content |
HEADER HYDROLASE 27-MAY-19 6RU1
TITLE CRYSTAL STRUCTURE OF GLUCURONOYL ESTERASE FROM CERRENA UNICOLOR
TITLE 2 INACTIVE S270A VARIANT IN COMPLEX WITH THE ALDOURONIC ACID UM4X
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-O-METHYL-GLUCURONOYL METHYLESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: GLUCURONOYL ESTERASE,GE;
COMPND 6 EC: 3.1.1.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: 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 6RU1 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. 1.39 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) : 1.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 188017
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 9369
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 42.1393 - 4.3160 0.96 6269 336 0.1514 0.1568
REMARK 3 2 4.3160 - 3.4262 0.98 6065 310 0.1429 0.1511
REMARK 3 3 3.4262 - 2.9932 0.99 6037 332 0.1590 0.1705
REMARK 3 4 2.9932 - 2.7196 0.99 6023 311 0.1615 0.1734
REMARK 3 5 2.7196 - 2.5247 0.99 6059 305 0.1598 0.1630
REMARK 3 6 2.5247 - 2.3759 0.99 5979 323 0.1586 0.1787
REMARK 3 7 2.3759 - 2.2569 1.00 5999 313 0.1575 0.1664
REMARK 3 8 2.2569 - 2.1587 1.00 5965 307 0.1573 0.1697
REMARK 3 9 2.1587 - 2.0756 1.00 6015 299 0.1528 0.1609
REMARK 3 10 2.0756 - 2.0039 1.00 5917 331 0.1561 0.1959
REMARK 3 11 2.0039 - 1.9413 1.00 5988 321 0.1543 0.1763
REMARK 3 12 1.9413 - 1.8858 1.00 5953 332 0.1559 0.1735
REMARK 3 13 1.8858 - 1.8361 1.00 5937 281 0.1551 0.1672
REMARK 3 14 1.8361 - 1.7913 1.00 5959 312 0.1593 0.1577
REMARK 3 15 1.7913 - 1.7506 1.00 5957 303 0.1633 0.1833
REMARK 3 16 1.7506 - 1.7134 1.00 5954 296 0.1683 0.2092
REMARK 3 17 1.7134 - 1.6791 1.00 5924 326 0.1657 0.1845
REMARK 3 18 1.6791 - 1.6474 1.00 5938 302 0.1728 0.2009
REMARK 3 19 1.6474 - 1.6180 1.00 5907 324 0.1684 0.1929
REMARK 3 20 1.6180 - 1.5906 1.00 5908 300 0.1676 0.1875
REMARK 3 21 1.5906 - 1.5649 1.00 5908 325 0.1706 0.1900
REMARK 3 22 1.5649 - 1.5408 1.00 5880 330 0.1774 0.2048
REMARK 3 23 1.5408 - 1.5182 1.00 5899 330 0.1928 0.2132
REMARK 3 24 1.5182 - 1.4968 1.00 5909 276 0.1952 0.2149
REMARK 3 25 1.4968 - 1.4765 1.00 5909 305 0.2031 0.2173
REMARK 3 26 1.4765 - 1.4574 1.00 5881 314 0.2071 0.2257
REMARK 3 27 1.4574 - 1.4391 1.00 5924 303 0.2176 0.2284
REMARK 3 28 1.4391 - 1.4218 1.00 5928 295 0.2239 0.2589
REMARK 3 29 1.4218 - 1.4053 1.00 5827 314 0.2290 0.2441
REMARK 3 30 1.4053 - 1.3895 0.98 5830 313 0.2362 0.2542
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.16
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 : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 73 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.1927 7.7104 35.8964
REMARK 3 T TENSOR
REMARK 3 T11: 0.1128 T22: 0.1167
REMARK 3 T33: 0.1343 T12: 0.0041
REMARK 3 T13: -0.0352 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 2.6729 L22: 2.2778
REMARK 3 L33: 4.9425 L12: 0.1291
REMARK 3 L13: -1.4450 L23: 0.8110
