HEADER CELL ADHESION 26-SEP-15 5DZY
TITLE PROTOCADHERIN BETA 8 EXTRACELLULAR CADHERIN DOMAINS 1-4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PCDHB8 PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 29-446;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PCDHB8;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F
KEYWDS CADHERIN, DIMER, EXTRACELLULAR, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.GOODMAN,F.BAHNA,S.MANNEPALLI,B.HONIG,L.SHAPIRO
REVDAT 6 27-SEP-23 5DZY 1 HETSYN LINK
REVDAT 5 29-JUL-20 5DZY 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 01-NOV-17 5DZY 1 JRNL REMARK
REVDAT 3 01-JUN-16 5DZY 1 JRNL
REVDAT 2 25-MAY-16 5DZY 1 JRNL
REVDAT 1 04-MAY-16 5DZY 0
JRNL AUTH K.M.GOODMAN,R.RUBINSTEIN,C.A.THU,F.BAHNA,S.MANNEPALLI,
JRNL AUTH 2 G.AHLSEN,C.RITTENHOUSE,T.MANIATIS,B.HONIG,L.SHAPIRO
JRNL TITL STRUCTURAL BASIS OF DIVERSE HOMOPHILIC RECOGNITION BY
JRNL TITL 2 CLUSTERED ALPHA- AND BETA-PROTOCADHERINS.
JRNL REF NEURON V. 90 709 2016
JRNL REFN ISSN 0896-6273
JRNL PMID 27161523
JRNL DOI 10.1016/J.NEURON.2016.04.004
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 62.5
REMARK 3 NUMBER OF REFLECTIONS : 53465
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2714
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 29.9878 - 7.6969 0.94 4284 235 0.1961 0.2324
REMARK 3 2 7.6969 - 6.1264 0.95 4187 196 0.2440 0.3169
REMARK 3 3 6.1264 - 5.3570 0.98 4256 226 0.2254 0.2725
REMARK 3 4 5.3570 - 4.8694 0.97 4179 236 0.1864 0.2468
REMARK 3 5 4.8694 - 4.5217 0.97 4156 214 0.2052 0.2612
REMARK 3 6 4.5217 - 4.2559 0.98 4173 231 0.2296 0.2925
REMARK 3 7 4.2559 - 4.0433 0.99 4195 227 0.2432 0.2912
REMARK 3 8 4.0433 - 3.8676 0.99 4219 220 0.2741 0.3051
REMARK 3 9 3.8676 - 3.7190 0.92 3896 221 0.2892 0.3582
REMARK 3 10 3.7190 - 3.5909 0.72 3040 199 0.2917 0.3429
REMARK 3 11 3.5909 - 3.4788 0.54 2290 106 0.2694 0.3009
REMARK 3 12 3.4788 - 3.3795 0.43 1846 90 0.2813 0.3432
REMARK 3 13 3.3795 - 3.2906 0.35 1482 64 0.2741 0.3370
REMARK 3 14 3.2906 - 3.2105 0.28 1203 69 0.2477 0.3366
REMARK 3 15 3.2105 - 3.1375 0.23 976 54 0.2429 0.3206
REMARK 3 16 3.1375 - 3.0708 0.19 818 43 0.2515 0.3154
REMARK 3 17 3.0708 - 3.0095 0.15 637 34 0.2586 0.3766
REMARK 3 18 3.0095 - 2.9527 0.12 517 27 0.2800 0.5468
REMARK 3 19 2.9527 - 2.9000 0.09 397 22 0.2807 0.4833
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) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.370
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 19477
REMARK 3 ANGLE : 0.517 26724
REMARK 3 CHIRALITY : 0.022 3322
REMARK 3 PLANARITY : 0.003 3483
REMARK 3 DIHEDRAL : 8.024 7117
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 3:98))
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9604 -59.8577 34.4836
REMARK 3 T TENSOR
REMARK 3 T11: 1.7459 T22: 1.0539
REMARK 3 T33: 0.6393 T12: -0.1200
REMARK 3 T13: 0.1611 T23: -0.0637
REMARK 3 L TENSOR
REMARK 3 L11: 3.2610 L22: 2.9946
REMARK 3 L33: 2.3812 L12: -1.9077
REMARK 3 L13: 2.7776 L23: -1.8802
REMARK 3 S TENSOR
REMARK 3 S11: 0.4231 S12: -0.3027 S13: 0.6677
REMARK 3 S21: -0.4397 S22: -0.4929 S23: -0.5736
REMARK 3 S31: 0.0563 S32: 0.3015 S33: -0.0548
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 2:98))
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4780 -47.7302-100.0196
REMARK 3 T TENSOR
REMARK 3 T11: 0.6845 T22: 1.1487
REMARK 3 T33: 0.5673 T12: -0.1138
REMARK 3 T13: -0.0854 T23: -0.1104
REMARK 3 L TENSOR
REMARK 3 L11: 4.6941 L22: 5.5573
REMARK 3 L33: 6.9083 L12: -3.1797
REMARK 3 L13: 2.0119 L23: -4.2649
REMARK 3 S TENSOR
REMARK 3 S11: -0.3378 S12: -0.0080 S13: 0.7260
REMARK 3 S21: -0.7030 S22: 0.0517 S23: -0.1862
REMARK 3 S31: 0.3157 S32: -1.3661 S33: 0.3073
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C' AND ((RESSEQ 2:98))
REMARK 3 ORIGIN FOR THE GROUP (A): -25.9405 -32.8242 -11.5213
REMARK 3 T TENSOR
REMARK 3 T11: 1.9018 T22: 1.4773
REMARK 3 T33: 0.6479 T12: 0.1780
REMARK 3 T13: -0.0287 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 4.1614 L22: 1.5611
REMARK 3 L33: 3.6924 L12: -2.4286
REMARK 3 L13: 3.8708 L23: -2.3460
REMARK 3 S TENSOR
REMARK 3 S11: -0.3976 S12: -0.4521 S13: 0.5175
REMARK 3 S21: 1.5473 S22: 0.1912 S23: 0.0098
REMARK 3 S31: 1.2217 S32: -0.5772 S33: 0.3023
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'D' AND ((RESSEQ 2:98))
REMARK 3 ORIGIN FOR THE GROUP (A): -32.6894 -33.0341-146.4996
REMARK 3 T TENSOR
REMARK 3 T11: 2.7799 T22: 2.7485
REMARK 3 T33: 0.4977 T12: -1.1624
REMARK 3 T13: 0.2903 T23: -0.1923
REMARK 3 L TENSOR
REMARK 3 L11: 0.7381 L22: 0.7108
REMARK 3 L33: 1.6657 L12: -0.6105
REMARK 3 L13: 0.2679 L23: -0.9268
REMARK 3 S TENSOR
REMARK 3 S11: -0.2425 S12: 1.0900 S13: 0.2170
REMARK 3 S21: -0.7630 S22: 0.3876 S23: -0.5734
REMARK 3 S31: 0.3366 S32: 0.3030 S33: 0.0341
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'E' AND ((RESSEQ 3:98))
REMARK 3 ORIGIN FOR THE GROUP (A): -60.5913 -57.1100-204.7009
REMARK 3 T TENSOR
REMARK 3 T11: 1.0748 T22: 1.4731
REMARK 3 T33: 0.5595 T12: -0.0163
REMARK 3 T13: 0.0720 T23: 0.2151
REMARK 3 L TENSOR
REMARK 3 L11: 3.8584 L22: 6.8791
REMARK 3 L33: 2.6801 L12: 2.7670
REMARK 3 L13: 2.2956 L23: 3.7680
REMARK 3 S TENSOR
REMARK 3 S11: -0.2760 S12: -0.2702 S13: 0.2045
REMARK 3 S21: -0.1447 S22: 0.4662 S23: 0.1753
REMARK 3 S31: -0.8723 S32: 0.6975 S33: -0.0233
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'F' AND ((RESSEQ 1:98))
REMARK 3 ORIGIN FOR THE GROUP (A): -57.4781 -39.9622 -70.2615
REMARK 3 T TENSOR
REMARK 3 T11: 0.7527 T22: 1.3043
REMARK 3 T33: 0.4860 T12: -0.2730
REMARK 3 T13: 0.0154 T23: 0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 2.4811 L22: 6.4896
REMARK 3 L33: 3.0245 L12: 0.4955
REMARK 3 L13: -0.5154 L23: 2.9107
REMARK 3 S TENSOR
REMARK 3 S11: 0.0390 S12: -0.0240 S13: -0.1291
REMARK 3 S21: 0.1563 S22: 0.0092 S23: 0.3371
REMARK 3 S31: 0.2217 S32: 0.7327 S33: -0.0363
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 99:206))
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4218 -53.9346 -8.9181
REMARK 3 T TENSOR
REMARK 3 T11: 1.2454 T22: 1.1913
REMARK 3 T33: 0.4608 T12: 0.1633
REMARK 3 T13: 0.0305 T23: 0.0976
REMARK 3 L TENSOR
REMARK 3 L11: 2.6237 L22: 1.2375
REMARK 3 L33: 5.6571 L12: 0.1220
REMARK 3 L13: -0.7818 L23: 1.9129
REMARK 3 S TENSOR
REMARK 3 S11: 0.0204 S12: -1.0391 S13: -0.1410
REMARK 3 S21: 0.7341 S22: 0.1716 S23: 0.2011
REMARK 3 S31: -0.0868 S32: -0.5851 S33: -0.1829
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 99:206))
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7539 -57.5093 -57.1895
REMARK 3 T TENSOR
REMARK 3 T11: 0.4855 T22: 0.5230
REMARK 3 T33: 0.3144 T12: -0.0392
REMARK 3 T13: -0.0343 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 4.2287 L22: 4.1675
REMARK 3 L33: 7.5381 L12: -0.9660
REMARK 3 L13: -2.6953 L23: 0.7662
REMARK 3 S TENSOR
REMARK 3 S11: -0.0987 S12: 0.2899 S13: -0.1205
REMARK 3 S21: -0.2935 S22: 0.0152 S23: 0.2303
REMARK 3 S31: 0.2978 S32: -0.7982 S33: 0.1598
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND ((RESSEQ 99:206))
REMARK 3 ORIGIN FOR THE GROUP (A): -36.5669 -31.8909 -54.3961
REMARK 3 T TENSOR
REMARK 3 T11: 0.4420 T22: 0.5203
REMARK 3 T33: 0.4234 T12: -0.1545
REMARK 3 T13: 0.0665 T23: 0.0926
REMARK 3 L TENSOR
REMARK 3 L11: 4.9192 L22: 2.8385
REMARK 3 L33: 9.0434 L12: 0.1242
REMARK 3 L13: -1.9420 L23: 1.9060
REMARK 3 S TENSOR
REMARK 3 S11: 0.0374 S12: -0.1160 S13: -0.1404
REMARK 3 S21: 0.4806 S22: 0.1086 S23: -0.0344
REMARK 3 S31: 0.2671 S32: -0.0872 S33: -0.1353
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND ((RESSEQ 99:206))
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8534 -35.6737-102.8899
REMARK 3 T TENSOR
REMARK 3 T11: 1.1083 T22: 1.5629
REMARK 3 T33: 0.5732 T12: -0.1068
REMARK 3 T13: 0.0674 T23: -0.2148
REMARK 3 L TENSOR
REMARK 3 L11: 1.1526 L22: 3.0803
REMARK 3 L33: 5.3288 L12: 0.7521
REMARK 3 L13: -0.0609 L23: 0.9361
REMARK 3 S TENSOR
REMARK 3 S11: -0.3977 S12: 0.9252 S13: -0.2026
REMARK 3 S21: -1.0714 S22: 0.2551 S23: -0.0064
REMARK 3 S31: 1.1251 S32: 0.7714 S33: 0.0789
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'E' AND ((RESSEQ 99:206))
REMARK 3 ORIGIN FOR THE GROUP (A): -52.8540 -46.2400-162.1782
REMARK 3 T TENSOR
REMARK 3 T11: 0.9304 T22: 1.5709
REMARK 3 T33: 0.4993 T12: -0.0922
REMARK 3 T13: 0.0883 T23: -0.0873
REMARK 3 L TENSOR
REMARK 3 L11: 1.1893 L22: 1.6043
REMARK 3 L33: 7.2055 L12: -0.1198
REMARK 3 L13: -1.3655 L23: -1.3881
REMARK 3 S TENSOR
REMARK 3 S11: -0.1874 S12: 0.4438 S13: -0.0209
REMARK 3 S21: -0.4965 S22: 0.0808 S23: -0.2895
REMARK 3 S31: -0.0178 S32: 1.3885 S33: -0.0293
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'F' AND ((RESSEQ 99:206))
REMARK 3 ORIGIN FOR THE GROUP (A): -56.8035 -51.8919-112.8409
REMARK 3 T TENSOR
REMARK 3 T11: 0.4648 T22: 0.6361
REMARK 3 T33: 0.3655 T12: -0.1129
REMARK 3 T13: -0.0335 T23: -0.0738
REMARK 3 L TENSOR
REMARK 3 L11: 3.8690 L22: 3.0223
REMARK 3 L33: 8.0008 L12: -1.3616
REMARK 3 L13: -2.6044 L23: -1.8528
REMARK 3 S TENSOR
REMARK 3 S11: -0.0778 S12: 0.0867 S13: 0.0700
REMARK 3 S21: 0.1399 S22: -0.0344 S23: -0.0477
REMARK 3 S31: 0.6522 S32: 0.2519 S33: 0.0878
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 207:311))
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7268 -37.6306 -56.6642
REMARK 3 T TENSOR
REMARK 3 T11: 0.4153 T22: 0.6533
REMARK 3 T33: 0.3893 T12: 0.2489
REMARK 3 T13: -0.0466 T23: -0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 2.9064 L22: 2.3602
REMARK 3 L33: 3.6288 L12: -0.3208
REMARK 3 L13: 0.7261 L23: -1.0935
REMARK 3 S TENSOR
REMARK 3 S11: 0.0101 S12: 0.3404 S13: -0.0890
REMARK 3 S21: 0.0441 S22: 0.0131 S23: 0.0548
REMARK 3 S31: -0.5304 S32: 0.0484 S33: -0.0050
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 207:311))
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1261 -56.9467 -7.5283
REMARK 3 T TENSOR
REMARK 3 T11: 1.4185 T22: 0.8628
REMARK 3 T33: 0.6172 T12: -0.1001
REMARK 3 T13: -0.3353 T23: 0.1644
REMARK 3 L TENSOR
REMARK 3 L11: 2.5836 L22: 0.8263
REMARK 3 L33: 3.2888 L12: -1.2555
REMARK 3 L13: 2.9095 L23: -1.3626
REMARK 3 S TENSOR
REMARK 3 S11: -0.2170 S12: 0.5374 S13: 0.2527
REMARK 3 S21: 0.8691 S22: -0.4863 S23: -0.4350
REMARK 3 S31: -1.2492 S32: 1.4248 S33: 0.6008
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND ((RESSEQ 207:311))
REMARK 3 ORIGIN FOR THE GROUP (A): -41.2066 -21.1967-103.9149
REMARK 3 T TENSOR
REMARK 3 T11: 0.7651 T22: 1.0028
REMARK 3 T33: 0.4767 T12: -0.4851
REMARK 3 T13: -0.1425 T23: 0.0680
REMARK 3 L TENSOR
REMARK 3 L11: 0.7139 L22: 1.7314
REMARK 3 L33: 1.5345 L12: -0.7560
REMARK 3 L13: 0.2729 L23: -0.8576
REMARK 3 S TENSOR
REMARK 3 S11: -0.4183 S12: 0.3518 S13: -0.1285
REMARK 3 S21: -0.6582 S22: 0.3428 S23: -0.1338
REMARK 3 S31: -0.5259 S32: 1.0463 S33: 0.0442
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND ((RESSEQ 207:311))
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6326 -26.9841 -53.6107
REMARK 3 T TENSOR
REMARK 3 T11: 0.3973 T22: 0.7200
REMARK 3 T33: 0.4239 T12: 0.1825
REMARK 3 T13: -0.0290 T23: 0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 3.6196 L22: 3.4363
REMARK 3 L33: 1.8761 L12: 0.2281
REMARK 3 L13: 0.9148 L23: 0.7790
REMARK 3 S TENSOR
REMARK 3 S11: 0.1333 S12: -0.1280 S13: -0.1415
REMARK 3 S21: 0.3399 S22: -0.1131 S23: 0.1466
REMARK 3 S31: -0.0184 S32: 0.0276 S33: -0.1288
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'E' AND ((RESSEQ 207:311))
REMARK 3 ORIGIN FOR THE GROUP (A): -61.2161 -31.4421-114.6615
