| content |
HEADER HYDROLASE 31-MAY-19 6RV8
TITLE CRYSTAL STRUCTURE OF GLUCURONOYL ESTERASE FROM CERRENA UNICOLOR
TITLE 2 COVALENT COMPLEX WITH THE ALDOURONIC ACID UXXR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-O-METHYL-GLUCURONOYL METHYLESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLUCURONOYL ESTERASE,GE;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CERRENA UNICOLOR;
SOURCE 3 ORGANISM_TAXID: 90312;
SOURCE 4 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: X-33;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PPICZ-ALPHA
KEYWDS CE15, ESTERASE, ALPHA/BETA-HYDROLASE, LIGAND-BOUND, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.A.ERNST,C.MOSBECH,A.LANGKILDE,P.WESTH,A.MEYER,J.W.AGGER,S.LARSEN
REVDAT 1 18-MAR-20 6RV8 0
JRNL AUTH H.A.ERNST,C.MOSBECH,A.E.LANGKILDE,P.WESTH,A.S.MEYER,
JRNL AUTH 2 J.W.AGGER,S.LARSEN
JRNL TITL THE STRUCTURAL BASIS OF FUNGAL GLUCURONOYL ESTERASE ACTIVITY
JRNL TITL 2 ON NATURAL SUBSTRATES.
JRNL REF NAT COMMUN V. 11 1026 2020
JRNL REFN ESSN 2041-1723
JRNL PMID 32094331
JRNL DOI 10.1038/S41467-020-14833-9
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.45
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 80245
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 3997
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 44.4662 - 5.6800 1.00 2989 153 0.1524 0.1725
REMARK 3 2 5.6800 - 4.5098 1.00 2815 156 0.1280 0.1377
REMARK 3 3 4.5098 - 3.9401 1.00 2759 155 0.1232 0.1536
REMARK 3 4 3.9401 - 3.5800 1.00 2768 127 0.1364 0.1768
REMARK 3 5 3.5800 - 3.3235 1.00 2728 143 0.1523 0.1882
REMARK 3 6 3.3235 - 3.1276 1.00 2730 138 0.1622 0.1816
REMARK 3 7 3.1276 - 2.9710 1.00 2693 161 0.1600 0.1964
REMARK 3 8 2.9710 - 2.8417 1.00 2689 139 0.1673 0.1980
REMARK 3 9 2.8417 - 2.7323 1.00 2675 136 0.1586 0.1951
REMARK 3 10 2.7323 - 2.6381 1.00 2702 142 0.1555 0.1888
REMARK 3 11 2.6381 - 2.5556 1.00 2685 135 0.1536 0.1997
REMARK 3 12 2.5556 - 2.4825 1.00 2676 138 0.1483 0.1953
REMARK 3 13 2.4825 - 2.4172 1.00 2669 138 0.1517 0.1885
REMARK 3 14 2.4172 - 2.3582 1.00 2645 144 0.1464 0.1733
REMARK 3 15 2.3582 - 2.3046 1.00 2674 127 0.1511 0.1789
REMARK 3 16 2.3046 - 2.2556 1.00 2642 146 0.1487 0.1712
REMARK 3 17 2.2556 - 2.2105 0.99 2652 150 0.1521 0.1761
REMARK 3 18 2.2105 - 2.1687 0.99 2665 127 0.1427 0.1600
REMARK 3 19 2.1687 - 2.1300 0.99 2632 130 0.1482 0.1758
REMARK 3 20 2.1300 - 2.0939 0.99 2659 137 0.1460 0.1915
REMARK 3 21 2.0939 - 2.0601 0.99 2620 140 0.1503 0.2154
REMARK 3 22 2.0601 - 2.0284 0.99 2616 150 0.1532 0.2087
REMARK 3 23 2.0284 - 1.9986 0.99 2623 142 0.1508 0.1956
REMARK 3 24 1.9986 - 1.9705 0.98 2553 136 0.1545 0.2155
REMARK 3 25 1.9705 - 1.9438 0.97 2621 135 0.1659 0.2110
REMARK 3 26 1.9438 - 1.9186 0.96 2505 152 0.1844 0.2386
REMARK 3 27 1.9186 - 1.8946 0.89 2372 115 0.1910 0.1900
REMARK 3 28 1.8946 - 1.8718 0.82 2166 114 0.1960 0.2401
REMARK 3 29 1.8718 - 1.8500 0.76 2025 91 0.2188 0.2555
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.690
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.33
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 80 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 70.2727 49.4888 26.9122
REMARK 3 T TENSOR
REMARK 3 T11: 0.2648 T22: 0.2607
REMARK 3 T33: 0.1673 T12: -0.0288
REMARK 3 T13: -0.0528 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 2.7532 L22: 4.0153
REMARK 3 L33: 2.8737 L12: 0.4448
REMARK 3 L13: -0.8092 L23: -0.1141
REMARK 3 S TENSOR
REMARK 3 S11: 0.0833 S12: -0.4435 S13: 0.1217
REMARK 3 S21: 0.2185 S22: -0.1010 S23: -0.0968
REMARK 3 S31: -0.2192 S32: 0.0032 S33: 0.0015
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 100 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.8915 44.5952 30.7042
REMARK 3 T TENSOR
REMARK 3 T11: 0.2167 T22: 0.1763
REMARK 3 T33: 0.1616 T12: -0.0123
REMARK 3 T13: -0.0142 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 2.5169 L22: 2.2979