REMARK 3 S TENSOR
REMARK 3 S11: 0.0917 S12: -0.2199 S13: 0.2505
REMARK 3 S21: 0.1756 S22: -0.0351 S23: 0.0444
REMARK 3 S31: -0.2286 S32: -0.1040 S33: -0.0490
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4706 10.3454 27.8826
REMARK 3 T TENSOR
REMARK 3 T11: 0.1049 T22: 0.0749
REMARK 3 T33: 0.1037 T12: -0.0007
REMARK 3 T13: 0.0151 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 1.6945 L22: 0.5526
REMARK 3 L33: 0.6267 L12: -0.4834
REMARK 3 L13: 0.3699 L23: -0.0693
REMARK 3 S TENSOR
REMARK 3 S11: 0.0155 S12: -0.0538 S13: -0.0186
REMARK 3 S21: 0.0587 S22: -0.0069 S23: 0.0632
REMARK 3 S31: -0.0006 S32: -0.0625 S33: -0.0094
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9469 17.0840 19.2897
REMARK 3 T TENSOR
REMARK 3 T11: 0.1051 T22: 0.1363
REMARK 3 T33: 0.1672 T12: 0.0380
REMARK 3 T13: 0.0075 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.9943 L22: 6.9876
REMARK 3 L33: 5.4545 L12: 1.5171
REMARK 3 L13: 1.1202 L23: 5.4445
REMARK 3 S TENSOR
REMARK 3 S11: 0.0125 S12: -0.0079 S13: 0.0311
REMARK 3 S21: -0.3602 S22: 0.0461 S23: 0.0225
REMARK 3 S31: -0.3190 S32: -0.1027 S33: -0.0418
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 173 THROUGH 205 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2043 -1.9259 18.5195
REMARK 3 T TENSOR
REMARK 3 T11: 0.1157 T22: 0.1359
REMARK 3 T33: 0.1709 T12: -0.0277
REMARK 3 T13: -0.0013 T23: -0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 1.2087 L22: 0.8757
REMARK 3 L33: 3.3358 L12: -0.5153
REMARK 3 L13: -1.1884 L23: -0.0917
REMARK 3 S TENSOR
REMARK 3 S11: -0.1210 S12: 0.0793 S13: -0.1299
REMARK 3 S21: 0.0102 S22: 0.0132 S23: 0.1751
REMARK 3 S31: 0.2551 S32: -0.3177 S33: 0.0879
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 370 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9477 6.8238 17.1337
REMARK 3 T TENSOR
REMARK 3 T11: 0.1089 T22: 0.0928
REMARK 3 T33: 0.1018 T12: 0.0037
REMARK 3 T13: -0.0013 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.5470 L22: 0.5353
REMARK 3 L33: 0.3676 L12: 0.0190
REMARK 3 L13: -0.0691 L23: -0.0540
REMARK 3 S TENSOR
REMARK 3 S11: 0.0060 S12: 0.0378 S13: 0.0336
REMARK 3 S21: -0.0059 S22: -0.0117 S23: 0.0402
REMARK 3 S31: -0.0123 S32: -0.0226 S33: 0.0045
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 371 THROUGH 458 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0894 -10.1377 20.9270
REMARK 3 T TENSOR
REMARK 3 T11: 0.1276 T22: 0.0757
REMARK 3 T33: 0.1191 T12: 0.0019
REMARK 3 T13: -0.0018 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 1.0710 L22: 0.6407
REMARK 3 L33: 0.8617 L12: 0.0964
REMARK 3 L13: -0.1445 L23: 0.1776
REMARK 3 S TENSOR
REMARK 3 S11: 0.0084 S12: 0.0016 S13: -0.0912
REMARK 3 S21: 0.0174 S22: -0.0210 S23: 0.0474
REMARK 3 S31: 0.0683 S32: -0.0155 S33: 0.0132
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 73 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.4556 48.0951 31.2272
REMARK 3 T TENSOR
REMARK 3 T11: 0.1090 T22: 0.0935