REMARK 3 T TENSOR
REMARK 3 T11: 0.4498 T22: 0.6957
REMARK 3 T33: 0.4654 T12: -0.4808
REMARK 3 T13: -0.1632 T23: -0.0735
REMARK 3 L TENSOR
REMARK 3 L11: 2.4471 L22: 0.5084
REMARK 3 L33: 4.7407 L12: -0.7017
REMARK 3 L13: -1.0074 L23: -0.7973
REMARK 3 S TENSOR
REMARK 3 S11: -0.2594 S12: -0.2560 S13: 0.0758
REMARK 3 S21: -0.0039 S22: 0.5297 S23: 0.4346
REMARK 3 S31: -1.2671 S32: -0.1237 S33: 0.2717
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'F' AND ((RESSEQ 207:311))
REMARK 3 ORIGIN FOR THE GROUP (A): -69.9293 -58.5115-161.2576
REMARK 3 T TENSOR
REMARK 3 T11: 1.0792 T22: 0.9551
REMARK 3 T33: 0.5494 T12: 0.1642
REMARK 3 T13: -0.0602 T23: -0.2509
REMARK 3 L TENSOR
REMARK 3 L11: 1.9247 L22: 1.9677
REMARK 3 L33: 3.0999 L12: 1.9521
REMARK 3 L13: 2.3635 L23: 2.5115
REMARK 3 S TENSOR
REMARK 3 S11: -0.1970 S12: -0.3477 S13: 0.3643
REMARK 3 S21: -0.3818 S22: -0.5981 S23: 0.4053
REMARK 3 S31: 0.2624 S32: -1.3866 S33: 0.7893
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 312:416))
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2076 -24.4686-103.9735
REMARK 3 T TENSOR
REMARK 3 T11: 1.0552 T22: 0.9584
REMARK 3 T33: 0.5298 T12: 0.2702
REMARK 3 T13: -0.0298 T23: 0.1037
REMARK 3 L TENSOR
REMARK 3 L11: 4.5255 L22: 3.4953
REMARK 3 L33: 3.5154 L12: 0.4161
REMARK 3 L13: 1.1849 L23: 0.6324
REMARK 3 S TENSOR
REMARK 3 S11: -0.2257 S12: 0.6384 S13: 0.2208
REMARK 3 S21: -0.1102 S22: 0.4361 S23: 0.0582
REMARK 3 S31: -2.1597 S32: -1.8827 S33: -0.2528
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 312:415))
REMARK 3 ORIGIN FOR THE GROUP (A): 32.4308 -64.0983 39.5891
REMARK 3 T TENSOR
REMARK 3 T11: 1.7511 T22: 0.7712
REMARK 3 T33: 0.5311 T12: 0.2685
REMARK 3 T13: -0.0557 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 2.5748 L22: 3.6608
REMARK 3 L33: 6.6695 L12: 0.5401
REMARK 3 L13: -0.0291 L23: -1.7057
REMARK 3 S TENSOR
REMARK 3 S11: -0.2458 S12: 0.1036 S13: 0.0471
REMARK 3 S21: 0.2724 S22: -0.1225 S23: 0.0726
REMARK 3 S31: 1.9345 S32: 1.4856 S33: 0.1797
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND ((RESSEQ 312:416))
REMARK 3 ORIGIN FOR THE GROUP (A): -50.7466 -17.3087-152.3583
REMARK 3 T TENSOR
REMARK 3 T11: 2.1250 T22: 3.0522
REMARK 3 T33: 0.5397 T12: -1.2799
REMARK 3 T13: -0.3353 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 0.1628 L22: 0.7156
REMARK 3 L33: 1.0169 L12: -0.4505
REMARK 3 L13: 0.4153 L23: -0.4284
REMARK 3 S TENSOR
REMARK 3 S11: -0.6155 S12: 1.2052 S13: -0.2327
REMARK 3 S21: -0.6248 S22: 0.0845 S23: 0.1037
REMARK 3 S31: -0.4886 S32: -0.0717 S33: -0.1640
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND ((RESSEQ 312:413))
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8565 -26.7805 -6.8891
REMARK 3 T TENSOR
REMARK 3 T11: 2.2305 T22: 2.2112
REMARK 3 T33: 0.7334 T12: 0.9482
REMARK 3 T13: -0.4958 T23: -0.3051
REMARK 3 L TENSOR
REMARK 3 L11: 0.7384 L22: 0.3384
REMARK 3 L33: 2.3727 L12: 0.3329
REMARK 3 L13: -0.4431 L23: -0.8872
REMARK 3 S TENSOR
REMARK 3 S11: -0.9293 S12: -0.9794 S13: 0.7488
REMARK 3 S21: 1.5892 S22: 0.5315 S23: -1.1882
REMARK 3 S31: -0.5697 S32: 0.8635 S33: 0.1790
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'E' AND ((RESSEQ 312:415))
REMARK 3 ORIGIN FOR THE GROUP (A): -66.2757 -18.0772 -67.5924
REMARK 3 T TENSOR
REMARK 3 T11: 1.1648 T22: 0.8065
REMARK 3 T33: 0.6312 T12: -0.0354
REMARK 3 T13: -0.0097 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 3.7408 L22: 4.5886
REMARK 3 L33: 7.1034 L12: 0.8891
REMARK 3 L13: 1.2520 L23: 1.1969
REMARK 3 S TENSOR
REMARK 3 S11: 0.1698 S12: -0.1940 S13: 0.3165
REMARK 3 S21: 0.6470 S22: -0.2288 S23: 0.0589
REMARK 3 S31: -1.5385 S32: -0.2070 S33: 0.0768
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'F' AND ((RESSEQ 312:415))
REMARK 3 ORIGIN FOR THE GROUP (A): -80.8504 -70.9738-208.3831
REMARK 3 T TENSOR
REMARK 3 T11: 1.2954 T22: 0.7682
REMARK 3 T33: 0.5278 T12: 0.0252
REMARK 3 T13: -0.0775 T23: -0.0943
REMARK 3 L TENSOR
REMARK 3 L11: 5.1754 L22: 3.7516
REMARK 3 L33: 2.9038 L12: -0.0048
REMARK 3 L13: -1.6946 L23: 1.0566
REMARK 3 S TENSOR
REMARK 3 S11: -0.2707 S12: 0.1908 S13: -0.3364
REMARK 3 S21: -0.3476 S22: 0.0357 S23: 0.2295
REMARK 3 S31: 1.8525 S32: 0.0431 S33: 0.0675
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 5DZY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000214078.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53465
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.90000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
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: 5DZX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG550MME, PEG20000, CALCIUM CHLORIDE,
REMARK 280 MAGNESIUM CHLORIDE, TRIS, BICINE, PH 8.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
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 42.57000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 163.09500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 68.53500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 163.09500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.57000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 68.53500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: DIMER BY ANALYTICAL ULTRACENTRIFUGATION
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, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, J, K
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, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLU A 1
REMARK 465 ALA A 2
REMARK 465 ASP A 417
REMARK 465 ASN A 418
REMARK 465 HIS A 419
REMARK 465 HIS A 420
REMARK 465 HIS A 421
REMARK 465 HIS A 422
REMARK 465 HIS A 423
REMARK 465 HIS A 424
REMARK 465 HIS A 425
REMARK 465 HIS A 426
REMARK 465 ASN B 416
REMARK 465 ASP B 417
REMARK 465 ASN B 418
REMARK 465 HIS B 419
REMARK 465 HIS B 420
REMARK 465 HIS B 421
REMARK 465 HIS B 422
REMARK 465 HIS B 423
REMARK 465 HIS B 424
REMARK 465 HIS B 425
REMARK 465 HIS B 426
REMARK 465 GLU C 1
REMARK 465 ASP C 417
REMARK 465 ASN C 418
REMARK 465 HIS C 419
REMARK 465 HIS C 420
REMARK 465 HIS C 421
REMARK 465 HIS C 422
REMARK 465 HIS C 423
REMARK 465 HIS C 424
REMARK 465 HIS C 425
REMARK 465 HIS C 426
REMARK 465 GLU D 1
REMARK 465 ASP D 414
REMARK 465 ILE D 415
REMARK 465 ASN D 416
REMARK 465 ASP D 417
REMARK 465 ASN D 418
REMARK 465 HIS D 419
REMARK 465 HIS D 420
REMARK 465 HIS D 421
REMARK 465 HIS D 422
REMARK 465 HIS D 423
REMARK 465 HIS D 424
REMARK 465 HIS D 425
REMARK 465 HIS D 426
REMARK 465 GLU E 1
REMARK 465 ALA E 2
REMARK 465 ASN E 416
REMARK 465 ASP E 417
REMARK 465 ASN E 418
REMARK 465 HIS E 419
REMARK 465 HIS E 420
REMARK 465 HIS E 421
REMARK 465 HIS E 422
REMARK 465 HIS E 423
REMARK 465 HIS E 424
REMARK 465 HIS E 425
REMARK 465 HIS E 426
REMARK 465 ASN F 416
REMARK 465 ASP F 417
REMARK 465 ASN F 418
REMARK 465 HIS F 419
REMARK 465 HIS F 420
REMARK 465 HIS F 421
REMARK 465 HIS F 422
REMARK 465 HIS F 423
REMARK 465 HIS F 424
REMARK 465 HIS F 425
REMARK 465 HIS F 426
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 GLU A 12 CG CD OE1 OE2
REMARK 470 LEU A 31 CG CD1 CD2
REMARK 470 ARG A 53 NE CZ NH1 NH2
REMARK 470 LYS A 59 CG CD CE NZ
REMARK 470 LEU A 76 CG CD1 CD2
REMARK 470 PHE A 89 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 104 CG CD OE1 OE2
REMARK 470 MET A 110 CG SD CE
REMARK 470 ARG A 161 CD NE CZ NH1 NH2
REMARK 470 TYR A 163 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 176 CG CD OE1 OE2
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 GLN A 255 CG CD OE1 NE2
REMARK 470 GLN A 261 CG CD OE1 NE2
REMARK 470 GLU A 329 CG CD OE1 OE2
REMARK 470 ASN A 330 CG OD1 ND2
REMARK 470 ASN A 358 CG OD1 ND2
REMARK 470 LYS A 365 CG CD CE NZ
REMARK 470 ILE A 415 CG1 CG2 CD1
REMARK 470 ASN A 416 CG OD1 ND2
REMARK 470 GLU B 1 CG CD OE1 OE2
REMARK 470 GLN B 22 CG CD OE1 NE2
REMARK 470 ARG B 27 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 ARG B 53 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 59 CG CD CE NZ
REMARK 470 GLU B 83 CG CD OE1 OE2
REMARK 470 ARG B 161 CD NE CZ NH1 NH2
REMARK 470 LEU B 232 CG CD1 CD2
REMARK 470 ARG B 239 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 273 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 275 CG CD CE NZ
REMARK 470 LYS B 317 CG CD CE NZ
REMARK 470 ASN B 330 CG OD1 ND2
REMARK 470 GLU B 333 CG CD OE1 OE2
REMARK 470 ASN B 358 CG OD1 ND2
REMARK 470 LEU B 360 CG CD1 CD2
REMARK 470 LYS B 365 CG CD CE NZ
REMARK 470 LYS B 369 CG CD CE NZ
REMARK 470 GLU B 377 CG CD OE1 OE2
REMARK 470 ARG B 378 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 415 CG1 CG2 CD1
REMARK 470 GLU C 12 CG CD OE1 OE2
REMARK 470 ASP C 23 CG OD1 OD2
REMARK 470 LEU C 26 CG CD1 CD2
REMARK 470 ARG C 27 CD NE CZ NH1 NH2
REMARK 470 ILE C 38 CG1 CG2 CD1
REMARK 470 GLU C 45 CG CD OE1 OE2
REMARK 470 GLN C 48 CG CD OE1 NE2
REMARK 470 LEU C 49 CG CD1 CD2
REMARK 470 ARG C 53 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 57 CG CD1 CD2
REMARK 470 LYS C 59 CG CD CE NZ
REMARK 470 LYS C 61 CD CE NZ
REMARK 470 PHE C 78 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE C 88 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS C 194 CG CD CE NZ
REMARK 470 LYS C 317 CD CE NZ
REMARK 470 GLU C 329 CG CD OE1 OE2
REMARK 470 GLU C 333 CG CD OE1 OE2
REMARK 470 ILE C 356 CG1 CG2 CD1
REMARK 470 ASN C 358 CG OD1 ND2
REMARK 470 LEU C 363 CG CD1 CD2
REMARK 470 LYS C 365 CG CD CE NZ
REMARK 470 LYS C 369 CG CD CE NZ
REMARK 470 ASN C 370 CG OD1 ND2
REMARK 470 ASN C 385 CG OD1 ND2
REMARK 470 ILE C 390 CG1 CG2 CD1
REMARK 470 SER C 413 OG
REMARK 470 ILE C 415 CG1 CG2 CD1
REMARK 470 ASN C 416 CG OD1 ND2
REMARK 470 GLU D 12 CG CD OE1 OE2
REMARK 470 ASN D 19 CG OD1 ND2
REMARK 470 GLN D 22 CG CD OE1 NE2
REMARK 470 ARG D 27 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 43 CG OD1 ND2
REMARK 470 LYS D 44 CG CD CE NZ
REMARK 470 LEU D 47 CG CD1 CD2
REMARK 470 ARG D 53 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 59 CG CD CE NZ
REMARK 470 LYS D 61 CG CD CE NZ
REMARK 470 GLN D 94 CG CD OE1 NE2
REMARK 470 ARG D 201 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 329 CG CD OE1 OE2
REMARK 470 ASN D 330 CG OD1 ND2
REMARK 470 VAL D 336 CG1 CG2
REMARK 470 LYS D 365 CG CD CE NZ
REMARK 470 LYS D 369 CD CE NZ
REMARK 470 GLU D 377 CG CD OE1 OE2
REMARK 470 ARG D 378 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 381 CG OD1 OD2
REMARK 470 GLU D 383 CG CD OE1 OE2
REMARK 470 SER D 384 OG
REMARK 470 ASN D 385 CG OD1 ND2
REMARK 470 TYR D 388 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG D 401 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 411 CG CD OE1 NE2
REMARK 470 ARG E 27 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 30 CG CD OE1 OE2
REMARK 470 ASN E 43 CG OD1 ND2
REMARK 470 LYS E 44 CG CD CE NZ
REMARK 470 LYS E 59 CG CD CE NZ
REMARK 470 GLU E 60 CG CD OE1 OE2
REMARK 470 GLU E 104 CG CD OE1 OE2
REMARK 470 ARG E 161 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 232 CG CD1 CD2
REMARK 470 GLN E 255 CG CD OE1 NE2
REMARK 470 GLN E 261 CG CD OE1 NE2
REMARK 470 LYS E 317 CG CD CE NZ
REMARK 470 GLU E 329 CG CD OE1 OE2
REMARK 470 GLU E 333 CG CD OE1 OE2
REMARK 470 LYS E 365 CG CD CE NZ
REMARK 470 LYS E 369 CG CD CE NZ
REMARK 470 GLU E 383 CG CD OE1 OE2
REMARK 470 GLU F 1 CG CD OE1 OE2
REMARK 470 ARG F 27 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 30 CG CD OE1 OE2
REMARK 470 LYS F 44 CG CD CE NZ
REMARK 470 ARG F 53 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 59 CG CD CE NZ
REMARK 470 GLU F 60 CG CD OE1 OE2