REMARK 3 L33: 1.4882 L12: 0.1432
REMARK 3 L13: 0.2910 L23: 0.2156
REMARK 3 S TENSOR
REMARK 3 S11: -0.0155 S12: -0.2589 S13: -0.0323
REMARK 3 S21: 0.2429 S22: 0.0424 S23: -0.0803
REMARK 3 S31: -0.0146 S32: -0.0664 S33: 0.0006
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.3700 47.6585 15.8531
REMARK 3 T TENSOR
REMARK 3 T11: 0.2220 T22: 0.1591
REMARK 3 T33: 0.1917 T12: -0.0028
REMARK 3 T13: 0.0076 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.4840 L22: 0.8814
REMARK 3 L33: 0.4341 L12: -0.1754
REMARK 3 L13: -0.0086 L23: 0.0269
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: 0.0051 S13: -0.0354
REMARK 3 S21: 0.0640 S22: -0.0181 S23: 0.1910
REMARK 3 S31: -0.0051 S32: -0.0602 S33: 0.0164
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 318 THROUGH 422 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.4134 39.9484 12.7079
REMARK 3 T TENSOR
REMARK 3 T11: 0.2128 T22: 0.1471
REMARK 3 T33: 0.1880 T12: 0.0068
REMARK 3 T13: -0.0036 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.5682 L22: 0.3264
REMARK 3 L33: 0.8115 L12: 0.0398
REMARK 3 L13: 0.0119 L23: -0.2840
REMARK 3 S TENSOR
REMARK 3 S11: 0.0098 S12: 0.0337 S13: -0.0770
REMARK 3 S21: 0.0287 S22: -0.0321 S23: -0.0168
REMARK 3 S31: 0.0545 S32: 0.0225 S33: 0.0231
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 423 THROUGH 460 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.5516 31.2445 16.4809
REMARK 3 T TENSOR
REMARK 3 T11: 0.2467 T22: 0.1430
REMARK 3 T33: 0.2223 T12: 0.0262
REMARK 3 T13: 0.0020 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.5722 L22: 0.6935
REMARK 3 L33: 0.5512 L12: 0.3235
REMARK 3 L13: 0.0986 L23: -0.1696
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: -0.0297 S13: -0.1411
REMARK 3 S21: 0.0617 S22: -0.0228 S23: -0.0090
REMARK 3 S31: 0.1224 S32: 0.0611 S33: 0.0615
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 80 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.2957 7.0640 31.0683
REMARK 3 T TENSOR
REMARK 3 T11: 0.2619 T22: 0.2764
REMARK 3 T33: 0.2225 T12: 0.0155
REMARK 3 T13: -0.0664 T23: -0.0639
REMARK 3 L TENSOR
REMARK 3 L11: 2.9195 L22: 4.2954
REMARK 3 L33: 3.2290 L12: 0.1984
REMARK 3 L13: -1.0046 L23: 0.3909
REMARK 3 S TENSOR
REMARK 3 S11: -0.1081 S12: -0.4757 S13: 0.3187
REMARK 3 S21: 0.0855 S22: 0.0328 S23: -0.0996
REMARK 3 S31: -0.3245 S32: 0.0001 S33: 0.0262
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 100 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.0250 7.2049 31.6415
REMARK 3 T TENSOR
REMARK 3 T11: 0.2284 T22: 0.2347
REMARK 3 T33: 0.1879 T12: 0.0350
REMARK 3 T13: 0.0214 T23: -0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 2.4753 L22: 1.2392
REMARK 3 L33: 0.8354 L12: -0.3272
REMARK 3 L13: 0.6299 L23: -0.3093
REMARK 3 S TENSOR
REMARK 3 S11: -0.0856 S12: -0.2720 S13: 0.1494
REMARK 3 S21: 0.1956 S22: 0.0680 S23: 0.0837
REMARK 3 S31: -0.1716 S32: -0.2689 S33: 0.0082
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 205 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3515 4.1324 21.3053
REMARK 3 T TENSOR
REMARK 3 T11: 0.1795 T22: 0.3635
REMARK 3 T33: 0.2958 T12: 0.0341
REMARK 3 T13: -0.0022 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 1.5523 L22: 1.3527
REMARK 3 L33: 2.4651 L12: -0.7315
REMARK 3 L13: -0.4996 L23: 0.1940
REMARK 3 S TENSOR
REMARK 3 S11: -0.0135 S12: 0.0339 S13: 0.1319
REMARK 3 S21: 0.0474 S22: 0.0104 S23: 0.2774
REMARK 3 S31: -0.0418 S32: -0.4398 S33: 0.0409
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.2795 17.6296 14.8780
REMARK 3 T TENSOR
REMARK 3 T11: 0.2843 T22: 0.2305
REMARK 3 T33: 0.3162 T12: 0.0711
REMARK 3 T13: -0.0505 T23: 0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 1.5486 L22: 1.6369
REMARK 3 L33: 1.6830 L12: 0.4418
REMARK 3 L13: -0.1717 L23: 0.6833
REMARK 3 S TENSOR
REMARK 3 S11: 0.0187 S12: 0.0847 S13: 0.2579
REMARK 3 S21: -0.1396 S22: 0.0008 S23: 0.2784