REMARK 3 T33: 0.0900 T12: -0.0039
REMARK 3 T13: -0.0223 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 2.5519 L22: 2.1122
REMARK 3 L33: 2.9697 L12: 0.2756
REMARK 3 L13: -0.3693 L23: -0.5563
REMARK 3 S TENSOR
REMARK 3 S11: -0.0048 S12: -0.2560 S13: 0.0728
REMARK 3 S21: 0.2106 S22: 0.0007 S23: 0.0471
REMARK 3 S31: -0.0580 S32: -0.0685 S33: -0.0193
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.3612 48.5357 15.3563
REMARK 3 T TENSOR
REMARK 3 T11: 0.1290 T22: 0.0961
REMARK 3 T33: 0.1114 T12: 0.0045
REMARK 3 T13: -0.0037 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.3702 L22: 0.3982
REMARK 3 L33: 0.2572 L12: -0.0670
REMARK 3 L13: -0.0632 L23: 0.0158
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: 0.0135 S13: -0.0136
REMARK 3 S21: 0.0101 S22: 0.0001 S23: 0.0704
REMARK 3 S31: 0.0009 S32: -0.0173 S33: 0.0085
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 318 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.5623 57.4484 10.8506
REMARK 3 T TENSOR
REMARK 3 T11: 0.1322 T22: 0.0697
REMARK 3 T33: 0.0957 T12: -0.0107
REMARK 3 T13: 0.0018 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 3.2658 L22: 0.8912
REMARK 3 L33: 2.8299 L12: -1.5001
REMARK 3 L13: 1.9188 L23: -0.3587
REMARK 3 S TENSOR
REMARK 3 S11: -0.0137 S12: 0.1120 S13: 0.1467
REMARK 3 S21: 0.0175 S22: -0.0848 S23: -0.0418
REMARK 3 S31: -0.1455 S32: 0.1002 S33: 0.0979
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 339 THROUGH 422 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.4517 36.2756 13.5659
REMARK 3 T TENSOR
REMARK 3 T11: 0.1232 T22: 0.1003
REMARK 3 T33: 0.1130 T12: 0.0108
REMARK 3 T13: -0.0035 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.3832 L22: 0.5728
REMARK 3 L33: 0.3144 L12: 0.2023
REMARK 3 L13: -0.0819 L23: -0.1559
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: 0.0345 S13: -0.0481
REMARK 3 S21: -0.0319 S22: -0.0169 S23: 0.0027
REMARK 3 S31: 0.0502 S32: -0.0020 S33: 0.0168
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 423 THROUGH 458 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.8387 31.9595 15.7687
REMARK 3 T TENSOR
REMARK 3 T11: 0.1304 T22: 0.0932
REMARK 3 T33: 0.1220 T12: 0.0224
REMARK 3 T13: -0.0028 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.8744 L22: 0.6048
REMARK 3 L33: 0.3792 L12: 0.4736
REMARK 3 L13: 0.0153 L23: 0.0594
REMARK 3 S TENSOR
REMARK 3 S11: 0.0200 S12: -0.0273 S13: -0.1115
REMARK 3 S21: 0.0155 S22: -0.0147 S23: -0.0321
REMARK 3 S31: 0.0372 S32: 0.0661 S33: 0.0060
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 6RU1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1292102594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-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 : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
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 : 188224
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.390
