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HEADER VIRAL PROTEIN 03-MAY-24 8ZDX
TITLE CRYSTAL STRUCTURE OF MJHKU4R-COV-1 RBD BOUND TO HDPP4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE IV MEMBRANE FORM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SPIKE GLYCOPROTEIN;
COMPND 8 CHAIN: D, B;
COMPND 9 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: SEQUENCE REFERENCE FOR SOURCE ORGANISM PANGOLIN
COMPND 12 CORONAVIRUS HKU4 IS NOT AVAILABLE IN UNIPROT AT THE TIME OF
COMPND 13 BIOCURATION. CURRENT SEQUENCE REFERENCE IS FROM UNIPROT ID
COMPND 14 A0AAE8ZFM2.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DPP4, ADCP2, CD26;
SOURCE 6 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 274590;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: PANGOLIN CORONAVIRUS HKU4;
SOURCE 10 ORGANISM_TAXID: 3027597;
SOURCE 11 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 274590
KEYWDS COMPLEX OF A PANGOLIN CORONAVIRUS SPIKE PROTEIN BOUND TO RECEPTOR,
KEYWDS 2 VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.YANG,Z.LI,Y.XU,S.ZHANG
REVDAT 1 30-OCT-24 8ZDX 0
JRNL AUTH M.YANG,Z.LI,Y.XU,S.ZHANG
JRNL TITL CRYSTAL STRUCTURE OF MJHKU4R-COV-1 RBD BOUND TO HDPP4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 78995
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 3934
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.6900 - 7.7300 1.00 2771 148 0.1633 0.2064
REMARK 3 2 7.7300 - 6.2000 1.00 2756 132 0.1960 0.2533
REMARK 3 3 6.2000 - 5.4300 1.00 2741 137 0.1857 0.2395
REMARK 3 4 5.4300 - 4.9500 1.00 2703 152 0.1611 0.2096
REMARK 3 5 4.9400 - 4.6000 1.00 2741 152 0.1522 0.1732
REMARK 3 6 4.6000 - 4.3300 1.00 2718 131 0.1518 0.1689
REMARK 3 7 4.3300 - 4.1100 1.00 2708 140 0.1689 0.2020
REMARK 3 8 4.1100 - 3.9400 1.00 2714 126 0.1812 0.2299
REMARK 3 9 3.9400 - 3.7800 1.00 2710 149 0.1956 0.2641
REMARK 3 10 3.7800 - 3.6600 1.00 2747 135 0.2000 0.2397
REMARK 3 11 3.6600 - 3.5400 1.00 2724 129 0.2137 0.2711
REMARK 3 12 3.5400 - 3.4400 1.00 2683 146 0.2246 0.2866
REMARK 3 13 3.4400 - 3.3500 1.00 2731 147 0.2343 0.2928
REMARK 3 14 3.3500 - 3.2700 1.00 2670 120 0.2393 0.2882
REMARK 3 15 3.2700 - 3.2000 1.00 2751 141 0.2568 0.3142
REMARK 3 16 3.2000 - 3.1300 1.00 2672 130 0.2535 0.3252
REMARK 3 17 3.1300 - 3.0700 1.00 2729 146 0.2620 0.3347
REMARK 3 18 3.0700 - 3.0100 1.00 2702 143 0.2939 0.3335
REMARK 3 19 3.0100 - 2.9500 1.00 2723 136 0.3086 0.3434
REMARK 3 20 2.9500 - 2.9000 1.00 2671 147 0.3141 0.3157
REMARK 3 21 2.9000 - 2.8600 1.00 2703 173 0.3298 0.3675
REMARK 3 22 2.8600 - 2.8100 1.00 2708 127 0.3409 0.4115
REMARK 3 23 2.8100 - 2.7700 1.00 2672 149 0.3583 0.3806
REMARK 3 24 2.7700 - 2.7300 1.00 2736 132 0.3707 0.3999
REMARK 3 25 2.7300 - 2.7000 1.00 2673 132 0.3807 0.3821
REMARK 3 26 2.7000 - 2.6600 1.00 2689 172 0.3914 0.3919
REMARK 3 27 2.6600 - 2.6300 0.99 2678 152 0.4061 0.4591
REMARK 3 28 2.6300 - 2.6000 0.70 1837 110 0.4262 0.4757
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.140
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 : 0.002 15837
REMARK 3 ANGLE : 0.485 21531
REMARK 3 CHIRALITY : 0.045 2337
REMARK 3 PLANARITY : 0.003 2724
REMARK 3 DIHEDRAL : 14.973 5727
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 27
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 38 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6251 75.5172 129.5702
REMARK 3 T TENSOR
REMARK 3 T11: 0.8467 T22: 1.7137
REMARK 3 T33: 1.0240 T12: 0.1014
REMARK 3 T13: 0.0699 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 1.4714 L22: 0.4140
REMARK 3 L33: 2.5751 L12: 0.5518
REMARK 3 L13: -0.2797 L23: 0.4343
REMARK 3 S TENSOR
REMARK 3 S11: -0.3257 S12: -0.5838 S13: 0.3538
REMARK 3 S21: 0.0548 S22: -0.1901 S23: 0.4321
REMARK 3 S31: 0.0391 S32: -1.1666 S33: 0.3761
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 206 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9587 81.2449 134.5050
REMARK 3 T TENSOR
REMARK 3 T11: 0.8164 T22: 1.1697
REMARK 3 T33: 0.8242 T12: 0.0369
REMARK 3 T13: 0.0421 T23: 0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 1.2405 L22: 2.4332
REMARK 3 L33: 2.3395 L12: -0.2456
REMARK 3 L13: 0.4353 L23: 0.3723
REMARK 3 S TENSOR
REMARK 3 S11: -0.0962 S12: -0.3581 S13: 0.0984
REMARK 3 S21: 0.0735 S22: -0.0038 S23: 0.2961
REMARK 3 S31: -0.3711 S32: -0.1667 S33: 0.1914
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 207 THROUGH 363 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3423 65.3174 136.3304