REMARK 3 S31: -0.3413 S32: -0.2854 S33: 0.0002
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 236 THROUGH 317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1989 2.4483 20.5607
REMARK 3 T TENSOR
REMARK 3 T11: 0.1836 T22: 0.1960
REMARK 3 T33: 0.1837 T12: 0.0159
REMARK 3 T13: 0.0017 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 2.7126 L22: 1.0876
REMARK 3 L33: 0.7728 L12: -0.4042
REMARK 3 L13: -0.3821 L23: -0.0575
REMARK 3 S TENSOR
REMARK 3 S11: -0.0688 S12: -0.1155 S13: 0.0296
REMARK 3 S21: 0.0908 S22: 0.0573 S23: 0.1988
REMARK 3 S31: -0.0606 S32: -0.1913 S33: 0.0121
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 318 THROUGH 408 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.9343 -1.6374 18.5214
REMARK 3 T TENSOR
REMARK 3 T11: 0.1737 T22: 0.1553
REMARK 3 T33: 0.1730 T12: 0.0060
REMARK 3 T13: 0.0043 T23: -0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 0.8227 L22: 0.9182
REMARK 3 L33: 1.2409 L12: 0.0205
REMARK 3 L13: 0.2548 L23: 0.1408
REMARK 3 S TENSOR
REMARK 3 S11: -0.0187 S12: -0.0121 S13: 0.0160
REMARK 3 S21: 0.0264 S22: -0.0317 S23: 0.0504
REMARK 3 S31: -0.0143 S32: -0.0910 S33: 0.0450
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 409 THROUGH 432 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2300 -14.9639 24.2545
REMARK 3 T TENSOR
REMARK 3 T11: 0.2374 T22: 0.3062
REMARK 3 T33: 0.3563 T12: -0.0759
REMARK 3 T13: 0.0403 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 2.6888 L22: 2.5853
REMARK 3 L33: 2.1725 L12: -0.5882
REMARK 3 L13: 0.2432 L23: 0.3115
REMARK 3 S TENSOR
REMARK 3 S11: -0.0131 S12: -0.2110 S13: -0.3580
REMARK 3 S21: 0.1107 S22: 0.0057 S23: 0.2418
REMARK 3 S31: 0.3810 S32: -0.3217 S33: 0.0474
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 433 THROUGH 460 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.5790 -10.6490 23.2071
REMARK 3 T TENSOR
REMARK 3 T11: 0.1848 T22: 0.1412
REMARK 3 T33: 0.1652 T12: 0.0133
REMARK 3 T13: -0.0073 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 1.0510 L22: 1.1346
REMARK 3 L33: 2.1082 L12: 0.0125
REMARK 3 L13: 0.3461 L23: 0.2183
REMARK 3 S TENSOR
REMARK 3 S11: -0.0099 S12: -0.0256 S13: -0.0323
REMARK 3 S21: 0.0525 S22: 0.0267 S23: -0.0480
REMARK 3 S31: 0.0964 S32: 0.0508 S33: -0.0139
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 6RV8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1292102672.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.3
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85042
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 44.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 24.20
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.9
REMARK 200 DATA REDUNDANCY IN SHELL : 17.70
REMARK 200 R MERGE FOR SHELL (I) : 1.15800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6RTV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM ACETATE, 0.1 M BIS-TRIS
REMARK 280 PH 5.5, 17% W/V PEG10000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 130.53100
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 42.37500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.37500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 65.26550
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.37500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 42.37500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 195.79650
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 42.37500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.37500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.26550
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 42.37500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.37500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 195.79650
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 130.53100
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 850 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLN A 2