REMARK 200 RESOLUTION RANGE LOW (A) : 49.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 1.00200
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 (%): 54.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7, 0.1 M KCL, 25% W/V
REMARK 280 SOKALAN CP7, VAPOR DIFFUSION, HANGING DROP, 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 130.40750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 42.12000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.12000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 65.20375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.12000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 42.12000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 195.61125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 42.12000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.12000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.20375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 42.12000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.12000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 195.61125
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 130.40750
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 886 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 GLU A 459
REMARK 465 ASN A 460
REMARK 465 LEU A 461
REMARK 465 TYR A 462
REMARK 465 PHE A 463
REMARK 465 GLN A 464
REMARK 465 GLY A 465
REMARK 465 VAL A 466
REMARK 465 ASP A 467
REMARK 465 HIS A 468
REMARK 465 HIS A 469
REMARK 465 HIS A 470
REMARK 465 HIS A 471
REMARK 465 HIS A 472
REMARK 465 HIS A 473
REMARK 465 GLU B 459
REMARK 465 ASN B 460
REMARK 465 LEU B 461
REMARK 465 TYR B 462
REMARK 465 PHE B 463
REMARK 465 GLN B 464
REMARK 465 GLY B 465
REMARK 465 VAL B 466
REMARK 465 ASP B 467
REMARK 465 HIS B 468
REMARK 465 HIS B 469
REMARK 465 HIS B 470
REMARK 465 HIS B 471
REMARK 465 HIS B 472
REMARK 465 HIS B 473
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 96.15 -161.33
REMARK 500 ARG A 109 -32.19 -132.03
REMARK 500 ARG A 109 -30.83 -132.74
REMARK 500 SER A 162 -12.64 88.13
REMARK 500 GLN A 213 47.64 -147.33
REMARK 500 GLN A 213 47.64 -150.65
REMARK 500 SER A 215 -171.62 -173.06
REMARK 500 ALA A 270 -129.30 62.15
REMARK 500 ASN A 325 -168.38 -161.49
REMARK 500 PRO A 343 36.55 -83.61
REMARK 500 SER A 370 65.15 64.38
REMARK 500 TRP A 449 -33.25 -134.10
REMARK 500 ASN B 92 93.88 -162.51
REMARK 500 ARG B 109 -32.61 -131.10
REMARK 500 ARG B 109 -30.42 -132.27
REMARK 500 GLN B 213 47.87 -146.37
REMARK 500 ALA B 270 -127.95 62.59
REMARK 500 PRO B 343 34.23 -83.54
REMARK 500 SER B 370 64.90 66.37
REMARK 500 TRP B 449 -33.02 -135.62
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 NA B 509 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 259 O
REMARK 620 2 GOL B 507 O2 99.5
REMARK 620 3 GOL B 507 O3 169.2 70.1
REMARK 620 4 HOH B 806 O 97.4 163.2 93.1
REMARK 620 5 HOH B 812 O 90.5 91.4 92.3 88.2
REMARK 620 6 HOH B 804 O 84.3 92.7 93.3 89.3 173.9
REMARK 620 N 1 2 3 4 5