REMARK 3 T TENSOR
REMARK 3 T11: 0.8561 T22: 1.1675
REMARK 3 T33: 0.7852 T12: -0.0014
REMARK 3 T13: 0.0145 T23: 0.2252
REMARK 3 L TENSOR
REMARK 3 L11: 0.9804 L22: 1.0693
REMARK 3 L33: 1.9218 L12: -0.1574
REMARK 3 L13: 0.1526 L23: -0.2473
REMARK 3 S TENSOR
REMARK 3 S11: 0.0048 S12: -0.5806 S13: -0.1309
REMARK 3 S21: 0.3856 S22: 0.0255 S23: 0.0214
REMARK 3 S31: 0.3675 S32: -0.3105 S33: -0.0310
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 364 THROUGH 413 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7002 47.6270 144.3336
REMARK 3 T TENSOR
REMARK 3 T11: 1.3207 T22: 1.5849
REMARK 3 T33: 1.0180 T12: -0.2955
REMARK 3 T13: 0.0852 T23: 0.4794
REMARK 3 L TENSOR
REMARK 3 L11: 2.3204 L22: 1.5959
REMARK 3 L33: 2.9154 L12: 0.6787
REMARK 3 L13: 0.9981 L23: -0.4544
REMARK 3 S TENSOR
REMARK 3 S11: 0.1673 S12: -0.9377 S13: -0.5889
REMARK 3 S21: 0.3444 S22: 0.1957 S23: 0.2878
REMARK 3 S31: 0.4234 S32: -0.2422 S33: -0.3486
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 414 THROUGH 712 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5798 50.2637 118.6783
REMARK 3 T TENSOR
REMARK 3 T11: 0.9315 T22: 0.9867
REMARK 3 T33: 0.8501 T12: -0.2847
REMARK 3 T13: 0.0227 T23: 0.2558
REMARK 3 L TENSOR
REMARK 3 L11: 1.4589 L22: 0.7684
REMARK 3 L33: 2.4038 L12: 0.1368
REMARK 3 L13: -0.0129 L23: -0.2262
REMARK 3 S TENSOR
REMARK 3 S11: 0.0242 S12: -0.4068 S13: -0.4492
REMARK 3 S21: 0.1338 S22: -0.0067 S23: 0.1881
REMARK 3 S31: 0.9054 S32: -0.7133 S33: -0.0099
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 713 THROUGH 766 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.8055 62.2736 101.1393
REMARK 3 T TENSOR
REMARK 3 T11: 0.7152 T22: 0.8286
REMARK 3 T33: 0.7571 T12: -0.0738
REMARK 3 T13: 0.0070 T23: 0.1324
REMARK 3 L TENSOR
REMARK 3 L11: 2.4487 L22: 3.4573
REMARK 3 L33: 4.5915 L12: -0.3909
REMARK 3 L13: -0.3011 L23: -0.2973
REMARK 3 S TENSOR
REMARK 3 S11: 0.2132 S12: -0.0059 S13: -0.0712
REMARK 3 S21: -0.0920 S22: -0.0999 S23: 0.3219
REMARK 3 S31: 0.5269 S32: -0.7330 S33: -0.0916
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 38 THROUGH 143 )
REMARK 3 ORIGIN FOR THE GROUP (A): 66.4731 65.0216 76.0695
REMARK 3 T TENSOR
REMARK 3 T11: 0.7348 T22: 0.9680
REMARK 3 T33: 0.7756 T12: 0.1880
REMARK 3 T13: -0.0070 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 2.6651 L22: 1.0396
REMARK 3 L33: 1.3778 L12: 0.8743
REMARK 3 L13: 0.1555 L23: 0.6919
REMARK 3 S TENSOR
REMARK 3 S11: -0.0648 S12: 0.2916 S13: -0.2500
REMARK 3 S21: 0.0873 S22: 0.2276 S23: -0.3649
REMARK 3 S31: 0.4424 S32: 0.7324 S33: -0.1807
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 144 THROUGH 297 )
REMARK 3 ORIGIN FOR THE GROUP (A): 66.3629 83.3748 94.1906
REMARK 3 T TENSOR
REMARK 3 T11: 0.4807 T22: 0.8266
REMARK 3 T33: 0.6753 T12: 0.0068
REMARK 3 T13: 0.0059 T23: 0.0646
REMARK 3 L TENSOR
REMARK 3 L11: 1.4705 L22: 1.3186
REMARK 3 L33: 1.7624 L12: 0.4600
REMARK 3 L13: -0.1499 L23: -0.3931
REMARK 3 S TENSOR
REMARK 3 S11: 0.0023 S12: 0.0057 S13: -0.1134
REMARK 3 S21: 0.0784 S22: 0.0126 S23: -0.2559
REMARK 3 S31: 0.0497 S32: 0.6405 S33: -0.0171
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 298 THROUGH 766 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.6268 82.7309 75.1564
REMARK 3 T TENSOR
REMARK 3 T11: 0.4969 T22: 0.6690
REMARK 3 T33: 0.6097 T12: 0.0863
REMARK 3 T13: -0.0290 T23: 0.1418
REMARK 3 L TENSOR
REMARK 3 L11: 1.0374 L22: 0.8732
REMARK 3 L33: 1.8702 L12: 0.1755
REMARK 3 L13: -0.3013 L23: 0.2537
REMARK 3 S TENSOR
REMARK 3 S11: 0.0100 S12: 0.3160 S13: 0.1314
REMARK 3 S21: -0.1729 S22: 0.0107 S23: 0.0985
REMARK 3 S31: -0.2111 S32: -0.1615 S33: -0.0227
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 389 THROUGH 403 )
REMARK 3 ORIGIN FOR THE GROUP (A): 84.9665 122.7556 114.3075
REMARK 3 T TENSOR
REMARK 3 T11: 1.1525 T22: 1.7176
REMARK 3 T33: 0.6603 T12: 0.0366
REMARK 3 T13: 0.0438 T23: 0.0759
REMARK 3 L TENSOR
REMARK 3 L11: 1.4440 L22: 1.8742
REMARK 3 L33: 2.2140 L12: -1.2171
REMARK 3 L13: -0.2366 L23: -1.1613
REMARK 3 S TENSOR
REMARK 3 S11: 0.1416 S12: -1.1616 S13: 0.3251
REMARK 3 S21: 0.9366 S22: -0.1474 S23: -0.2415
REMARK 3 S31: -0.4967 S32: 0.9522 S33: 0.0389
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 404 THROUGH 492 )
REMARK 3 ORIGIN FOR THE GROUP (A): 88.1163 121.2784 101.5751
REMARK 3 T TENSOR
REMARK 3 T11: 0.6855 T22: 1.1268
REMARK 3 T33: 0.7313 T12: 0.0579
REMARK 3 T13: -0.0489 T23: -0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 1.8780 L22: 4.0306