REMARK 465 ALA A 3
REMARK 465 SER A 4
REMARK 465 ALA A 5
REMARK 465 PRO A 6
REMARK 465 GLN A 7
REMARK 465 TRP A 8
REMARK 465 GLY A 9
REMARK 465 GLN A 10
REMARK 465 CYS A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 ILE A 14
REMARK 465 GLY A 15
REMARK 465 TRP A 16
REMARK 465 THR A 17
REMARK 465 GLY A 18
REMARK 465 PRO A 19
REMARK 465 THR A 20
REMARK 465 ALA A 21
REMARK 465 CYS A 22
REMARK 465 PRO A 23
REMARK 465 SER A 24
REMARK 465 GLY A 25
REMARK 465 TRP A 26
REMARK 465 ALA A 27
REMARK 465 CYS A 28
REMARK 465 GLN A 29
REMARK 465 GLN A 30
REMARK 465 LEU A 31
REMARK 465 ASN A 32
REMARK 465 ALA A 33
REMARK 465 TYR A 34
REMARK 465 TYR A 35
REMARK 465 SER A 36
REMARK 465 GLN A 37
REMARK 465 CYS A 38
REMARK 465 LEU A 39
REMARK 465 GLN A 40
REMARK 465 GLY A 41
REMARK 465 ALA A 42
REMARK 465 ALA A 43
REMARK 465 PRO A 44
REMARK 465 ALA A 45
REMARK 465 PRO A 46
REMARK 465 ALA A 47
REMARK 465 ARG A 48
REMARK 465 THR A 49
REMARK 465 THR A 50
REMARK 465 ALA A 51
REMARK 465 ALA A 52
REMARK 465 PRO A 53
REMARK 465 PRO A 54
REMARK 465 PRO A 55
REMARK 465 PRO A 56
REMARK 465 PRO A 57
REMARK 465 ALA A 58
REMARK 465 THR A 59
REMARK 465 THR A 60
REMARK 465 ALA A 61
REMARK 465 ALA A 62
REMARK 465 PRO A 63
REMARK 465 PRO A 64
REMARK 465 PRO A 65
REMARK 465 PRO A 66
REMARK 465 THR A 67
REMARK 465 THR A 68
REMARK 465 SER A 69
REMARK 465 ALA A 70
REMARK 465 PRO A 71
REMARK 465 THR A 72
REMARK 465 GLY A 73
REMARK 465 SER A 74
REMARK 465 SER A 75
REMARK 465 PRO A 76
REMARK 465 VAL A 77
REMARK 465 ALA A 78
REMARK 465 GLY A 79
REMARK 465 GLU A 461
REMARK 465 GLN A 462
REMARK 465 LYS A 463
REMARK 465 LEU A 464
REMARK 465 ILE A 465
REMARK 465 SER A 466
REMARK 465 GLU A 467
REMARK 465 GLU A 468
REMARK 465 ASP A 469
REMARK 465 LEU A 470
REMARK 465 ASN A 471
REMARK 465 SER A 472
REMARK 465 ALA A 473
REMARK 465 VAL A 474
REMARK 465 ASP A 475
REMARK 465 HIS A 476
REMARK 465 HIS A 477
REMARK 465 HIS A 478
REMARK 465 HIS A 479
REMARK 465 HIS A 480
REMARK 465 HIS A 481
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 ALA B 3
REMARK 465 SER B 4
REMARK 465 ALA B 5
REMARK 465 PRO B 6
REMARK 465 GLN B 7
REMARK 465 TRP B 8
REMARK 465 GLY B 9
REMARK 465 GLN B 10
REMARK 465 CYS B 11
REMARK 465 GLY B 12
REMARK 465 GLY B 13
REMARK 465 ILE B 14
REMARK 465 GLY B 15
REMARK 465 TRP B 16
REMARK 465 THR B 17
REMARK 465 GLY B 18
REMARK 465 PRO B 19
REMARK 465 THR B 20
REMARK 465 ALA B 21
REMARK 465 CYS B 22
REMARK 465 PRO B 23
REMARK 465 SER B 24
REMARK 465 GLY B 25
REMARK 465 TRP B 26
REMARK 465 ALA B 27
REMARK 465 CYS B 28
REMARK 465 GLN B 29
REMARK 465 GLN B 30
REMARK 465 LEU B 31
REMARK 465 ASN B 32
REMARK 465 ALA B 33
REMARK 465 TYR B 34
REMARK 465 TYR B 35
REMARK 465 SER B 36
REMARK 465 GLN B 37
REMARK 465 CYS B 38
REMARK 465 LEU B 39
REMARK 465 GLN B 40
REMARK 465 GLY B 41
REMARK 465 ALA B 42
REMARK 465 ALA B 43
REMARK 465 PRO B 44
REMARK 465 ALA B 45
REMARK 465 PRO B 46
REMARK 465 ALA B 47
REMARK 465 ARG B 48
REMARK 465 THR B 49
REMARK 465 THR B 50
REMARK 465 ALA B 51
REMARK 465 ALA B 52
REMARK 465 PRO B 53
REMARK 465 PRO B 54
REMARK 465 PRO B 55
REMARK 465 PRO B 56
REMARK 465 PRO B 57
REMARK 465 ALA B 58
REMARK 465 THR B 59
REMARK 465 THR B 60
REMARK 465 ALA B 61
REMARK 465 ALA B 62
REMARK 465 PRO B 63
REMARK 465 PRO B 64
REMARK 465 PRO B 65
REMARK 465 PRO B 66
REMARK 465 THR B 67
REMARK 465 THR B 68
REMARK 465 SER B 69
REMARK 465 ALA B 70
REMARK 465 PRO B 71
REMARK 465 THR B 72
REMARK 465 GLY B 73
REMARK 465 SER B 74
REMARK 465 SER B 75
REMARK 465 PRO B 76
REMARK 465 VAL B 77
REMARK 465 ALA B 78
REMARK 465 GLY B 79
REMARK 465 GLU B 461
REMARK 465 GLN B 462
REMARK 465 LYS B 463
REMARK 465 LEU B 464
REMARK 465 ILE B 465
REMARK 465 SER B 466
REMARK 465 GLU B 467
REMARK 465 GLU B 468
REMARK 465 ASP B 469
REMARK 465 LEU B 470
REMARK 465 ASN B 471
REMARK 465 SER B 472