REMARK 470 GLU F 222 CG CD OE1 OE2
REMARK 470 LYS F 275 CG CD CE NZ
REMARK 470 LYS F 317 CD CE NZ
REMARK 470 ASN F 358 CG OD1 ND2
REMARK 470 LYS F 365 CG CD CE NZ
REMARK 470 LYS F 369 CG CD CE NZ
REMARK 470 ARG F 401 CG CD NE CZ NH1 NH2
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 OG1 THR D 199 C2 MAN D 505 2.13
REMARK 500 O ASN E 99 NZ LYS E 194 2.15
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 156 42.29 -103.33
REMARK 500 SER A 158 -129.40 62.19
REMARK 500 ASP A 159 42.61 -80.20
REMARK 500 ASP A 173 112.10 -161.26
REMARK 500 GLU A 176 -60.64 -101.15
REMARK 500 ASP A 294 -163.83 -77.88
REMARK 500 ASN A 312 81.70 -67.82
REMARK 500 ASN A 330 32.92 -95.79
REMARK 500 GLU A 333 74.40 52.88
REMARK 500 ASP A 343 113.31 -163.11
REMARK 500 PRO A 361 30.45 -77.08
REMARK 500 PRO A 366 97.22 -68.04
REMARK 500 ASP A 414 -154.73 -84.87
REMARK 500 SER B 158 -102.12 48.08
REMARK 500 ASP B 159 35.91 -82.21
REMARK 500 ASP B 173 104.77 -160.46
REMARK 500 GLU B 176 -61.81 -101.46
REMARK 500 ASN B 208 84.21 -66.60
REMARK 500 ILE B 268 -61.09 -93.57
REMARK 500 ALA B 282 -75.95 -86.20
REMARK 500 ASP B 294 -158.17 -83.39
REMARK 500 GLU B 329 -70.90 -70.33
REMARK 500 ASN B 330 38.60 -89.33
REMARK 500 ASP B 343 109.73 -160.83
REMARK 500 SER B 413 -162.46 -120.93
REMARK 500 ASP B 414 -4.21 64.32
REMARK 500 ARG C 157 -148.05 -105.92
REMARK 500 ASP C 159 8.94 56.76
REMARK 500 LEU C 232 98.15 -65.07
REMARK 500 ILE C 268 -62.24 -97.44
REMARK 500 ALA C 282 -81.37 -71.54
REMARK 500 ASP C 294 -161.83 -78.20
REMARK 500 GLU C 329 -74.99 -72.01
REMARK 500 ASN C 330 38.90 -89.73
REMARK 500 VAL C 336 -71.08 -77.22
REMARK 500 ASP C 414 -2.50 65.79
REMARK 500 ASN D 19 90.37 -67.52
REMARK 500 ILE D 117 34.95 -93.72
REMARK 500 SER D 158 -107.67 67.74
REMARK 500 ASP D 173 103.91 -160.83
REMARK 500 ASN D 208 81.38 -66.64
REMARK 500 PRO D 262 31.65 -86.10
REMARK 500 ALA D 282 -72.95 -89.52
REMARK 500 ASN D 312 78.12 -67.25
REMARK 500 LEU D 323 -76.67 -80.89
REMARK 500 GLU D 333 76.68 53.77
REMARK 500 PRO E 146 107.86 -51.23
REMARK 500 SER E 158 -119.12 55.19
REMARK 500 GLU E 176 -62.79 -101.08
REMARK 500 ASN E 208 86.58 -65.59
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
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 CA A 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 9 OE1
REMARK 620 2 GLU A 65 OE2 90.8
REMARK 620 3 ASP A 97 OD1 79.2 65.0
REMARK 620 4 ILE A 98 O 91.1 158.8 94.6
REMARK 620 5 ASP A 100 OD1 87.8 130.9 160.0 70.3
REMARK 620 6 ASP A 133 OD1 177.3 89.8 103.4 89.4 89.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 9 OE2
REMARK 620 2 ASP A 63 OD1 70.5
REMARK 620 3 GLU A 65 OE1 58.4 88.7
REMARK 620 4 ASP A 100 OD1 87.4 154.2 90.9
REMARK 620 5 ASP A 100 OD2 83.6 116.9 124.5 44.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 510 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 99 OD1
REMARK 620 2 HIS A 101 O 91.8
REMARK 620 3 ASP A 131 OD1 143.2 84.6
REMARK 620 4 ASP A 131 OD2 165.2 99.4 48.5
REMARK 620 5 ASP A 133 OD2 78.5 94.9 65.4 109.8
REMARK 620 6 ASN A 137 O 81.1 164.0 92.5 90.3 69.7
REMARK 620 7 ASP A 188 OD2 68.9 129.1 138.2 96.4 124.2 61.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 511 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 116 OE2
REMARK 620 2 ASP A 173 OD1 80.3
REMARK 620 3 GLU A 175 OE1 70.1 90.3
REMARK 620 4 ASP A 209 OD1 83.0 162.6 88.8
REMARK 620 5 ASP A 209 OD2 71.3 123.4 122.0 44.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 512 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 116 OE1
REMARK 620 2 GLU A 175 OE1 82.0
REMARK 620 3 GLU A 175 OE2 118.9 47.8
REMARK 620 4 ASP A 206 OD1 96.4 121.2 86.1
REMARK 620 5 ILE A 207 O 81.1 157.2 154.8 75.9
REMARK 620 6 ASP A 209 OD1 90.7 93.7 119.9 145.0 71.4
REMARK 620 7 ASP A 242 OD1 170.9 106.0 70.1 83.1 90.0 84.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 513 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 208 OD1
REMARK 620 2 ASN A 210 O 74.2
REMARK 620 3 ASP A 240 OD1 138.8 78.3
REMARK 620 4 ASP A 240 OD2 167.3 118.3 48.4
REMARK 620 5 ASP A 242 OD2 60.7 75.8 83.3 117.8
REMARK 620 6 HIS A 246 O 94.4 163.1 104.1 72.9 87.8
REMARK 620 7 ASP A 294 OD2 71.8 87.8 137.2 109.5 132.3 100.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 514 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 225 OE2
REMARK 620 2 ASP A 279 OD1 75.0
REMARK 620 3 GLU A 281 OE1 86.3 92.1
REMARK 620 4 ASP A 313 OD1 102.3 169.9 97.5
REMARK 620 5 ASP A 313 OD2 80.6 119.9 140.2 50.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 515 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 225 OE1
REMARK 620 2 GLU A 281 OE1 71.5
REMARK 620 3 GLU A 281 OE2 99.0 51.2
REMARK 620 4 ASP A 310 OD1 87.6 113.3 72.5
REMARK 620 5 VAL A 311 O 87.1 151.6 154.6 83.3
REMARK 620 6 ASP A 313 OD1 88.7 93.8 137.7 149.8 66.6
REMARK 620 7 ASP A 345 OD1 166.8 95.4 72.7 99.2 104.8 90.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 516 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 312 OD1
REMARK 620 2 ASN A 314 O 85.2
REMARK 620 3 ASP A 343 OD1 142.9 94.7
REMARK 620 4 ASP A 343 OD2 159.6 115.1 42.6
REMARK 620 5 ASP A 345 OD2 73.0 79.0 70.6 111.0
REMARK 620 6 ASN A 349 O 100.5 169.2 75.2 59.8 93.7
REMARK 620 7 ASP A 396 OD2 74.9 90.5 142.1 101.9 146.9 99.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 514 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 9 OE2
REMARK 620 2 GLU B 10 OE2 78.4
REMARK 620 3 ASP B 63 OD1 80.1 56.5
REMARK 620 4 GLU B 65 OE1 65.1 136.8 93.6
REMARK 620 5 ASP B 100 OD2 109.4 84.8 138.1 127.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 515 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 9 OE1
REMARK 620 2 GLU B 65 OE1 70.0
REMARK 620 3 GLU B 65 OE2 92.4 44.2
REMARK 620 4 ASP B 97 OD1 71.0 111.5 84.9
REMARK 620 5 ILE B 98 O 86.3 152.3 155.7 71.7
REMARK 620 6 ASP B 100 OD1 92.4 99.4 137.7 135.9 66.6
REMARK 620 7 ASP B 133 OD1 174.6 115.3 91.1 105.3 88.9 87.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 516 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 99 OD1
REMARK 620 2 HIS B 101 O 98.7
REMARK 620 3 ASP B 131 OD2 158.1 103.0
REMARK 620 4 ASP B 133 OD2 82.6 92.5 98.5
REMARK 620 5 ASN B 137 O 86.3 167.2 72.9 76.4
REMARK 620 6 ASP B 188 OD2 67.7 130.2 96.0 129.7 62.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 517 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 116 OE1
REMARK 620 2 GLU B 175 OE1 73.3
REMARK 620 3 GLU B 175 OE2 102.6 45.9
REMARK 620 4 ASP B 206 OD1 104.4 137.1 96.1
REMARK 620 5 ILE B 207 O 89.6 139.1 167.6 82.5
REMARK 620 6 ASP B 209 OD1 83.2 74.2 112.1 148.7 67.0
REMARK 620 7 ASP B 242 OD1 159.4 93.1 76.8 96.1 91.1 78.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 518 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 116 OE2
REMARK 620 2 ASP B 173 OD1 69.0
REMARK 620 3 GLU B 175 OE1 60.5 65.6
REMARK 620 4 ASP B 209 OD2 63.8 132.8 91.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 519 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 208 OD1
REMARK 620 2 ASN B 210 O 80.8
REMARK 620 3 ASP B 240 OD1 143.8 77.5
REMARK 620 4 ASP B 240 OD2 167.8 111.4 44.7
REMARK 620 5 ASP B 242 OD2 67.1 83.6 81.9 113.5
REMARK 620 6 HIS B 246 O 103.9 166.7 92.2 64.4 86.8
REMARK 620 7 ASP B 294 OD2 77.0 79.8 126.0 103.9 142.4 113.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 520 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 225 OE2
REMARK 620 2 ASP B 279 OD1 73.6
REMARK 620 3 GLU B 281 OE1 92.1 92.2
REMARK 620 4 ASP B 313 OD1 87.0 156.3 102.3
REMARK 620 5 ASP B 313 OD2 64.9 113.0 137.1 44.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 521 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 225 OE1
REMARK 620 2 GLU B 281 OE1 81.1
REMARK 620 3 GLU B 281 OE2 114.3 45.4
REMARK 620 4 ASP B 310 OD1 99.0 116.2 80.5
REMARK 620 5 VAL B 311 O 101.7 165.3 140.3 77.8
REMARK 620 6 ASP B 313 OD1 91.7 98.0 124.6 145.3 67.6
REMARK 620 7 ASP B 345 OD1 160.5 79.9 52.8 93.2 95.7 86.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 522 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 312 OD1
REMARK 620 2 ASN B 314 O 93.4
REMARK 620 3 ASP B 343 OD1 142.0 85.1
REMARK 620 4 ASP B 343 OD2 158.0 108.5 43.6
REMARK 620 5 ASP B 345 OD2 73.7 80.1 68.6 108.6
REMARK 620 6 ASN B 349 O 95.7 158.3 75.5 63.5 83.6
REMARK 620 7 ASP B 396 OD2 65.2 100.5 152.3 110.0 138.9 101.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 507 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 9 OE2
REMARK 620 2 GLU C 10 OE2 80.7
REMARK 620 3 ASP C 63 OD1 81.5 56.3
REMARK 620 4 GLU C 65 OE1 63.2 136.7 93.5
REMARK 620 5 ASP C 100 OD2 98.7 87.4 143.4 119.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 9 OE1
REMARK 620 2 GLU C 65 OE2 91.1
REMARK 620 3 ASP C 97 OD1 77.8 80.0
REMARK 620 4 ILE C 98 O 88.7 158.8 79.2
REMARK 620 5 ASP C 100 OD1 88.1 130.0 147.5 71.2
REMARK 620 6 ASP C 133 OD1 170.8 85.5 110.0 97.5 87.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 99 OD1
REMARK 620 2 HIS C 101 O 87.7
REMARK 620 3 ASP C 131 OD1 147.2 103.7
REMARK 620 4 ASP C 131 OD2 149.5 116.1 49.2
REMARK 620 5 ASP C 133 OD2 79.1 99.1 68.9 113.0
REMARK 620 6 ASN C 137 O 80.6 167.2 83.8 76.7 73.7
REMARK 620 7 ASP C 188 OD2 67.2 119.4 127.5 83.9 126.0 60.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 510 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 116 OE2
REMARK 620 2 ASP C 173 OD1 80.7
REMARK 620 3 GLU C 175 OE1 73.7 106.6
REMARK 620 4 ASP C 209 OD2 75.8 126.0 112.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 511 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 116 OE1
REMARK 620 2 GLU C 175 OE1 76.9
REMARK 620 3 GLU C 175 OE2 111.4 49.1
REMARK 620 4 ASP C 206 OD1 100.5 125.2 84.6
REMARK 620 5 ILE C 207 O 91.7 157.4 152.1 75.7
REMARK 620 6 ASP C 209 OD1 89.2 86.8 120.5 147.8 73.4
REMARK 620 7 ASP C 242 OD1 163.8 96.8 73.4 95.3 88.9 75.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 512 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 208 OD1
REMARK 620 2 ASN C 210 O 84.0
REMARK 620 3 ASP C 240 OD1 144.9 80.6
REMARK 620 4 ASP C 240 OD2 155.8 120.0 51.5
REMARK 620 5 ASP C 242 OD2 60.4 77.7 85.5 123.6
REMARK 620 6 HIS C 246 O 92.3 163.4 93.6 65.4 86.4
REMARK 620 7 ASP C 294 OD2 71.8 85.5 137.4 105.3 130.4 108.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 513 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 225 OE2
REMARK 620 2 ASP C 279 OD1 72.8
REMARK 620 3 GLU C 281 OE1 87.8 104.2
REMARK 620 4 ASP C 313 OD1 85.4 148.2 97.6
REMARK 620 5 ASP C 313 OD2 68.8 103.5 136.0 45.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 514 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 225 OE1
REMARK 620 2 GLU C 281 OE1 82.5
REMARK 620 3 GLU C 281 OE2 112.3 51.0
REMARK 620 4 ASP C 310 OD1 88.2 110.0 70.7
REMARK 620 5 VAL C 311 O 97.2 175.4 132.8 74.5
REMARK 620 6 ASP C 313 OD1 96.2 105.5 136.9 144.5 69.9
REMARK 620 7 ASP C 345 OD1 168.2 86.4 56.8 91.8 94.2 90.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 515 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 312 OD1
REMARK 620 2 ASN C 314 O 82.8
REMARK 620 3 ASP C 343 OD1 153.1 104.0
REMARK 620 4 ASP C 343 OD2 143.6 125.4 50.8
REMARK 620 5 ASP C 345 OD2 64.3 87.5 89.7 131.0
REMARK 620 6 ASN C 349 O 80.3 163.1 91.1 70.2 85.1
REMARK 620 7 ASP C 396 OD2 57.0 83.3 148.7 99.9 121.3 87.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 507 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 9 OE1