REMARK 3 L33: 3.5281 L12: 1.4658
REMARK 3 L13: 0.6621 L23: -0.5884
REMARK 3 S TENSOR
REMARK 3 S11: 0.0180 S12: -0.4472 S13: -0.1246
REMARK 3 S21: 0.1241 S22: -0.1093 S23: -0.4896
REMARK 3 S31: 0.0115 S32: 0.7738 S33: 0.0095
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 493 THROUGH 514 )
REMARK 3 ORIGIN FOR THE GROUP (A): 76.6209 110.5119 104.6592
REMARK 3 T TENSOR
REMARK 3 T11: 0.8081 T22: 0.8001
REMARK 3 T33: 0.5341 T12: -0.0527
REMARK 3 T13: 0.0850 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 3.4617 L22: 4.8377
REMARK 3 L33: 2.9024 L12: -0.5757
REMARK 3 L13: -1.1897 L23: -1.0969
REMARK 3 S TENSOR
REMARK 3 S11: -0.1187 S12: -0.7229 S13: -0.0067
REMARK 3 S21: 0.7635 S22: 0.2330 S23: -0.1411
REMARK 3 S31: -0.1681 S32: 1.1841 S33: -0.1725
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 515 THROUGH 534 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.2591 117.1995 90.5914
REMARK 3 T TENSOR
REMARK 3 T11: 0.8077 T22: 1.0824
REMARK 3 T33: 0.7678 T12: 0.0311
REMARK 3 T13: -0.0751 T23: 0.0742
REMARK 3 L TENSOR
REMARK 3 L11: 5.9581 L22: 3.3934
REMARK 3 L33: 1.2789 L12: 3.0709
REMARK 3 L13: 1.0310 L23: 1.9211
REMARK 3 S TENSOR
REMARK 3 S11: -0.0184 S12: 0.1710 S13: 0.1669
REMARK 3 S21: -0.0953 S22: 0.2340 S23: -0.1249
REMARK 3 S31: -0.1108 S32: 0.3359 S33: -0.1608
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 535 THROUGH 546 )
REMARK 3 ORIGIN FOR THE GROUP (A): 69.0128 109.5343 105.5635
REMARK 3 T TENSOR
REMARK 3 T11: 1.0691 T22: 1.4278
REMARK 3 T33: 0.8609 T12: -0.0446
REMARK 3 T13: 0.1227 T23: 0.1320
REMARK 3 L TENSOR
REMARK 3 L11: 3.2156 L22: 0.8292
REMARK 3 L33: 1.9425 L12: -1.1892
REMARK 3 L13: 0.4358 L23: 0.6995
REMARK 3 S TENSOR
REMARK 3 S11: 0.3755 S12: -1.2030 S13: -0.3104
REMARK 3 S21: 1.1047 S22: -0.1539 S23: 0.0428
REMARK 3 S31: 0.4995 S32: -0.0205 S33: -0.0242
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 547 THROUGH 560 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.1649 116.8829 97.8855
REMARK 3 T TENSOR
REMARK 3 T11: 0.7653 T22: 1.1417
REMARK 3 T33: 0.8312 T12: 0.0085
REMARK 3 T13: -0.0030 T23: 0.0442
REMARK 3 L TENSOR
REMARK 3 L11: 7.2413 L22: 7.3103
REMARK 3 L33: 4.8595 L12: -0.3505
REMARK 3 L13: 1.8462 L23: 0.1576
REMARK 3 S TENSOR
REMARK 3 S11: -0.2068 S12: -0.8084 S13: 0.5367
REMARK 3 S21: 0.4475 S22: -0.0331 S23: 0.6648
REMARK 3 S31: 0.0617 S32: -0.6682 S33: 0.2904
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 561 THROUGH 574 )
REMARK 3 ORIGIN FOR THE GROUP (A): 75.0728 106.0670 102.8462
REMARK 3 T TENSOR
REMARK 3 T11: 0.8797 T22: 0.7111
REMARK 3 T33: 0.8784 T12: -0.0530
REMARK 3 T13: 0.0585 T23: 0.1414
REMARK 3 L TENSOR
REMARK 3 L11: 4.9373 L22: 4.6232
REMARK 3 L33: 3.0564 L12: -1.6860
REMARK 3 L13: 0.9201 L23: -0.2861
REMARK 3 S TENSOR
REMARK 3 S11: 0.0789 S12: -0.6181 S13: -0.1078
REMARK 3 S21: 0.2123 S22: 0.2245 S23: -0.4030
REMARK 3 S31: 0.5888 S32: 0.4580 S33: -0.3967
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 575 THROUGH 596 )
REMARK 3 ORIGIN FOR THE GROUP (A): 90.5080 130.8129 104.7449
REMARK 3 T TENSOR
REMARK 3 T11: 0.8989 T22: 1.2727
REMARK 3 T33: 0.8033 T12: -0.0430
REMARK 3 T13: 0.0033 T23: -0.1353
REMARK 3 L TENSOR
REMARK 3 L11: 4.5878 L22: 2.3745
REMARK 3 L33: 5.2846 L12: 2.7188
REMARK 3 L13: -0.9242 L23: -2.4074
REMARK 3 S TENSOR
REMARK 3 S11: 0.1735 S12: -0.2203 S13: 0.5011
REMARK 3 S21: 1.2097 S22: 0.1038 S23: -0.2436
REMARK 3 S31: -1.0918 S32: 0.6679 S33: -0.3218
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 389 THROUGH 407 )
REMARK 3 ORIGIN FOR THE GROUP (A): 73.6558 70.1361 164.5601
REMARK 3 T TENSOR
REMARK 3 T11: 1.0959 T22: 2.0418
REMARK 3 T33: 1.0325 T12: -0.3927
REMARK 3 T13: 0.0834 T23: 0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 0.2025 L22: 0.9401
REMARK 3 L33: 0.2283 L12: -0.1387
REMARK 3 L13: -0.1430 L23: -0.2256
REMARK 3 S TENSOR
REMARK 3 S11: -0.2132 S12: 0.4761 S13: 0.3900
REMARK 3 S21: -0.2298 S22: 0.3833 S23: -0.4179
REMARK 3 S31: -0.6899 S32: 1.2655 S33: -0.2998
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 408 THROUGH 418 )
REMARK 3 ORIGIN FOR THE GROUP (A): 77.4184 64.7723 173.3283
REMARK 3 T TENSOR
REMARK 3 T11: 1.0036 T22: 2.0363
REMARK 3 T33: 1.2528 T12: -0.0388
REMARK 3 T13: -0.0546 T23: -0.2418
REMARK 3 L TENSOR
REMARK 3 L11: 0.2866 L22: 1.7034
REMARK 3 L33: 3.2871 L12: 0.0546
REMARK 3 L13: 0.1240 L23: 1.7623
REMARK 3 S TENSOR
REMARK 3 S11: -0.3092 S12: 0.1657 S13: 0.4442
REMARK 3 S21: 0.2405 S22: 0.6282 S23: -0.9054
