727 CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY
SEQRES 50 F 727 ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL
SEQRES 51 F 727 ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR
SEQRES 52 F 727 LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ASP GLY
SEQRES 53 F 727 CYS GLY LEU GLU ASN LEU TYR PHE GLN GLY GLY LYS ASN
SEQRES 54 F 727 ALA GLN CYS LYS LYS LYS LEU GLN ALA LEU LYS LYS LYS
SEQRES 55 F 727 ASN ALA GLN LEU LYS TRP LYS LEU GLN ALA LEU LYS LYS
SEQRES 56 F 727 LYS LEU ALA GLN GLY GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 G 1137 PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL
SEQRES 2 G 1137 ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA
SEQRES 3 G 1137 ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR
SEQRES 4 G 1137 ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR
SEQRES 5 G 1137 SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO
SEQRES 6 G 1137 PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA
SEQRES 7 G 1137 SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO
SEQRES 8 G 1137 THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR
SEQRES 9 G 1137 GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN
SEQRES 10 G 1137 ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU
SEQRES 11 G 1137 GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE
SEQRES 12 G 1137 SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG
SEQRES 13 G 1137 ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE
SEQRES 14 G 1137 SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE
SEQRES 15 G 1137 THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER
SEQRES 16 G 1137 LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR
SEQRES 17 G 1137 THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE
SEQRES 18 G 1137 HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE
SEQRES 19 G 1137 LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER
SEQRES 20 G 1137 LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA
SEQRES 21 G 1137 GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE
SEQRES 22 G 1137 GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA
SEQRES 23 G 1137 SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP
SEQRES 24 G 1137 PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU
SEQRES 25 G 1137 LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER
SEQRES 26 G 1137 SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER
SEQRES 27 G 1137 ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL
SEQRES 28 G 1137 GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO
SEQRES 29 G 1137 PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU
SEQRES 30 G 1137 ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR
SEQRES 31 G 1137 GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU
SEQRES 32 G 1137 GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE
SEQRES 33 G 1137 PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU
SEQRES 34 G 1137 VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER
SEQRES 35 G 1137 LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP
SEQRES 36 G 1137 LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR
SEQRES 37 G 1137 ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY
SEQRES 38 G 1137 TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU
SEQRES 39 G 1137 GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR
SEQRES 40 G 1137 VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL
SEQRES 41 G 1137 VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA
SEQRES 42 G 1137 VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER
SEQRES 43 G 1137 PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER
SEQRES 44 G 1137 SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY
SEQRES 45 G 1137 GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL
SEQRES 46 G 1137 GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO
SEQRES 47 G 1137 VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA
SEQRES 48 G 1137 GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL
SEQRES 49 G 1137 VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU
SEQRES 50 G 1137 TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG
SEQRES 51 G 1137 ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP
SEQRES 52 G 1137 PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR
SEQRES 53 G 1137 LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU
SEQRES 54 G 1137 LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER
SEQRES 55 G 1137 CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU
SEQRES 56 G 1137 ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG
SEQRES 57 G 1137 ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR
SEQRES 58 G 1137 PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA
SEQRES 59 G 1137 ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER
SEQRES 60 G 1137 PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU
SEQRES 61 G 1137 GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU
SEQRES 62 G 1137 ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA
SEQRES 63 G 1137 GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN
SEQRES 64 G 1137 GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA
SEQRES 65 G 1137 PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG
SEQRES 66 G 1137 ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR
SEQRES 67 G 1137 PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU
SEQRES 68 G 1137 GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU
SEQRES 69 G 1137 ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU
SEQRES 70 G 1137 GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER
SEQRES 71 G 1137 SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU
SEQRES 72 G 1137 SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR
SEQRES 73 G 1137 GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER
SEQRES 74 G 1137 ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA
SEQRES 75 G 1137 VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO
SEQRES 76 G 1137 SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA
SEQRES 77 G 1137 SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU
SEQRES 78 G 1137 ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP
SEQRES 79 G 1137 VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR
SEQRES 80 G 1137 LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE
SEQRES 81 G 1137 LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE
SEQRES 82 G 1137 THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN
SEQRES 83 G 1137 GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU
SEQRES 84 G 1137 LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU
SEQRES 85 G 1137 TYR PHE GLN GLY GLY GLU ASN ALA GLN CYS GLU LYS GLU
SEQRES 86 G 1137 LEU GLN ALA LEU GLU LYS GLU ASN ALA GLN LEU GLU TRP
SEQRES 87 G 1137 GLU LEU GLN ALA LEU GLU LYS GLU LEU ALA GLN TRP SER
SEQRES 88 G 1137 HIS PRO GLN PHE GLU LYS
SEQRES 1 H 727 GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU
SEQRES 2 H 727 CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS
SEQRES 3 H 727 LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG
SEQRES 4 H 727 CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA
SEQRES 5 H 727 ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR
SEQRES 6 H 727 GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO
SEQRES 7 H 727 GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA
SEQRES 8 H 727 ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO
SEQRES 9 H 727 ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET
SEQRES 10 H 727 LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP
SEQRES 11 H 727 LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG
SEQRES 12 H 727 ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO
SEQRES 13 H 727 PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS
SEQRES 14 H 727 PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE
SEQRES 15 H 727 ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE
SEQRES 16 H 727 GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU
SEQRES 17 H 727 ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL
SEQRES 18 H 727 ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR
SEQRES 19 H 727 ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE
SEQRES 20 H 727 ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN
SEQRES 21 H 727 ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG
SEQRES 22 H 727 SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA
SEQRES 23 H 727 HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA
SEQRES 24 H 727 VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR
SEQRES 25 H 727 GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU
SEQRES 26 H 727 ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR
SEQRES 27 H 727 ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA
SEQRES 28 H 727 LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS
SEQRES 29 H 727 SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP
SEQRES 30 H 727 CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN
SEQRES 31 H 727 VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER
SEQRES 32 H 727 PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR
SEQRES 33 H 727 VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP
SEQRES 34 H 727 GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE
SEQRES 35 H 727 LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE
SEQRES 36 H 727 GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER
SEQRES 37 H 727 GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER
SEQRES 38 H 727 ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN
SEQRES 39 H 727 CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE
SEQRES 40 H 727 TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU
SEQRES 41 H 727 ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY
SEQRES 42 H 727 LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE
SEQRES 43 H 727 GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY
SEQRES 44 H 727 CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY
SEQRES 45 H 727 ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR
SEQRES 46 H 727 GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER
SEQRES 47 H 727 PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS
SEQRES 48 H 727 PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA
SEQRES 49 H 727 CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY
SEQRES 50 H 727 ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL
SEQRES 51 H 727 ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR
SEQRES 52 H 727 LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ASP GLY
SEQRES 53 H 727 CYS GLY LEU GLU ASN LEU TYR PHE GLN GLY GLY LYS ASN
SEQRES 54 H 727 ALA GLN CYS LYS LYS LYS LEU GLN ALA LEU LYS LYS LYS
SEQRES 55 H 727 ASN ALA GLN LEU LYS TRP LYS LEU GLN ALA LEU LYS LYS
SEQRES 56 H 727 LYS LEU ALA GLN GLY GLY HIS HIS HIS HIS HIS HIS
HET NAG I 1 14
HET NAG I 2 14
HET BMA I 3 11
HET MAN I 4 11
HET MAN I 5 11
HET NAG J 1 14
HET NAG J 2 14
HET BMA J 3 11
HET MAN J 4 11
HET MAN J 5 11
HET MAN J 6 11
HET MAN J 7 11
HET MAN J 8 11
HET MAN J 9 11
HET MAN J 10 11
HET NAG K 1 14
HET NAG K 2 14
HET BMA K 3 11
HET MAN K 4 11
HET NAG L 1 14
HET NAG L 2 14
HET BMA L 3 11
HET NAG M 1 14
HET NAG M 2 14
HET NAG N 1 14
HET NAG N 2 14
HET BMA N 3 11
HET MAN N 4 11
HET NAG O 1 14
HET NAG O 2 14
HET BMA O 3 11
HET MAN O 4 11
HET MAN O 5 11
HET MAN O 6 11
HET MAN O 7 11
HET NAG P 1 14
HET NAG P 2 14
HET BMA P 3 11
HET MAN P 4 11
HET MAN P 5 11
HET NAG Q 1 14
HET NAG Q 2 14
HET BMA Q 3 11
HET MAN Q 4 11
HET MAN Q 5 11
HET NAG R 1 14
HET NAG R 2 14
HET BMA R 3 11
HET MAN R 4 11
HET MAN R 5 11
HET MAN R 6 11
HET NAG S 1 14
HET NAG S 2 14
HET BMA S 3 11
HET MAN S 4 11
HET NAG T 1 14
HET NAG T 2 14
HET BMA T 3 11
HET MAN T 4 11
HET NAG U 1 14
HET NAG U 2 14
HET BMA U 3 11
HET MAN U 4 11
HET MAN U 5 11
HET NAG V 1 14
HET NAG V 2 14
HET BMA V 3 11
HET MAN V 4 11
HET MAN V 5 11
HET NAG W 1 14
HET NAG W 2 14
HET BMA W 3 11
HET MAN W 4 11
HET MAN W 5 11
HET MAN W 6 11
HET MAN W 7 11
HET NAG X 1 14
HET NAG X 2 14
HET BMA X 3 11
HET MAN X 4 11
HET NAG Y 1 14
HET NAG Y 2 14
HET BMA Y 3 11
HET MAN Y 4 11
HET MAN Y 5 11
HET CA A2005 1
HET CA A2006 1
HET CA A2007 1
HET MG A2009 1
HET NAG A3031 14
HET NAG A3042 14
HET NAG A3678 14
HET NAG A3920 14
HET CA B2002 1
HET NAG B3232 14
HET NAG B3620 14
HET CA C2005 1
HET CA C2006 1
HET CA C2007 1
HET NAG C3031 14
HET NAG C3042 14
HET NAG C3678 14
HET NAG C3920 14
HET NAG D3232 14
HET NAG D3620 14
HET CA D2002 1
HET CA E2005 1
HET CA E2006 1
HET CA E2007 1
HET NAG E3031 14
HET NAG E3042 14
HET NAG E3678 14
HET NAG E3920 14
HET CA F2002 1
HET NAG F3094 14
HET NAG F3190 14
HET NAG F3620 14
HET CA G2005 1
HET CA G2006 1
HET CA G2007 1
HET NAG G3031 14
HET NAG G3042 14
HET NAG G3678 14
HET NAG G3920 14
HET CA H2002 1
HET NAG H3094 14
HET NAG H3190 14
HET NAG H3232 14
HET NAG H3620 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM MG MAGNESIUM ION
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 9 NAG 61(C8 H15 N O6)
FORMUL 9 BMA 16(C6 H12 O6)
FORMUL 9 MAN 35(C6 H12 O6)
FORMUL 26 CA 16(CA 2+)
FORMUL 29 MG MG 2+
FORMUL 70 HOH *67(H2 O)
HELIX 1 AA1 SER A 144 SER A 160 1 17
HELIX 2 AA2 THR A 183 SER A 190 1 8
HELIX 3 AA3 PRO A 193 SER A 199 1 7
HELIX 4 AA4 TYR A 208 ARG A 219 1 12
HELIX 5 AA5 HIS A 222 GLY A 226 5 5
HELIX 6 AA6 ASP A 249 GLY A 261 1 13
HELIX 7 AA7 LEU A 271 GLN A 274 5 4
HELIX 8 AA8 ASN A 275 ALA A 286 1 12
HELIX 9 AA9 PRO A 289 HIS A 293 1 5
HELIX 10 AB1 ALA A 302 ALA A 316 1 15
HELIX 11 AB2 GLY A 352 SER A 357 1 6
HELIX 12 AB3 ASN A 378 ARG A 382 5 5
HELIX 13 AB4 ARG A 407 THR A 411 5 5
HELIX 14 AB5 GLY A 526 ARG A 531 1 6
HELIX 15 AB6 GLY A 555 SER A 559 1 5
HELIX 16 AB7 PRO A 614 GLU A 619 1 6
HELIX 17 AB8 ASP A 990 LYS A 997 1 8
HELIX 18 AB9 TRP A 1036 LEU A 1041 1 6
HELIX 19 AC1 GLU A 1067 PHE A 1069 5 3
HELIX 20 AC2 SER B 10 GLU B 16 1 7
HELIX 21 AC3 PRO B 35 ILE B 38 5 4
HELIX 22 AC4 THR B 42 ARG B 49 1 8
HELIX 23 AC5 ALA B 52 ASP B 54 5 3
HELIX 24 AC6 SER B 114 SER B 116 5 3
HELIX 25 AC7 MET B 117 LYS B 125 1 9
HELIX 26 AC8 LEU B 127 ASN B 136 1 10
HELIX 27 AC9 HIS B 161 ASN B 167 1 7
HELIX 28 AD1 ASN B 191 GLY B 200 1 10
HELIX 29 AD2 GLY B 213 ALA B 222 1 10
HELIX 30 AD3 ASP B 250 ALA B 255 5 6
HELIX 31 AD4 LYS B 272 PHE B 277 5 6
HELIX 32 AD5 SER B 281 ASN B 292 1 12
HELIX 33 AD6 MET B 304 LYS B 310 1 7
HELIX 34 AD7 ASN B 329 SER B 342 1 14
HELIX 35 AD8 SER B 435 GLY B 439 5 5
HELIX 36 AD9 GLU B 470 SER B 474 5 5
HELIX 37 AE1 ILE B 482 GLY B 486 5 5
HELIX 38 AE2 PRO B 599 LYS B 602 5 4
HELIX 39 AE3 TYR B 603 LYS B 611 1 9
HELIX 40 AE4 ASN B 620 CYS B 625 1 6
HELIX 41 AE5 GLY C 352 SER C 357 1 6
HELIX 42 AE6 ARG C 407 THR C 411 5 5
HELIX 43 AE7 GLY C 526 ARG C 531 1 6
HELIX 44 AE8 GLY C 555 SER C 559 1 5
HELIX 45 AE9 PRO C 614 PHE C 618 5 5
HELIX 46 AF1 SER C 922 GLU C 926 5 5
HELIX 47 AF2 ASP C 990 ASN C 998 1 9
HELIX 48 AF3 GLY C 1035 LEU C 1041 5 7
HELIX 49 AF4 GLU C 1067 PHE C 1069 5 3
HELIX 50 AF5 SER D 10 GLU D 16 1 7
HELIX 51 AF6 PRO D 35 ILE D 38 5 4
HELIX 52 AF7 THR D 42 GLY D 50 1 9
HELIX 53 AF8 ALA D 52 ASP D 54 5 3