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 GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
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: AD2
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: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GCV B
REMARK 800 502 through XYP B 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6RTV RELATED DB: PDB
REMARK 900 APO-FORM OF SAME PROTEIN
DBREF1 6RU1 A 79 458 UNP GCE_CERUI
DBREF2 6RU1 A A0A0A7EQR3 95 474
DBREF1 6RU1 B 79 458 UNP GCE_CERUI
DBREF2 6RU1 B A0A0A7EQR3 95 474
SEQADV 6RU1 GLU A 73 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 ALA A 74 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 GLU A 75 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 ALA A 76 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 GLU A 77 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 PHE A 78 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 ALA A 270 UNP A0A0A7EQR SER 286 ENGINEERED MUTATION
SEQADV 6RU1 GLU A 459 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 ASN A 460 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 LEU A 461 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 TYR A 462 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 PHE A 463 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 GLN A 464 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 GLY A 465 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 VAL A 466 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 ASP A 467 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 HIS A 468 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 HIS A 469 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 HIS A 470 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 HIS A 471 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 HIS A 472 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 HIS A 473 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 GLU B 73 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 ALA B 74 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 GLU B 75 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 ALA B 76 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 GLU B 77 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 PHE B 78 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 ALA B 270 UNP A0A0A7EQR SER 286 ENGINEERED MUTATION
SEQADV 6RU1 GLU B 459 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 ASN B 460 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 LEU B 461 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 TYR B 462 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 PHE B 463 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 GLN B 464 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 GLY B 465 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 VAL B 466 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 ASP B 467 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 HIS B 468 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 HIS B 469 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 HIS B 470 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 HIS B 471 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 HIS B 472 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU1 HIS B 473 UNP A0A0A7EQR EXPRESSION TAG