REMARK 3 S31: -0.2555 S32: 1.7278 S33: -0.4007
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 419 THROUGH 434 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.0129 73.5847 175.2416
REMARK 3 T TENSOR
REMARK 3 T11: 1.3805 T22: 1.3819
REMARK 3 T33: 1.1898 T12: 0.0502
REMARK 3 T13: -0.0355 T23: -0.1486
REMARK 3 L TENSOR
REMARK 3 L11: 4.3127 L22: 4.3218
REMARK 3 L33: 4.4960 L12: 0.0622
REMARK 3 L13: 1.8113 L23: -3.0061
REMARK 3 S TENSOR
REMARK 3 S11: -1.0063 S12: -0.0604 S13: 0.1630
REMARK 3 S21: 0.5679 S22: 1.1466 S23: -0.9818
REMARK 3 S31: -1.2880 S32: -0.2901 S33: -0.0535
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 435 THROUGH 455 )
REMARK 3 ORIGIN FOR THE GROUP (A): 69.3139 64.5397 176.8782
REMARK 3 T TENSOR
REMARK 3 T11: 1.0873 T22: 1.7141
REMARK 3 T33: 1.0128 T12: -0.1144
REMARK 3 T13: -0.0198 T23: -0.2256
REMARK 3 L TENSOR
REMARK 3 L11: 3.9739 L22: 4.8952
REMARK 3 L33: 5.6116 L12: -1.2996
REMARK 3 L13: 0.8381 L23: -1.8454
REMARK 3 S TENSOR
REMARK 3 S11: -0.1454 S12: -0.9178 S13: 0.5523
REMARK 3 S21: 0.6733 S22: 0.6116 S23: -0.8035
REMARK 3 S31: -0.6004 S32: 0.4693 S33: -0.3251
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 456 THROUGH 492 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.8664 64.1475 166.1362
REMARK 3 T TENSOR
REMARK 3 T11: 0.9101 T22: 1.2831
REMARK 3 T33: 0.8710 T12: 0.0168
REMARK 3 T13: 0.0966 T23: 0.1549
REMARK 3 L TENSOR
REMARK 3 L11: 2.0208 L22: 3.6056
REMARK 3 L33: 3.8742 L12: -0.9518
REMARK 3 L13: 0.8906 L23: -1.1395
REMARK 3 S TENSOR
REMARK 3 S11: -0.0138 S12: -0.5427 S13: 0.0785
REMARK 3 S21: -0.2592 S22: 0.4222 S23: 0.2328
REMARK 3 S31: -0.0597 S32: -0.4047 S33: -0.5875
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 493 THROUGH 503 )
REMARK 3 ORIGIN FOR THE GROUP (A): 68.5964 80.9510 160.2954
REMARK 3 T TENSOR
REMARK 3 T11: 1.7302 T22: 1.5023
REMARK 3 T33: 1.0510 T12: -0.2804
REMARK 3 T13: -0.0068 T23: 0.1045
REMARK 3 L TENSOR
REMARK 3 L11: 5.0920 L22: 2.1183
REMARK 3 L33: 1.1926 L12: 1.2105
REMARK 3 L13: -1.7211 L23: -1.4545
REMARK 3 S TENSOR
REMARK 3 S11: -0.1546 S12: -0.8159 S13: -0.0097
REMARK 3 S21: 0.1153 S22: 0.7240 S23: -0.3163
REMARK 3 S31: 1.1731 S32: -0.6965 S33: -0.5269
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 504 THROUGH 547 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.3243 57.7308 150.0669
REMARK 3 T TENSOR
REMARK 3 T11: 1.2115 T22: 1.4383
REMARK 3 T33: 0.8837 T12: -0.0071
REMARK 3 T13: 0.0416 T23: 0.2970
REMARK 3 L TENSOR
REMARK 3 L11: 4.0066 L22: 2.1919
REMARK 3 L33: 5.1471 L12: -0.8090
REMARK 3 L13: 1.5884 L23: 2.7051
REMARK 3 S TENSOR
REMARK 3 S11: 0.3723 S12: 0.4876 S13: 0.1285
REMARK 3 S21: -0.2768 S22: 0.1808 S23: 0.0328
REMARK 3 S31: 0.1899 S32: 0.7362 S33: -0.4950
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 548 THROUGH 569 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.0857 54.8817 145.2679
REMARK 3 T TENSOR
REMARK 3 T11: 1.2877 T22: 1.6077
REMARK 3 T33: 0.9255 T12: 0.1457
REMARK 3 T13: -0.0058 T23: 0.1827
REMARK 3 L TENSOR
REMARK 3 L11: 3.7955 L22: 6.0241
REMARK 3 L33: 2.7773 L12: -2.5687
REMARK 3 L13: -1.9106 L23: 3.5875
REMARK 3 S TENSOR
REMARK 3 S11: -0.0250 S12: 0.4688 S13: -0.4982
REMARK 3 S21: -0.3465 S22: 0.3229 S23: -0.0699
REMARK 3 S31: 0.4510 S32: 0.3590 S33: -0.0558
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 570 THROUGH 583 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.3046 73.6947 165.1845
REMARK 3 T TENSOR
REMARK 3 T11: 1.2370 T22: 1.3769
REMARK 3 T33: 1.0799 T12: -0.2504
REMARK 3 T13: 0.0187 T23: 0.1346
REMARK 3 L TENSOR
REMARK 3 L11: 2.1405 L22: 0.9788
REMARK 3 L33: 4.8882 L12: 0.8007
REMARK 3 L13: 1.2543 L23: 2.1490
REMARK 3 S TENSOR
REMARK 3 S11: -0.2536 S12: 0.3906 S13: 1.1430
REMARK 3 S21: -0.4606 S22: -0.3347 S23: -0.4362
REMARK 3 S31: -1.0191 S32: 0.7399 S33: 0.5438
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 584 THROUGH 594 )
REMARK 3 ORIGIN FOR THE GROUP (A): 77.1168 57.2191 182.3013
REMARK 3 T TENSOR
REMARK 3 T11: 1.3291 T22: 1.9702
REMARK 3 T33: 1.2543 T12: 0.2133
REMARK 3 T13: -0.3725 T23: -0.1738
REMARK 3 L TENSOR
REMARK 3 L11: 5.3099 L22: 6.5311
REMARK 3 L33: 4.2587 L12: 5.7067
REMARK 3 L13: 1.1158 L23: -0.0731
REMARK 3 S TENSOR
REMARK 3 S11: 0.1005 S12: -0.7922 S13: -0.6764
REMARK 3 S21: 1.7982 S22: -0.3706 S23: -2.8655
REMARK 3 S31: 0.6007 S32: 2.0474 S33: 0.1859
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 8ZDX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 08-MAY-24.