HELIX 54 AF9 SER D 114 SER D 116 5 3
HELIX 55 AG1 MET D 117 LYS D 125 1 9
HELIX 56 AG2 LEU D 127 ASN D 136 1 10
HELIX 57 AG3 HIS D 161 ASN D 167 1 7
HELIX 58 AG4 ASN D 191 GLY D 200 1 10
HELIX 59 AG5 GLY D 213 ALA D 222 1 10
HELIX 60 AG6 CYS D 224 GLY D 229 1 6
HELIX 61 AG7 ASP D 250 ALA D 255 5 6
HELIX 62 AG8 TYR D 271 GLU D 276 5 6
HELIX 63 AG9 SER D 281 ASN D 292 1 12
HELIX 64 AH1 MET D 304 ILE D 315 1 12
HELIX 65 AH2 ASN D 329 SER D 342 1 14
HELIX 66 AH3 ILE D 482 GLY D 486 5 5
HELIX 67 AH4 TYR D 603 LYS D 611 1 9
HELIX 68 AH5 ASN D 620 CYS D 625 1 6
HELIX 69 AH6 GLY E 352 SER E 357 1 6
HELIX 70 AH7 ASN E 378 ARG E 382 5 5
HELIX 71 AH8 ARG E 407 THR E 411 5 5
HELIX 72 AH9 GLY E 526 ARG E 531 1 6
HELIX 73 AI1 GLY E 555 SER E 559 1 5
HELIX 74 AI2 LEU E 725 ASN E 729 5 5
HELIX 75 AI3 ASP E 990 ILE E 995 1 6
HELIX 76 AI4 GLY E 1035 LEU E 1041 5 7
HELIX 77 AI5 GLU E 1067 PHE E 1069 5 3
HELIX 78 AI6 SER F 10 GLU F 16 1 7
HELIX 79 AI7 PRO F 35 ILE F 38 5 4
HELIX 80 AI8 THR F 42 ARG F 49 1 8
HELIX 81 AI9 ALA F 52 ASP F 54 5 3
HELIX 82 AJ1 SER F 114 SER F 116 5 3
HELIX 83 AJ2 MET F 117 LYS F 125 1 9
HELIX 84 AJ3 LEU F 127 THR F 139 1 13
HELIX 85 AJ4 HIS F 161 ASN F 167 1 7
HELIX 86 AJ5 ASN F 191 LYS F 201 1 11
HELIX 87 AJ6 GLY F 213 ALA F 223 1 11
HELIX 88 AJ7 CYS F 224 GLY F 229 1 6
HELIX 89 AJ8 ASP F 250 ALA F 255 5 6
HELIX 90 AJ9 TYR F 271 GLU F 276 5 6
HELIX 91 AK1 SER F 281 ASN F 292 1 12
HELIX 92 AK2 THR F 301 LYS F 310 1 10
HELIX 93 AK3 LYS F 310 ILE F 315 1 6
HELIX 94 AK4 ASN F 329 ARG F 344 1 16
HELIX 95 AK5 GLU F 470 CYS F 475 5 6
HELIX 96 AK6 ILE F 482 GLY F 486 5 5
HELIX 97 AK7 CYS F 600 LYS F 602 5 3
HELIX 98 AK8 TYR F 603 PHE F 612 1 10
HELIX 99 AK9 LYS F 614 GLY F 618 5 5
HELIX 100 AL1 GLY G 352 SER G 357 1 6
HELIX 101 AL2 ASN G 378 ARG G 382 5 5
HELIX 102 AL3 ARG G 407 THR G 411 5 5
HELIX 103 AL4 GLY G 526 ARG G 531 1 6
HELIX 104 AL5 GLY G 555 SER G 559 1 5
HELIX 105 AL6 PRO G 614 GLU G 619 1 6
HELIX 106 AL7 LEU G 647 LEU G 652 1 6
HELIX 107 AL8 LEU G 725 ASN G 729 5 5
HELIX 108 AL9 ASP G 990 LYS G 997 1 8
HELIX 109 AM1 GLY G 1035 GLN G 1039 5 5
HELIX 110 AM2 GLU G 1067 PHE G 1069 5 3
HELIX 111 AM3 SER H 10 GLU H 16 1 7
HELIX 112 AM4 PRO H 35 ILE H 38 5 4
HELIX 113 AM5 THR H 42 ARG H 49 1 8
HELIX 114 AM6 ALA H 52 ASP H 54 5 3
HELIX 115 AM7 SER H 114 SER H 116 5 3
HELIX 116 AM8 MET H 117 LYS H 125 1 9
HELIX 117 AM9 LEU H 127 ASN H 136 1 10
HELIX 118 AN1 HIS H 161 ASN H 167 1 7
HELIX 119 AN2 ASN H 191 GLY H 200 1 10
HELIX 120 AN3 GLY H 213 CYS H 224 1 12
HELIX 121 AN4 ASP H 250 ALA H 255 5 6
HELIX 122 AN5 TYR H 271 GLU H 276 5 6
HELIX 123 AN6 SER H 281 ASN H 292 1 12
HELIX 124 AN7 MET H 304 GLU H 313 1 10
HELIX 125 AN8 ASN H 329 SER H 342 1 14
HELIX 126 AN9 GLN H 469 CYS H 475 5 7
HELIX 127 AO1 ILE H 482 GLY H 486 5 5
HELIX 128 AO2 PRO H 599 LYS H 602 5 4
HELIX 129 AO3 TYR H 603 GLU H 613 1 11
SHEET 1 AA1 4 LEU A 3 ARG A 12 0
SHEET 2 AA1 4 GLN A 590 THR A 596 -1 O VAL A 591 N PHE A 11
SHEET 3 AA1 4 ASP A 582 ALA A 587 -1 N VAL A 585 O LEU A 592
SHEET 4 AA1 4 LEU A 569 GLN A 573 -1 N GLN A 573 O ASP A 582
SHEET 1 AA2 4 SER A 21 TYR A 25 0
SHEET 2 AA2 4 TRP A 29 ALA A 40 -1 O TRP A 29 N TYR A 25
SHEET 3 AA2 4 GLN A 43 GLY A 51 -1 O TYR A 48 N VAL A 32
SHEET 4 AA2 4 CYS A 57 PRO A 59 -1 O GLU A 58 N GLN A 49
SHEET 1 AA3 4 SER A 76 THR A 80 0
SHEET 2 AA3 4 GLN A 85 CYS A 97 -1 O LEU A 87 N ALA A 78
SHEET 3 AA3 4 ASN A 100 LEU A 110 -1 O ASN A 100 N CYS A 97
SHEET 4 AA3 4 GLN A 117 LEU A 119 -1 O LEU A 119 N CYS A 107
SHEET 1 AA4 6 PHE A 178 PHE A 182 0
SHEET 2 AA4 6 THR A 167 PHE A 174 -1 N GLN A 173 O GLN A 179
SHEET 3 AA4 6 GLN A 131 ASP A 138 1 N ILE A 137 O PHE A 174
SHEET 4 AA4 6 ALA A 232 THR A 239 1 O ILE A 236 N LEU A 136
SHEET 5 AA4 6 ILE A 262 VAL A 269 1 O ILE A 263 N LYS A 233
SHEET 6 AA4 6 ILE A 294 VAL A 297 1 O VAL A 297 N GLY A 268
SHEET 1 AA5 3 VAL A 347 ALA A 350 0
SHEET 2 AA5 3 GLY A 359 LEU A 362 -1 O GLY A 359 N ALA A 350
SHEET 3 AA5 3 THR A 370 ILE A 372 -1 O ILE A 372 N ALA A 360
SHEET 1 AA6 4 SER A 389 LEU A 394 0
SHEET 2 AA6 4 GLN A 399 ALA A 405 -1 O SER A 400 N ALA A 393
SHEET 3 AA6 4 LYS A 413 VAL A 420 -1 O LYS A 413 N ALA A 405
SHEET 4 AA6 4 GLN A 423 THR A 431 -1 O GLN A 423 N VAL A 420
SHEET 1 AA7 4 LEU A 443 VAL A 446 0
SHEET 2 AA7 4 LEU A 456 GLY A 460 -1 O LEU A 458 N CYS A 444
SHEET 3 AA7 4 VAL A 473 PRO A 477 -1 O SER A 474 N ILE A 459
SHEET 4 AA7 4 ALA A 489 LEU A 491 -1 O ALA A 489 N VAL A 475
SHEET 1 AA8 2 ARG A 469 GLY A 471 0
SHEET 2 AA8 2 HIS A 497 PHE A 502 1 O HIS A 497 N GLY A 470
SHEET 1 AA9 4 LEU A 506 GLY A 510 0
SHEET 2 AA9 4 ASP A 519 ALA A 524 -1 O ASP A 519 N GLY A 510
SHEET 3 AA9 4 ALA A 533 VAL A 540 -1 O PHE A 537 N VAL A 520
SHEET 4 AA9 4 SER A 544 ILE A 545 -1 O SER A 544 N VAL A 540
SHEET 1 AB1 4 LEU A 506 GLY A 510 0
SHEET 2 AB1 4 ASP A 519 ALA A 524 -1 O ASP A 519 N GLY A 510
SHEET 3 AB1 4 ALA A 533 VAL A 540 -1 O PHE A 537 N VAL A 520
SHEET 4 AB1 4 GLN A 551 ALA A 554 -1 O ILE A 553 N VAL A 534
SHEET 1 AB2 2 VAL A 599 LEU A 600 0
SHEET 2 AB2 2 MET A 733 LEU A 734 1 O MET A 733 N LEU A 600
SHEET 1 AB3 4 VAL A 602 ILE A 609 0
SHEET 2 AB3 4 THR A 629 ILE A 639 -1 O GLN A 632 N ILE A 609
SHEET 3 AB3 4 HIS A 692 LEU A 700 -1 O LEU A 698 N VAL A 631
SHEET 4 AB3 4 THR A 672 PHE A 673 -1 N THR A 672 O LEU A 699
SHEET 1 AB4 4 SER A 680 LEU A 687 0
SHEET 2 AB4 4 SER A 654 LEU A 662 -1 N LEU A 660 O LEU A 681
SHEET 3 AB4 4 ILE A 711 LEU A 719 -1 O THR A 718 N THR A 657
SHEET 4 AB4 4 TYR A 741 LEU A 746 -1 O LEU A 746 N ILE A 711
SHEET 1 AB5 4 LEU A 762 SER A 767 0
SHEET 2 AB5 4 GLU A 781 ASN A 790 -1 O MET A 787 N SER A 765
SHEET 3 AB5 4 GLN A 856 VAL A 865 -1 O ILE A 857 N VAL A 788
SHEET 4 AB5 4 LEU A 808 ARG A 811 -1 N SER A 809 O ASP A 864
SHEET 1 AB6 7 THR C 828 PRO C 833 0
SHEET 2 AB6 7 THR C 839 ARG C 845 -1 O SER C 841 N ALA C 832
SHEET 3 AB6 7 THR C 799 PRO C 805 -1 N HIS C 804 O TRP C 840
SHEET 4 AB6 7 ARG C 874 SER C 882 -1 O ASN C 880 N THR C 801
SHEET 5 AB6 7 PHE C 895 VAL C 905 -1 O LEU C 897 N LEU C 877
SHEET 6 AB6 7 PHE A 895 VAL A 905 -1 N GLU A 898 O GLN C 896
SHEET 7 AB6 7 TYR A1060 GLN A1062 1 O SER A1061 N TYR A 903
SHEET 1 AB7 7 THR C 828 PRO C 833 0
SHEET 2 AB7 7 THR C 839 ARG C 845 -1 O SER C 841 N ALA C 832
SHEET 3 AB7 7 THR C 799 PRO C 805 -1 N HIS C 804 O TRP C 840
SHEET 4 AB7 7 ARG C 874 SER C 882 -1 O ASN C 880 N THR C 801
SHEET 5 AB7 7 PHE C 895 VAL C 905 -1 O LEU C 897 N LEU C 877
SHEET 6 AB7 7 PHE A 895 VAL A 905 -1 N GLU A 898 O GLN C 896
SHEET 7 AB7 7 LEU A 774 VAL A 776 1 N VAL A 776 O LYS A 902
SHEET 1 AB8 4 LEU C 774 VAL C 776 0
SHEET 2 AB8 4 PHE C 895 VAL C 905 1 O LYS C 902 N VAL C 776
SHEET 3 AB8 4 PHE A 895 VAL A 905 -1 N GLU A 898 O GLN C 896
SHEET 4 AB8 4 TYR A1060 GLN A1062 1 O SER A1061 N TYR A 903
SHEET 1 AB9 7 TYR C1060 GLN C1062 0
SHEET 2 AB9 7 PHE C 895 VAL C 905 1 N TYR C 903 O SER C1061
SHEET 3 AB9 7 PHE A 895 VAL A 905 -1 N GLU A 898 O GLN C 896
SHEET 4 AB9 7 ARG A 874 SER A 882 -1 N LEU A 875 O LEU A 899
SHEET 5 AB9 7 THR A 799 PRO A 805 -1 N THR A 801 O ASN A 880
SHEET 6 AB9 7 THR A 839 ILE A 846 -1 O CYS A 844 N ILE A 800
SHEET 7 AB9 7 LEU A 827 VAL A 834 -1 N ASP A 830 O SER A 843
SHEET 1 AC1 7 LEU A 827 VAL A 834 0
SHEET 2 AC1 7 THR A 839 ILE A 846 -1 O SER A 843 N ASP A 830
SHEET 3 AC1 7 THR A 799 PRO A 805 -1 N ILE A 800 O CYS A 844
SHEET 4 AC1 7 ARG A 874 SER A 882 -1 O ASN A 880 N THR A 801
SHEET 5 AC1 7 PHE A 895 VAL A 905 -1 O LEU A 899 N LEU A 875
SHEET 6 AC1 7 PHE C 895 VAL C 905 -1 O GLN C 896 N GLU A 898
SHEET 7 AC1 7 TYR C1060 GLN C1062 1 O SER C1061 N TYR C 903
SHEET 1 AC2 2 SER A 795 TYR A 796 0