REMARK 620 2 GLU D 65 OE2 90.7
REMARK 620 3 ASP D 97 OD1 88.3 101.6
REMARK 620 4 ILE D 98 O 92.5 171.4 70.6
REMARK 620 5 ASP D 100 OD1 92.9 119.6 138.8 68.2
REMARK 620 6 ASP D 133 OD1 166.8 79.1 101.9 98.8 85.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 63 OD1
REMARK 620 2 GLU D 65 OE1 84.9
REMARK 620 3 ASP D 100 OD2 122.0 102.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 99 OD1
REMARK 620 2 HIS D 101 O 88.0
REMARK 620 3 ASP D 131 OD1 139.9 109.9
REMARK 620 4 ASP D 131 OD2 146.5 124.3 43.2
REMARK 620 5 ASP D 133 OD2 81.6 110.1 58.8 93.5
REMARK 620 6 ASN D 137 O 70.2 155.5 82.2 79.3 57.0
REMARK 620 7 ASP D 188 OD2 64.3 125.7 121.5 87.1 110.5 55.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 116 OE2
REMARK 620 2 ASP D 173 OD1 85.3
REMARK 620 3 GLU D 175 OE1 67.7 68.2
REMARK 620 4 ASP D 209 OD2 69.6 154.6 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 510 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 116 OE1
REMARK 620 2 GLU D 175 OE1 88.0
REMARK 620 3 GLU D 175 OE2 121.8 46.7
REMARK 620 4 ASP D 206 OD1 102.9 128.5 87.4
REMARK 620 5 ILE D 207 O 74.8 146.2 162.9 84.3
REMARK 620 6 ASP D 209 OD1 81.6 82.3 116.9 148.6 66.7
REMARK 620 7 ASP D 242 OD1 153.2 94.9 77.3 96.0 88.7 72.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 511 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 208 OD1
REMARK 620 2 ASN D 210 O 80.5
REMARK 620 3 ASP D 240 OD1 142.5 77.5
REMARK 620 4 ASP D 240 OD2 167.3 111.8 48.0
REMARK 620 5 ASP D 242 OD2 63.4 74.7 81.5 122.0
REMARK 620 6 HIS D 246 O 94.9 166.7 99.5 73.9 92.1
REMARK 620 7 ASP D 294 OD2 68.2 84.0 137.7 108.4 129.4 106.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 512 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 225 OE1
REMARK 620 2 GLU D 225 OE2 42.2
REMARK 620 3 ASP D 279 OD1 133.2 91.2
REMARK 620 4 GLU D 281 OE1 91.2 74.8 76.6
REMARK 620 5 ASP D 313 OD1 65.2 106.4 161.1 101.0
REMARK 620 6 ASP D 313 OD2 79.2 112.0 128.7 151.9 51.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 513 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 225 OE1
REMARK 620 2 GLU D 281 OE1 92.3
REMARK 620 3 GLU D 281 OE2 127.6 48.5
REMARK 620 4 ASP D 310 OD1 99.5 117.1 77.6
REMARK 620 5 VAL D 311 O 67.5 152.4 159.0 85.8
REMARK 620 6 ASP D 313 OD1 70.0 91.4 131.0 150.5 64.6
REMARK 620 7 ASP D 345 OD1 157.4 89.6 68.7 99.6 102.0 87.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 514 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 312 OD1
REMARK 620 2 ASN D 314 O 88.1
REMARK 620 3 ASP D 343 OD1 145.0 90.2
REMARK 620 4 ASP D 343 OD2 155.2 115.3 48.8
REMARK 620 5 ASP D 345 OD2 71.9 81.5 73.2 117.4
REMARK 620 6 ASN D 349 O 93.5 171.6 83.7 64.5 91.1
REMARK 620 7 ASP D 396 OD2 67.0 93.1 148.0 102.0 138.7 95.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 9 OE2
REMARK 620 2 ASP E 63 OD1 78.2
REMARK 620 3 GLU E 65 OE1 62.3 90.5
REMARK 620 4 ASP E 100 OD1 106.5 166.3 103.1
REMARK 620 5 ASP E 100 OD2 114.2 121.2 147.5 45.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 510 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 9 OE1
REMARK 620 2 GLU E 65 OE2 95.2
REMARK 620 3 ASP E 97 OD1 84.3 61.6
REMARK 620 4 ILE E 98 O 98.2 148.9 92.0
REMARK 620 5 ASP E 100 OD1 99.3 133.2 163.6 71.7
REMARK 620 6 ASP E 133 OD1 173.6 80.8 89.4 83.0 87.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 511 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN E 99 OD1
REMARK 620 2 HIS E 101 O 97.7
REMARK 620 3 ASP E 131 OD1 144.8 93.0
REMARK 620 4 ASP E 131 OD2 157.8 102.7 43.0
REMARK 620 5 ASP E 133 OD2 88.1 101.7 56.9 96.2
REMARK 620 6 ASN E 137 O 84.4 169.5 79.7 77.2 68.0
REMARK 620 7 ASP E 188 OD2 77.0 130.7 119.5 83.1 126.6 59.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 512 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 116 OE2
REMARK 620 2 ASP E 173 OD1 80.4
REMARK 620 3 GLU E 175 OE1 81.7 106.8
REMARK 620 4 ASP E 209 OD2 64.6 126.5 106.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 513 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 116 OE1
REMARK 620 2 GLU E 175 OE1 78.4
REMARK 620 3 GLU E 175 OE2 118.2 48.9
REMARK 620 4 ASP E 206 OD1 105.8 127.2 88.0
REMARK 620 5 ILE E 207 O 87.9 147.6 153.9 84.7
REMARK 620 6 ASP E 209 OD1 88.8 83.8 110.9 147.4 66.5
REMARK 620 7 ASP E 242 OD1 165.4 96.3 65.1 88.3 89.7 77.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 514 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN E 208 OD1
REMARK 620 2 ASN E 210 O 87.1
REMARK 620 3 ASP E 240 OD1 147.7 73.9
REMARK 620 4 ASP E 240 OD2 166.6 104.6 44.8
REMARK 620 5 ASP E 242 OD2 69.9 81.5 81.5 117.8
REMARK 620 6 HIS E 246 O 95.6 170.6 99.5 73.9 91.1
REMARK 620 7 ASP E 294 OD2 67.8 84.6 133.7 106.3 135.8 104.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 515 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 225 OE2
REMARK 620 2 ASP E 279 OD1 72.9
REMARK 620 3 GLU E 281 OE1 78.8 77.7
REMARK 620 4 ASP E 313 OD1 102.8 166.4 114.6
REMARK 620 5 ASP E 313 OD2 85.7 113.0 157.6 53.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 516 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 225 OE1
REMARK 620 2 GLU E 281 OE2 108.5
REMARK 620 3 ASP E 310 OD1 88.1 102.2
REMARK 620 4 VAL E 311 O 87.7 160.9 88.1
REMARK 620 5 ASP E 313 OD1 86.4 107.2 150.3 62.6
REMARK 620 6 ASP E 345 OD1 162.1 67.9 109.8 93.6 78.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 517 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN E 312 OD1
REMARK 620 2 ASN E 314 O 92.4
REMARK 620 3 ASP E 343 OD2 157.4 109.4
REMARK 620 4 ASP E 345 OD2 73.6 74.1 106.2
REMARK 620 5 ASN E 349 O 95.9 159.3 61.5 90.1
REMARK 620 6 ASP E 396 OD2 72.2 99.6 108.4 144.9 101.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 9 OE2
REMARK 620 2 GLU F 10 OE2 90.0
REMARK 620 3 ASP F 63 OD1 62.5 74.2
REMARK 620 4 GLU F 65 OE1 57.3 140.7 71.5
REMARK 620 5 ASP F 100 OD2 100.3 93.6 158.2 111.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 507 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 9 OE1
REMARK 620 2 GLU F 65 OE2 86.0
REMARK 620 3 ASP F 97 OD1 72.2 94.3
REMARK 620 4 ILE F 98 O 84.6 162.1 68.3
REMARK 620 5 ASP F 100 OD1 92.3 128.3 134.1 67.3
REMARK 620 6 ASP F 133 OD1 177.3 92.5 110.2 97.4 86.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN F 99 OD1
REMARK 620 2 HIS F 101 O 95.5
REMARK 620 3 ASP F 131 OD1 150.0 89.2
REMARK 620 4 ASP F 131 OD2 160.7 97.5 44.7
REMARK 620 5 ASP F 133 OD2 88.0 92.4 62.2 105.7
REMARK 620 6 ASN F 137 O 91.9 170.8 81.7 76.8 82.3
REMARK 620 7 ASP F 188 OD2 74.5 121.4 127.3 86.6 142.7 66.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 116 OE2
REMARK 620 2 ASP F 173 OD1 77.9
REMARK 620 3 GLU F 175 OE1 83.9 76.1
REMARK 620 4 ASP F 209 OD2 62.6 138.6 109.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 510 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 116 OE1
REMARK 620 2 GLU F 175 OE1 80.9
REMARK 620 3 GLU F 175 OE2 120.1 50.9
REMARK 620 4 ASP F 206 OD1 104.6 128.5 86.0
REMARK 620 5 ILE F 207 O 85.8 153.6 152.1 76.9
REMARK 620 6 ASP F 209 OD1 89.5 91.2 120.0 139.1 65.9
REMARK 620 7 ASP F 242 OD1 163.8 100.4 70.9 87.3 86.3 74.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 511 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN F 208 OD1
REMARK 620 2 ASN F 210 O 85.7
REMARK 620 3 ASP F 240 OD1 150.3 76.8
REMARK 620 4 ASP F 240 OD2 159.5 114.7 45.8
REMARK 620 5 ASP F 242 OD2 71.7 83.7 82.6 110.9
REMARK 620 6 HIS F 246 O 94.6 166.5 96.9 66.0 83.6
REMARK 620 7 ASP F 294 OD2 72.0 86.5 129.6 105.7 142.9 106.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 512 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 225 OE1
REMARK 620 2 ASP F 279 OD1 97.9
REMARK 620 3 GLU F 281 OE1 78.2 80.1
REMARK 620 4 ASP F 313 OD1 97.8 164.1 105.1
REMARK 620 5 ASP F 313 OD2 98.2 129.3 150.4 45.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 513 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 225 OE2
REMARK 620 2 GLU F 281 OE1 100.0
REMARK 620 3 GLU F 281 OE2 136.3 46.9
REMARK 620 4 ASP F 310 OD1 93.8 112.2 79.2
REMARK 620 5 VAL F 311 O 65.3 162.1 151.0 80.2
REMARK 620 6 ASP F 313 OD1 73.8 103.0 132.6 144.3 64.2
REMARK 620 7 ASP F 345 OD1 151.8 100.7 71.7 95.9 90.4 83.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 514 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN F 312 OD1
REMARK 620 2 ASN F 314 O 89.9
REMARK 620 3 ASP F 343 OD1 144.9 88.7
REMARK 620 4 ASP F 343 OD2 158.5 111.5 43.3
REMARK 620 5 ASP F 345 OD2 77.3 75.2 68.4 109.7
REMARK 620 6 ASN F 349 O 92.1 172.2 85.3 67.1 97.9
REMARK 620 7 ASP F 396 OD2 65.8 100.9 148.4 105.9 143.0 86.9
REMARK 620 N 1 2 3 4 5 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DZV RELATED DB: PDB
REMARK 900 RELATED ID: 5DZW RELATED DB: PDB
REMARK 900 RELATED ID: 5DZX RELATED DB: PDB
DBREF 5DZY A 1 418 UNP A8E4K6 A8E4K6_MOUSE 29 446
DBREF 5DZY B 1 418 UNP A8E4K6 A8E4K6_MOUSE 29 446
DBREF 5DZY C 1 418 UNP A8E4K6 A8E4K6_MOUSE 29 446
DBREF 5DZY D 1 418 UNP A8E4K6 A8E4K6_MOUSE 29 446
DBREF 5DZY E 1 418 UNP A8E4K6 A8E4K6_MOUSE 29 446
DBREF 5DZY F 1 418 UNP A8E4K6 A8E4K6_MOUSE 29 446
SEQADV 5DZY HIS A 419 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS A 420 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS A 421 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS A 422 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS A 423 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS A 424 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS A 425 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS A 426 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS B 419 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS B 420 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS B 421 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS B 422 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS B 423 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS B 424 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS B 425 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS B 426 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS C 419 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS C 420 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS C 421 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS C 422 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS C 423 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS C 424 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS C 425 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS C 426 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS D 419 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS D 420 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS D 421 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS D 422 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS D 423 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS D 424 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS D 425 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS D 426 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS E 419 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS E 420 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS E 421 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS E 422 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS E 423 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS E 424 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS E 425 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS E 426 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS F 419 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS F 420 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS F 421 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS F 422 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS F 423 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS F 424 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS F 425 UNP A8E4K6 EXPRESSION TAG