REMARK 100 THE DEPOSITION ID IS D_1300047544.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-23
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 : SSRF
REMARK 200 BEAMLINE : BL02U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979183
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79444
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.950
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.8500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES (PH 7.0) AND 10% (WT/VOL)
REMARK 280 PEG 6000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 60.95050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, B, E, F, G, H, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B 595
REMARK 465 LEU B 596
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 ARG A 40 -132.04 -134.10
REMARK 500 SER A 64 -152.30 -144.62
REMARK 500 HIS A 66 5.40 -158.86
REMARK 500 ASN A 74 17.42 58.43
REMARK 500 GLN A 123 -89.61 -116.34
REMARK 500 TRP A 124 -153.87 -105.05
REMARK 500 TYR A 128 148.56 -170.43
REMARK 500 HIS A 162 40.16 -144.90
REMARK 500 PRO A 178 0.43 -61.20
REMARK 500 ILE A 193 -63.13 -127.10
REMARK 500 ASP A 200 -152.23 -82.10
REMARK 500 VAL A 207 -75.94 -117.07
REMARK 500 SER A 242 -150.62 63.03
REMARK 500 ALA A 306 -72.93 -105.26
REMARK 500 THR A 307 -141.10 -92.82
REMARK 500 GLN A 320 40.20 -76.99
REMARK 500 GLU A 378 -33.39 69.44
REMARK 500 TRP A 402 -179.94 -170.52
REMARK 500 LYS A 441 72.12 -114.03
REMARK 500 CYS A 444 95.45 -69.65
REMARK 500 ASN A 450 69.69 -162.66
REMARK 500 ASP A 515 -159.66 -148.39
REMARK 500 ARG A 597 40.32 -152.97
REMARK 500 THR A 600 -77.64 -114.94
REMARK 500 ASN A 621 5.15 -69.63
REMARK 500 SER A 630 -117.34 53.71
REMARK 500 ASP A 678 -96.02 -109.50
REMARK 500 ARG A 691 33.20 -99.23
REMARK 500 ASN A 710 -86.78 -86.72
REMARK 500 ASP A 739 -161.51 -101.57
REMARK 500 GLN C 123 -92.31 -103.57
REMARK 500 TRP C 124 -147.32 -100.17
REMARK 500 HIS C 162 23.18 -140.05
REMARK 500 ILE C 193 -64.27 -123.15
REMARK 500 SER C 242 -159.81 58.21
REMARK 500 SER C 275 36.26 -88.20
REMARK 500 ALA C 306 -72.47 -96.24
REMARK 500 THR C 307 -168.31 -102.93
REMARK 500 GLN C 320 41.42 -79.63
REMARK 500 ASN C 420 41.79 -107.86
REMARK 500 TYR C 547 -57.14 -128.52
REMARK 500 HIS C 592 20.48 -73.74
REMARK 500 ARG C 597 52.54 -154.24
REMARK 500 THR C 600 -93.35 -112.65
REMARK 500 SER C 630 -115.01 55.56
REMARK 500 PRO C 674 64.39 -69.79
REMARK 500 ASP C 678 -91.23 -131.36
REMARK 500 ASN C 679 29.79 -142.74
REMARK 500 ALA C 707 33.91 -99.30
REMARK 500 ASN C 710 -78.83 -85.92
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8ZDX A 38 766 UNP P27487 DPP4_HUMAN 38 766
DBREF 8ZDX C 38 766 UNP P27487 DPP4_HUMAN 38 766
DBREF1 8ZDX D 389 596 UNP A0AAE8ZFM2_9BETC
DBREF2 8ZDX D A0AAE8ZFM2 389 596
DBREF1 8ZDX B 389 596 UNP A0AAE8ZFM2_9BETC
DBREF2 8ZDX B A0AAE8ZFM2 389 596
SEQADV 8ZDX ALA D 482 UNP A0AAE8ZFM SER 482 CONFLICT
SEQADV 8ZDX GLU D 544 UNP A0AAE8ZFM VAL 544 CONFLICT
SEQADV 8ZDX ALA B 482 UNP A0AAE8ZFM SER 482 CONFLICT
SEQADV 8ZDX GLU B 544 UNP A0AAE8ZFM VAL 544 CONFLICT
SEQRES 1 A 729 ASP SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS
SEQRES 2 A 729 ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE
SEQRES 3 A 729 SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE
SEQRES 4 A 729 LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE
SEQRES 5 A 729 LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE
SEQRES 6 A 729 ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU
SEQRES 7 A 729 LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR
SEQRES 8 A 729 THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN
SEQRES 9 A 729 LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP
SEQRES 10 A 729 VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL
SEQRES 11 A 729 TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU
SEQRES 12 A 729 PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE
SEQRES 13 A 729 ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU
SEQRES 14 A 729 VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN
SEQRES 15 A 729 GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU
SEQRES 16 A 729 VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER
SEQRES 17 A 729 LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS
SEQRES 18 A 729 ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL
SEQRES 19 A 729 ASN THR ASP SER LEU SER SER VAL THR ASN ALA THR SER
SEQRES 20 A 729 ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP
SEQRES 21 A 729 HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG
SEQRES 22 A 729 ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER
SEQRES 23 A 729 VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG
SEQRES 24 A 729 TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER
SEQRES 25 A 729 THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO
SEQRES 26 A 729 HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE
SEQRES 27 A 729 SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN
SEQRES 28 A 729 ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR
SEQRES 29 A 729 TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR
SEQRES 30 A 729 LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY
SEQRES 31 A 729 GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR
SEQRES 32 A 729 LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG
SEQRES 33 A 729 CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS
SEQRES 34 A 729 TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU
SEQRES 35 A 729 TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG
SEQRES 36 A 729 VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN
SEQRES 37 A 729 ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE
SEQRES 38 A 729 LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO
SEQRES 39 A 729 PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU
SEQRES 40 A 729 ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR
SEQRES 41 A 729 VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR
SEQRES 42 A 729 GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER
SEQRES 43 A 729 GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG
SEQRES 44 A 729 ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA
SEQRES 45 A 729 ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS
SEQRES 46 A 729 ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL
SEQRES 47 A 729 THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS
SEQRES 48 A 729 CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR
SEQRES 49 A 729 TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO
SEQRES 50 A 729 THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR
SEQRES 51 A 729 VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR
SEQRES 52 A 729 LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE
SEQRES 53 A 729 GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL
SEQRES 54 A 729 GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP
SEQRES 55 A 729 HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR
SEQRES 56 A 729 THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU
SEQRES 57 A 729 PRO
SEQRES 1 C 729 ASP SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS
SEQRES 2 C 729 ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE
SEQRES 3 C 729 SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE
SEQRES 4 C 729 LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE
SEQRES 5 C 729 LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE
SEQRES 6 C 729 ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU
SEQRES 7 C 729 LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR
SEQRES 8 C 729 THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN
SEQRES 9 C 729 LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP
SEQRES 10 C 729 VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL
SEQRES 11 C 729 TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU
SEQRES 12 C 729 PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE
SEQRES 13 C 729 ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU
SEQRES 14 C 729 VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN
SEQRES 15 C 729 GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU
SEQRES 16 C 729 VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER
SEQRES 17 C 729 LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS
SEQRES 18 C 729 ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL
SEQRES 19 C 729 ASN THR ASP SER LEU SER SER VAL THR ASN ALA THR SER
SEQRES 20 C 729 ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP
SEQRES 21 C 729 HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG
SEQRES 22 C 729 ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER
SEQRES 23 C 729 VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG
SEQRES 24 C 729 TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER
SEQRES 25 C 729 THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO
SEQRES 26 C 729 HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE
SEQRES 27 C 729 SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN
SEQRES 28 C 729 ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR
SEQRES 29 C 729 TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR
SEQRES 30 C 729 LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY
SEQRES 31 C 729 GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR
SEQRES 32 C 729 LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG
SEQRES 33 C 729 CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS
SEQRES 34 C 729 TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU
SEQRES 35 C 729 TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG
SEQRES 36 C 729 VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN
SEQRES 37 C 729 ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE
SEQRES 38 C 729 LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO
SEQRES 39 C 729 PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU
SEQRES 40 C 729 ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR
SEQRES 41 C 729 VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR
SEQRES 42 C 729 GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER
SEQRES 43 C 729 GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG
SEQRES 44 C 729 ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA
SEQRES 45 C 729 ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS
SEQRES 46 C 729 ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL
SEQRES 47 C 729 THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS
SEQRES 48 C 729 CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR
SEQRES 49 C 729 TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO
SEQRES 50 C 729 THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR
SEQRES 51 C 729 VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR
SEQRES 52 C 729 LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE
SEQRES 53 C 729 GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL
SEQRES 54 C 729 GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP
SEQRES 55 C 729 HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR
SEQRES 56 C 729 THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU
SEQRES 57 C 729 PRO
SEQRES 1 D 208 LYS GLU CYS ASP PHE THR PRO MET LEU VAL GLY VAL PRO
SEQRES 2 D 208 PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE THR ASN
SEQRES 3 D 208 CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE MET
SEQRES 4 D 208 VAL ASN GLU PHE SER CYS ASN GLY ILE SER PRO ASP ALA
SEQRES 5 D 208 ILE ALA ARG GLY CYS TYR SER SER LEU THR VAL ASP TYR
SEQRES 6 D 208 PHE ALA TYR PRO LEU SER MET ARG SER TYR ILE GLN PRO
SEQRES 7 D 208 GLY SER ALA GLY ASP ILE SER LEU TYR ASN TYR LYS GLN
SEQRES 8 D 208 SER PHE ALA ASN PRO THR CYS ARG VAL LEU ALA THR ALA
SEQRES 9 D 208 PRO ALA ASN LEU THR LEU THR LYS PRO SER ALA TYR GLY
SEQRES 10 D 208 TYR PHE GLN LYS CYS SER ARG VAL SER GLY GLU HIS ASN
SEQRES 11 D 208 SER VAL GLU THR PRO LEU TYR ILE ASN PRO GLY GLU TYR