SHEET 2 AC2 2 ILE A 850 PHE A 851 -1 O PHE A 851 N SER A 795
SHEET 1 AC3 4 THR A 907 SER A 911 0
SHEET 2 AC3 4 SER A 929 ASN A 940 -1 O GLN A 937 N SER A 910
SHEET 3 AC3 4 GLU A1023 SER A1033 -1 O LEU A1032 N HIS A 930
SHEET 4 AC3 4 GLU A 968 SER A 970 -1 N SER A 970 O THR A1027
SHEET 1 AC4 4 GLU A 961 ALA A 962 0
SHEET 2 AC4 4 LEU A 946 LEU A 958 -1 N LEU A 958 O GLU A 961
SHEET 3 AC4 4 SER A1046 THR A1054 -1 O THR A1054 N SER A 949
SHEET 4 AC4 4 VAL A1000 LEU A1001 1 N LEU A1001 O SER A1046
SHEET 1 AC5 5 SER A 980 ILE A 984 0
SHEET 2 AC5 5 GLY A1007 PHE A1018 -1 O ARG A1012 N SER A 980
SHEET 3 AC5 5 LEU A 946 LEU A 958 -1 N GLU A 957 O GLY A1007
SHEET 4 AC5 5 SER A1046 THR A1054 -1 O THR A1054 N SER A 949
SHEET 5 AC5 5 ARG A1071 VAL A1077 -1 O THR A1076 N VAL A1047
SHEET 1 AC6 3 CYS B 40 ASP B 41 0
SHEET 2 AC6 3 THR B 22 CYS B 24 -1 N THR B 22 O ASP B 41
SHEET 3 AC6 3 ILE B 56 MET B 57 -1 O MET B 57 N TRP B 23
SHEET 1 AC7 6 LEU B 62 THR B 65 0
SHEET 2 AC7 6 LYS B 80 LEU B 85 -1 O THR B 82 N GLU B 64
SHEET 3 AC7 6 ILE B 414 PRO B 421 1 O GLN B 418 N LEU B 83
SHEET 4 AC7 6 GLN B 402 LEU B 409 -1 N GLN B 402 O VAL B 419
SHEET 5 AC7 6 VAL B 345 HIS B 349 -1 N ASP B 348 O ARG B 407
SHEET 6 AC7 6 GLY B 376 CYS B 378 -1 O GLY B 376 N LEU B 347
SHEET 1 AC8 4 LEU B 76 SER B 77 0
SHEET 2 AC8 4 ALA B 91 PHE B 97 -1 O THR B 96 N SER B 77
SHEET 3 AC8 4 ILE B 387 ALA B 395 -1 O VAL B 393 N ALA B 91
SHEET 4 AC8 4 LEU B 356 TYR B 360 -1 N THR B 359 O LYS B 392
SHEET 1 AC9 6 PHE B 182 THR B 189 0
SHEET 2 AC9 6 ARG B 143 PHE B 149 -1 N SER B 148 O ARG B 183
SHEET 3 AC9 6 ILE B 105 ASP B 112 1 N MET B 111 O PHE B 149
SHEET 4 AC9 6 THR B 234 THR B 241 1 O THR B 234 N ASP B 106
SHEET 5 AC9 6 ILE B 294 VAL B 300 1 O ILE B 297 N PHE B 239
SHEET 6 AC9 6 ALA B 319 GLU B 322 1 O ALA B 319 N PHE B 298
SHEET 1 AD1 2 GLY B 441 LEU B 443 0
SHEET 2 AD1 2 CYS B 448 CYS B 450 -1 O ARG B 449 N PHE B 442
SHEET 1 AD2 2 TYR B 454 ILE B 455 0
SHEET 2 AD2 2 CYS B 461 GLN B 462 -1 O CYS B 461 N ILE B 455
SHEET 1 AD3 2 ILE B 507 TYR B 508 0
SHEET 2 AD3 2 CYS B 514 ASP B 515 -1 O CYS B 514 N TYR B 508
SHEET 1 AD4 2 ARG B 521 TYR B 522 0
SHEET 2 AD4 2 GLN B 525 VAL B 526 -1 O GLN B 525 N TYR B 522
SHEET 1 AD5 2 GLY B 533 PHE B 536 0
SHEET 2 AD5 2 LYS B 539 CYS B 542 -1 O LYS B 539 N PHE B 536
SHEET 1 AD6 2 PHE B 546 GLU B 547 0
SHEET 2 AD6 2 CYS B 553 GLU B 554 -1 O CYS B 553 N GLU B 547
SHEET 1 AD7 2 ARG B 573 CYS B 574 0
SHEET 2 AD7 2 CYS B 579 GLU B 580 -1 O GLU B 580 N ARG B 573
SHEET 1 AD8 4 LEU B 628 LEU B 630 0
SHEET 2 AD8 4 TYR B 663 VAL B 667 1 O ILE B 665 N GLN B 629
SHEET 3 AD8 4 TRP B 649 GLN B 656 -1 N GLU B 655 O LEU B 664
SHEET 4 AD8 4 ARG B 638 ARG B 643 -1 N ARG B 638 O LEU B 654
SHEET 1 AD9 4 THR C 9 ARG C 12 0
SHEET 2 AD9 4 GLN C 590 ARG C 595 -1 O LEU C 593 N THR C 9
SHEET 3 AD9 4 ASP C 582 GLY C 586 -1 N LEU C 583 O LEU C 594
SHEET 4 AD9 4 LEU C 569 GLN C 573 -1 N SER C 570 O ALA C 584
SHEET 1 AE1 4 SER C 21 TYR C 25 0
SHEET 2 AE1 4 TRP C 29 GLY C 33 -1 O GLY C 33 N SER C 21
SHEET 3 AE1 4 LEU C 47 GLY C 51 -1 O CYS C 50 N VAL C 30
SHEET 4 AE1 4 CYS C 57 PRO C 59 -1 O GLU C 58 N GLN C 49
SHEET 1 AE2 4 SER C 76 THR C 80 0
SHEET 2 AE2 4 GLN C 85 GLU C 96 -1 O LEU C 87 N ALA C 78
SHEET 3 AE2 4 MET C 101 GLY C 111 -1 O PHE C 108 N ALA C 88
SHEET 4 AE2 4 GLN C 114 LEU C 119 -1 O LEU C 119 N CYS C 107
SHEET 1 AE3 4 SER C 338 VAL C 340 0
SHEET 2 AE3 4 VAL C 347 ALA C 350 -1 O GLY C 349 N SER C 338
SHEET 3 AE3 4 GLY C 359 LEU C 362 -1 O PHE C 361 N LEU C 348
SHEET 4 AE3 4 THR C 370 ILE C 372 -1 O ILE C 372 N ALA C 360
SHEET 1 AE4 4 THR C 390 ALA C 393 0
SHEET 2 AE4 4 SER C 400 ALA C 405 -1 O VAL C 402 N GLU C 391
SHEET 3 AE4 4 LYS C 413 VAL C 420 -1 O LYS C 413 N ALA C 405
SHEET 4 AE4 4 GLN C 423 THR C 431 -1 O ALA C 428 N ILE C 416
SHEET 1 AE5 4 SER C 442 VAL C 446 0
SHEET 2 AE5 4 LEU C 456 GLU C 466 -1 O LEU C 456 N VAL C 446
SHEET 3 AE5 4 ARG C 469 PRO C 477 -1 O GLY C 471 N TYR C 464
SHEET 4 AE5 4 ALA C 489 LEU C 491 -1 O LEU C 491 N VAL C 473
SHEET 1 AE6 4 SER C 442 VAL C 446 0
SHEET 2 AE6 4 LEU C 456 GLU C 466 -1 O LEU C 456 N VAL C 446
SHEET 3 AE6 4 ARG C 469 PRO C 477 -1 O GLY C 471 N TYR C 464
SHEET 4 AE6 4 HIS C 497 PHE C 502 1 O HIS C 497 N GLY C 470
SHEET 1 AE7 4 LEU C 506 GLY C 510 0
SHEET 2 AE7 4 ASP C 519 ALA C 524 -1 O ASP C 519 N GLY C 510
SHEET 3 AE7 4 ALA C 533 VAL C 540 -1 O PHE C 537 N VAL C 520
SHEET 4 AE7 4 SER C 544 ILE C 545 -1 O SER C 544 N VAL C 540
SHEET 1 AE8 4 LEU C 506 GLY C 510 0
SHEET 2 AE8 4 ASP C 519 ALA C 524 -1 O ASP C 519 N GLY C 510
SHEET 3 AE8 4 ALA C 533 VAL C 540 -1 O PHE C 537 N VAL C 520
SHEET 4 AE8 4 ARG C 552 ALA C 554 -1 O ILE C 553 N VAL C 534
SHEET 1 AE9 2 VAL C 599 LEU C 600 0
SHEET 2 AE9 2 MET C 733 LEU C 734 1 O MET C 733 N LEU C 600
SHEET 1 AF1 4 GLY C 603 ILE C 609 0
SHEET 2 AF1 4 THR C 629 TYR C 638 -1 O GLN C 632 N ILE C 609
SHEET 3 AF1 4 HIS C 692 LEU C 700 -1 O LEU C 698 N VAL C 631
SHEET 4 AF1 4 THR C 672 PHE C 673 -1 N THR C 672 O LEU C 699
SHEET 1 AF2 4 SER C 680 LEU C 687 0
SHEET 2 AF2 4 SER C 654 LEU C 662 -1 N LEU C 660 O LEU C 681
SHEET 3 AF2 4 ILE C 711 LEU C 719 -1 O THR C 718 N THR C 657
SHEET 4 AF2 4 TYR C 741 LEU C 746 -1 O LEU C 746 N ILE C 711
SHEET 1 AF3 4 LEU C 762 SER C 767 0
SHEET 2 AF3 4 GLU C 781 ASN C 790 -1 O TRP C 789 N GLY C 763
SHEET 3 AF3 4 GLN C 856 VAL C 865 -1 O ALA C 861 N ALA C 784
SHEET 4 AF3 4 LEU C 808 ARG C 811 -1 N SER C 809 O ASP C 864
SHEET 1 AF4 2 SER C 795 TYR C 796 0
SHEET 2 AF4 2 ILE C 850 PHE C 851 -1 O PHE C 851 N SER C 795
SHEET 1 AF5 4 THR C 907 SER C 911 0
SHEET 2 AF5 4 SER C 929 ASN C 940 -1 O GLN C 937 N SER C 910
SHEET 3 AF5 4 GLU C1023 SER C1033 -1 O LEU C1032 N HIS C 930
SHEET 4 AF5 4 TRP C 964 SER C 970 -1 N SER C 970 O THR C1027
SHEET 1 AF6 4 GLU C 961 ALA C 962 0
SHEET 2 AF6 4 LEU C 946 LEU C 958 -1 N LEU C 958 O GLU C 961
SHEET 3 AF6 4 SER C1046 THR C1054 -1 O THR C1054 N SER C 949
SHEET 4 AF6 4 VAL C1000 LEU C1001 1 N LEU C1001 O VAL C1048
SHEET 1 AF7 5 CYS C 979 ILE C 984 0
SHEET 2 AF7 5 GLY C1007 PHE C1018 -1 O ARG C1010 N GLU C 982
SHEET 3 AF7 5 LEU C 946 LEU C 958 -1 N ILE C 950 O CYS C1013
SHEET 4 AF7 5 SER C1046 THR C1054 -1 O THR C1054 N SER C 949
SHEET 5 AF7 5 ARG C1071 VAL C1077 -1 O ALA C1072 N ALA C1051
SHEET 1 AF8 3 CYS D 40 ASP D 41 0
SHEET 2 AF8 3 THR D 22 CYS D 24 -1 N THR D 22 O ASP D 41
SHEET 3 AF8 3 ILE D 56 MET D 57 -1 O MET D 57 N TRP D 23
SHEET 1 AF9 5 LEU D 62 THR D 65 0
SHEET 2 AF9 5 LYS D 80 LEU D 85 -1 O THR D 82 N GLU D 64
SHEET 3 AF9 5 ILE D 414 PRO D 421 1 O GLN D 418 N LEU D 83
SHEET 4 AF9 5 GLN D 402 ALA D 408 -1 N PHE D 404 O VAL D 417
SHEET 5 AF9 5 LEU D 347 HIS D 349 -1 N ASP D 348 O ARG D 407
SHEET 1 AG1 5 LEU D 76 SER D 77 0
SHEET 2 AG1 5 ALA D 91 PHE D 97 -1 O THR D 96 N SER D 77
SHEET 3 AG1 5 ILE D 387 ALA D 395 -1 O VAL D 391 N PHE D 93
SHEET 4 AG1 5 LEU D 356 PHE D 363 -1 N THR D 359 O LYS D 392
SHEET 5 AG1 5 THR D 369 GLN D 373 -1 O GLN D 373 N TYR D 360
SHEET 1 AG2 6 PHE D 182 THR D 189 0
SHEET 2 AG2 6 ARG D 143 PHE D 149 -1 N SER D 148 O ARG D 183
SHEET 3 AG2 6 ASP D 106 ASP D 112 1 N LEU D 107 O GLY D 145
SHEET 4 AG2 6 ARG D 235 ALA D 240 1 O ALA D 240 N LEU D 110
SHEET 5 AG2 6 ILE D 294 THR D 301 1 O ILE D 297 N LEU D 237
SHEET 6 AG2 6 ALA D 319 LEU D 323 1 O LEU D 323 N VAL D 300
SHEET 1 AG3 2 PHE D 442 GLU D 444 0
SHEET 2 AG3 2 ILE D 447 ARG D 449 -1 O ARG D 449 N PHE D 442
SHEET 1 AG4 2 TYR D 454 ILE D 455 0
SHEET 2 AG4 2 CYS D 461 GLN D 462 -1 O CYS D 461 N ILE D 455
SHEET 1 AG5 2 GLY D 488 VAL D 491 0
SHEET 2 AG5 2 GLN D 494 CYS D 497 -1 O GLN D 494 N VAL D 491
SHEET 1 AG6 2 ARG D 521 TYR D 522 0