SEQADV 5DZY HIS F 426 UNP A8E4K6 EXPRESSION TAG
SEQRES 1 A 426 GLU ALA ILE SER TYR SER MET PRO GLU GLU THR GLU SER
SEQRES 2 A 426 GLY TYR LEU VAL ALA ASN LEU ALA GLN ASP LEU GLY LEU
SEQRES 3 A 426 ARG VAL GLY GLU LEU THR THR ARG GLY ALA ARG ILE HIS
SEQRES 4 A 426 HIS ASN GLY ASN LYS GLU LEU LEU GLN LEU ASP ALA GLU
SEQRES 5 A 426 ARG GLY ASN LEU LEU LEU LYS GLU LYS PRO ASP ARG GLU
SEQRES 6 A 426 ALA LEU CYS GLY ALA THR GLU PRO CYS VAL LEU HIS PHE
SEQRES 7 A 426 GLN ILE ILE LEU GLU ASN PRO VAL GLN PHE PHE GLN THR
SEQRES 8 A 426 ASP LEU GLN PHE THR ASP ILE ASN ASP HIS PHE PRO GLU
SEQRES 9 A 426 PHE PRO ASP THR GLU MET LEU LEU LYS ILE GLN GLU ILE
SEQRES 10 A 426 ALA GLN PRO GLY THR VAL PHE PRO LEU LYS ALA ALA GLN
SEQRES 11 A 426 ASP PRO ASP ILE GLY SER ASN ALA VAL GLN ASN TYR THR
SEQRES 12 A 426 VAL SER PRO ASN LEU HIS PHE HIS VAL VAL THR LEU SER
SEQRES 13 A 426 ARG SER ASP ASP ARG LYS TYR PRO GLU LEU VAL LEU ASP
SEQRES 14 A 426 ARG ALA LEU ASP ARG GLU GLU GLN PRO GLU LEU THR LEU
SEQRES 15 A 426 ILE LEU THR ALA LEU ASP GLY GLY ALA PRO PRO LYS SER
SEQRES 16 A 426 GLY THR THR THR VAL ARG ILE GLU VAL VAL ASP ILE ASN
SEQRES 17 A 426 ASP ASN ALA PRO GLN PHE LEU GLN SER LEU TYR ALA VAL
SEQRES 18 A 426 GLU VAL PRO GLU ASN SER PRO LEU ASN ALA LEU VAL VAL
SEQRES 19 A 426 THR VAL SER ALA ARG ASP LEU ASP ALA GLY ILE HIS GLY
SEQRES 20 A 426 ASN VAL ALA TYR SER LEU PHE GLN GLY GLY GLY GLY PRO
SEQRES 21 A 426 GLN PRO PHE VAL ILE ASP GLU ILE THR GLY GLU ILE ARG
SEQRES 22 A 426 LEU LYS GLY ALA LEU ASP PHE GLU ALA THR SER TYR TYR
SEQRES 23 A 426 THR MET GLU ILE VAL ALA THR ASP SER GLY GLY LEU SER
SEQRES 24 A 426 GLY LYS CYS THR VAL ALA ILE GLN VAL LEU ASP VAL ASN
SEQRES 25 A 426 ASP ASN ALA PRO LYS LEU THR ILE SER SER LEU THR SER
SEQRES 26 A 426 SER ILE PRO GLU ASN ALA PRO GLU ALA VAL VAL ALA VAL
SEQRES 27 A 426 PHE SER VAL SER ASP PRO ASP SER GLY ASP ASN GLY ARG
SEQRES 28 A 426 MET VAL CYS SER ILE GLN ASN GLY LEU PRO PHE LEU LEU
SEQRES 29 A 426 LYS PRO THR PHE LYS ASN PHE TYR THR LEU VAL THR GLU
SEQRES 30 A 426 ARG PRO LEU ASP ARG GLU SER ASN ALA GLU TYR ASN ILE
SEQRES 31 A 426 THR ILE THR VAL SER ASP LEU GLY THR PRO ARG LEU THR
SEQRES 32 A 426 THR GLN HIS THR ILE THR VAL GLN VAL SER ASP ILE ASN
SEQRES 33 A 426 ASP ASN HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 426 GLU ALA ILE SER TYR SER MET PRO GLU GLU THR GLU SER
SEQRES 2 B 426 GLY TYR LEU VAL ALA ASN LEU ALA GLN ASP LEU GLY LEU
SEQRES 3 B 426 ARG VAL GLY GLU LEU THR THR ARG GLY ALA ARG ILE HIS
SEQRES 4 B 426 HIS ASN GLY ASN LYS GLU LEU LEU GLN LEU ASP ALA GLU
SEQRES 5 B 426 ARG GLY ASN LEU LEU LEU LYS GLU LYS PRO ASP ARG GLU
SEQRES 6 B 426 ALA LEU CYS GLY ALA THR GLU PRO CYS VAL LEU HIS PHE
SEQRES 7 B 426 GLN ILE ILE LEU GLU ASN PRO VAL GLN PHE PHE GLN THR
SEQRES 8 B 426 ASP LEU GLN PHE THR ASP ILE ASN ASP HIS PHE PRO GLU
SEQRES 9 B 426 PHE PRO ASP THR GLU MET LEU LEU LYS ILE GLN GLU ILE
SEQRES 10 B 426 ALA GLN PRO GLY THR VAL PHE PRO LEU LYS ALA ALA GLN
SEQRES 11 B 426 ASP PRO ASP ILE GLY SER ASN ALA VAL GLN ASN TYR THR
SEQRES 12 B 426 VAL SER PRO ASN LEU HIS PHE HIS VAL VAL THR LEU SER
SEQRES 13 B 426 ARG SER ASP ASP ARG LYS TYR PRO GLU LEU VAL LEU ASP
SEQRES 14 B 426 ARG ALA LEU ASP ARG GLU GLU GLN PRO GLU LEU THR LEU
SEQRES 15 B 426 ILE LEU THR ALA LEU ASP GLY GLY ALA PRO PRO LYS SER
SEQRES 16 B 426 GLY THR THR THR VAL ARG ILE GLU VAL VAL ASP ILE ASN
SEQRES 17 B 426 ASP ASN ALA PRO GLN PHE LEU GLN SER LEU TYR ALA VAL
SEQRES 18 B 426 GLU VAL PRO GLU ASN SER PRO LEU ASN ALA LEU VAL VAL
SEQRES 19 B 426 THR VAL SER ALA ARG ASP LEU ASP ALA GLY ILE HIS GLY
SEQRES 20 B 426 ASN VAL ALA TYR SER LEU PHE GLN GLY GLY GLY GLY PRO
SEQRES 21 B 426 GLN PRO PHE VAL ILE ASP GLU ILE THR GLY GLU ILE ARG
SEQRES 22 B 426 LEU LYS GLY ALA LEU ASP PHE GLU ALA THR SER TYR TYR
SEQRES 23 B 426 THR MET GLU ILE VAL ALA THR ASP SER GLY GLY LEU SER
SEQRES 24 B 426 GLY LYS CYS THR VAL ALA ILE GLN VAL LEU ASP VAL ASN
SEQRES 25 B 426 ASP ASN ALA PRO LYS LEU THR ILE SER SER LEU THR SER
SEQRES 26 B 426 SER ILE PRO GLU ASN ALA PRO GLU ALA VAL VAL ALA VAL
SEQRES 27 B 426 PHE SER VAL SER ASP PRO ASP SER GLY ASP ASN GLY ARG
SEQRES 28 B 426 MET VAL CYS SER ILE GLN ASN GLY LEU PRO PHE LEU LEU
SEQRES 29 B 426 LYS PRO THR PHE LYS ASN PHE TYR THR LEU VAL THR GLU
SEQRES 30 B 426 ARG PRO LEU ASP ARG GLU SER ASN ALA GLU TYR ASN ILE
SEQRES 31 B 426 THR ILE THR VAL SER ASP LEU GLY THR PRO ARG LEU THR
SEQRES 32 B 426 THR GLN HIS THR ILE THR VAL GLN VAL SER ASP ILE ASN
SEQRES 33 B 426 ASP ASN HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 426 GLU ALA ILE SER TYR SER MET PRO GLU GLU THR GLU SER
SEQRES 2 C 426 GLY TYR LEU VAL ALA ASN LEU ALA GLN ASP LEU GLY LEU
SEQRES 3 C 426 ARG VAL GLY GLU LEU THR THR ARG GLY ALA ARG ILE HIS
SEQRES 4 C 426 HIS ASN GLY ASN LYS GLU LEU LEU GLN LEU ASP ALA GLU
SEQRES 5 C 426 ARG GLY ASN LEU LEU LEU LYS GLU LYS PRO ASP ARG GLU
SEQRES 6 C 426 ALA LEU CYS GLY ALA THR GLU PRO CYS VAL LEU HIS PHE
SEQRES 7 C 426 GLN ILE ILE LEU GLU ASN PRO VAL GLN PHE PHE GLN THR
SEQRES 8 C 426 ASP LEU GLN PHE THR ASP ILE ASN ASP HIS PHE PRO GLU
SEQRES 9 C 426 PHE PRO ASP THR GLU MET LEU LEU LYS ILE GLN GLU ILE
SEQRES 10 C 426 ALA GLN PRO GLY THR VAL PHE PRO LEU LYS ALA ALA GLN
SEQRES 11 C 426 ASP PRO ASP ILE GLY SER ASN ALA VAL GLN ASN TYR THR
SEQRES 12 C 426 VAL SER PRO ASN LEU HIS PHE HIS VAL VAL THR LEU SER
SEQRES 13 C 426 ARG SER ASP ASP ARG LYS TYR PRO GLU LEU VAL LEU ASP
SEQRES 14 C 426 ARG ALA LEU ASP ARG GLU GLU GLN PRO GLU LEU THR LEU
SEQRES 15 C 426 ILE LEU THR ALA LEU ASP GLY GLY ALA PRO PRO LYS SER
SEQRES 16 C 426 GLY THR THR THR VAL ARG ILE GLU VAL VAL ASP ILE ASN
SEQRES 17 C 426 ASP ASN ALA PRO GLN PHE LEU GLN SER LEU TYR ALA VAL
SEQRES 18 C 426 GLU VAL PRO GLU ASN SER PRO LEU ASN ALA LEU VAL VAL
SEQRES 19 C 426 THR VAL SER ALA ARG ASP LEU ASP ALA GLY ILE HIS GLY
SEQRES 20 C 426 ASN VAL ALA TYR SER LEU PHE GLN GLY GLY GLY GLY PRO
SEQRES 21 C 426 GLN PRO PHE VAL ILE ASP GLU ILE THR GLY GLU ILE ARG
SEQRES 22 C 426 LEU LYS GLY ALA LEU ASP PHE GLU ALA THR SER TYR TYR
SEQRES 23 C 426 THR MET GLU ILE VAL ALA THR ASP SER GLY GLY LEU SER
SEQRES 24 C 426 GLY LYS CYS THR VAL ALA ILE GLN VAL LEU ASP VAL ASN
SEQRES 25 C 426 ASP ASN ALA PRO LYS LEU THR ILE SER SER LEU THR SER
SEQRES 26 C 426 SER ILE PRO GLU ASN ALA PRO GLU ALA VAL VAL ALA VAL
SEQRES 27 C 426 PHE SER VAL SER ASP PRO ASP SER GLY ASP ASN GLY ARG
SEQRES 28 C 426 MET VAL CYS SER ILE GLN ASN GLY LEU PRO PHE LEU LEU
SEQRES 29 C 426 LYS PRO THR PHE LYS ASN PHE TYR THR LEU VAL THR GLU
SEQRES 30 C 426 ARG PRO LEU ASP ARG GLU SER ASN ALA GLU TYR ASN ILE
SEQRES 31 C 426 THR ILE THR VAL SER ASP LEU GLY THR PRO ARG LEU THR
SEQRES 32 C 426 THR GLN HIS THR ILE THR VAL GLN VAL SER ASP ILE ASN
SEQRES 33 C 426 ASP ASN HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 D 426 GLU ALA ILE SER TYR SER MET PRO GLU GLU THR GLU SER
SEQRES 2 D 426 GLY TYR LEU VAL ALA ASN LEU ALA GLN ASP LEU GLY LEU
SEQRES 3 D 426 ARG VAL GLY GLU LEU THR THR ARG GLY ALA ARG ILE HIS
SEQRES 4 D 426 HIS ASN GLY ASN LYS GLU LEU LEU GLN LEU ASP ALA GLU
SEQRES 5 D 426 ARG GLY ASN LEU LEU LEU LYS GLU LYS PRO ASP ARG GLU
SEQRES 6 D 426 ALA LEU CYS GLY ALA THR GLU PRO CYS VAL LEU HIS PHE
SEQRES 7 D 426 GLN ILE ILE LEU GLU ASN PRO VAL GLN PHE PHE GLN THR
SEQRES 8 D 426 ASP LEU GLN PHE THR ASP ILE ASN ASP HIS PHE PRO GLU
SEQRES 9 D 426 PHE PRO ASP THR GLU MET LEU LEU LYS ILE GLN GLU ILE
SEQRES 10 D 426 ALA GLN PRO GLY THR VAL PHE PRO LEU LYS ALA ALA GLN
SEQRES 11 D 426 ASP PRO ASP ILE GLY SER ASN ALA VAL GLN ASN TYR THR
SEQRES 12 D 426 VAL SER PRO ASN LEU HIS PHE HIS VAL VAL THR LEU SER
SEQRES 13 D 426 ARG SER ASP ASP ARG LYS TYR PRO GLU LEU VAL LEU ASP
SEQRES 14 D 426 ARG ALA LEU ASP ARG GLU GLU GLN PRO GLU LEU THR LEU
SEQRES 15 D 426 ILE LEU THR ALA LEU ASP GLY GLY ALA PRO PRO LYS SER
SEQRES 16 D 426 GLY THR THR THR VAL ARG ILE GLU VAL VAL ASP ILE ASN
SEQRES 17 D 426 ASP ASN ALA PRO GLN PHE LEU GLN SER LEU TYR ALA VAL
SEQRES 18 D 426 GLU VAL PRO GLU ASN SER PRO LEU ASN ALA LEU VAL VAL
SEQRES 19 D 426 THR VAL SER ALA ARG ASP LEU ASP ALA GLY ILE HIS GLY
SEQRES 20 D 426 ASN VAL ALA TYR SER LEU PHE GLN GLY GLY GLY GLY PRO
SEQRES 21 D 426 GLN PRO PHE VAL ILE ASP GLU ILE THR GLY GLU ILE ARG
SEQRES 22 D 426 LEU LYS GLY ALA LEU ASP PHE GLU ALA THR SER TYR TYR
SEQRES 23 D 426 THR MET GLU ILE VAL ALA THR ASP SER GLY GLY LEU SER
SEQRES 24 D 426 GLY LYS CYS THR VAL ALA ILE GLN VAL LEU ASP VAL ASN
SEQRES 25 D 426 ASP ASN ALA PRO LYS LEU THR ILE SER SER LEU THR SER
SEQRES 26 D 426 SER ILE PRO GLU ASN ALA PRO GLU ALA VAL VAL ALA VAL
SEQRES 27 D 426 PHE SER VAL SER ASP PRO ASP SER GLY ASP ASN GLY ARG
SEQRES 28 D 426 MET VAL CYS SER ILE GLN ASN GLY LEU PRO PHE LEU LEU
SEQRES 29 D 426 LYS PRO THR PHE LYS ASN PHE TYR THR LEU VAL THR GLU
SEQRES 30 D 426 ARG PRO LEU ASP ARG GLU SER ASN ALA GLU TYR ASN ILE
SEQRES 31 D 426 THR ILE THR VAL SER ASP LEU GLY THR PRO ARG LEU THR
SEQRES 32 D 426 THR GLN HIS THR ILE THR VAL GLN VAL SER ASP ILE ASN
SEQRES 33 D 426 ASP ASN HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 E 426 GLU ALA ILE SER TYR SER MET PRO GLU GLU THR GLU SER
SEQRES 2 E 426 GLY TYR LEU VAL ALA ASN LEU ALA GLN ASP LEU GLY LEU
SEQRES 3 E 426 ARG VAL GLY GLU LEU THR THR ARG GLY ALA ARG ILE HIS
SEQRES 4 E 426 HIS ASN GLY ASN LYS GLU LEU LEU GLN LEU ASP ALA GLU
SEQRES 5 E 426 ARG GLY ASN LEU LEU LEU LYS GLU LYS PRO ASP ARG GLU
SEQRES 6 E 426 ALA LEU CYS GLY ALA THR GLU PRO CYS VAL LEU HIS PHE
SEQRES 7 E 426 GLN ILE ILE LEU GLU ASN PRO VAL GLN PHE PHE GLN THR
SEQRES 8 E 426 ASP LEU GLN PHE THR ASP ILE ASN ASP HIS PHE PRO GLU
SEQRES 9 E 426 PHE PRO ASP THR GLU MET LEU LEU LYS ILE GLN GLU ILE
SEQRES 10 E 426 ALA GLN PRO GLY THR VAL PHE PRO LEU LYS ALA ALA GLN
SEQRES 11 E 426 ASP PRO ASP ILE GLY SER ASN ALA VAL GLN ASN TYR THR
SEQRES 12 E 426 VAL SER PRO ASN LEU HIS PHE HIS VAL VAL THR LEU SER
SEQRES 13 E 426 ARG SER ASP ASP ARG LYS TYR PRO GLU LEU VAL LEU ASP
SEQRES 14 E 426 ARG ALA LEU ASP ARG GLU GLU GLN PRO GLU LEU THR LEU
SEQRES 15 E 426 ILE LEU THR ALA LEU ASP GLY GLY ALA PRO PRO LYS SER
SEQRES 16 E 426 GLY THR THR THR VAL ARG ILE GLU VAL VAL ASP ILE ASN
SEQRES 17 E 426 ASP ASN ALA PRO GLN PHE LEU GLN SER LEU TYR ALA VAL
SEQRES 18 E 426 GLU VAL PRO GLU ASN SER PRO LEU ASN ALA LEU VAL VAL
SEQRES 19 E 426 THR VAL SER ALA ARG ASP LEU ASP ALA GLY ILE HIS GLY
SEQRES 20 E 426 ASN VAL ALA TYR SER LEU PHE GLN GLY GLY GLY GLY PRO
SEQRES 21 E 426 GLN PRO PHE VAL ILE ASP GLU ILE THR GLY GLU ILE ARG
SEQRES 22 E 426 LEU LYS GLY ALA LEU ASP PHE GLU ALA THR SER TYR TYR
SEQRES 23 E 426 THR MET GLU ILE VAL ALA THR ASP SER GLY GLY LEU SER
SEQRES 24 E 426 GLY LYS CYS THR VAL ALA ILE GLN VAL LEU ASP VAL ASN
SEQRES 25 E 426 ASP ASN ALA PRO LYS LEU THR ILE SER SER LEU THR SER
SEQRES 26 E 426 SER ILE PRO GLU ASN ALA PRO GLU ALA VAL VAL ALA VAL
SEQRES 27 E 426 PHE SER VAL SER ASP PRO ASP SER GLY ASP ASN GLY ARG
SEQRES 28 E 426 MET VAL CYS SER ILE GLN ASN GLY LEU PRO PHE LEU LEU