SEQRES 1 A 401 GLU ALA GLU ALA GLU PHE GLY ALA CYS GLY ALA ILE ALA
SEQRES 2 A 401 SER THR VAL PRO ASN TYR ASN ASN ALA LYS LEU PRO ASP
SEQRES 3 A 401 PRO PHE THR PHE ALA ASN GLY THR ALA LEU ARG THR LYS
SEQRES 4 A 401 ALA ASP TRP SER CYS ARG ARG ALA GLU ILE SER ALA LEU
SEQRES 5 A 401 ILE GLN ASN TYR GLU ALA GLY THR LEU PRO PRO LYS PRO
SEQRES 6 A 401 PRO VAL VAL THR ALA SER PHE SER LYS SER GLY ASN THR
SEQRES 7 A 401 GLY THR LEU ALA ILE THR ALA GLY LEU SER ASN SER GLN
SEQRES 8 A 401 THR ILE LYS PHE SER PRO THR ILE SER TYR PRO SER GLY
SEQRES 9 A 401 THR PRO PRO ALA ASN GLY TRP PRO LEU ILE ILE ALA TYR
SEQRES 10 A 401 GLU GLY GLY SER ILE PRO ILE PRO ALA GLY VAL ALA THR
SEQRES 11 A 401 LEU THR TYR SER ASN SER ASP MET ALA GLN GLN ASN SER
SEQRES 12 A 401 ALA SER SER ARG GLY GLN GLY LEU PHE TYR GLN LEU TYR
SEQRES 13 A 401 GLY SER THR HIS SER ALA SER ALA MET THR ALA TRP VAL
SEQRES 14 A 401 TRP GLY VAL SER ARG ILE ILE ASP ALA LEU GLU MET THR
SEQRES 15 A 401 PRO THR ALA GLN ILE ASN THR GLN ARG ILE GLY VAL THR
SEQRES 16 A 401 GLY CYS ALA ARG ASP GLY LYS GLY ALA LEU MET ALA GLY
SEQRES 17 A 401 ALA PHE GLU GLU ARG ILE ALA LEU THR ILE PRO GLN GLU
SEQRES 18 A 401 SER GLY SER GLY GLY ASP ALA CYS TRP ARG LEU SER LYS
SEQRES 19 A 401 TYR GLU ILE ASP ASN GLY ASN GLN VAL GLN ASP ALA VAL
SEQRES 20 A 401 GLU ILE VAL GLY GLU ASN VAL TRP PHE SER THR ASN PHE
SEQRES 21 A 401 ASN ASN TYR VAL GLN LYS LEU PRO THR VAL PRO GLU ASP
SEQRES 22 A 401 HIS HIS LEU LEU ALA ALA MET VAL ALA PRO ARG ALA MET
SEQRES 23 A 401 ILE SER PHE GLU ASN THR ASP TYR LEU TRP LEU SER PRO
SEQRES 24 A 401 MET SER SER PHE GLY CYS MET THR ALA ALA HIS THR VAL
SEQRES 25 A 401 TRP GLN GLY LEU GLY ILE ALA ASP SER HIS GLY PHE ALA
SEQRES 26 A 401 GLN VAL GLY GLY HIS ALA HIS CYS ALA TRP PRO SER SER
SEQRES 27 A 401 LEU THR PRO GLN LEU ASN ALA PHE ILE ASN ARG PHE LEU
SEQRES 28 A 401 LEU ASP GLN SER ALA THR THR ASN VAL PHE THR THR ASN
SEQRES 29 A 401 ASN GLN PHE GLY LYS VAL GLN TRP ASN ALA ALA ASN TRP
SEQRES 30 A 401 ILE THR TRP THR THR PRO THR LEU THR GLU ASN LEU TYR
SEQRES 31 A 401 PHE GLN GLY VAL ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 B 401 GLU ALA GLU ALA GLU PHE GLY ALA CYS GLY ALA ILE ALA
SEQRES 2 B 401 SER THR VAL PRO ASN TYR ASN ASN ALA LYS LEU PRO ASP
SEQRES 3 B 401 PRO PHE THR PHE ALA ASN GLY THR ALA LEU ARG THR LYS
SEQRES 4 B 401 ALA ASP TRP SER CYS ARG ARG ALA GLU ILE SER ALA LEU
SEQRES 5 B 401 ILE GLN ASN TYR GLU ALA GLY THR LEU PRO PRO LYS PRO
SEQRES 6 B 401 PRO VAL VAL THR ALA SER PHE SER LYS SER GLY ASN THR