SHEET 2 AG6 2 GLN D 525 VAL D 526 -1 O GLN D 525 N TYR D 522
SHEET 1 AG7 2 GLY D 533 PHE D 536 0
SHEET 2 AG7 2 LYS D 539 CYS D 542 -1 O ARG D 541 N LEU D 534
SHEET 1 AG8 2 PHE D 546 GLU D 547 0
SHEET 2 AG8 2 CYS D 553 GLU D 554 -1 O CYS D 553 N GLU D 547
SHEET 1 AG9 4 LEU D 628 LEU D 630 0
SHEET 2 AG9 4 TYR D 663 VAL D 667 1 O ILE D 665 N GLN D 629
SHEET 3 AG9 4 TRP D 649 GLN D 656 -1 N GLU D 655 O LEU D 664
SHEET 4 AG9 4 ARG D 638 ARG D 643 -1 N CYS D 640 O TYR D 652
SHEET 1 AH1 4 THR E 9 ARG E 12 0
SHEET 2 AH1 4 GLN E 590 ARG E 595 -1 O LEU E 593 N THR E 9
SHEET 3 AH1 4 ASP E 582 ALA E 587 -1 N VAL E 585 O LEU E 592
SHEET 4 AH1 4 LEU E 569 GLN E 573 -1 N GLN E 573 O ASP E 582
SHEET 1 AH2 4 SER E 21 TYR E 25 0
SHEET 2 AH2 4 TRP E 29 ALA E 34 -1 O TRP E 29 N TYR E 25
SHEET 3 AH2 4 GLY E 46 GLY E 51 -1 O GLY E 46 N ALA E 34
SHEET 4 AH2 4 ALA E 56 PRO E 59 -1 O GLU E 58 N GLN E 49
SHEET 1 AH3 4 SER E 76 THR E 80 0
SHEET 2 AH3 4 GLN E 85 CYS E 97 -1 O LEU E 87 N ALA E 78
SHEET 3 AH3 4 ASN E 100 LEU E 110 -1 O PHE E 108 N ALA E 88
SHEET 4 AH3 4 GLN E 117 LEU E 119 -1 O LEU E 119 N CYS E 107
SHEET 1 AH4 4 ALA E 339 VAL E 340 0
SHEET 2 AH4 4 VAL E 347 ALA E 350 -1 O VAL E 347 N VAL E 340
SHEET 3 AH4 4 GLY E 359 LEU E 362 -1 O PHE E 361 N LEU E 348
SHEET 4 AH4 4 THR E 370 ILE E 372 -1 O ILE E 372 N ALA E 360
SHEET 1 AH5 4 THR E 390 LEU E 394 0
SHEET 2 AH5 4 GLN E 399 ALA E 405 -1 O VAL E 402 N GLU E 391
SHEET 3 AH5 4 LYS E 413 VAL E 420 -1 O LYS E 413 N ALA E 405
SHEET 4 AH5 4 GLN E 423 THR E 431 -1 O GLN E 423 N VAL E 420
SHEET 1 AH6 4 SER E 442 VAL E 446 0
SHEET 2 AH6 4 LEU E 456 GLY E 460 -1 O LEU E 458 N CYS E 444
SHEET 3 AH6 4 VAL E 473 PRO E 477 -1 O SER E 474 N ILE E 459
SHEET 4 AH6 4 ALA E 489 LEU E 491 -1 O ALA E 489 N VAL E 475
SHEET 1 AH7 3 TYR E 465 GLU E 466 0
SHEET 2 AH7 3 ARG E 469 GLY E 471 -1 O ARG E 469 N GLU E 466
SHEET 3 AH7 3 HIS E 497 PHE E 502 1 O PHE E 502 N GLY E 470
SHEET 1 AH8 4 LEU E 506 GLY E 510 0
SHEET 2 AH8 4 ASP E 519 ALA E 524 -1 O ASP E 519 N LEU E 509
SHEET 3 AH8 4 ALA E 533 VAL E 540 -1 O TYR E 535 N ILE E 522
SHEET 4 AH8 4 SER E 544 ILE E 545 -1 O SER E 544 N VAL E 540
SHEET 1 AH9 4 LEU E 506 GLY E 510 0
SHEET 2 AH9 4 ASP E 519 ALA E 524 -1 O ASP E 519 N LEU E 509
SHEET 3 AH9 4 ALA E 533 VAL E 540 -1 O TYR E 535 N ILE E 522
SHEET 4 AH9 4 GLN E 551 ALA E 554 -1 O GLN E 551 N LEU E 536
SHEET 1 AI1 2 VAL E 599 LEU E 600 0
SHEET 2 AI1 2 MET E 733 LEU E 734 1 O MET E 733 N LEU E 600
SHEET 1 AI2 4 VAL E 602 ILE E 609 0
SHEET 2 AI2 4 THR E 629 ILE E 639 -1 O GLN E 632 N ILE E 609
SHEET 3 AI2 4 HIS E 692 LEU E 700 -1 O LEU E 698 N VAL E 631
SHEET 4 AI2 4 THR E 672 PHE E 673 -1 N THR E 672 O LEU E 699
SHEET 1 AI3 4 SER E 680 LEU E 687 0
SHEET 2 AI3 4 SER E 654 LEU E 662 -1 N LEU E 660 O LEU E 681
SHEET 3 AI3 4 ILE E 711 THR E 718 -1 O ARG E 714 N ALA E 661
SHEET 4 AI3 4 PHE E 742 LEU E 746 -1 O LEU E 746 N ILE E 711
SHEET 1 AI4 4 LEU E 762 SER E 767 0
SHEET 2 AI4 4 GLU E 781 ASN E 790 -1 O GLU E 785 N SER E 767
SHEET 3 AI4 4 GLN E 856 VAL E 865 -1 O ALA E 861 N ALA E 784
SHEET 4 AI4 4 LEU E 808 ARG E 811 -1 N SER E 809 O ASP E 864
SHEET 1 AI5 7 LEU G 827 PRO G 833 0
SHEET 2 AI5 7 THR G 839 ILE G 846 -1 O SER G 841 N ALA G 832
SHEET 3 AI5 7 THR G 799 PRO G 805 -1 N ILE G 800 O CYS G 844
SHEET 4 AI5 7 ARG G 874 SER G 882 -1 O ASN G 880 N THR G 801
SHEET 5 AI5 7 PHE G 895 VAL G 905 -1 O LEU G 899 N LEU G 875
SHEET 6 AI5 7 PHE E 895 VAL E 905 -1 N GLN E 896 O GLU G 898
SHEET 7 AI5 7 TYR E1060 GLN E1062 1 O SER E1061 N TYR E 903
SHEET 1 AI6 7 LEU G 827 PRO G 833 0
SHEET 2 AI6 7 THR G 839 ILE G 846 -1 O SER G 841 N ALA G 832
SHEET 3 AI6 7 THR G 799 PRO G 805 -1 N ILE G 800 O CYS G 844
SHEET 4 AI6 7 ARG G 874 SER G 882 -1 O ASN G 880 N THR G 801
SHEET 5 AI6 7 PHE G 895 VAL G 905 -1 O LEU G 899 N LEU G 875
SHEET 6 AI6 7 PHE E 895 VAL E 905 -1 N GLN E 896 O GLU G 898
SHEET 7 AI6 7 LEU E 774 VAL E 776 1 N VAL E 776 O LYS E 902
SHEET 1 AI7 4 LEU G 774 VAL G 776 0
SHEET 2 AI7 4 PHE G 895 VAL G 905 1 O LYS G 902 N VAL G 776
SHEET 3 AI7 4 PHE E 895 VAL E 905 -1 N GLN E 896 O GLU G 898
SHEET 4 AI7 4 TYR E1060 GLN E1062 1 O SER E1061 N TYR E 903
SHEET 1 AI8 7 TYR G1060 GLN G1062 0
SHEET 2 AI8 7 PHE G 895 VAL G 905 1 N TYR G 903 O SER G1061
SHEET 3 AI8 7 PHE E 895 VAL E 905 -1 N GLN E 896 O GLU G 898
SHEET 4 AI8 7 ARG E 874 SER E 882 -1 N LEU E 875 O LEU E 899
SHEET 5 AI8 7 THR E 799 PRO E 805 -1 N THR E 801 O ASN E 880
SHEET 6 AI8 7 THR E 839 ILE E 846 -1 O CYS E 844 N ILE E 800
SHEET 7 AI8 7 LEU E 827 PRO E 833 -1 N THR E 828 O ARG E 845
SHEET 1 AI9 7 LEU E 827 PRO E 833 0
SHEET 2 AI9 7 THR E 839 ILE E 846 -1 O ARG E 845 N THR E 828
SHEET 3 AI9 7 THR E 799 PRO E 805 -1 N ILE E 800 O CYS E 844
SHEET 4 AI9 7 ARG E 874 SER E 882 -1 O ASN E 880 N THR E 801
SHEET 5 AI9 7 PHE E 895 VAL E 905 -1 O LEU E 899 N LEU E 875
SHEET 6 AI9 7 PHE G 895 VAL G 905 -1 O GLU G 898 N GLN E 896
SHEET 7 AI9 7 TYR G1060 GLN G1062 1 O SER G1061 N TYR G 903
SHEET 1 AJ1 4 THR E 907 SER E 911 0
SHEET 2 AJ1 4 SER E 929 ASN E 940 -1 O GLN E 937 N SER E 910
SHEET 3 AJ1 4 GLU E1023 SER E1033 -1 O PHE E1026 N TYR E 936
SHEET 4 AJ1 4 TRP E 964 SER E 970 -1 N MET E 965 O ASN E1031
SHEET 1 AJ2 4 GLU E 961 ALA E 962 0
SHEET 2 AJ2 4 LEU E 946 LEU E 958 -1 N LEU E 958 O GLU E 961
SHEET 3 AJ2 4 SER E1046 THR E1054 -1 O THR E1054 N SER E 949
SHEET 4 AJ2 4 VAL E1000 LEU E1001 1 N LEU E1001 O SER E1046
SHEET 1 AJ3 5 SER E 980 ILE E 984 0
SHEET 2 AJ3 5 GLY E1007 PHE E1018 -1 O ARG E1010 N GLU E 982
SHEET 3 AJ3 5 LEU E 946 LEU E 958 -1 N ILE E 950 O CYS E1013
SHEET 4 AJ3 5 SER E1046 THR E1054 -1 O THR E1054 N SER E 949
SHEET 5 AJ3 5 ARG E1071 VAL E1077 -1 O THR E1076 N VAL E1047
SHEET 1 AJ4 3 CYS F 40 ASP F 41 0
SHEET 2 AJ4 3 THR F 22 CYS F 24 -1 N THR F 22 O ASP F 41
SHEET 3 AJ4 3 ILE F 56 MET F 57 -1 O MET F 57 N TRP F 23
SHEET 1 AJ5 5 LEU F 62 THR F 65 0
SHEET 2 AJ5 5 LYS F 80 LEU F 85 -1 O THR F 82 N GLU F 64
SHEET 3 AJ5 5 ILE F 414 PRO F 421 1 O GLN F 418 N LEU F 83
SHEET 4 AJ5 5 GLN F 402 ALA F 408 -1 N PHE F 404 O VAL F 417
SHEET 5 AJ5 5 LEU F 347 HIS F 349 -1 N ASP F 348 O ARG F 407
SHEET 1 AJ6 5 LEU F 76 SER F 77 0
SHEET 2 AJ6 5 ALA F 91 PHE F 97 -1 O THR F 96 N SER F 77
SHEET 3 AJ6 5 ILE F 387 ALA F 395 -1 O VAL F 391 N PHE F 93
SHEET 4 AJ6 5 LEU F 356 PHE F 363 -1 N LYS F 357 O THR F 394
SHEET 5 AJ6 5 THR F 369 GLN F 373 -1 O HIS F 370 N SER F 362
SHEET 1 AJ7 6 PHE F 182 THR F 189 0
SHEET 2 AJ7 6 ARG F 143 PHE F 149 -1 N SER F 148 O ARG F 183
SHEET 3 AJ7 6 ILE F 105 ASP F 112 1 N TYR F 109 O GLY F 147
SHEET 4 AJ7 6 THR F 234 THR F 241 1 O VAL F 238 N LEU F 110
SHEET 5 AJ7 6 ILE F 294 VAL F 300 1 O ALA F 299 N PHE F 239
SHEET 6 AJ7 6 ALA F 319 GLU F 322 1 O ALA F 319 N PHE F 298
SHEET 1 AJ8 2 GLY F 441 GLU F 444 0
SHEET 2 AJ8 2 ILE F 447 CYS F 450 -1 O ILE F 447 N GLU F 444
SHEET 1 AJ9 2 TYR F 454 ILE F 455 0
SHEET 2 AJ9 2 CYS F 461 GLN F 462 -1 O CYS F 461 N ILE F 455
SHEET 1 AK1 2 GLY F 488 VAL F 491 0
SHEET 2 AK1 2 GLN F 494 CYS F 497 -1 O LEU F 496 N ASP F 489
SHEET 1 AK2 2 ILE F 507 TYR F 508 0
SHEET 2 AK2 2 CYS F 514 ASP F 515 -1 O CYS F 514 N TYR F 508
SHEET 1 AK3 2 ARG F 521 TYR F 522 0
SHEET 2 AK3 2 GLN F 525 VAL F 526 -1 O GLN F 525 N TYR F 522
SHEET 1 AK4 2 GLY F 533 PHE F 536 0
SHEET 2 AK4 2 LYS F 539 CYS F 542 -1 O LYS F 539 N PHE F 536
SHEET 1 AK5 2 PHE F 546 GLU F 547 0
SHEET 2 AK5 2 CYS F 553 GLU F 554 -1 O CYS F 553 N GLU F 547
SHEET 1 AK6 2 GLY F 572 CYS F 574 0
SHEET 2 AK6 2 CYS F 579 CYS F 581 -1 O GLU F 580 N ARG F 573
SHEET 1 AK7 4 LEU F 628 LEU F 630 0
SHEET 2 AK7 4 ARG F 662 GLU F 672 1 O ILE F 665 N GLN F 629