SEQRES 29 E 426 LYS PRO THR PHE LYS ASN PHE TYR THR LEU VAL THR GLU
SEQRES 30 E 426 ARG PRO LEU ASP ARG GLU SER ASN ALA GLU TYR ASN ILE
SEQRES 31 E 426 THR ILE THR VAL SER ASP LEU GLY THR PRO ARG LEU THR
SEQRES 32 E 426 THR GLN HIS THR ILE THR VAL GLN VAL SER ASP ILE ASN
SEQRES 33 E 426 ASP ASN HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 F 426 GLU ALA ILE SER TYR SER MET PRO GLU GLU THR GLU SER
SEQRES 2 F 426 GLY TYR LEU VAL ALA ASN LEU ALA GLN ASP LEU GLY LEU
SEQRES 3 F 426 ARG VAL GLY GLU LEU THR THR ARG GLY ALA ARG ILE HIS
SEQRES 4 F 426 HIS ASN GLY ASN LYS GLU LEU LEU GLN LEU ASP ALA GLU
SEQRES 5 F 426 ARG GLY ASN LEU LEU LEU LYS GLU LYS PRO ASP ARG GLU
SEQRES 6 F 426 ALA LEU CYS GLY ALA THR GLU PRO CYS VAL LEU HIS PHE
SEQRES 7 F 426 GLN ILE ILE LEU GLU ASN PRO VAL GLN PHE PHE GLN THR
SEQRES 8 F 426 ASP LEU GLN PHE THR ASP ILE ASN ASP HIS PHE PRO GLU
SEQRES 9 F 426 PHE PRO ASP THR GLU MET LEU LEU LYS ILE GLN GLU ILE
SEQRES 10 F 426 ALA GLN PRO GLY THR VAL PHE PRO LEU LYS ALA ALA GLN
SEQRES 11 F 426 ASP PRO ASP ILE GLY SER ASN ALA VAL GLN ASN TYR THR
SEQRES 12 F 426 VAL SER PRO ASN LEU HIS PHE HIS VAL VAL THR LEU SER
SEQRES 13 F 426 ARG SER ASP ASP ARG LYS TYR PRO GLU LEU VAL LEU ASP
SEQRES 14 F 426 ARG ALA LEU ASP ARG GLU GLU GLN PRO GLU LEU THR LEU
SEQRES 15 F 426 ILE LEU THR ALA LEU ASP GLY GLY ALA PRO PRO LYS SER
SEQRES 16 F 426 GLY THR THR THR VAL ARG ILE GLU VAL VAL ASP ILE ASN
SEQRES 17 F 426 ASP ASN ALA PRO GLN PHE LEU GLN SER LEU TYR ALA VAL
SEQRES 18 F 426 GLU VAL PRO GLU ASN SER PRO LEU ASN ALA LEU VAL VAL
SEQRES 19 F 426 THR VAL SER ALA ARG ASP LEU ASP ALA GLY ILE HIS GLY
SEQRES 20 F 426 ASN VAL ALA TYR SER LEU PHE GLN GLY GLY GLY GLY PRO
SEQRES 21 F 426 GLN PRO PHE VAL ILE ASP GLU ILE THR GLY GLU ILE ARG
SEQRES 22 F 426 LEU LYS GLY ALA LEU ASP PHE GLU ALA THR SER TYR TYR
SEQRES 23 F 426 THR MET GLU ILE VAL ALA THR ASP SER GLY GLY LEU SER
SEQRES 24 F 426 GLY LYS CYS THR VAL ALA ILE GLN VAL LEU ASP VAL ASN
SEQRES 25 F 426 ASP ASN ALA PRO LYS LEU THR ILE SER SER LEU THR SER
SEQRES 26 F 426 SER ILE PRO GLU ASN ALA PRO GLU ALA VAL VAL ALA VAL
SEQRES 27 F 426 PHE SER VAL SER ASP PRO ASP SER GLY ASP ASN GLY ARG
SEQRES 28 F 426 MET VAL CYS SER ILE GLN ASN GLY LEU PRO PHE LEU LEU
SEQRES 29 F 426 LYS PRO THR PHE LYS ASN PHE TYR THR LEU VAL THR GLU
SEQRES 30 F 426 ARG PRO LEU ASP ARG GLU SER ASN ALA GLU TYR ASN ILE
SEQRES 31 F 426 THR ILE THR VAL SER ASP LEU GLY THR PRO ARG LEU THR
SEQRES 32 F 426 THR GLN HIS THR ILE THR VAL GLN VAL SER ASP ILE ASN
SEQRES 33 F 426 ASP ASN HIS HIS HIS HIS HIS HIS HIS HIS
HET NAG G 1 14
HET FUC G 2 10
HET NAG H 1 14
HET FUC H 2 10
HET NAG I 1 14
HET NAG I 2 14
HET BMA I 3 11
HET MAN I 4 11
HET NAG I 5 14
HET GAL I 6 11
HET MAN I 7 11
HET NAG I 8 14
HET FUC I 9 10
HET NAG J 1 14
HET NAG J 2 14
HET BMA J 3 11
HET NAG K 1 14
HET FUC K 2 10
HET NAG L 1 14
HET NAG L 2 14
HET BMA L 3 11
HET MAN L 4 11
HET FUC L 5 10
HET MAN A 505 11
HET MAN A 506 11
HET MAN A 507 11
HET CA A 508 1
HET CA A 509 1
HET CA A 510 1
HET CA A 511 1
HET CA A 512 1
HET CA A 513 1
HET CA A 514 1
HET CA A 515 1
HET CA A 516 1
HET NAG B 501 14
HET MAN B 511 11
HET MAN B 512 11
HET MAN B 513 11
HET CA B 514 1
HET CA B 515 1
HET CA B 516 1
HET CA B 517 1
HET CA B 518 1
HET CA B 519 1
HET CA B 520 1
HET CA B 521 1
HET CA B 522 1
HET MAN C 504 11
HET MAN C 505 11
HET MAN C 506 11
HET CA C 507 1
HET CA C 508 1
HET CA C 509 1
HET CA C 510 1
HET CA C 511 1
HET CA C 512 1
HET CA C 513 1
HET CA C 514 1
HET CA C 515 1
HET MAN D 503 11
HET MAN D 504 11
HET MAN D 505 11
HET CA D 506 1
HET CA D 507 1
HET CA D 508 1
HET CA D 509 1
HET CA D 510 1
HET CA D 511 1
HET CA D 512 1
HET CA D 513 1
HET CA D 514 1
HET MAN E 506 11
HET MAN E 507 11
HET MAN E 508 11
HET CA E 509 1
HET CA E 510 1
HET CA E 511 1
HET CA E 512 1
HET CA E 513 1
HET CA E 514 1
HET CA E 515 1
HET CA E 516 1
HET CA E 517 1
HET NAG F 501 14
HET NAG F 502 14
HET MAN F 503 11
HET MAN F 504 11
HET MAN F 505 11
HET CA F 506 1
HET CA F 507 1
HET CA F 508 1
HET CA F 509 1
HET CA F 510 1
HET CA F 511 1
HET CA F 512 1
HET CA F 513 1
HET CA F 514 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM CA CALCIUM 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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
FORMUL 7 NAG 14(C8 H15 N O6)
FORMUL 7 FUC 5(C6 H12 O5)
FORMUL 9 BMA 3(C6 H12 O6)
FORMUL 9 MAN 21(C6 H12 O6)
FORMUL 9 GAL C6 H12 O6
FORMUL 16 CA 54(CA 2+)
FORMUL 88 HOH *6(H2 O)
HELIX 1 AA1 ASN A 19 GLY A 25 1 7
HELIX 2 AA2 GLY A 29 ARG A 34 1 6
HELIX 3 AA3 ASP A 63 CYS A 68 1 6
HELIX 4 AA4 ILE A 134 ASN A 137 5 4
HELIX 5 AA5 ALA A 243 GLY A 247 5 5
HELIX 6 AA6 SER A 346 GLY A 350 5 5
HELIX 7 AA7 ASN B 19 GLY B 25 1 7
HELIX 8 AA8 ARG B 27 ARG B 34 1 8
HELIX 9 AA9 ASP B 63 CYS B 68 1 6
HELIX 10 AB1 ILE B 134 ASN B 137 5 4
HELIX 11 AB2 ALA B 243 GLY B 247 5 5
HELIX 12 AB3 SER B 346 GLY B 350 5 5
HELIX 13 AB4 ASN C 19 GLY C 25 1 7
HELIX 14 AB5 ARG C 27 ARG C 34 1 8
HELIX 15 AB6 ASP C 63 CYS C 68 1 6
HELIX 16 AB7 ILE C 134 ASN C 137 5 4
HELIX 17 AB8 SER C 158 ASP C 160 5 3
HELIX 18 AB9 ALA C 243 GLY C 247 5 5
HELIX 19 AC1 SER C 346 GLY C 350 5 5
HELIX 20 AC2 ASN D 19 GLY D 25 1 7
HELIX 21 AC3 ARG D 27 ARG D 34 1 8
HELIX 22 AC4 ILE D 134 ASN D 137 5 4
HELIX 23 AC5 ALA D 243 GLY D 247 5 5
HELIX 24 AC6 SER D 346 GLY D 350 5 5
HELIX 25 AC7 LEU E 20 GLY E 25 1 6
HELIX 26 AC8 ARG E 27 ARG E 34 1 8
HELIX 27 AC9 ASP E 63 LEU E 67 5 5
HELIX 28 AD1 ILE E 134 ASN E 137 5 4
HELIX 29 AD2 ALA E 243 GLY E 247 5 5
HELIX 30 AD3 SER E 346 GLY E 350 5 5
HELIX 31 AD4 LEU F 20 GLY F 25 1 6
HELIX 32 AD5 ARG F 27 ARG F 34 1 8
HELIX 33 AD6 ASP F 63 CYS F 68 1 6
HELIX 34 AD7 ILE F 134 ASN F 137 5 4
HELIX 35 AD8 ALA F 243 GLY F 247 5 5
HELIX 36 AD9 SER F 346 GLY F 350 5 5
SHEET 1 AA1 4 SER A 4 PRO A 8 0
SHEET 2 AA1 4 GLN A 87 THR A 96 1 O GLN A 94 N TYR A 5
SHEET 3 AA1 4 VAL A 75 LEU A 82 -1 N PHE A 78 O THR A 91
SHEET 4 AA1 4 ARG A 37 HIS A 39 -1 N HIS A 39 O GLN A 79
SHEET 1 AA2 3 LEU A 16 ALA A 18 0
SHEET 2 AA2 3 ASN A 55 LEU A 58 -1 O LEU A 56 N ALA A 18
SHEET 3 AA2 3 LEU A 47 ASP A 50 -1 N GLN A 48 O LEU A 57
SHEET 1 AA3 4 GLU A 109 GLN A 115 0
SHEET 2 AA3 4 SER A 195 VAL A 205 1 O GLU A 203 N LEU A 112
SHEET 3 AA3 4 GLU A 179 ASP A 188 -1 N LEU A 182 O VAL A 200
SHEET 4 AA3 4 VAL A 139 VAL A 144 -1 N THR A 143 O THR A 185
SHEET 1 AA4 3 VAL A 123 PRO A 125 0
SHEET 2 AA4 3 TYR A 163 LEU A 168 -1 O LEU A 166 N PHE A 124
SHEET 3 AA4 3 PHE A 150 LEU A 155 -1 N VAL A 153 O GLU A 165
SHEET 1 AA5 2 GLN A 213 PHE A 214 0
SHEET 2 AA5 2 ALA A 238 ARG A 239 -1 O ARG A 239 N GLN A 213
SHEET 1 AA6 4 LEU A 218 PRO A 224 0
SHEET 2 AA6 4 SER A 299 LEU A 309 1 O ALA A 305 N TYR A 219
SHEET 3 AA6 4 TYR A 285 THR A 293 -1 N MET A 288 O VAL A 304
SHEET 4 AA6 4 ALA A 250 PHE A 254 -1 N SER A 252 O VAL A 291
SHEET 1 AA7 3 LEU A 232 THR A 235 0
SHEET 2 AA7 3 GLU A 271 LEU A 274 -1 O ILE A 272 N VAL A 234
SHEET 3 AA7 3 PHE A 263 ILE A 265 -1 N VAL A 264 O ARG A 273
SHEET 1 AA8 4 LYS A 317 SER A 322 0
SHEET 2 AA8 4 VAL A 335 SER A 342 -1 O VAL A 338 N SER A 321
SHEET 3 AA8 4 PHE A 371 THR A 376 -1 O LEU A 374 N ALA A 337
SHEET 4 AA8 4 PHE A 362 PHE A 368 -1 N LYS A 365 O THR A 373
SHEET 1 AA9 4 SER A 326 ILE A 327 0
SHEET 2 AA9 4 THR A 403 VAL A 412 1 O GLN A 411 N ILE A 327
SHEET 3 AA9 4 GLU A 387 ASP A 396 -1 N VAL A 394 O THR A 404
SHEET 4 AA9 4 MET A 352 SER A 355 -1 N SER A 355 O THR A 393
SHEET 1 AB1 4 ILE B 3 PRO B 8 0
SHEET 2 AB1 4 GLN B 87 THR B 96 1 O ASP B 92 N ILE B 3
SHEET 3 AB1 4 VAL B 75 LEU B 82 -1 N PHE B 78 O THR B 91
SHEET 4 AB1 4 ARG B 37 HIS B 39 -1 N HIS B 39 O GLN B 79
SHEET 1 AB2 3 LEU B 16 ALA B 18 0
SHEET 2 AB2 3 ASN B 55 LEU B 58 -1 O LEU B 56 N VAL B 17
SHEET 3 AB2 3 LEU B 47 ASP B 50 -1 N GLN B 48 O LEU B 57
SHEET 1 AB3 4 GLU B 109 GLN B 115 0
SHEET 2 AB3 4 THR B 197 VAL B 205 1 O GLU B 203 N LEU B 112
SHEET 3 AB3 4 GLU B 179 ASP B 188 -1 N LEU B 180 O ILE B 202
SHEET 4 AB3 4 VAL B 139 VAL B 144 -1 N THR B 143 O THR B 185
SHEET 1 AB4 3 VAL B 123 PRO B 125 0
SHEET 2 AB4 3 ARG B 161 LEU B 168 -1 O LEU B 166 N PHE B 124
SHEET 3 AB4 3 PHE B 150 ARG B 157 -1 N ARG B 157 O ARG B 161
SHEET 1 AB5 2 GLN B 213 PHE B 214 0
SHEET 2 AB5 2 ALA B 238 ARG B 239 -1 O ARG B 239 N GLN B 213
SHEET 1 AB6 4 LEU B 218 PRO B 224 0
SHEET 2 AB6 4 SER B 299 LEU B 309 1 O ALA B 305 N TYR B 219
SHEET 3 AB6 4 TYR B 285 THR B 293 -1 N MET B 288 O VAL B 304
SHEET 4 AB6 4 ALA B 250 PHE B 254 -1 N SER B 252 O VAL B 291
SHEET 1 AB7 3 LEU B 232 THR B 235 0
SHEET 2 AB7 3 GLU B 271 LEU B 274 -1 O ILE B 272 N VAL B 233
SHEET 3 AB7 3 PHE B 263 ILE B 265 -1 N VAL B 264 O ARG B 273
SHEET 1 AB8 4 LYS B 317 SER B 322 0
SHEET 2 AB8 4 VAL B 335 SER B 342 -1 O VAL B 338 N SER B 321
SHEET 3 AB8 4 PHE B 371 THR B 376 -1 O LEU B 374 N ALA B 337
SHEET 4 AB8 4 PHE B 362 PHE B 368 -1 N LEU B 363 O VAL B 375
SHEET 1 AB9 4 SER B 326 ILE B 327 0
SHEET 2 AB9 4 THR B 403 VAL B 412 1 O GLN B 411 N ILE B 327
SHEET 3 AB9 4 GLU B 387 ASP B 396 -1 N TYR B 388 O VAL B 410
SHEET 4 AB9 4 MET B 352 SER B 355 -1 N VAL B 353 O SER B 395
SHEET 1 AC1 4 ILE C 3 PRO C 8 0
SHEET 2 AC1 4 GLN C 87 THR C 96 1 O ASP C 92 N TYR C 5
SHEET 3 AC1 4 CYS C 74 LEU C 82 -1 N PHE C 78 O THR C 91
SHEET 4 AC1 4 ARG C 37 HIS C 39 -1 N HIS C 39 O GLN C 79
SHEET 1 AC2 3 LEU C 16 ALA C 18 0
SHEET 2 AC2 3 ASN C 55 LEU C 58 -1 O LEU C 56 N VAL C 17
SHEET 3 AC2 3 LEU C 47 ASP C 50 -1 N GLN C 48 O LEU C 57
SHEET 1 AC3 4 GLU C 109 GLN C 115 0
SHEET 2 AC3 4 THR C 197 VAL C 205 1 O ARG C 201 N LEU C 112
SHEET 3 AC3 4 GLU C 179 ASP C 188 -1 N LEU C 182 O VAL C 200
SHEET 4 AC3 4 VAL C 139 VAL C 144 -1 N THR C 143 O THR C 185
SHEET 1 AC4 3 VAL C 123 PRO C 125 0
SHEET 2 AC4 3 LYS C 162 LEU C 168 -1 O LEU C 166 N PHE C 124
SHEET 3 AC4 3 PHE C 150 SER C 156 -1 N LEU C 155 O TYR C 163
SHEET 1 AC5 2 GLN C 213 PHE C 214 0
SHEET 2 AC5 2 ALA C 238 ARG C 239 -1 O ARG C 239 N GLN C 213
SHEET 1 AC6 4 LEU C 218 PRO C 224 0
SHEET 2 AC6 4 SER C 299 LEU C 309 1 O LEU C 309 N VAL C 223
SHEET 3 AC6 4 TYR C 285 THR C 293 -1 N TYR C 286 O ILE C 306
SHEET 4 AC6 4 ALA C 250 GLN C 255 -1 N PHE C 254 O GLU C 289
SHEET 1 AC7 3 LEU C 232 THR C 235 0
SHEET 2 AC7 3 GLU C 271 LEU C 274 -1 O ILE C 272 N VAL C 234
SHEET 3 AC7 3 PHE C 263 VAL C 264 -1 N VAL C 264 O ARG C 273
SHEET 1 AC8 4 LYS C 317 SER C 322 0
SHEET 2 AC8 4 VAL C 335 SER C 342 -1 O VAL C 338 N SER C 321
SHEET 3 AC8 4 PHE C 371 THR C 376 -1 O LEU C 374 N ALA C 337
SHEET 4 AC8 4 PHE C 362 PHE C 368 -1 N LEU C 363 O VAL C 375
SHEET 1 AC9 4 SER C 326 PRO C 328 0
SHEET 2 AC9 4 THR C 403 SER C 413 1 O SER C 413 N ILE C 327
SHEET 3 AC9 4 GLU C 387 ASP C 396 -1 N TYR C 388 O VAL C 410
SHEET 4 AC9 4 MET C 352 SER C 355 -1 N VAL C 353 O SER C 395
SHEET 1 AD1 4 ILE D 3 PRO D 8 0
SHEET 2 AD1 4 THR D 91 THR D 96 1 O GLN D 94 N TYR D 5
SHEET 3 AD1 4 VAL D 75 LEU D 82 -1 N PHE D 78 O THR D 91
SHEET 4 AD1 4 ARG D 37 HIS D 39 -1 N HIS D 39 O GLN D 79
SHEET 1 AD2 4 ILE D 3 PRO D 8 0
SHEET 2 AD2 4 THR D 91 THR D 96 1 O GLN D 94 N TYR D 5
SHEET 3 AD2 4 VAL D 75 LEU D 82 -1 N PHE D 78 O THR D 91
SHEET 4 AD2 4 GLN D 87 PHE D 88 -1 O GLN D 87 N LEU D 82
SHEET 1 AD3 3 LEU D 16 ALA D 18 0
SHEET 2 AD3 3 ASN D 55 LEU D 58 -1 O LEU D 56 N VAL D 17
SHEET 3 AD3 3 LEU D 47 ASP D 50 -1 N GLN D 48 O LEU D 57
SHEET 1 AD4 4 GLU D 109 GLN D 115 0
SHEET 2 AD4 4 SER D 195 VAL D 205 1 O GLU D 203 N LEU D 112
SHEET 3 AD4 4 GLU D 179 ASP D 188 -1 N LEU D 182 O VAL D 200
SHEET 4 AD4 4 VAL D 139 VAL D 144 -1 N THR D 143 O THR D 185