REMARK 465 ALA B 473
REMARK 465 VAL B 474
REMARK 465 ASP B 475
REMARK 465 HIS B 476
REMARK 465 HIS B 477
REMARK 465 HIS B 478
REMARK 465 HIS B 479
REMARK 465 HIS B 480
REMARK 465 HIS B 481
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 OG SER B 270 C6 GCV B 505 1.62
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 ASN A 92 96.93 -161.75
REMARK 500 ARG A 109 -35.15 -130.36
REMARK 500 SER A 162 -8.98 86.62
REMARK 500 GLN A 213 46.41 -151.96
REMARK 500 SER A 215 -173.03 -172.41
REMARK 500 SER A 270 -128.65 62.88
REMARK 500 ASN A 325 -166.08 -161.50
REMARK 500 PRO A 343 33.74 -84.22
REMARK 500 SER A 370 65.65 63.35
REMARK 500 TRP A 449 -35.40 -133.12
REMARK 500 ASN B 92 98.53 -162.53
REMARK 500 GLU B 129 -20.75 -141.06
REMARK 500 GLN B 213 45.61 -149.93
REMARK 500 SER B 215 -172.61 -174.51
REMARK 500 SER B 270 -126.67 66.33
REMARK 500 ASN B 325 -168.63 -164.32
REMARK 500 SER B 370 66.60 65.49
REMARK 500 ASN B 437 19.74 58.87
REMARK 500 TRP B 449 -37.90 -135.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GCV B 505
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BXP A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide MAN A 504 bound
REMARK 800 to SER A 86
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide MAN A 503 bound
REMARK 800 to THR A 87
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound
REMARK 800 to ASN A 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide MAN B 507 bound
REMARK 800 to SER B 86
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide MAN B 506 bound
REMARK 800 to THR B 87
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 501 bound
REMARK 800 to ASN B 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues XYL B
REMARK 800 502 through GCV B 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6RTV RELATED DB: PDB
REMARK 900 RELATED ID: 6RU1 RELATED DB: PDB
REMARK 900 RELATED ID: 6RU2 RELATED DB: PDB
REMARK 900 RELATED ID: 6RV7 RELATED DB: PDB
DBREF1 6RV8 A 2 458 UNP GCE_CERUI
DBREF2 6RV8 A A0A0A7EQR3 18 474
DBREF1 6RV8 B 2 458 UNP GCE_CERUI
DBREF2 6RV8 B A0A0A7EQR3 18 474
SEQADV 6RV8 MET A 1 UNP A0A0A7EQR INITIATING METHIONINE
SEQADV 6RV8 GLY A 459 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 LEU A 460 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 GLU A 461 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 GLN A 462 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 LYS A 463 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 LEU A 464 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 ILE A 465 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 SER A 466 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 GLU A 467 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 GLU A 468 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 ASP A 469 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 LEU A 470 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 ASN A 471 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 SER A 472 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 ALA A 473 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 VAL A 474 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 ASP A 475 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 HIS A 476 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 HIS A 477 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 HIS A 478 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 HIS A 479 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 HIS A 480 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 HIS A 481 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 MET B 1 UNP A0A0A7EQR INITIATING METHIONINE