SEQRES 7 B 401 GLY THR LEU ALA ILE THR ALA GLY LEU SER ASN SER GLN
SEQRES 8 B 401 THR ILE LYS PHE SER PRO THR ILE SER TYR PRO SER GLY
SEQRES 9 B 401 THR PRO PRO ALA ASN GLY TRP PRO LEU ILE ILE ALA TYR
SEQRES 10 B 401 GLU GLY GLY SER ILE PRO ILE PRO ALA GLY VAL ALA THR
SEQRES 11 B 401 LEU THR TYR SER ASN SER ASP MET ALA GLN GLN ASN SER
SEQRES 12 B 401 ALA SER SER ARG GLY GLN GLY LEU PHE TYR GLN LEU TYR
SEQRES 13 B 401 GLY SER THR HIS SER ALA SER ALA MET THR ALA TRP VAL
SEQRES 14 B 401 TRP GLY VAL SER ARG ILE ILE ASP ALA LEU GLU MET THR
SEQRES 15 B 401 PRO THR ALA GLN ILE ASN THR GLN ARG ILE GLY VAL THR
SEQRES 16 B 401 GLY CYS ALA ARG ASP GLY LYS GLY ALA LEU MET ALA GLY
SEQRES 17 B 401 ALA PHE GLU GLU ARG ILE ALA LEU THR ILE PRO GLN GLU
SEQRES 18 B 401 SER GLY SER GLY GLY ASP ALA CYS TRP ARG LEU SER LYS
SEQRES 19 B 401 TYR GLU ILE ASP ASN GLY ASN GLN VAL GLN ASP ALA VAL
SEQRES 20 B 401 GLU ILE VAL GLY GLU ASN VAL TRP PHE SER THR ASN PHE
SEQRES 21 B 401 ASN ASN TYR VAL GLN LYS LEU PRO THR VAL PRO GLU ASP
SEQRES 22 B 401 HIS HIS LEU LEU ALA ALA MET VAL ALA PRO ARG ALA MET
SEQRES 23 B 401 ILE SER PHE GLU ASN THR ASP TYR LEU TRP LEU SER PRO
SEQRES 24 B 401 MET SER SER PHE GLY CYS MET THR ALA ALA HIS THR VAL
SEQRES 25 B 401 TRP GLN GLY LEU GLY ILE ALA ASP SER HIS GLY PHE ALA
SEQRES 26 B 401 GLN VAL GLY GLY HIS ALA HIS CYS ALA TRP PRO SER SER
SEQRES 27 B 401 LEU THR PRO GLN LEU ASN ALA PHE ILE ASN ARG PHE LEU
SEQRES 28 B 401 LEU ASP GLN SER ALA THR THR ASN VAL PHE THR THR ASN
SEQRES 29 B 401 ASN GLN PHE GLY LYS VAL GLN TRP ASN ALA ALA ASN TRP
SEQRES 30 B 401 ILE THR TRP THR THR PRO THR LEU THR GLU ASN LEU TYR
SEQRES 31 B 401 PHE GLN GLY VAL ASP HIS HIS HIS HIS HIS HIS
HET NAG A 501 14
HET EDO A 502 10
HET GOL A 503 14
HET GOL A 504 14
HET GOL A 505 14
HET NAG B 501 14
HET GCV B 502 23
HET XYP B 503 17
HET XYP B 504 18
HET GOL B 505 14
HET GOL B 506 14
HET GOL B 507 14
HET GOL B 508 14
HET NA B 509 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM GCV 4-O-METHYL-ALPHA-D-GLUCURONIC ACID
HETNAM XYP BETA-D-XYLOPYRANOSE
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 EDO C2 H6 O2
FORMUL 5 GOL 7(C3 H8 O3)
FORMUL 9 GCV C7 H12 O7
FORMUL 9 XYP 2(C5 H10 O5)
FORMUL 14 NA NA 1+
FORMUL 15 HOH *734(H2 O)
HELIX 1 AA1 ALA A 74 GLY A 79 1 6
HELIX 2 AA2 THR A 110 GLU A 129 1 20
HELIX 3 AA3 SER A 206 ALA A 211 1 6
HELIX 4 AA4 SER A 215 ARG A 219 5 5
HELIX 5 AA5 GLY A 222 GLY A 229 1 8
HELIX 6 AA6 SER A 235 MET A 253 1 19
HELIX 7 AA7 THR A 254 ALA A 257 5 4
HELIX 8 AA8 ALA A 270 GLU A 283 1 14
HELIX 9 AA9 CYS A 301 ASN A 311 1 11
HELIX 10 AB1 ASP A 317 ASN A 325 1 9
HELIX 11 AB2 SER A 329 TYR A 335 5 7
HELIX 12 AB3 LYS A 338 VAL A 342 5 5
HELIX 13 AB4 ASP A 345 MET A 352 1 8
HELIX 14 AB5 TYR A 366 LEU A 369 5 4
HELIX 15 AB6 SER A 370 LEU A 388 1 19
HELIX 16 AB7 ILE A 390 ASP A 392 5 3
HELIX 17 AB8 PRO A 408 SER A 410 5 3
HELIX 18 AB9 LEU A 411 LEU A 423 1 13
HELIX 19 AC1 ASN A 445 TRP A 449 5 5