SHEET 1 AD5 3 VAL D 123 PRO D 125 0
SHEET 2 AD5 3 ARG D 161 LEU D 168 -1 O LEU D 166 N PHE D 124
SHEET 3 AD5 3 PHE D 150 ARG D 157 -1 N VAL D 153 O GLU D 165
SHEET 1 AD6 2 GLN D 213 PHE D 214 0
SHEET 2 AD6 2 ALA D 238 ARG D 239 -1 O ARG D 239 N GLN D 213
SHEET 1 AD7 4 LEU D 218 PRO D 224 0
SHEET 2 AD7 4 SER D 299 LEU D 309 1 O ALA D 305 N TYR D 219
SHEET 3 AD7 4 TYR D 285 THR D 293 -1 N ALA D 292 O GLY D 300
SHEET 4 AD7 4 ALA D 250 PHE D 254 -1 N SER D 252 O VAL D 291
SHEET 1 AD8 3 LEU D 232 THR D 235 0
SHEET 2 AD8 3 GLU D 271 LEU D 274 -1 O ILE D 272 N VAL D 234
SHEET 3 AD8 3 PHE D 263 VAL D 264 -1 N VAL D 264 O ARG D 273
SHEET 1 AD9 4 LYS D 317 SER D 322 0
SHEET 2 AD9 4 VAL D 335 SER D 342 -1 O SER D 340 N THR D 319
SHEET 3 AD9 4 PHE D 371 THR D 376 -1 O LEU D 374 N ALA D 337
SHEET 4 AD9 4 PHE D 362 PHE D 368 -1 N LYS D 365 O THR D 373
SHEET 1 AE1 4 SER D 326 PRO D 328 0
SHEET 2 AE1 4 THR D 403 SER D 413 1 O SER D 413 N ILE D 327
SHEET 3 AE1 4 GLU D 387 ASP D 396 -1 N ILE D 390 O ILE D 408
SHEET 4 AE1 4 MET D 352 SER D 355 -1 N SER D 355 O THR D 393
SHEET 1 AE2 4 SER E 4 PRO E 8 0
SHEET 2 AE2 4 GLN E 87 THR E 96 1 O ASP E 92 N TYR E 5
SHEET 3 AE2 4 CYS E 74 LEU E 82 -1 N PHE E 78 O THR E 91
SHEET 4 AE2 4 ARG E 37 HIS E 40 -1 N HIS E 39 O GLN E 79
SHEET 1 AE3 3 LEU E 16 ASN E 19 0
SHEET 2 AE3 3 ASN E 55 LEU E 58 -1 O LEU E 56 N ALA E 18
SHEET 3 AE3 3 LEU E 47 ASP E 50 -1 N GLN E 48 O LEU E 57
SHEET 1 AE4 4 GLU E 109 GLN E 115 0
SHEET 2 AE4 4 SER E 195 VAL E 205 1 O GLU E 203 N LEU E 112
SHEET 3 AE4 4 GLU E 179 ASP E 188 -1 N LEU E 180 O ILE E 202
SHEET 4 AE4 4 VAL E 139 VAL E 144 -1 N THR E 143 O THR E 185
SHEET 1 AE5 3 VAL E 123 PRO E 125 0
SHEET 2 AE5 3 ARG E 161 LEU E 168 -1 O LEU E 166 N PHE E 124
SHEET 3 AE5 3 PHE E 150 ARG E 157 -1 N ARG E 157 O ARG E 161
SHEET 1 AE6 2 GLN E 213 PHE E 214 0
SHEET 2 AE6 2 ALA E 238 ARG E 239 -1 O ARG E 239 N GLN E 213
SHEET 1 AE7 4 LEU E 218 PRO E 224 0
SHEET 2 AE7 4 SER E 299 LEU E 309 1 O LEU E 309 N VAL E 223
SHEET 3 AE7 4 TYR E 285 THR E 293 -1 N TYR E 286 O ILE E 306
SHEET 4 AE7 4 ALA E 250 PHE E 254 -1 N PHE E 254 O GLU E 289
SHEET 1 AE8 3 LEU E 232 THR E 235 0
SHEET 2 AE8 3 GLU E 271 LEU E 274 -1 O ILE E 272 N VAL E 234
SHEET 3 AE8 3 PHE E 263 ILE E 265 -1 N VAL E 264 O ARG E 273
SHEET 1 AE9 4 LYS E 317 SER E 322 0
SHEET 2 AE9 4 VAL E 335 SER E 342 -1 O SER E 340 N THR E 319
SHEET 3 AE9 4 PHE E 371 THR E 376 -1 O LEU E 374 N ALA E 337
SHEET 4 AE9 4 PHE E 362 PHE E 368 -1 N LEU E 363 O VAL E 375
SHEET 1 AF1 4 SER E 326 PRO E 328 0
SHEET 2 AF1 4 THR E 403 SER E 413 1 O SER E 413 N ILE E 327
SHEET 3 AF1 4 GLU E 387 ASP E 396 -1 N ILE E 390 O ILE E 408
SHEET 4 AF1 4 MET E 352 SER E 355 -1 N VAL E 353 O SER E 395
SHEET 1 AF2 4 SER F 4 PRO F 8 0
SHEET 2 AF2 4 GLN F 87 THR F 96 1 O GLN F 94 N TYR F 5
SHEET 3 AF2 4 VAL F 75 LEU F 82 -1 N PHE F 78 O THR F 91
SHEET 4 AF2 4 ARG F 37 HIS F 40 -1 N HIS F 39 O GLN F 79
SHEET 1 AF3 3 LEU F 16 ASN F 19 0
SHEET 2 AF3 3 ASN F 55 LEU F 58 -1 O LEU F 56 N VAL F 17
SHEET 3 AF3 3 LEU F 47 ASP F 50 -1 N GLN F 48 O LEU F 57
SHEET 1 AF4 4 GLU F 109 GLN F 115 0
SHEET 2 AF4 4 SER F 195 VAL F 205 1 O GLU F 203 N LEU F 112
SHEET 3 AF4 4 GLU F 179 ASP F 188 -1 N LEU F 182 O VAL F 200
SHEET 4 AF4 4 VAL F 139 VAL F 144 -1 N THR F 143 O THR F 185
SHEET 1 AF5 3 VAL F 123 PRO F 125 0
SHEET 2 AF5 3 ARG F 161 LEU F 168 -1 O LEU F 166 N PHE F 124
SHEET 3 AF5 3 PHE F 150 ARG F 157 -1 N LEU F 155 O TYR F 163
SHEET 1 AF6 2 GLN F 213 PHE F 214 0
SHEET 2 AF6 2 ALA F 238 ARG F 239 -1 O ARG F 239 N GLN F 213
SHEET 1 AF7 4 LEU F 218 PRO F 224 0
SHEET 2 AF7 4 SER F 299 LEU F 309 1 O GLN F 307 N VAL F 223
SHEET 3 AF7 4 TYR F 285 THR F 293 -1 N ALA F 292 O GLY F 300
SHEET 4 AF7 4 ALA F 250 PHE F 254 -1 N PHE F 254 O GLU F 289
SHEET 1 AF8 3 LEU F 232 THR F 235 0
SHEET 2 AF8 3 GLU F 271 LEU F 274 -1 O ILE F 272 N VAL F 234
SHEET 3 AF8 3 PHE F 263 ILE F 265 -1 N VAL F 264 O ARG F 273
SHEET 1 AF9 4 LYS F 317 SER F 322 0
SHEET 2 AF9 4 VAL F 335 SER F 342 -1 O VAL F 338 N SER F 321
SHEET 3 AF9 4 PHE F 371 THR F 376 -1 O LEU F 374 N ALA F 337
SHEET 4 AF9 4 PHE F 362 PHE F 368 -1 N LEU F 363 O VAL F 375
SHEET 1 AG1 4 SER F 326 ILE F 327 0
SHEET 2 AG1 4 THR F 403 VAL F 412 1 O GLN F 411 N ILE F 327
SHEET 3 AG1 4 GLU F 387 ASP F 396 -1 N VAL F 394 O THR F 404
SHEET 4 AG1 4 MET F 352 SER F 355 -1 N VAL F 353 O SER F 395
SSBOND 1 CYS A 68 CYS A 74 1555 1555 2.03
SSBOND 2 CYS B 68 CYS B 74 1555 1555 2.03
SSBOND 3 CYS C 68 CYS C 74 1555 1555 2.03
SSBOND 4 CYS D 68 CYS D 74 1555 1555 2.03
SSBOND 5 CYS E 68 CYS E 74 1555 1555 2.03
SSBOND 6 CYS F 68 CYS F 74 1555 1555 2.03
LINK ND2 ASN A 141 C1 NAG G 1 1555 1555 1.44
LINK OG SER A 195 C1 MAN A 505 1555 1555 1.44
LINK OG1 THR A 197 C1 MAN A 506 1555 1555 1.44
LINK OG1 THR A 199 C1 MAN A 507 1555 1555 1.44
LINK ND2 ASN A 389 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN B 141 C1 NAG B 501 1555 1555 1.44
LINK OG SER B 195 C1 MAN B 511 1555 1555 1.44
LINK OG1 THR B 197 C1 MAN B 512 1555 1555 1.44
LINK OG1 THR B 199 C1 MAN B 513 1555 1555 1.44
LINK ND2 ASN B 389 C1 NAG I 1 1555 1555 1.43
LINK ND2 ASN C 141 C1 NAG J 1 1555 1555 1.43
LINK OG SER C 195 C1 MAN C 504 1555 1555 1.44
LINK OG1 THR C 197 C1 MAN C 505 1555 1555 1.44
LINK OG1 THR C 199 C1 MAN C 506 1555 1555 1.44
LINK ND2 ASN D 141 C1 NAG K 1 1555 1555 1.44
LINK OG SER D 195 C1 MAN D 503 1555 1555 1.45
LINK OG1 THR D 197 C1 MAN D 504 1555 1555 1.44
LINK OG1 THR D 199 C1 MAN D 505 1555 1555 1.44
LINK OG SER E 195 C1 MAN E 506 1555 1555 1.44
LINK OG1 THR E 197 C1 MAN E 507 1555 1555 1.44
LINK OG1 THR E 199 C1 MAN E 508 1555 1555 1.44
LINK ND2 ASN E 389 C1 NAG L 1 1555 1555 1.44
LINK ND2 ASN F 141 C1 NAG F 501 1555 1555 1.44
LINK OG SER F 195 C1 MAN F 503 1555 1555 1.45
LINK OG1 THR F 197 C1 MAN F 504 1555 1555 1.44
LINK OG1 THR F 199 C1 MAN F 505 1555 1555 1.44
LINK ND2 ASN F 389 C1 NAG F 502 1555 1555 1.44
LINK O6 NAG G 1 C1 FUC G 2 1555 1555 1.44
LINK O6 NAG H 1 C1 FUC H 2 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.43
LINK O6 NAG I 1 C1 FUC I 9 1555 1555 1.44
LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45
LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.45
LINK O6 BMA I 3 C1 MAN I 7 1555 1555 1.44
LINK O4 MAN I 4 C1 NAG I 5 1555 1555 1.44
LINK O4 NAG I 5 C1 GAL I 6 1555 1555 1.44
LINK O4 MAN I 7 C1 NAG I 8 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44
LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.45
LINK O6 NAG K 1 C1 FUC K 2 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44
LINK O6 NAG L 1 C1 FUC L 5 1555 1555 1.44
LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.44
LINK O3 BMA L 3 C1 MAN L 4 1555 1555 1.44
LINK OE1 GLU A 9 CA CA A 508 1555 1555 2.84
LINK OE2 GLU A 9 CA CA A 509 1555 1555 2.93
LINK OD1 ASP A 63 CA CA A 509 1555 1555 2.48
LINK OE2 GLU A 65 CA CA A 508 1555 1555 2.40
LINK OE1 GLU A 65 CA CA A 509 1555 1555 2.66
LINK OD1 ASP A 97 CA CA A 508 1555 1555 2.57
LINK O ILE A 98 CA CA A 508 1555 1555 2.58
LINK OD1 ASN A 99 CA CA A 510 1555 1555 2.47
LINK OD1 ASP A 100 CA CA A 508 1555 1555 2.55
LINK OD1 ASP A 100 CA CA A 509 1555 1555 3.11
LINK OD2 ASP A 100 CA CA A 509 1555 1555 2.23
LINK O HIS A 101 CA CA A 510 1555 1555 2.47
LINK OE2 GLU A 116 CA CA A 511 1555 1555 2.18
LINK OE1 GLU A 116 CA CA A 512 1555 1555 2.45
LINK OD1 ASP A 131 CA CA A 510 1555 1555 2.90
LINK OD2 ASP A 131 CA CA A 510 1555 1555 2.23
LINK OD1 ASP A 133 CA CA A 508 1555 1555 2.81
LINK OD2 ASP A 133 CA CA A 510 1555 1555 2.31
LINK O ASN A 137 CA CA A 510 1555 1555 2.68
LINK OD1 ASP A 173 CA CA A 511 1555 1555 2.49
LINK OE1 GLU A 175 CA CA A 511 1555 1555 2.49
LINK OE1 GLU A 175 CA CA A 512 1555 1555 2.93
LINK OE2 GLU A 175 CA CA A 512 1555 1555 2.28
LINK OD2 ASP A 188 CA CA A 510 1555 1555 2.31
LINK OD1 ASP A 206 CA CA A 512 1555 1555 2.97
LINK O ILE A 207 CA CA A 512 1555 1555 2.45
LINK OD1 ASN A 208 CA CA A 513 1555 1555 2.37
LINK OD1 ASP A 209 CA CA A 511 1555 1555 3.10
LINK OD2 ASP A 209 CA CA A 511 1555 1555 2.28
LINK OD1 ASP A 209 CA CA A 512 1555 1555 2.45
LINK O ASN A 210 CA CA A 513 1555 1555 2.55
LINK OE2 GLU A 225 CA CA A 514 1555 1555 2.22
LINK OE1 GLU A 225 CA CA A 515 1555 1555 3.08
LINK OD1 ASP A 240 CA CA A 513 1555 1555 2.92
LINK OD2 ASP A 240 CA CA A 513 1555 1555 2.14
LINK OD1 ASP A 242 CA CA A 512 1555 1555 2.50
LINK OD2 ASP A 242 CA CA A 513 1555 1555 3.05
LINK O HIS A 246 CA CA A 513 1555 1555 2.57
LINK OD1 ASP A 279 CA CA A 514 1555 1555 2.49
LINK OE1 GLU A 281 CA CA A 514 1555 1555 2.48
LINK OE1 GLU A 281 CA CA A 515 1555 1555 2.74
LINK OE2 GLU A 281 CA CA A 515 1555 1555 2.24
LINK OD2 ASP A 294 CA CA A 513 1555 1555 2.87
LINK OD1 ASP A 310 CA CA A 515 1555 1555 2.67
LINK O VAL A 311 CA CA A 515 1555 1555 2.46
LINK OD1 ASN A 312 CA CA A 516 1555 1555 2.77
LINK OD1 ASP A 313 CA CA A 514 1555 1555 2.71
LINK OD2 ASP A 313 CA CA A 514 1555 1555 2.44
LINK OD1 ASP A 313 CA CA A 515 1555 1555 2.61
LINK O ASN A 314 CA CA A 516 1555 1555 2.59
LINK OD1 ASP A 343 CA CA A 516 1555 1555 3.15
LINK OD2 ASP A 343 CA CA A 516 1555 1555 2.81
LINK OD1 ASP A 345 CA CA A 515 1555 1555 2.78
LINK OD2 ASP A 345 CA CA A 516 1555 1555 2.45
LINK O ASN A 349 CA CA A 516 1555 1555 2.49
LINK OD2 ASP A 396 CA CA A 516 1555 1555 2.98
LINK OE2 GLU B 9 CA CA B 514 1555 1555 2.45
LINK OE1 GLU B 9 CA CA B 515 1555 1555 2.97
LINK OE2 GLU B 10 CA CA B 514 1555 1555 2.91
LINK OD1 ASP B 63 CA CA B 514 1555 1555 2.63
LINK OE1 GLU B 65 CA CA B 514 1555 1555 2.51
LINK OE1 GLU B 65 CA CA B 515 1555 1555 3.15
LINK OE2 GLU B 65 CA CA B 515 1555 1555 2.28
LINK OD1 ASP B 97 CA CA B 515 1555 1555 2.38
LINK O ILE B 98 CA CA B 515 1555 1555 2.71
LINK OD1 ASN B 99 CA CA B 516 1555 1555 2.49
LINK OD2 ASP B 100 CA CA B 514 1555 1555 2.32
LINK OD1 ASP B 100 CA CA B 515 1555 1555 2.41
LINK O HIS B 101 CA CA B 516 1555 1555 2.48
LINK OE1 GLU B 116 CA CA B 517 1555 1555 2.47
LINK OE2 GLU B 116 CA CA B 518 1555 1555 2.25
LINK OD2 ASP B 131 CA CA B 516 1555 1555 2.62
LINK OD1 ASP B 133 CA CA B 515 1555 1555 2.60
LINK OD2 ASP B 133 CA CA B 516 1555 1555 2.54
LINK O ASN B 137 CA CA B 516 1555 1555 2.70
LINK OD1 ASP B 173 CA CA B 518 1555 1555 2.65
LINK OE1 GLU B 175 CA CA B 517 1555 1555 3.05
LINK OE2 GLU B 175 CA CA B 517 1555 1555 2.25
LINK OE1 GLU B 175 CA CA B 518 1555 1555 2.79
LINK OD2 ASP B 188 CA CA B 516 1555 1555 2.33
LINK OD1 ASP B 206 CA CA B 517 1555 1555 2.54
LINK O ILE B 207 CA CA B 517 1555 1555 2.50
LINK OD1 ASN B 208 CA CA B 519 1555 1555 2.45
LINK OD1 ASP B 209 CA CA B 517 1555 1555 2.53
LINK OD2 ASP B 209 CA CA B 518 1555 1555 2.32
LINK O ASN B 210 CA CA B 519 1555 1555 2.55
LINK OE2 GLU B 225 CA CA B 520 1555 1555 2.27
LINK OE1 GLU B 225 CA CA B 521 1555 1555 2.63
LINK OD1 ASP B 240 CA CA B 519 1555 1555 3.11
LINK OD2 ASP B 240 CA CA B 519 1555 1555 2.35
LINK OD1 ASP B 242 CA CA B 517 1555 1555 2.72
LINK OD2 ASP B 242 CA CA B 519 1555 1555 2.61
LINK O HIS B 246 CA CA B 519 1555 1555 2.62
LINK OD1 ASP B 279 CA CA B 520 1555 1555 2.54
LINK OE1 GLU B 281 CA CA B 520 1555 1555 2.48
LINK OE1 GLU B 281 CA CA B 521 1555 1555 2.98
LINK OE2 GLU B 281 CA CA B 521 1555 1555 2.66
LINK OD2 ASP B 294 CA CA B 519 1555 1555 2.88
LINK OD1 ASP B 310 CA CA B 521 1555 1555 2.63
LINK O VAL B 311 CA CA B 521 1555 1555 2.49
LINK OD1 ASN B 312 CA CA B 522 1555 1555 2.54
LINK OD1 ASP B 313 CA CA B 520 1555 1555 2.96
LINK OD2 ASP B 313 CA CA B 520 1555 1555 2.81
LINK OD1 ASP B 313 CA CA B 521 1555 1555 2.64