SEQADV 6RV8 GLY B 459 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 LEU B 460 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 GLU B 461 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 GLN B 462 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 LYS B 463 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 LEU B 464 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 ILE B 465 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 SER B 466 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 GLU B 467 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 GLU B 468 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 ASP B 469 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 LEU B 470 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 ASN B 471 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 SER B 472 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 ALA B 473 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 VAL B 474 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 ASP B 475 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 HIS B 476 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 HIS B 477 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 HIS B 478 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 HIS B 479 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 HIS B 480 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV8 HIS B 481 UNP A0A0A7EQR EXPRESSION TAG
SEQRES 1 A 481 MET GLN ALA SER ALA PRO GLN TRP GLY GLN CYS GLY GLY
SEQRES 2 A 481 ILE GLY TRP THR GLY PRO THR ALA CYS PRO SER GLY TRP
SEQRES 3 A 481 ALA CYS GLN GLN LEU ASN ALA TYR TYR SER GLN CYS LEU
SEQRES 4 A 481 GLN GLY ALA ALA PRO ALA PRO ALA ARG THR THR ALA ALA
SEQRES 5 A 481 PRO PRO PRO PRO PRO ALA THR THR ALA ALA PRO PRO PRO
SEQRES 6 A 481 PRO THR THR SER ALA PRO THR GLY SER SER PRO VAL ALA
SEQRES 7 A 481 GLY ALA CYS GLY ALA ILE ALA SER THR VAL PRO ASN TYR
SEQRES 8 A 481 ASN ASN ALA LYS LEU PRO ASP PRO PHE THR PHE ALA ASN
SEQRES 9 A 481 GLY THR ALA LEU ARG THR LYS ALA ASP TRP SER CYS ARG
SEQRES 10 A 481 ARG ALA GLU ILE SER ALA LEU ILE GLN ASN TYR GLU ALA
SEQRES 11 A 481 GLY THR LEU PRO PRO LYS PRO PRO VAL VAL THR ALA SER
SEQRES 12 A 481 PHE SER LYS SER GLY ASN THR GLY THR LEU ALA ILE THR
SEQRES 13 A 481 ALA GLY LEU SER ASN SER GLN THR ILE LYS PHE SER PRO
SEQRES 14 A 481 THR ILE SER TYR PRO SER GLY THR PRO PRO ALA ASN GLY
SEQRES 15 A 481 TRP PRO LEU ILE ILE ALA TYR GLU GLY GLY SER ILE PRO
SEQRES 16 A 481 ILE PRO ALA GLY VAL ALA THR LEU THR TYR SER ASN SER
SEQRES 17 A 481 ASP MET ALA GLN GLN ASN SER ALA SER SER ARG GLY GLN
SEQRES 18 A 481 GLY LEU PHE TYR GLN LEU TYR GLY SER THR HIS SER ALA
SEQRES 19 A 481 SER ALA MET THR ALA TRP VAL TRP GLY VAL SER ARG ILE
SEQRES 20 A 481 ILE ASP ALA LEU GLU MET THR PRO THR ALA GLN ILE ASN
SEQRES 21 A 481 THR GLN ARG ILE GLY VAL THR GLY CYS SER ARG ASP GLY
SEQRES 22 A 481 LYS GLY ALA LEU MET ALA GLY ALA PHE GLU GLU ARG ILE
SEQRES 23 A 481 ALA LEU THR ILE PRO GLN GLU SER GLY SER GLY GLY ASP
SEQRES 24 A 481 ALA CYS TRP ARG LEU SER LYS TYR GLU ILE ASP ASN GLY
SEQRES 25 A 481 ASN GLN VAL GLN ASP ALA VAL GLU ILE VAL GLY GLU ASN
SEQRES 26 A 481 VAL TRP PHE SER THR ASN PHE ASN ASN TYR VAL GLN LYS
SEQRES 27 A 481 LEU PRO THR VAL PRO GLU ASP HIS HIS LEU LEU ALA ALA
SEQRES 28 A 481 MET VAL ALA PRO ARG ALA MET ILE SER PHE GLU ASN THR
SEQRES 29 A 481 ASP TYR LEU TRP LEU SER PRO MET SER SER PHE GLY CYS
SEQRES 30 A 481 MET THR ALA ALA HIS THR VAL TRP GLN GLY LEU GLY ILE
SEQRES 31 A 481 ALA ASP SER HIS GLY PHE ALA GLN VAL GLY GLY HIS ALA
SEQRES 32 A 481 HIS CYS ALA TRP PRO SER SER LEU THR PRO GLN LEU ASN
SEQRES 33 A 481 ALA PHE ILE ASN ARG PHE LEU LEU ASP GLN SER ALA THR
SEQRES 34 A 481 THR ASN VAL PHE THR THR ASN ASN GLN PHE GLY LYS VAL
SEQRES 35 A 481 GLN TRP ASN ALA ALA ASN TRP ILE THR TRP THR THR PRO
SEQRES 36 A 481 THR LEU THR GLY LEU GLU GLN LYS LEU ILE SER GLU GLU
SEQRES 37 A 481 ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 B 481 MET GLN ALA SER ALA PRO GLN TRP GLY GLN CYS GLY GLY
SEQRES 2 B 481 ILE GLY TRP THR GLY PRO THR ALA CYS PRO SER GLY TRP