SEQRES 12 D 208 SER ILE CYS ARG SER PHE SER PRO TYR GLY PHE SER GLU
SEQRES 13 D 208 ASP GLY GLU VAL PHE ARG ARG GLN LEU THR GLN TYR GLU
SEQRES 14 D 208 GLY GLY GLY ILE LEU VAL GLY VAL GLY ALA LYS LEU ALA
SEQRES 15 D 208 MET THR ASP LYS LEU GLU MET GLY PHE ILE ILE SER VAL
SEQRES 16 D 208 GLN TYR GLY THR ASP THR ASN SER VAL CYS PRO MET LEU
SEQRES 1 B 208 LYS GLU CYS ASP PHE THR PRO MET LEU VAL GLY VAL PRO
SEQRES 2 B 208 PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE THR ASN
SEQRES 3 B 208 CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE MET
SEQRES 4 B 208 VAL ASN GLU PHE SER CYS ASN GLY ILE SER PRO ASP ALA
SEQRES 5 B 208 ILE ALA ARG GLY CYS TYR SER SER LEU THR VAL ASP TYR
SEQRES 6 B 208 PHE ALA TYR PRO LEU SER MET ARG SER TYR ILE GLN PRO
SEQRES 7 B 208 GLY SER ALA GLY ASP ILE SER LEU TYR ASN TYR LYS GLN
SEQRES 8 B 208 SER PHE ALA ASN PRO THR CYS ARG VAL LEU ALA THR ALA
SEQRES 9 B 208 PRO ALA ASN LEU THR LEU THR LYS PRO SER ALA TYR GLY
SEQRES 10 B 208 TYR PHE GLN LYS CYS SER ARG VAL SER GLY GLU HIS ASN
SEQRES 11 B 208 SER VAL GLU THR PRO LEU TYR ILE ASN PRO GLY GLU TYR
SEQRES 12 B 208 SER ILE CYS ARG SER PHE SER PRO TYR GLY PHE SER GLU
SEQRES 13 B 208 ASP GLY GLU VAL PHE ARG ARG GLN LEU THR GLN TYR GLU
SEQRES 14 B 208 GLY GLY GLY ILE LEU VAL GLY VAL GLY ALA LYS LEU ALA
SEQRES 15 B 208 MET THR ASP LYS LEU GLU MET GLY PHE ILE ILE SER VAL
SEQRES 16 B 208 GLN TYR GLY THR ASP THR ASN SER VAL CYS PRO MET LEU
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG C 801 14
HET EPE C 802 15
HET NAG D 601 14
HET NAG B 601 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
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 EPE HEPES
FORMUL 5 NAG 16(C8 H15 N O6)
FORMUL 5 BMA 2(C6 H12 O6)
FORMUL 14 EPE C8 H18 N2 O4 S
FORMUL 17 HOH *23(H2 O)
HELIX 1 AA1 THR A 44 LYS A 50 1 7
HELIX 2 AA2 ASN A 92 ASP A 96 5 5
HELIX 3 AA3 ASP A 200 VAL A 207 1 8
HELIX 4 AA4 VAL A 341 GLN A 344 5 4
HELIX 5 AA5 GLU A 421 MET A 425 5 5
HELIX 6 AA6 LYS A 463 ALA A 465 5 3
HELIX 7 AA7 ASN A 497 GLN A 505 1 9
HELIX 8 AA8 ASN A 562 THR A 570 1 9
HELIX 9 AA9 GLN A 586 HIS A 592 1 7
HELIX 10 AB1 ALA A 593 ASN A 595 5 3
HELIX 11 AB2 THR A 600 LYS A 615 1 16
HELIX 12 AB3 SER A 630 GLY A 641 1 12
HELIX 13 AB4 ARG A 658 TYR A 662 5 5
HELIX 14 AB5 ASP A 663 GLY A 672 1 10
HELIX 15 AB6 ASN A 679 ASN A 685 1 7
HELIX 16 AB7 SER A 686 THR A 687 5 2
HELIX 17 AB8 VAL A 688 VAL A 698 5 11
HELIX 18 AB9 HIS A 712 GLY A 727 1 16
HELIX 19 AC1 SER A 744 PHE A 763 1 20
HELIX 20 AC2 THR C 44 LYS C 50 1 7
HELIX 21 AC3 ASP C 200 VAL C 207 1 8
HELIX 22 AC4 PRO C 290 ILE C 295 1 6
HELIX 23 AC5 VAL C 341 GLN C 344 5 4
HELIX 24 AC6 GLU C 421 MET C 425 5 5
HELIX 25 AC7 LYS C 463 ALA C 465 5 3
HELIX 26 AC8 ASN C 497 GLN C 505 1 9
HELIX 27 AC9 ASN C 562 THR C 570 1 9
HELIX 28 AD1 GLY C 587 HIS C 592 1 6
HELIX 29 AD2 ALA C 593 ASN C 595 5 3
HELIX 30 AD3 THR C 600 MET C 616 1 17
HELIX 31 AD4 SER C 630 GLY C 641 1 12
HELIX 32 AD5 ASP C 663 MET C 671 1 9
HELIX 33 AD6 ASN C 679 SER C 686 1 8
HELIX 34 AD7 VAL C 688 VAL C 698 5 11
HELIX 35 AD8 HIS C 712 ASP C 725 1 14
HELIX 36 AD9 SER C 744 PHE C 763 1 20
HELIX 37 AE1 PHE D 393 LEU D 397 5 5
HELIX 38 AE2 GLN D 403 PHE D 407 5 5
HELIX 39 AE3 ASN D 418 LEU D 425 1 8
HELIX 40 AE4 ASP D 439 ARG D 443 5 5
HELIX 41 AE5 PRO D 457 GLN D 465 5 9
HELIX 42 AE6 GLY D 470 ASN D 476 1 7
HELIX 43 AE7 GLY D 515 SER D 519 5 5
HELIX 44 AE8 CYS D 534 SER D 538 5 5
HELIX 45 AE9 PHE B 393 VAL B 398 5 6
HELIX 46 AF1 ASN B 418 LEU B 425 1 8
HELIX 47 AF2 ASP B 439 ARG B 443 5 5
HELIX 48 AF3 PRO B 457 ILE B 464 5 8
HELIX 49 AF4 GLY B 470 ASN B 476 1 7
HELIX 50 AF5 SER B 532 PHE B 537 5 6
SHEET 1 AA1 4 ARG A 61 TRP A 62 0
SHEET 2 AA1 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 AA1 4 ASN A 75 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 AA1 4 SER A 86 LEU A 90 -1 O LEU A 90 N ILE A 76
SHEET 1 AA2 3 ILE A 102 ILE A 107 0
SHEET 2 AA2 3 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AA2 3 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 1 AA3 4 TRP A 154 TRP A 157 0
SHEET 2 AA3 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 AA3 4 ASP A 171 LYS A 175 -1 O ASP A 171 N TRP A 168
SHEET 4 AA3 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AA4 3 ILE A 194 ASN A 196 0
SHEET 2 AA4 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA4 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 AA5 4 ILE A 194 ASN A 196 0
SHEET 2 AA5 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA5 4 THR A 265 ASN A 272 -1 O LYS A 267 N GLN A 227
SHEET 4 AA5 4 ILE A 285 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 AA6 2 LEU A 235 PHE A 240 0
SHEET 2 AA6 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 AA7 4 HIS A 298 TRP A 305 0
SHEET 2 AA7 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 AA7 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 AA7 4 TRP A 337 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 AA8 4 HIS A 298 TRP A 305 0
SHEET 2 AA8 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 AA8 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 AA8 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 AA9 4 HIS A 363 PHE A 364 0
SHEET 2 AA9 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AA9 4 ARG A 382 GLN A 388 -1 O CYS A 385 N LYS A 373
SHEET 4 AA9 4 LYS A 391 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AB1 4 VAL A 404 LEU A 410 0
SHEET 2 AB1 4 TYR A 414 SER A 419 -1 O ILE A 418 N ILE A 405
SHEET 3 AB1 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 AB1 4 THR A 443 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 AB2 4 CYS A 454 PHE A 461 0
SHEET 2 AB2 4 TYR A 467 PRO A 475 -1 O ARG A 471 N SER A 458
SHEET 3 AB2 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AB2 4 ARG A 492 GLU A 495 -1 O ARG A 492 N LEU A 482
SHEET 1 AB3 8 SER A 511 LEU A 519 0
SHEET 2 AB3 8 THR A 522 LEU A 530 -1 O PHE A 524 N ILE A 517
SHEET 3 AB3 8 ILE A 574 ASP A 579 -1 O VAL A 575 N ILE A 529