LINK O ASN B 314 CA CA B 522 1555 1555 2.51
LINK OD1 ASP B 343 CA CA B 522 1555 1555 3.12
LINK OD2 ASP B 343 CA CA B 522 1555 1555 2.70
LINK OD1 ASP B 345 CA CA B 521 1555 1555 3.11
LINK OD2 ASP B 345 CA CA B 522 1555 1555 2.71
LINK O ASN B 349 CA CA B 522 1555 1555 2.55
LINK OD2 ASP B 396 CA CA B 522 1555 1555 2.77
LINK OE2 GLU C 9 CA CA C 507 1555 1555 2.62
LINK OE1 GLU C 9 CA CA C 508 1555 1555 2.82
LINK OE2 GLU C 10 CA CA C 507 1555 1555 3.01
LINK OD1 ASP C 63 CA CA C 507 1555 1555 2.52
LINK OE1 GLU C 65 CA CA C 507 1555 1555 2.68
LINK OE2 GLU C 65 CA CA C 508 1555 1555 2.47
LINK OD1 ASP C 97 CA CA C 508 1555 1555 2.44
LINK O ILE C 98 CA CA C 508 1555 1555 2.53
LINK OD1 ASN C 99 CA CA C 509 1555 1555 2.52
LINK OD2 ASP C 100 CA CA C 507 1555 1555 2.23
LINK OD1 ASP C 100 CA CA C 508 1555 1555 2.42
LINK O HIS C 101 CA CA C 509 1555 1555 2.43
LINK OE2 GLU C 116 CA CA C 510 1555 1555 2.16
LINK OE1 GLU C 116 CA CA C 511 1555 1555 2.58
LINK OD1 ASP C 131 CA CA C 509 1555 1555 2.73
LINK OD2 ASP C 131 CA CA C 509 1555 1555 2.52
LINK OD1 ASP C 133 CA CA C 508 1555 1555 2.83
LINK OD2 ASP C 133 CA CA C 509 1555 1555 2.38
LINK O ASN C 137 CA CA C 509 1555 1555 2.73
LINK OD1 ASP C 173 CA CA C 510 1555 1555 2.47
LINK OE1 GLU C 175 CA CA C 510 1555 1555 2.47
LINK OE1 GLU C 175 CA CA C 511 1555 1555 2.86
LINK OE2 GLU C 175 CA CA C 511 1555 1555 2.24
LINK OD2 ASP C 188 CA CA C 509 1555 1555 2.30
LINK OD1 ASP C 206 CA CA C 511 1555 1555 3.06
LINK O ILE C 207 CA CA C 511 1555 1555 2.43
LINK OD1 ASN C 208 CA CA C 512 1555 1555 2.44
LINK OD2 ASP C 209 CA CA C 510 1555 1555 2.23
LINK OD1 ASP C 209 CA CA C 511 1555 1555 2.41
LINK O ASN C 210 CA CA C 512 1555 1555 2.52
LINK OE2 GLU C 225 CA CA C 513 1555 1555 2.46
LINK OE1 GLU C 225 CA CA C 514 1555 1555 2.79
LINK OD1 ASP C 240 CA CA C 512 1555 1555 2.70
LINK OD2 ASP C 240 CA CA C 512 1555 1555 2.27
LINK OD1 ASP C 242 CA CA C 511 1555 1555 2.59
LINK OD2 ASP C 242 CA CA C 512 1555 1555 2.93
LINK O HIS C 246 CA CA C 512 1555 1555 2.65
LINK OD1 ASP C 279 CA CA C 513 1555 1555 2.59
LINK OE1 GLU C 281 CA CA C 513 1555 1555 2.48
LINK OE1 GLU C 281 CA CA C 514 1555 1555 2.63
LINK OE2 GLU C 281 CA CA C 514 1555 1555 2.45
LINK OD2 ASP C 294 CA CA C 512 1555 1555 2.96
LINK OD1 ASP C 310 CA CA C 514 1555 1555 2.68
LINK O VAL C 311 CA CA C 514 1555 1555 2.48
LINK OD1 ASN C 312 CA CA C 515 1555 1555 2.96
LINK OD1 ASP C 313 CA CA C 513 1555 1555 2.92
LINK OD2 ASP C 313 CA CA C 513 1555 1555 2.69
LINK OD1 ASP C 313 CA CA C 514 1555 1555 2.48
LINK O ASN C 314 CA CA C 515 1555 1555 2.50
LINK OD1 ASP C 343 CA CA C 515 1555 1555 2.55
LINK OD2 ASP C 343 CA CA C 515 1555 1555 2.56
LINK OD1 ASP C 345 CA CA C 514 1555 1555 3.13
LINK OD2 ASP C 345 CA CA C 515 1555 1555 2.58
LINK O ASN C 349 CA CA C 515 1555 1555 2.61
LINK OD2 ASP C 396 CA CA C 515 1555 1555 3.09
LINK OE1 GLU D 9 CA CA D 507 1555 1555 2.69
LINK OD1 ASP D 63 CA CA D 506 1555 1555 2.53
LINK OE1 GLU D 65 CA CA D 506 1555 1555 2.73
LINK OE2 GLU D 65 CA CA D 507 1555 1555 2.50
LINK OD1 ASP D 97 CA CA D 507 1555 1555 2.58
LINK O ILE D 98 CA CA D 507 1555 1555 2.64
LINK OD1 ASN D 99 CA CA D 508 1555 1555 2.74
LINK OD2 ASP D 100 CA CA D 506 1555 1555 2.47
LINK OD1 ASP D 100 CA CA D 507 1555 1555 2.49
LINK O HIS D 101 CA CA D 508 1555 1555 2.46
LINK OE2 GLU D 116 CA CA D 509 1555 1555 2.17
LINK OE1 GLU D 116 CA CA D 510 1555 1555 2.47
LINK OD1 ASP D 131 CA CA D 508 1555 1555 3.18
LINK OD2 ASP D 131 CA CA D 508 1555 1555 2.61
LINK OD1 ASP D 133 CA CA D 507 1555 1555 2.94
LINK OD2 ASP D 133 CA CA D 508 1555 1555 2.69
LINK O ASN D 137 CA CA D 508 1555 1555 3.10
LINK OD1 ASP D 173 CA CA D 509 1555 1555 2.51
LINK OE1 GLU D 175 CA CA D 509 1555 1555 2.57
LINK OE1 GLU D 175 CA CA D 510 1555 1555 3.00
LINK OE2 GLU D 175 CA CA D 510 1555 1555 2.29
LINK OD2 ASP D 188 CA CA D 508 1555 1555 2.25
LINK OD1 ASP D 206 CA CA D 510 1555 1555 2.63
LINK O ILE D 207 CA CA D 510 1555 1555 2.53
LINK OD1 ASN D 208 CA CA D 511 1555 1555 2.46
LINK OD2 ASP D 209 CA CA D 509 1555 1555 2.35
LINK OD1 ASP D 209 CA CA D 510 1555 1555 2.55
LINK O ASN D 210 CA CA D 511 1555 1555 2.50
LINK OE1 GLU D 225 CA CA D 512 1555 1555 3.01
LINK OE2 GLU D 225 CA CA D 512 1555 1555 3.09
LINK OE1 GLU D 225 CA CA D 513 1555 1555 2.62
LINK OD1 ASP D 240 CA CA D 511 1555 1555 2.94
LINK OD2 ASP D 240 CA CA D 511 1555 1555 2.19
LINK OD1 ASP D 242 CA CA D 510 1555 1555 2.57
LINK OD2 ASP D 242 CA CA D 511 1555 1555 2.84
LINK O HIS D 246 CA CA D 511 1555 1555 2.55
LINK OD1 ASP D 279 CA CA D 512 1555 1555 2.73
LINK OE1 GLU D 281 CA CA D 512 1555 1555 2.55
LINK OE1 GLU D 281 CA CA D 513 1555 1555 2.90
LINK OE2 GLU D 281 CA CA D 513 1555 1555 2.25
LINK OD2 ASP D 294 CA CA D 511 1555 1555 2.94
LINK OD1 ASP D 310 CA CA D 513 1555 1555 2.63
LINK O VAL D 311 CA CA D 513 1555 1555 2.50
LINK OD1 ASN D 312 CA CA D 514 1555 1555 2.81
LINK OD1 ASP D 313 CA CA D 512 1555 1555 2.69
LINK OD2 ASP D 313 CA CA D 512 1555 1555 2.37
LINK OD1 ASP D 313 CA CA D 513 1555 1555 2.75
LINK O ASN D 314 CA CA D 514 1555 1555 2.57
LINK OD1 ASP D 343 CA CA D 514 1555 1555 2.81
LINK OD2 ASP D 343 CA CA D 514 1555 1555 2.41
LINK OD1 ASP D 345 CA CA D 513 1555 1555 2.95
LINK OD2 ASP D 345 CA CA D 514 1555 1555 2.43
LINK O ASN D 349 CA CA D 514 1555 1555 2.61
LINK OD2 ASP D 396 CA CA D 514 1555 1555 3.00
LINK OE2 GLU E 9 CA CA E 509 1555 1555 2.34
LINK OE1 GLU E 9 CA CA E 510 1555 1555 2.68
LINK OD1 ASP E 63 CA CA E 509 1555 1555 2.48
LINK OE1 GLU E 65 CA CA E 509 1555 1555 2.63
LINK OE2 GLU E 65 CA CA E 510 1555 1555 2.59
LINK OD1 ASP E 97 CA CA E 510 1555 1555 2.75
LINK O ILE E 98 CA CA E 510 1555 1555 2.58
LINK OD1 ASN E 99 CA CA E 511 1555 1555 2.48
LINK OD1 ASP E 100 CA CA E 509 1555 1555 3.10
LINK OD2 ASP E 100 CA CA E 509 1555 1555 2.24
LINK OD1 ASP E 100 CA CA E 510 1555 1555 2.49
LINK O HIS E 101 CA CA E 511 1555 1555 2.52
LINK OE2 GLU E 116 CA CA E 512 1555 1555 2.19
LINK OE1 GLU E 116 CA CA E 513 1555 1555 2.58
LINK OD1 ASP E 131 CA CA E 511 1555 1555 3.16
LINK OD2 ASP E 131 CA CA E 511 1555 1555 2.70
LINK OD1 ASP E 133 CA CA E 510 1555 1555 2.93
LINK OD2 ASP E 133 CA CA E 511 1555 1555 2.45
LINK O ASN E 137 CA CA E 511 1555 1555 2.73
LINK OD1 ASP E 173 CA CA E 512 1555 1555 2.49
LINK OE1 GLU E 175 CA CA E 512 1555 1555 2.54
LINK OE1 GLU E 175 CA CA E 513 1555 1555 2.86
LINK OE2 GLU E 175 CA CA E 513 1555 1555 2.31
LINK OD2 ASP E 188 CA CA E 511 1555 1555 2.36
LINK OD1 ASP E 206 CA CA E 513 1555 1555 2.73
LINK O ILE E 207 CA CA E 513 1555 1555 2.51
LINK OD1 ASN E 208 CA CA E 514 1555 1555 2.50
LINK OD2 ASP E 209 CA CA E 512 1555 1555 2.32
LINK OD1 ASP E 209 CA CA E 513 1555 1555 2.54
LINK O ASN E 210 CA CA E 514 1555 1555 2.48
LINK OE2 GLU E 225 CA CA E 515 1555 1555 2.23
LINK OE1 GLU E 225 CA CA E 516 1555 1555 2.85
LINK OD1 ASP E 240 CA CA E 514 1555 1555 3.11
LINK OD2 ASP E 240 CA CA E 514 1555 1555 2.34
LINK OD1 ASP E 242 CA CA E 513 1555 1555 2.60
LINK OD2 ASP E 242 CA CA E 514 1555 1555 2.89
LINK O HIS E 246 CA CA E 514 1555 1555 2.63
LINK OD1 ASP E 279 CA CA E 515 1555 1555 2.71
LINK OE1 GLU E 281 CA CA E 515 1555 1555 2.51
LINK OE2 GLU E 281 CA CA E 516 1555 1555 2.23
LINK OD2 ASP E 294 CA CA E 514 1555 1555 2.87
LINK OD1 ASP E 310 CA CA E 516 1555 1555 2.50
LINK O VAL E 311 CA CA E 516 1555 1555 2.46
LINK OD1 ASN E 312 CA CA E 517 1555 1555 2.71
LINK OD1 ASP E 313 CA CA E 515 1555 1555 2.56
LINK OD2 ASP E 313 CA CA E 515 1555 1555 2.30
LINK OD1 ASP E 313 CA CA E 516 1555 1555 2.86
LINK O ASN E 314 CA CA E 517 1555 1555 2.48
LINK OD2 ASP E 343 CA CA E 517 1555 1555 2.76
LINK OD1 ASP E 345 CA CA E 516 1555 1555 3.20
LINK OD2 ASP E 345 CA CA E 517 1555 1555 2.36
LINK O ASN E 349 CA CA E 517 1555 1555 2.65
LINK OD2 ASP E 396 CA CA E 517 1555 1555 2.50
LINK OE2 GLU F 9 CA CA F 506 1555 1555 2.53
LINK OE1 GLU F 9 CA CA F 507 1555 1555 3.06
LINK OE2 GLU F 10 CA CA F 506 1555 1555 2.80
LINK OD1 ASP F 63 CA CA F 506 1555 1555 2.53
LINK OE1 GLU F 65 CA CA F 506 1555 1555 2.88
LINK OE2 GLU F 65 CA CA F 507 1555 1555 2.36
LINK OD1 ASP F 97 CA CA F 507 1555 1555 2.45
LINK O ILE F 98 CA CA F 507 1555 1555 2.68
LINK OD1 ASN F 99 CA CA F 508 1555 1555 2.55
LINK OD2 ASP F 100 CA CA F 506 1555 1555 2.23
LINK OD1 ASP F 100 CA CA F 507 1555 1555 2.46
LINK O HIS F 101 CA CA F 508 1555 1555 2.47
LINK OE2 GLU F 116 CA CA F 509 1555 1555 2.30
LINK OE1 GLU F 116 CA CA F 510 1555 1555 2.55
LINK OD1 ASP F 131 CA CA F 508 1555 1555 3.04
LINK OD2 ASP F 131 CA CA F 508 1555 1555 2.65
LINK OD1 ASP F 133 CA CA F 507 1555 1555 2.54
LINK OD2 ASP F 133 CA CA F 508 1555 1555 2.34
LINK O ASN F 137 CA CA F 508 1555 1555 2.53
LINK OD1 ASP F 173 CA CA F 509 1555 1555 2.50
LINK OE1 GLU F 175 CA CA F 509 1555 1555 2.51
LINK OE1 GLU F 175 CA CA F 510 1555 1555 2.60
LINK OE2 GLU F 175 CA CA F 510 1555 1555 2.51
LINK OD2 ASP F 188 CA CA F 508 1555 1555 2.22
LINK OD1 ASP F 206 CA CA F 510 1555 1555 2.79
LINK O ILE F 207 CA CA F 510 1555 1555 2.64
LINK OD1 ASN F 208 CA CA F 511 1555 1555 2.42
LINK OD2 ASP F 209 CA CA F 509 1555 1555 2.44
LINK OD1 ASP F 209 CA CA F 510 1555 1555 2.54
LINK O ASN F 210 CA CA F 511 1555 1555 2.53
LINK OE1 GLU F 225 CA CA F 512 1555 1555 2.72
LINK OE2 GLU F 225 CA CA F 513 1555 1555 2.42
LINK OD1 ASP F 240 CA CA F 511 1555 1555 3.04
LINK OD2 ASP F 240 CA CA F 511 1555 1555 2.37
LINK OD1 ASP F 242 CA CA F 510 1555 1555 3.00
LINK OD2 ASP F 242 CA CA F 511 1555 1555 2.48
LINK O HIS F 246 CA CA F 511 1555 1555 2.80
LINK OD1 ASP F 279 CA CA F 512 1555 1555 2.91
LINK OE1 GLU F 281 CA CA F 512 1555 1555 2.49
LINK OE1 GLU F 281 CA CA F 513 1555 1555 2.97
LINK OE2 GLU F 281 CA CA F 513 1555 1555 2.35
LINK OD2 ASP F 294 CA CA F 511 1555 1555 2.89
LINK OD1 ASP F 310 CA CA F 513 1555 1555 2.70
LINK O VAL F 311 CA CA F 513 1555 1555 2.70
LINK OD1 ASN F 312 CA CA F 514 1555 1555 2.71
LINK OD1 ASP F 313 CA CA F 512 1555 1555 2.98
LINK OD2 ASP F 313 CA CA F 512 1555 1555 2.57
LINK OD1 ASP F 313 CA CA F 513 1555 1555 2.58
LINK O ASN F 314 CA CA F 514 1555 1555 2.48
LINK OD1 ASP F 343 CA CA F 514 1555 1555 3.12
LINK OD2 ASP F 343 CA CA F 514 1555 1555 2.75
LINK OD1 ASP F 345 CA CA F 513 1555 1555 2.80
LINK OD2 ASP F 345 CA CA F 514 1555 1555 2.47
LINK O ASN F 349 CA CA F 514 1555 1555 2.52
LINK OD2 ASP F 396 CA CA F 514 1555 1555 2.91
CISPEP 1 GLU A 72 PRO A 73 0 1.27
CISPEP 2 ASN A 84 PRO A 85 0 -2.34
CISPEP 3 ALA A 191 PRO A 192 0 -0.72
CISPEP 4 THR A 399 PRO A 400 0 -0.84
CISPEP 5 GLU B 72 PRO B 73 0 0.54
CISPEP 6 ASN B 84 PRO B 85 0 -3.45
CISPEP 7 ALA B 191 PRO B 192 0 -1.09
CISPEP 8 THR B 399 PRO B 400 0 -0.87
CISPEP 9 GLU C 72 PRO C 73 0 0.59
CISPEP 10 ASN C 84 PRO C 85 0 -0.68
CISPEP 11 ALA C 191 PRO C 192 0 -0.57
CISPEP 12 THR C 399 PRO C 400 0 -1.69
CISPEP 13 GLU D 72 PRO D 73 0 0.02
CISPEP 14 ASN D 84 PRO D 85 0 -1.51
CISPEP 15 ALA D 191 PRO D 192 0 -0.76
CISPEP 16 THR D 399 PRO D 400 0 -1.95
CISPEP 17 GLU E 72 PRO E 73 0 0.26
CISPEP 18 ASN E 84 PRO E 85 0 -6.36
CISPEP 19 ALA E 191 PRO E 192 0 -0.83
CISPEP 20 THR E 399 PRO E 400 0 -1.63
CISPEP 21 GLU F 72 PRO F 73 0 3.08
CISPEP 22 ASN F 84 PRO F 85 0 -3.30
CISPEP 23 ALA F 191 PRO F 192 0 -0.75
CISPEP 24 THR F 399 PRO F 400 0 -0.64
CRYST1 85.140 137.070 326.190 90.00 90.00 90.00 P 21 21 21 24
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011745 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007296 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003066 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