SEQRES 3 B 481 ALA CYS GLN GLN LEU ASN ALA TYR TYR SER GLN CYS LEU
SEQRES 4 B 481 GLN GLY ALA ALA PRO ALA PRO ALA ARG THR THR ALA ALA
SEQRES 5 B 481 PRO PRO PRO PRO PRO ALA THR THR ALA ALA PRO PRO PRO
SEQRES 6 B 481 PRO THR THR SER ALA PRO THR GLY SER SER PRO VAL ALA
SEQRES 7 B 481 GLY ALA CYS GLY ALA ILE ALA SER THR VAL PRO ASN TYR
SEQRES 8 B 481 ASN ASN ALA LYS LEU PRO ASP PRO PHE THR PHE ALA ASN
SEQRES 9 B 481 GLY THR ALA LEU ARG THR LYS ALA ASP TRP SER CYS ARG
SEQRES 10 B 481 ARG ALA GLU ILE SER ALA LEU ILE GLN ASN TYR GLU ALA
SEQRES 11 B 481 GLY THR LEU PRO PRO LYS PRO PRO VAL VAL THR ALA SER
SEQRES 12 B 481 PHE SER LYS SER GLY ASN THR GLY THR LEU ALA ILE THR
SEQRES 13 B 481 ALA GLY LEU SER ASN SER GLN THR ILE LYS PHE SER PRO
SEQRES 14 B 481 THR ILE SER TYR PRO SER GLY THR PRO PRO ALA ASN GLY
SEQRES 15 B 481 TRP PRO LEU ILE ILE ALA TYR GLU GLY GLY SER ILE PRO
SEQRES 16 B 481 ILE PRO ALA GLY VAL ALA THR LEU THR TYR SER ASN SER
SEQRES 17 B 481 ASP MET ALA GLN GLN ASN SER ALA SER SER ARG GLY GLN
SEQRES 18 B 481 GLY LEU PHE TYR GLN LEU TYR GLY SER THR HIS SER ALA
SEQRES 19 B 481 SER ALA MET THR ALA TRP VAL TRP GLY VAL SER ARG ILE
SEQRES 20 B 481 ILE ASP ALA LEU GLU MET THR PRO THR ALA GLN ILE ASN
SEQRES 21 B 481 THR GLN ARG ILE GLY VAL THR GLY CYS SER ARG ASP GLY
SEQRES 22 B 481 LYS GLY ALA LEU MET ALA GLY ALA PHE GLU GLU ARG ILE
SEQRES 23 B 481 ALA LEU THR ILE PRO GLN GLU SER GLY SER GLY GLY ASP
SEQRES 24 B 481 ALA CYS TRP ARG LEU SER LYS TYR GLU ILE ASP ASN GLY
SEQRES 25 B 481 ASN GLN VAL GLN ASP ALA VAL GLU ILE VAL GLY GLU ASN
SEQRES 26 B 481 VAL TRP PHE SER THR ASN PHE ASN ASN TYR VAL GLN LYS
SEQRES 27 B 481 LEU PRO THR VAL PRO GLU ASP HIS HIS LEU LEU ALA ALA
SEQRES 28 B 481 MET VAL ALA PRO ARG ALA MET ILE SER PHE GLU ASN THR
SEQRES 29 B 481 ASP TYR LEU TRP LEU SER PRO MET SER SER PHE GLY CYS
SEQRES 30 B 481 MET THR ALA ALA HIS THR VAL TRP GLN GLY LEU GLY ILE
SEQRES 31 B 481 ALA ASP SER HIS GLY PHE ALA GLN VAL GLY GLY HIS ALA
SEQRES 32 B 481 HIS CYS ALA TRP PRO SER SER LEU THR PRO GLN LEU ASN
SEQRES 33 B 481 ALA PHE ILE ASN ARG PHE LEU LEU ASP GLN SER ALA THR
SEQRES 34 B 481 THR ASN VAL PHE THR THR ASN ASN GLN PHE GLY LYS VAL
SEQRES 35 B 481 GLN TRP ASN ALA ALA ASN TRP ILE THR TRP THR THR PRO
SEQRES 36 B 481 THR LEU THR GLY LEU GLU GLN LYS LEU ILE SER GLU GLU
SEQRES 37 B 481 ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS
HET NAG A 501 14
HET EDO A 502 10
HET MAN A 503 22
HET MAN A 504 22
HET BXP A 505 37
HET NAG B 501 14
HET XYL B 502 21
HET XYP B 503 17
HET XYP B 504 17
HET GCV B 505 22
HET MAN B 506 22
HET MAN B 507 22
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM MAN ALPHA-D-MANNOSE
HETNAM BXP 4-O-BETA-D-XYLOPYRANOSYL-BETA-D-XYLOPYRANOSE
HETNAM XYL D-XYLITOL
HETNAM XYP BETA-D-XYLOPYRANOSE
HETNAM GCV 4-O-METHYL-ALPHA-D-GLUCURONIC ACID
HETSYN EDO ETHYLENE GLYCOL
HETSYN BXP XYLOBIOSE
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 EDO C2 H6 O2
FORMUL 5 MAN 4(C6 H12 O6)
FORMUL 7 BXP C10 H18 O9
FORMUL 9 XYL C5 H12 O5
FORMUL 9 XYP 2(C5 H10 O5)
FORMUL 9 GCV C7 H12 O7
FORMUL 12 HOH *579(H2 O)
HELIX 1 AA1 THR A 110 GLU A 129 1 20
HELIX 2 AA2 SER A 206 ALA A 211 1 6
HELIX 3 AA3 SER A 215 ARG A 219 5 5
HELIX 4 AA4 GLY A 222 GLY A 229 1 8
HELIX 5 AA5 SER A 235 MET A 253 1 19
HELIX 6 AA6 THR A 254 ALA A 257 5 4
HELIX 7 AA7 SER A 270 GLU A 283 1 14
HELIX 8 AA8 CYS A 301 ASN A 311 1 11
HELIX 9 AA9 ASP A 317 ASN A 325 1 9
HELIX 10 AB1 SER A 329 TYR A 335 5 7
HELIX 11 AB2 LYS A 338 VAL A 342 5 5
HELIX 12 AB3 ASP A 345 MET A 352 1 8
HELIX 13 AB4 TYR A 366 LEU A 369 5 4
HELIX 14 AB5 SER A 370 LEU A 388 1 19
HELIX 15 AB6 ILE A 390 ASP A 392 5 3
HELIX 16 AB7 PRO A 408 SER A 410 5 3
HELIX 17 AB8 LEU A 411 LEU A 423 1 13
HELIX 18 AB9 ASN A 445 TRP A 449 5 5
HELIX 19 AC1 ALA B 112 GLU B 129 1 18
HELIX 20 AC2 SER B 206 ALA B 211 1 6