SHEET 3 AK7 4 TRP F 649 GLN F 657 -1 N GLU F 655 O LEU F 664
SHEET 4 AK7 4 CYS F 640 ARG F 643 -1 N CYS F 640 O TYR F 652
SHEET 1 AK8 4 THR G 9 ARG G 12 0
SHEET 2 AK8 4 GLN G 590 ARG G 595 -1 O LEU G 593 N THR G 9
SHEET 3 AK8 4 ASP G 582 ALA G 587 -1 N LEU G 583 O LEU G 594
SHEET 4 AK8 4 LEU G 569 GLN G 573 -1 N SER G 570 O ALA G 584
SHEET 1 AK9 4 VAL G 22 TYR G 25 0
SHEET 2 AK9 4 TRP G 29 GLY G 33 -1 O TRP G 29 N TYR G 25
SHEET 3 AK9 4 LEU G 47 CYS G 50 -1 O CYS G 50 N VAL G 30
SHEET 4 AK9 4 CYS G 57 PRO G 59 -1 O GLU G 58 N GLN G 49
SHEET 1 AL1 2 ILE G 38 ALA G 40 0
SHEET 2 AL1 2 GLN G 43 THR G 44 -1 O GLN G 43 N THR G 39
SHEET 1 AL2 4 SER G 76 THR G 80 0
SHEET 2 AL2 4 GLN G 85 GLU G 96 -1 O LEU G 87 N ALA G 78
SHEET 3 AL2 4 MET G 101 LEU G 110 -1 O PHE G 108 N ALA G 88
SHEET 4 AL2 4 GLN G 117 LEU G 119 -1 O LEU G 119 N CYS G 107
SHEET 1 AL3 4 ALA G 339 VAL G 340 0
SHEET 2 AL3 4 VAL G 347 GLY G 349 -1 O VAL G 347 N VAL G 340
SHEET 3 AL3 4 ALA G 360 LEU G 362 -1 O PHE G 361 N LEU G 348
SHEET 4 AL3 4 THR G 370 ILE G 372 -1 O THR G 370 N LEU G 362
SHEET 1 AL4 4 THR G 390 TRP G 395 0
SHEET 2 AL4 4 VAL G 398 ALA G 405 -1 O SER G 400 N ALA G 393
SHEET 3 AL4 4 LYS G 413 VAL G 420 -1 O LYS G 413 N ALA G 405
SHEET 4 AL4 4 GLN G 423 THR G 431 -1 O LYS G 427 N ILE G 416
SHEET 1 AL5 4 LEU G 443 VAL G 446 0
SHEET 2 AL5 4 LEU G 456 GLY G 460 -1 O LEU G 456 N VAL G 446
SHEET 3 AL5 4 VAL G 473 PRO G 477 -1 O SER G 474 N ILE G 459
SHEET 4 AL5 4 ALA G 489 LEU G 491 -1 O ALA G 489 N VAL G 475
SHEET 1 AL6 2 ARG G 469 GLY G 471 0
SHEET 2 AL6 2 HIS G 497 PHE G 502 1 O HIS G 497 N GLY G 470
SHEET 1 AL7 4 LEU G 506 GLY G 510 0
SHEET 2 AL7 4 ASP G 519 GLY G 523 -1 O ASP G 519 N GLY G 510
SHEET 3 AL7 4 ALA G 533 VAL G 540 -1 O TYR G 535 N ILE G 522
SHEET 4 AL7 4 SER G 544 ILE G 545 -1 O SER G 544 N VAL G 540
SHEET 1 AL8 4 LEU G 506 GLY G 510 0
SHEET 2 AL8 4 ASP G 519 GLY G 523 -1 O ASP G 519 N GLY G 510
SHEET 3 AL8 4 ALA G 533 VAL G 540 -1 O TYR G 535 N ILE G 522
SHEET 4 AL8 4 ARG G 552 ALA G 554 -1 O ILE G 553 N VAL G 534
SHEET 1 AL9 2 VAL G 599 LEU G 600 0
SHEET 2 AL9 2 MET G 733 LEU G 734 1 O MET G 733 N LEU G 600
SHEET 1 AM1 4 VAL G 602 ILE G 609 0
SHEET 2 AM1 4 THR G 629 ILE G 639 -1 O GLN G 632 N ILE G 609
SHEET 3 AM1 4 HIS G 692 LEU G 700 -1 O PHE G 696 N SER G 633
SHEET 4 AM1 4 THR G 672 PHE G 673 -1 N THR G 672 O LEU G 699
SHEET 1 AM2 3 SER G 680 LEU G 681 0
SHEET 2 AM2 3 SER G 655 LEU G 662 -1 N LEU G 660 O LEU G 681
SHEET 3 AM2 3 VAL G 684 VAL G 686 -1 O ARG G 685 N VAL G 656
SHEET 1 AM3 4 SER G 680 LEU G 681 0
SHEET 2 AM3 4 SER G 655 LEU G 662 -1 N LEU G 660 O LEU G 681
SHEET 3 AM3 4 ILE G 711 LEU G 719 -1 O ASN G 716 N ASP G 659
SHEET 4 AM3 4 TYR G 741 LEU G 746 -1 O PHE G 742 N LEU G 715
SHEET 1 AM4 4 LEU G 762 SER G 767 0
SHEET 2 AM4 4 GLU G 781 ASN G 790 -1 O MET G 787 N SER G 765
SHEET 3 AM4 4 GLN G 856 VAL G 865 -1 O ALA G 861 N ALA G 784
SHEET 4 AM4 4 LEU G 808 TYR G 810 -1 N SER G 809 O ASP G 864
SHEET 1 AM5 4 THR G 907 SER G 911 0
SHEET 2 AM5 4 SER G 929 ASN G 940 -1 O GLN G 937 N SER G 910
SHEET 3 AM5 4 GLU G1023 SER G1033 -1 O LEU G1028 N HIS G 934
SHEET 4 AM5 4 TRP G 964 SER G 970 -1 N GLU G 968 O LYS G1029
SHEET 1 AM6 4 GLU G 961 ALA G 962 0
SHEET 2 AM6 4 VAL G 948 LEU G 958 -1 N LEU G 958 O GLU G 961
SHEET 3 AM6 4 SER G1046 THR G1054 -1 O GLU G1052 N ASN G 951
SHEET 4 AM6 4 VAL G1000 LEU G1001 1 N LEU G1001 O SER G1046
SHEET 1 AM7 5 CYS G 979 ILE G 984 0
SHEET 2 AM7 5 GLY G1007 VAL G1015 -1 O ARG G1012 N SER G 980
SHEET 3 AM7 5 VAL G 948 LEU G 958 -1 N ILE G 950 O CYS G1013
SHEET 4 AM7 5 SER G1046 THR G1054 -1 O GLU G1052 N ASN G 951
SHEET 5 AM7 5 ARG G1071 VAL G1077 -1 O ALA G1072 N ALA G1051
SHEET 1 AM8 3 CYS H 40 ASP H 41 0
SHEET 2 AM8 3 THR H 22 CYS H 24 -1 N THR H 22 O ASP H 41
SHEET 3 AM8 3 ILE H 56 MET H 57 -1 O MET H 57 N TRP H 23
SHEET 1 AM9 5 LEU H 62 THR H 65 0
SHEET 2 AM9 5 LYS H 80 LEU H 85 -1 O THR H 82 N GLU H 64
SHEET 3 AM9 5 ILE H 414 PRO H 421 1 O GLN H 418 N LEU H 83
SHEET 4 AM9 5 GLN H 402 ALA H 408 -1 N PHE H 404 O VAL H 417
SHEET 5 AM9 5 LEU H 347 HIS H 349 -1 N ASP H 348 O ARG H 407
SHEET 1 AN1 4 LEU H 76 SER H 77 0
SHEET 2 AN1 4 ALA H 91 PHE H 97 -1 O THR H 96 N SER H 77
SHEET 3 AN1 4 ILE H 387 ALA H 395 -1 O VAL H 391 N PHE H 93
SHEET 4 AN1 4 LEU H 356 PHE H 363 -1 N THR H 359 O LYS H 392
SHEET 1 AN2 6 PHE H 182 HIS H 184 0
SHEET 2 AN2 6 ARG H 143 PHE H 149 -1 N SER H 148 O ARG H 183
SHEET 3 AN2 6 ASP H 106 ASP H 112 1 N LEU H 107 O GLY H 145
SHEET 4 AN2 6 ARG H 235 THR H 241 1 O LEU H 236 N TYR H 108
SHEET 5 AN2 6 ILE H 294 THR H 301 1 O ALA H 299 N PHE H 239
SHEET 6 AN2 6 ALA H 319 LEU H 323 1 O ALA H 319 N PHE H 298
SHEET 1 AN3 2 LEU H 443 GLU H 444 0
SHEET 2 AN3 2 ILE H 447 CYS H 448 -1 O ILE H 447 N GLU H 444
SHEET 1 AN4 2 TYR H 454 ILE H 455 0
SHEET 2 AN4 2 CYS H 461 GLN H 462 -1 O CYS H 461 N ILE H 455
SHEET 1 AN5 2 GLY H 488 VAL H 491 0
SHEET 2 AN5 2 GLN H 494 CYS H 497 -1 O GLN H 494 N VAL H 491
SHEET 1 AN6 2 ARG H 521 TYR H 522 0
SHEET 2 AN6 2 GLN H 525 VAL H 526 -1 O GLN H 525 N TYR H 522
SHEET 1 AN7 2 GLY H 533 PHE H 536 0
SHEET 2 AN7 2 LYS H 539 CYS H 542 -1 O ARG H 541 N LEU H 534
SHEET 1 AN8 2 PHE H 546 GLU H 547 0
SHEET 2 AN8 2 CYS H 553 GLU H 554 -1 O CYS H 553 N GLU H 547
SHEET 1 AN9 2 GLY H 572 CYS H 574 0
SHEET 2 AN9 2 CYS H 579 CYS H 581 -1 O GLU H 580 N ARG H 573
SHEET 1 AO1 4 LEU H 628 LEU H 630 0
SHEET 2 AO1 4 TYR H 663 VAL H 667 1 O ILE H 665 N GLN H 629
SHEET 3 AO1 4 TRP H 649 GLN H 656 -1 N GLU H 655 O LEU H 664
SHEET 4 AO1 4 ARG H 638 ARG H 643 -1 N ARG H 638 O LEU H 654
SSBOND 1 CYS A 50 CYS A 57 1555 1555 2.03
SSBOND 2 CYS A 89 CYS A 107 1555 1555 2.03
SSBOND 3 CYS A 97 CYS A 126 1555 1555 2.03
SSBOND 4 CYS A 476 CYS A 487 1555 1555 2.03
SSBOND 5 CYS A 620 CYS A 703 1555 1555 2.03
SSBOND 6 CYS A 636 CYS A 693 1555 1555 2.03
SSBOND 7 CYS A 752 CYS A 758 1555 1555 2.03
SSBOND 8 CYS A 829 CYS A 844 1555 1555 2.03
SSBOND 9 CYS A 979 CYS A 1013 1555 1555 2.04
SSBOND 10 CYS A 1003 CYS A 1008 1555 1555 2.02
SSBOND 11 CYS B 3 CYS B 21 1555 1555 2.03
SSBOND 12 CYS B 11 CYS B 425 1555 1555 2.04
SSBOND 13 CYS B 14 CYS B 40 1555 1555 2.03
SSBOND 14 CYS B 24 CYS B 51 1555 1555 2.03
SSBOND 15 CYS B 169 CYS B 176 1555 1555 2.02
SSBOND 16 CYS B 224 CYS B 264 1555 1555 2.03
SSBOND 17 CYS B 364 CYS B 378 1555 1555 2.02
SSBOND 18 CYS B 398 CYS B 423 1555 1555 2.02
SSBOND 19 CYS B 427 CYS B 445 1555 1555 2.03
SSBOND 20 CYS B 437 CYS B 448 1555 1555 2.02
SSBOND 21 CYS B 450 CYS B 459 1555 1555 2.03
SSBOND 22 CYS B 461 CYS B 492 1555 1555 2.03
SSBOND 23 CYS B 475 CYS B 490 1555 1555 2.04
SSBOND 24 CYS B 484 CYS B 495 1555 1555 2.03
SSBOND 25 CYS B 497 CYS B 512 1555 1555 2.03
SSBOND 26 CYS B 514 CYS B 537 1555 1555 2.02
SSBOND 27 CYS B 519 CYS B 535 1555 1555 2.03
SSBOND 28 CYS B 527 CYS B 540 1555 1555 2.03
SSBOND 29 CYS B 542 CYS B 551 1555 1555 2.03
SSBOND 30 CYS B 553 CYS B 576 1555 1555 2.02
SSBOND 31 CYS B 560 CYS B 574 1555 1555 2.03
SSBOND 32 CYS B 568 CYS B 579 1555 1555 2.03
SSBOND 33 CYS B 581 CYS B 590 1555 1555 2.03
SSBOND 34 CYS B 593 CYS B 596 1555 1555 2.04
SSBOND 35 CYS B 600 CYS B 640 1555 1555 2.03
SSBOND 36 CYS B 606 CYS B 625 1555 1555 2.03
SSBOND 37 CYS B 609 CYS B 621 1555 1555 2.02
SSBOND 38 CYS B 648 CYS B 673 1555 1555 2.03
SSBOND 39 CYS C 50 CYS C 57 1555 1555 2.03
SSBOND 40 CYS C 89 CYS C 107 1555 1555 2.03
SSBOND 41 CYS C 97 CYS C 126 1555 1555 2.03
SSBOND 42 CYS C 476 CYS C 487 1555 1555 2.03
SSBOND 43 CYS C 620 CYS C 703 1555 1555 2.03
SSBOND 44 CYS C 636 CYS C 693 1555 1555 2.04
SSBOND 45 CYS C 752 CYS C 758 1555 1555 2.02
SSBOND 46 CYS C 829 CYS C 844 1555 1555 2.03