SHEET 4 AB3 8 LEU A 542 ASP A 545 1 N LEU A 543 O ILE A 574
SHEET 5 AB3 8 ILE A 624 TRP A 629 1 O ALA A 625 N LEU A 542
SHEET 6 AB3 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 AB3 8 GLU A 699 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 AB3 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 AB4 2 LYS C 41 THR C 42 0
SHEET 2 AB4 2 VAL C 507 GLN C 508 1 O GLN C 508 N LYS C 41
SHEET 1 AB5 4 ARG C 61 TRP C 62 0
SHEET 2 AB5 4 GLU C 67 GLN C 72 -1 O LEU C 69 N ARG C 61
SHEET 3 AB5 4 ASN C 75 ASN C 80 -1 O ASN C 75 N GLN C 72
SHEET 4 AB5 4 SER C 86 LEU C 90 -1 O PHE C 89 N ILE C 76
SHEET 1 AB6 4 ASP C 104 ILE C 107 0
SHEET 2 AB6 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AB6 4 TYR C 128 ASP C 136 -1 O ASP C 133 N LEU C 116
SHEET 4 AB6 4 GLN C 141 ILE C 143 -1 O ILE C 143 N ILE C 134
SHEET 1 AB7 4 TRP C 154 TRP C 157 0
SHEET 2 AB7 4 LEU C 164 TRP C 168 -1 O VAL C 167 N TRP C 154
SHEET 3 AB7 4 ASP C 171 LYS C 175 -1 O TYR C 173 N TYR C 166
SHEET 4 AB7 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AB8 3 ILE C 194 ASN C 196 0
SHEET 2 AB8 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AB8 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AB9 4 ILE C 194 ASN C 196 0
SHEET 2 AB9 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AB9 4 THR C 265 ASN C 272 -1 O LYS C 267 N GLN C 227
SHEET 4 AB9 4 SER C 284 GLN C 286 -1 O ILE C 285 N VAL C 270
SHEET 1 AC1 2 LEU C 235 PHE C 240 0
SHEET 2 AC1 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 AC2 4 HIS C 298 TRP C 305 0
SHEET 2 AC2 4 ARG C 310 ARG C 317 -1 O LEU C 316 N TYR C 299
SHEET 3 AC2 4 TYR C 322 TYR C 330 -1 O VAL C 324 N TRP C 315
SHEET 4 AC2 4 TRP C 337 CYS C 339 -1 O ASN C 338 N ASP C 329
SHEET 1 AC3 4 HIS C 298 TRP C 305 0
SHEET 2 AC3 4 ARG C 310 ARG C 317 -1 O LEU C 316 N TYR C 299
SHEET 3 AC3 4 TYR C 322 TYR C 330 -1 O VAL C 324 N TRP C 315
SHEET 4 AC3 4 HIS C 345 MET C 348 -1 O HIS C 345 N MET C 325
SHEET 1 AC4 4 HIS C 363 PHE C 364 0
SHEET 2 AC4 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AC4 4 ARG C 382 GLN C 388 -1 O CYS C 385 N LYS C 373
SHEET 4 AC4 4 LYS C 391 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AC5 4 VAL C 404 LEU C 410 0
SHEET 2 AC5 4 TYR C 414 SER C 419 -1 O ILE C 418 N ILE C 405
SHEET 3 AC5 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AC5 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AC6 4 TYR C 457 PHE C 461 0
SHEET 2 AC6 4 TYR C 467 CYS C 472 -1 O ARG C 471 N SER C 458
SHEET 3 AC6 4 LEU C 479 SER C 484 -1 O LEU C 479 N CYS C 472
SHEET 4 AC6 4 LYS C 489 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AC7 8 SER C 511 ILE C 518 0
SHEET 2 AC7 8 LYS C 523 LEU C 530 -1 O TYR C 526 N ASP C 515
SHEET 3 AC7 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AC7 8 TYR C 540 VAL C 546 1 N LEU C 543 O ILE C 574
SHEET 5 AC7 8 VAL C 619 TRP C 629 1 O ASP C 620 N TYR C 540
SHEET 6 AC7 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AC7 8 GLU C 699 GLY C 705 1 O LEU C 701 N ALA C 652
SHEET 8 AC7 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AC8 5 LYS D 408 PHE D 412 0
SHEET 2 AC8 5 SER D 448 ALA D 455 -1 O LEU D 449 N PHE D 412
SHEET 3 AC8 5 LEU D 575 GLN D 584 -1 O SER D 582 N THR D 450
SHEET 4 AC8 5 THR D 485 ALA D 492 -1 N CYS D 486 O ILE D 581
SHEET 5 AC8 5 MET D 427 ASN D 434 -1 N ASN D 429 O LEU D 489
SHEET 1 AC9 4 VAL D 520 PRO D 523 0
SHEET 2 AC9 4 TYR D 504 SER D 514 -1 N SER D 514 O VAL D 520
SHEET 3 AC9 4 ILE D 561 LEU D 569 -1 O ALA D 567 N TYR D 506
SHEET 4 AC9 4 GLU D 547 GLN D 552 -1 N PHE D 549 O GLY D 564
SHEET 1 AD1 5 LYS B 408 PHE B 412 0
SHEET 2 AD1 5 LEU B 449 ALA B 455 -1 O VAL B 451 N LEU B 410
SHEET 3 AD1 5 GLU B 576 VAL B 583 -1 O SER B 582 N THR B 450
SHEET 4 AD1 5 THR B 485 THR B 491 -1 N ALA B 490 O MET B 577
SHEET 5 AD1 5 MET B 427 ASN B 434 -1 N MET B 427 O THR B 491
SHEET 1 AD2 4 VAL B 520 PRO B 523 0
SHEET 2 AD2 4 TYR B 504 SER B 514 -1 N ARG B 512 O THR B 522
SHEET 3 AD2 4 ILE B 561 LEU B 569 -1 O VAL B 565 N GLN B 508
SHEET 4 AD2 4 VAL B 548 GLN B 552 -1 N PHE B 549 O GLY B 564
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.03
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.03
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.03
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.03
SSBOND 6 CYS C 328 CYS C 339 1555 1555 2.03
SSBOND 7 CYS C 385 CYS C 394 1555 1555 2.03
SSBOND 8 CYS C 444 CYS C 447 1555 1555 2.03
SSBOND 9 CYS C 454 CYS C 472 1555 1555 2.04
SSBOND 10 CYS C 649 CYS C 762 1555 1555 2.03
SSBOND 11 CYS D 391 CYS D 415 1555 1555 2.03
SSBOND 12 CYS D 433 CYS D 486 1555 1555 2.04
SSBOND 13 CYS D 445 CYS D 593 1555 1555 2.04
SSBOND 14 CYS D 510 CYS D 534 1555 1555 2.04
SSBOND 15 CYS B 391 CYS B 415 1555 1555 2.03
SSBOND 16 CYS B 433 CYS B 486 1555 1555 2.03
SSBOND 17 CYS B 510 CYS B 534 1555 1555 2.04
LINK ND2 ASN A 85 C1 NAG A 801 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG A 802 1555 1555 1.45
LINK ND2 ASN A 219 C1 NAG A 803 1555 1555 1.45
LINK ND2 ASN A 229 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN C 85 C1 NAG C 801 1555 1555 1.44
LINK ND2 ASN C 219 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN C 229 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN C 281 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN C 321 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN D 418 C1 NAG D 601 1555 1555 1.45
LINK ND2 ASN B 418 C1 NAG B 601 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
CISPEP 1 GLY A 474 PRO A 475 0 1.75
CISPEP 2 GLY C 474 PRO C 475 0 2.84
CRYST1 74.980 121.901 144.664 90.00 93.82 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013337 0.000000 0.000891 0.00000
SCALE2 0.000000 0.008203 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006928 0.00000
TER 5972 PRO A 766
TER 11944 PRO C 766
TER 13558 LEU D 596
TER 15156 PRO B 594
MASTER 689 0 19 50 117 0 0 615436 4 306 146
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