HELIX 21 AC3 SER B 215 ARG B 219 5 5
HELIX 22 AC4 GLY B 222 GLY B 229 1 8
HELIX 23 AC5 SER B 235 MET B 253 1 19
HELIX 24 AC6 THR B 254 ALA B 257 5 4
HELIX 25 AC7 SER B 270 GLU B 283 1 14
HELIX 26 AC8 CYS B 301 ASN B 311 1 11
HELIX 27 AC9 ASP B 317 ASN B 325 1 9
HELIX 28 AD1 SER B 329 TYR B 335 5 7
HELIX 29 AD2 LYS B 338 VAL B 342 5 5
HELIX 30 AD3 ASP B 345 MET B 352 1 8
HELIX 31 AD4 TYR B 366 LEU B 369 5 4
HELIX 32 AD5 SER B 370 LEU B 388 1 19
HELIX 33 AD6 ILE B 390 ASP B 392 5 3
HELIX 34 AD7 PRO B 408 SER B 410 5 3
HELIX 35 AD8 LEU B 411 LEU B 423 1 13
HELIX 36 AD9 ASN B 445 TRP B 449 5 5
SHEET 1 AA1 3 VAL A 139 SER A 147 0
SHEET 2 AA1 3 THR A 150 GLY A 158 -1 O THR A 152 N SER A 145
SHEET 3 AA1 3 THR A 164 PHE A 167 -1 O PHE A 167 N ILE A 155
SHEET 1 AA210 VAL A 139 SER A 147 0
SHEET 2 AA210 THR A 150 GLY A 158 -1 O THR A 152 N SER A 145
SHEET 3 AA210 THR A 170 SER A 172 -1 O ILE A 171 N GLY A 151
SHEET 4 AA210 ALA A 201 TYR A 205 -1 O THR A 202 N SER A 172
SHEET 5 AA210 TRP A 183 TYR A 189 1 N ALA A 188 O LEU A 203
SHEET 6 AA210 ILE A 259 CYS A 269 1 O GLY A 265 N ILE A 187
SHEET 7 AA210 LEU A 288 GLN A 292 1 O ILE A 290 N VAL A 266
SHEET 8 AA210 ALA A 357 ASN A 363 1 O ILE A 359 N THR A 289
SHEET 9 AA210 HIS A 394 VAL A 399 1 O GLY A 395 N MET A 358
SHEET 10 AA210 PHE A 433 THR A 434 1 O THR A 434 N PHE A 396
SHEET 1 AA3 3 VAL B 139 SER B 147 0
SHEET 2 AA3 3 THR B 150 SER B 160 -1 O THR B 150 N SER B 147
SHEET 3 AA3 3 GLN B 163 PHE B 167 -1 O PHE B 167 N ILE B 155
SHEET 1 AA410 VAL B 139 SER B 147 0
SHEET 2 AA410 THR B 150 SER B 160 -1 O THR B 150 N SER B 147
SHEET 3 AA410 THR B 170 SER B 172 -1 O ILE B 171 N GLY B 151
SHEET 4 AA410 ALA B 201 TYR B 205 -1 O THR B 202 N SER B 172
SHEET 5 AA410 TRP B 183 TYR B 189 1 N ALA B 188 O LEU B 203
SHEET 6 AA410 ILE B 259 CYS B 269 1 O GLY B 265 N ILE B 187
SHEET 7 AA410 LEU B 288 GLN B 292 1 O ILE B 290 N VAL B 266
SHEET 8 AA410 ALA B 357 ASN B 363 1 O PHE B 361 N PRO B 291
SHEET 9 AA410 HIS B 394 VAL B 399 1 O GLY B 395 N MET B 358
SHEET 10 AA410 PHE B 433 THR B 434 1 O THR B 434 N PHE B 396
SSBOND 1 CYS A 81 CYS A 116 1555 1555 2.05
SSBOND 2 CYS A 269 CYS A 405 1555 1555 2.06
SSBOND 3 CYS A 301 CYS A 377 1555 1555 2.11
SSBOND 4 CYS B 81 CYS B 116 1555 1555 2.05
SSBOND 5 CYS B 269 CYS B 405 1555 1555 2.06
SSBOND 6 CYS B 301 CYS B 377 1555 1555 2.09
LINK OG SER A 86 C1 MAN A 504 1555 1555 1.45
LINK OG1 THR A 87 C1 MAN A 503 1555 1555 1.47
LINK ND2 ASN A 104 C1 NAG A 501 1555 1555 1.44
LINK OG SER B 86 C1 MAN B 507 1555 1555 1.47
LINK OG1 THR B 87 C1 MAN B 506 1555 1555 1.44
LINK ND2 ASN B 104 C1 NAG B 501 1555 1555 1.47
LINK O4 XYL B 502 C1B XYP B 503 1555 1555 1.42
LINK O4B XYP B 503 C1B XYP B 504 1555 1555 1.37
LINK O2B XYP B 504 C1 GCV B 505 1555 1555 1.46
CISPEP 1 ALA A 354 PRO A 355 0 4.85
CISPEP 2 ALA B 354 PRO B 355 0 7.79
SITE 1 AC1 4 LYS A 274 GLN A 316 GLU A 324 TRP A 368
SITE 1 AC2 4 THR A 330 ASN A 331 ASN A 333 ASN A 334
SITE 1 AC3 1 SER A 86
SITE 1 AC4 6 THR A 87 ASN A 127 TYR A 128 TYR A 335
SITE 2 AC4 6 HOH A 606 HOH A 611
SITE 1 AC5 7 CYS A 81 ALA A 83 PHE A 102 ASN A 104
SITE 2 AC5 7 THR A 106 HOH A 638 ASN B 92
SITE 1 AC6 2 ILE B 84 SER B 86
SITE 1 AC7 7 SER A 427 THR B 87 ASN B 127 TYR B 128
SITE 2 AC7 7 TYR B 335 HOH B 606 HOH B 715
SITE 1 AC8 8 ASN A 92 CYS B 81 ALA B 83 PHE B 102
SITE 2 AC8 8 ASN B 104 THR B 106 HOH B 626 HOH B 629
SITE 1 AC9 13 SER B 270 ARG B 271 LYS B 274 GLN B 316
SITE 2 AC9 13 GLU B 320 GLU B 324 TRP B 368 LEU B 369
SITE 3 AC9 13 HIS B 404 HOH B 688 HOH B 714 HOH B 779
SITE 4 AC9 13 HOH B 815
CRYST1 84.750 84.750 261.062 90.00 90.00 90.00 P 41 21 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011799 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011799 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003831 0.00000
TER 2892 LEU A 460
TER 5773 LEU B 460
MASTER 752 0 12 36 26 0 16 6 6454 2 258 74
END |