SSBOND 47 CYS C 1003 CYS C 1008 1555 1555 2.03
SSBOND 48 CYS D 3 CYS D 21 1555 1555 2.03
SSBOND 49 CYS D 11 CYS D 425 1555 1555 2.04
SSBOND 50 CYS D 14 CYS D 40 1555 1555 2.03
SSBOND 51 CYS D 24 CYS D 51 1555 1555 2.03
SSBOND 52 CYS D 169 CYS D 176 1555 1555 2.03
SSBOND 53 CYS D 224 CYS D 264 1555 1555 2.03
SSBOND 54 CYS D 364 CYS D 378 1555 1555 2.04
SSBOND 55 CYS D 398 CYS D 423 1555 1555 2.04
SSBOND 56 CYS D 427 CYS D 445 1555 1555 2.03
SSBOND 57 CYS D 437 CYS D 448 1555 1555 2.03
SSBOND 58 CYS D 450 CYS D 459 1555 1555 2.03
SSBOND 59 CYS D 461 CYS D 492 1555 1555 2.02
SSBOND 60 CYS D 475 CYS D 490 1555 1555 2.03
SSBOND 61 CYS D 484 CYS D 495 1555 1555 2.03
SSBOND 62 CYS D 497 CYS D 512 1555 1555 2.03
SSBOND 63 CYS D 514 CYS D 537 1555 1555 2.03
SSBOND 64 CYS D 519 CYS D 535 1555 1555 2.03
SSBOND 65 CYS D 527 CYS D 540 1555 1555 2.03
SSBOND 66 CYS D 542 CYS D 551 1555 1555 2.03
SSBOND 67 CYS D 553 CYS D 576 1555 1555 2.02
SSBOND 68 CYS D 560 CYS D 574 1555 1555 2.03
SSBOND 69 CYS D 568 CYS D 579 1555 1555 2.03
SSBOND 70 CYS D 581 CYS D 590 1555 1555 2.03
SSBOND 71 CYS D 593 CYS D 596 1555 1555 2.03
SSBOND 72 CYS D 600 CYS D 640 1555 1555 2.04
SSBOND 73 CYS D 606 CYS D 625 1555 1555 2.03
SSBOND 74 CYS D 609 CYS D 621 1555 1555 2.02
SSBOND 75 CYS D 648 CYS D 673 1555 1555 2.03
SSBOND 76 CYS E 50 CYS E 57 1555 1555 2.03
SSBOND 77 CYS E 89 CYS E 107 1555 1555 2.03
SSBOND 78 CYS E 97 CYS E 126 1555 1555 2.04
SSBOND 79 CYS E 476 CYS E 487 1555 1555 2.04
SSBOND 80 CYS E 620 CYS E 703 1555 1555 2.03
SSBOND 81 CYS E 636 CYS E 693 1555 1555 2.03
SSBOND 82 CYS E 752 CYS E 758 1555 1555 2.03
SSBOND 83 CYS E 829 CYS E 844 1555 1555 2.03
SSBOND 84 CYS E 979 CYS E 1013 1555 1555 2.04
SSBOND 85 CYS E 1003 CYS E 1008 1555 1555 2.02
SSBOND 86 CYS F 3 CYS F 21 1555 1555 2.03
SSBOND 87 CYS F 11 CYS F 425 1555 1555 2.04
SSBOND 88 CYS F 14 CYS F 40 1555 1555 2.03
SSBOND 89 CYS F 24 CYS F 51 1555 1555 2.03
SSBOND 90 CYS F 169 CYS F 176 1555 1555 2.03
SSBOND 91 CYS F 224 CYS F 264 1555 1555 2.02
SSBOND 92 CYS F 398 CYS F 423 1555 1555 2.03
SSBOND 93 CYS F 427 CYS F 445 1555 1555 2.03
SSBOND 94 CYS F 437 CYS F 459 1555 1555 2.03
SSBOND 95 CYS F 461 CYS F 492 1555 1555 2.01
SSBOND 96 CYS F 475 CYS F 490 1555 1555 2.03
SSBOND 97 CYS F 484 CYS F 495 1555 1555 2.03
SSBOND 98 CYS F 497 CYS F 512 1555 1555 2.02
SSBOND 99 CYS F 514 CYS F 537 1555 1555 2.03
SSBOND 100 CYS F 519 CYS F 535 1555 1555 2.02
SSBOND 101 CYS F 527 CYS F 540 1555 1555 2.03
SSBOND 102 CYS F 542 CYS F 551 1555 1555 2.03
SSBOND 103 CYS F 568 CYS F 579 1555 1555 2.03
SSBOND 104 CYS F 581 CYS F 590 1555 1555 2.02
SSBOND 105 CYS F 593 CYS F 596 1555 1555 2.03
SSBOND 106 CYS F 600 CYS F 640 1555 1555 2.03
SSBOND 107 CYS F 606 CYS F 625 1555 1555 2.03
SSBOND 108 CYS F 648 CYS F 673 1555 1555 2.03
SSBOND 109 CYS G 50 CYS G 57 1555 1555 2.03
SSBOND 110 CYS G 89 CYS G 107 1555 1555 2.03
SSBOND 111 CYS G 97 CYS G 126 1555 1555 2.03
SSBOND 112 CYS G 476 CYS G 487 1555 1555 2.04
SSBOND 113 CYS G 620 CYS G 703 1555 1555 2.03
SSBOND 114 CYS G 636 CYS G 693 1555 1555 2.04
SSBOND 115 CYS G 752 CYS G 758 1555 1555 2.03
SSBOND 116 CYS G 829 CYS G 844 1555 1555 2.03
SSBOND 117 CYS G 979 CYS G 1013 1555 1555 2.03
SSBOND 118 CYS G 1003 CYS G 1008 1555 1555 2.02
SSBOND 119 CYS H 3 CYS H 21 1555 1555 2.03
SSBOND 120 CYS H 11 CYS H 425 1555 1555 2.04
SSBOND 121 CYS H 14 CYS H 40 1555 1555 2.03
SSBOND 122 CYS H 24 CYS H 51 1555 1555 2.03
SSBOND 123 CYS H 169 CYS H 176 1555 1555 2.03
SSBOND 124 CYS H 224 CYS H 264 1555 1555 2.02
SSBOND 125 CYS H 364 CYS H 378 1555 1555 2.02
SSBOND 126 CYS H 398 CYS H 423 1555 1555 2.04
SSBOND 127 CYS H 427 CYS H 445 1555 1555 2.03
SSBOND 128 CYS H 437 CYS H 448 1555 1555 2.03
SSBOND 129 CYS H 450 CYS H 459 1555 1555 2.03
SSBOND 130 CYS H 461 CYS H 492 1555 1555 2.03
SSBOND 131 CYS H 475 CYS H 490 1555 1555 2.03
SSBOND 132 CYS H 484 CYS H 495 1555 1555 2.03
SSBOND 133 CYS H 497 CYS H 512 1555 1555 2.03
SSBOND 134 CYS H 514 CYS H 537 1555 1555 2.03
SSBOND 135 CYS H 519 CYS H 535 1555 1555 2.02
SSBOND 136 CYS H 527 CYS H 540 1555 1555 2.03
SSBOND 137 CYS H 542 CYS H 551 1555 1555 2.03
SSBOND 138 CYS H 553 CYS H 576 1555 1555 2.02
SSBOND 139 CYS H 560 CYS H 574 1555 1555 2.02
SSBOND 140 CYS H 568 CYS H 579 1555 1555 2.02
SSBOND 141 CYS H 581 CYS H 590 1555 1555 2.03
SSBOND 142 CYS H 593 CYS H 596 1555 1555 2.03
SSBOND 143 CYS H 600 CYS H 640 1555 1555 2.02
SSBOND 144 CYS H 606 CYS H 625 1555 1555 2.03
SSBOND 145 CYS H 609 CYS H 621 1555 1555 2.02
SSBOND 146 CYS H 648 CYS H 673 1555 1555 2.03
LINK ND2 ASN A 42 C1 NAG A3042 1555 1555 1.47
LINK ND2 ASN A 70 C1 NAG I 1 1555 1555 1.43
LINK ND2 ASN A 373 C1 NAG J 1 1555 1555 1.45
LINK ND2 ASN A 678 C1 NAG A3678 1555 1555 1.40
LINK ND2 ASN A 716 C1 NAG K 1 1555 1555 1.45
LINK ND2 ASN A 880 C1 NAG L 1 1555 1555 1.45
LINK ND2 ASN A 920 C1 NAG A3920 1555 1555 1.45
LINK ND2 ASN A1031 C1 NAG A3031 1555 1555 1.43
LINK ND2 ASN B 94 C1 NAG M 1 1555 1555 1.43
LINK ND2 ASN B 232 C1 NAG B3232 1555 1555 1.41
LINK ND2 ASN B 620 C1 NAG B3620 1555 1555 1.41
LINK ND2 ASN C 42 C1 NAG C3042 1555 1555 1.49
LINK ND2 ASN C 70 C1 NAG N 1 1555 1555 1.43
LINK ND2 ASN C 373 C1 NAG O 1 1555 1555 1.43
LINK ND2 ASN C 678 C1 NAG C3678 1555 1555 1.41
LINK ND2 ASN C 716 C1 NAG P 1 1555 1555 1.46
LINK ND2 ASN C 880 C1 NAG Q 1 1555 1555 1.46
LINK ND2 ASN C 920 C1 NAG C3920 1555 1555 1.44
LINK ND2 ASN C1031 C1 NAG C3031 1555 1555 1.45
LINK ND2 ASN D 232 C1 NAG D3232 1555 1555 1.46
LINK ND2 ASN D 620 C1 NAG D3620 1555 1555 1.44
LINK ND2 ASN E 42 C1 NAG E3042 1555 1555 1.43
LINK ND2 ASN E 70 C1 NAG R 1 1555 1555 1.44
LINK ND2 ASN E 373 C1 NAG S 1 1555 1555 1.44
LINK ND2 ASN E 678 C1 NAG E3678 1555 1555 1.39
LINK ND2 ASN E 716 C1 NAG T 1 1555 1555 1.44
LINK ND2 ASN E 880 C1 NAG U 1 1555 1555 1.44
LINK ND2 ASN E 920 C1 NAG E3920 1555 1555 1.42
LINK ND2 ASN E1031 C1 NAG E3031 1555 1555 1.43
LINK ND2 ASN F 94 C1 NAG F3094 1555 1555 1.45
LINK ND2 ASN F 190 C1 NAG F3190 1555 1555 1.41
LINK ND2 ASN F 620 C1 NAG F3620 1555 1555 1.43
LINK ND2 ASN G 42 C1 NAG G3042 1555 1555 1.48
LINK ND2 ASN G 70 C1 NAG V 1 1555 1555 1.44
LINK ND2 ASN G 373 C1 NAG W 1 1555 1555 1.44
LINK ND2 ASN G 678 C1 NAG G3678 1555 1555 1.40
LINK ND2 ASN G 716 C1 NAG X 1 1555 1555 1.47
LINK ND2 ASN G 880 C1 NAG Y 1 1555 1555 1.44
LINK ND2 ASN G 920 C1 NAG G3920 1555 1555 1.44
LINK ND2 ASN G1031 C1 NAG G3031 1555 1555 1.43
LINK ND2 ASN H 94 C1 NAG H3094 1555 1555 1.42
LINK ND2 ASN H 190 C1 NAG H3190 1555 1555 1.40
LINK ND2 ASN H 232 C1 NAG H3232 1555 1555 1.48
LINK ND2 ASN H 620 C1 NAG H3620 1555 1555 1.47
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.42
LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.44
LINK O6 BMA I 3 C1 MAN I 4 1555 1555 1.44
LINK O6 MAN I 4 C1 MAN I 5 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45
LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.43
LINK O3 BMA J 3 C1 MAN J 4 1555 1555 1.45
LINK O6 BMA J 3 C1 MAN J 7 1555 1555 1.47
LINK O2 MAN J 4 C1 MAN J 5 1555 1555 1.45
LINK O6 MAN J 5 C1 MAN J 6 1555 1555 1.45
LINK O6 MAN J 7 C1 MAN J 8 1555 1555 1.42
LINK O3 MAN J 7 C1 MAN J 10 1555 1555 1.45
LINK O2 MAN J 8 C1 MAN J 9 1555 1555 1.44
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44
LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.45
LINK O6 BMA K 3 C1 MAN K 4 1555 1555 1.45
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.43
LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.44
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44
LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.43
LINK O3 BMA N 3 C1 MAN N 4 1555 1555 1.44
LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44
LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.46
LINK O6 BMA O 3 C1 MAN O 4 1555 1555 1.44
LINK O3 BMA O 3 C1 MAN O 7 1555 1555 1.42
LINK O6 MAN O 4 C1 MAN O 5 1555 1555 1.45
LINK O2 MAN O 5 C1 MAN O 6 1555 1555 1.44
LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.43
LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.44
LINK O6 BMA P 3 C1 MAN P 4 1555 1555 1.45
LINK O3 MAN P 4 C1 MAN P 5 1555 1555 1.45
LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45
LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.45
LINK O3 BMA Q 3 C1 MAN Q 4 1555 1555 1.45
LINK O6 BMA Q 3 C1 MAN Q 5 1555 1555 1.45
LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.45
LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.45
LINK O6 BMA R 3 C1 MAN R 4 1555 1555 1.41
LINK O3 BMA R 3 C1 MAN R 6 1555 1555 1.44
LINK O6 MAN R 4 C1 MAN R 5 1555 1555 1.43
LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44
LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.44
LINK O3 BMA S 3 C1 MAN S 4 1555 1555 1.45
LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44
LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.45
LINK O6 BMA T 3 C1 MAN T 4 1555 1555 1.44
LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.42
LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.44
LINK O3 BMA U 3 C1 MAN U 4 1555 1555 1.45
LINK O6 BMA U 3 C1 MAN U 5 1555 1555 1.44
LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45
LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.44
LINK O3 BMA V 3 C1 MAN V 4 1555 1555 1.46
LINK O6 BMA V 3 C1 MAN V 5 1555 1555 1.47
LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.43
LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.45
LINK O3 BMA W 3 C1 MAN W 4 1555 1555 1.47
LINK O6 BMA W 3 C1 MAN W 6 1555 1555 1.42
LINK O2 MAN W 4 C1 MAN W 5 1555 1555 1.44
LINK O6 MAN W 6 C1 MAN W 7 1555 1555 1.47
LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44
LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.46
LINK O6 BMA X 3 C1 MAN X 4 1555 1555 1.44
LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.46
LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.43
LINK O3 BMA Y 3 C1 MAN Y 4 1555 1555 1.45
LINK O2 MAN Y 4 C1 MAN Y 5 1555 1555 1.47
LINK OG SER A 140 MG MG A2009 1555 1555 2.14
LINK OG SER A 142 MG MG A2009 1555 1555 2.08
LINK OD1 ASP A 240 MG MG A2009 1555 1555 2.21
LINK OD1 ASP A 447 CA CA A2005 1555 1555 2.25
LINK OD1 ASP A 449 CA CA A2005 1555 1555 2.49
LINK OD1 ASP A 451 CA CA A2005 1555 1555 2.26
LINK OD2 ASP A 451 CA CA A2005 1555 1555 3.08
LINK O SER A 453 CA CA A2005 1555 1555 2.55
LINK OD1 ASP A 455 CA CA A2005 1555 1555 2.30
LINK OD2 ASP A 455 CA CA A2005 1555 1555 2.36
LINK OD1 ASP A 511 CA CA A2006 1555 1555 2.41
LINK OD1 ASN A 513 CA CA A2006 1555 1555 2.43
LINK OD1 ASP A 515 CA CA A2006 1555 1555 2.45
LINK O LEU A 517 CA CA A2006 1555 1555 2.53
LINK OD2 ASP A 519 CA CA A2006 1555 1555 2.46
LINK OD1 ASP A 574 CA CA A2007 1555 1555 2.38
LINK OG1 THR A 576 CA CA A2007 1555 1555 2.40
LINK OD1 ASP A 578 CA CA A2007 1555 1555 2.37
LINK O LEU A 580 CA CA A2007 1555 1555 2.55
LINK OD1 ASP A 582 CA CA A2007 1555 1555 2.42
LINK OD2 ASP A 582 CA CA A2007 1555 1555 2.89
LINK CA CA A2007 O HOH A4020 1555 1555 3.14
LINK MG MG A2009 O HOH A4008 1555 1555 2.13
LINK MG MG A2009 O HOH A4011 1555 1555 2.33
LINK MG MG A2009 O HOH A4012 1555 1555 2.04
LINK O SER B 116 CA CA B2002 1555 1555 2.40
LINK OD2 ASP B 120 CA CA B2002 1555 1555 2.38
LINK OE2 GLU B 325 CA CA B2002 1555 1555 3.02
LINK OD1 ASP C 447 CA CA C2005 1555 1555 3.10
LINK OD1 ASP C 449 CA CA C2005 1555 1555 2.41
LINK OD2 ASP C 449 CA CA C2005 1555 1555 2.95
LINK OD1 ASP C 451 CA CA C2005 1555 1555 2.48
LINK OD2 ASP C 451 CA CA C2005 1555 1555 2.56
LINK OD1 ASP C 455 CA CA C2005 1555 1555 2.48
LINK OD2 ASP C 455 CA CA C2005 1555 1555 2.59
LINK OD1 ASP C 511 CA CA C2006 1555 1555 2.36
LINK OD1 ASN C 513 CA CA C2006 1555 1555 2.40
LINK OD1 ASP C 515 CA CA C2006 1555 1555 2.40
LINK O LEU C 517 CA CA C2006 1555 1555 2.33
LINK OD2 ASP C 519 CA CA C2006 1555 1555 2.44
LINK OD1 ASP C 574 CA CA C2007 1555 1555 2.41
LINK OG1 THR C 576 CA CA C2007 1555 1555 2.33
LINK OD1 ASP C 578 CA CA C2007 1555 1555 2.37
LINK O LEU C 580 CA CA C2007 1555 1555 2.09
LINK OD1 ASP C 582 CA CA C2007 1555 1555 2.44
LINK OD2 ASP C 582 CA CA C2007 1555 1555 2.84
LINK CA CA C2005 O HOH C4003 1555 1555 2.43
LINK CA CA C2007 O HOH C4007 1555 1555 2.45
LINK O SER D 116 CA CA D2002 1555 1555 2.43
LINK OE2 GLU D 325 CA CA D2002 1555 1555 2.41
LINK OD1 ASP E 447 CA CA E2005 1555 1555 2.93
LINK OD1 ASP E 451 CA CA E2005 1555 1555 2.33
LINK OD2 ASP E 451 CA CA E2005 1555 1555 2.67
LINK O SER E 453 CA CA E2005 1555 1555 2.48
LINK OD1 ASP E 455 CA CA E2005 1555 1555 2.49
LINK OD2 ASP E 455 CA CA E2005 1555 1555 2.54
LINK OD1 ASP E 511 CA CA E2006 1555 1555 2.39
LINK OD1 ASN E 513 CA CA E2006 1555 1555 2.38
LINK OD1 ASP E 515 CA CA E2006 1555 1555 2.43
LINK O LEU E 517 CA CA E2006 1555 1555 2.41
LINK OD1 ASP E 519 CA CA E2006 1555 1555 3.16
LINK OD2 ASP E 519 CA CA E2006 1555 1555 2.48
LINK OD1 ASP E 574 CA CA E2007 1555 1555 2.36
LINK OG1 THR E 576 CA CA E2007 1555 1555 2.38
LINK OD1 ASP E 578 CA CA E2007 1555 1555 2.46
LINK O LEU E 580 CA CA E2007 1555 1555 2.42
LINK OD1 ASP E 582 CA CA E2007 1555 1555 2.40
LINK OD2 ASP E 582 CA CA E2007 1555 1555 2.44
LINK CA CA E2005 O HOH E4001 1555 1555 2.14
LINK O SER F 116 CA CA F2002 1555 1555 2.48
LINK OD2 ASP F 120 CA CA F2002 1555 1555 2.42
LINK OE1 GLU F 325 CA CA F2002 1555 1555 2.45
LINK OD1 ASP G 447 CA CA G2005 1555 1555 2.30
LINK OD1 ASP G 449 CA CA G2005 1555 1555 2.46
LINK OD1 ASP G 451 CA CA G2005 1555 1555 2.38
LINK O SER G 453 CA CA G2005 1555 1555 2.51
LINK OD1 ASP G 455 CA CA G2005 1555 1555 2.39
LINK OD2 ASP G 455 CA CA G2005 1555 1555 2.47
LINK OD1 ASP G 511 CA CA G2006 1555 1555 2.35
LINK OD1 ASN G 513 CA CA G2006 1555 1555 2.42
LINK OD1 ASP G 515 CA CA G2006 1555 1555 2.36
LINK O LEU G 517 CA CA G2006 1555 1555 2.47
LINK OD1 ASP G 519 CA CA G2006 1555 1555 3.16
LINK OD2 ASP G 519 CA CA G2006 1555 1555 2.48
LINK OG1 THR G 576 CA CA G2007 1555 1555 2.51
LINK OD1 ASP G 578 CA CA G2007 1555 1555 2.28
LINK O LEU G 580 CA CA G2007 1555 1555 2.56
LINK OD1 ASP G 582 CA CA G2007 1555 1555 2.32
LINK O SER H 116 CA CA H2002 1555 1555 2.39
LINK OD2 ASP H 120 CA CA H2002 1555 1555 2.32
LINK O GLU H 325 CA CA H2002 1555 1555 3.10
LINK OE2 GLU H 325 CA CA H2002 1555 1555 2.34
CISPEP 1 LEU A 119 PRO A 120 0 -8.12
CISPEP 2 ARG A 164 PRO A 165 0 2.35
CISPEP 3 LYS A 288 PRO A 289 0 1.88
CISPEP 4 ILE A 609 PRO A 610 0 3.72
CISPEP 5 SER B 77 PRO B 78 0 -3.44
CISPEP 6 LEU B 155 PRO B 156 0 6.08
CISPEP 7 LEU B 587 PRO B 588 0 -10.93
CISPEP 8 LEU C 119 PRO C 120 0 -3.58
CISPEP 9 ILE C 609 PRO C 610 0 4.49
CISPEP 10 SER D 77 PRO D 78 0 -1.61
CISPEP 11 LEU D 155 PRO D 156 0 -1.32
CISPEP 12 LEU D 587 PRO D 588 0 -0.47
CISPEP 13 LEU E 119 PRO E 120 0 -4.99
CISPEP 14 ILE E 609 PRO E 610 0 -2.23
CISPEP 15 SER F 77 PRO F 78 0 -0.74
CISPEP 16 LEU F 155 PRO F 156 0 -5.54
CISPEP 17 LEU F 587 PRO F 588 0 -6.55
CISPEP 18 LEU G 119 PRO G 120 0 -9.52
CISPEP 19 ILE G 609 PRO G 610 0 0.82
CISPEP 20 SER H 77 PRO H 78 0 -0.47
CISPEP 21 LEU H 155 PRO H 156 0 0.22
CISPEP 22 LEU H 587 PRO H 588 0 4.59
CRYST1 132.030 163.480 536.650 90.00 90.00 90.00 P 21 21 21 16
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 0.007574 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006117 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001863 0.00000
(ATOM LINES ARE NOT SHOWN.)
END