HELIX 20 AC2 ALA B 74 GLY B 79 1 6
HELIX 21 AC3 THR B 110 GLU B 129 1 20
HELIX 22 AC4 SER B 206 ALA B 211 1 6
HELIX 23 AC5 SER B 215 ARG B 219 5 5
HELIX 24 AC6 GLY B 222 GLY B 229 1 8
HELIX 25 AC7 SER B 235 MET B 253 1 19
HELIX 26 AC8 THR B 254 ALA B 257 5 4
HELIX 27 AC9 ALA B 270 GLU B 283 1 14
HELIX 28 AD1 CYS B 301 ASN B 311 1 11
HELIX 29 AD2 ASP B 317 ASN B 325 1 9
HELIX 30 AD3 SER B 329 TYR B 335 5 7
HELIX 31 AD4 LYS B 338 VAL B 342 5 5
HELIX 32 AD5 ASP B 345 MET B 352 1 8
HELIX 33 AD6 TYR B 366 LEU B 369 5 4
HELIX 34 AD7 SER B 370 LEU B 388 1 19
HELIX 35 AD8 ILE B 390 ASP B 392 5 3
HELIX 36 AD9 PRO B 408 SER B 410 5 3
HELIX 37 AE1 LEU B 411 LEU B 423 1 13
HELIX 38 AE2 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 PHE A 361 N PRO A 291
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 152 N SER B 145
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 152 N SER B 145
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 ILE B 359 N THR B 289
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 2.04
SSBOND 2 CYS A 269 CYS A 405 1555 1555 2.06
SSBOND 3 CYS A 301 CYS A 377 1555 1555 2.14
SSBOND 4 CYS B 81 CYS B 116 1555 1555 2.05
SSBOND 5 CYS B 269 CYS B 405 1555 1555 2.05
SSBOND 6 CYS B 301 CYS B 377 1555 1555 2.13
LINK ND2 ASN A 104 C1 NAG A 501 1555 1555 1.45
LINK ND2 ASN B 104 C1 NAG B 501 1555 1555 1.44
LINK O ILE B 259 NA NA B 509 1555 1555 2.35
LINK C1 GCV B 502 O2B XYP B 503 1555 1555 1.44
LINK C1B XYP B 503 O4B XYP B 504 1555 1555 1.40
LINK O2 GOL B 507 NA NA B 509 1555 1555 2.49
LINK O3 GOL B 507 NA NA B 509 1555 1555 2.35
LINK NA NA B 509 O HOH B 806 1555 1555 2.35
LINK NA NA B 509 O HOH B 812 1555 1555 2.47
LINK NA NA B 509 O HOH B 804 1555 1555 2.44
CISPEP 1 ALA A 354 PRO A 355 0 6.64
CISPEP 2 ALA B 354 PRO B 355 0 7.99
SITE 1 AC1 4 LYS A 274 GLN A 316 GLU A 324 TRP A 368
SITE 1 AC2 7 PHE A 282 GLU A 283 GLU A 284 ARG A 285
SITE 2 AC2 7 HOH A 653 HOH A 773 HOH A 790
SITE 1 AC3 8 TYR A 91 THR A 101 PHE A 102 ALA A 103
SITE 2 AC3 8 ARG A 117 PRO A 343 HOH A 605 HOH A 880
SITE 1 AC4 7 LYS A 136 PRO A 138 VAL A 139 VAL A 140
SITE 2 AC4 7 MET A 253 HOH A 837 MET B 253
SITE 1 AC5 8 PHE B 282 GLU B 283 GLU B 284 ARG B 285
SITE 2 AC5 8 HOH B 658 HOH B 709 HOH B 785 HOH B 792
SITE 1 AC6 7 TYR B 91 THR B 101 PHE B 102 ALA B 103
SITE 2 AC6 7 ARG B 117 PRO B 343 HOH B 605
SITE 1 AC7 10 GLU A 252 GLU B 252 PRO B 255 ILE B 259
SITE 2 AC7 10 THR B 261 NA B 509 HOH B 751 HOH B 762
SITE 3 AC7 10 HOH B 800 HOH B 844
SITE 1 AC8 6 PRO B 413 THR B 429 THR B 430 ASN B 431
SITE 2 AC8 6 HOH B 753 HOH B 769
SITE 1 AC9 5 ILE B 259 GOL B 507 HOH B 804 HOH B 806
SITE 2 AC9 5 HOH B 812
SITE 1 AD1 15 GLU A 73 GLU A 75 CYS A 81 ALA A 83
SITE 2 AD1 15 ILE A 84 PHE A 102 ASN A 104 THR A 106
SITE 3 AD1 15 HOH A 632 HOH A 635 HOH A 728 HOH A 809
SITE 4 AD1 15 HOH A 820 HOH A 839 ASN B 92
SITE 1 AD2 14 ASN A 92 GLU B 73 GLU B 75 CYS B 81
SITE 2 AD2 14 ALA B 83 ILE B 84 PHE B 102 ASN B 104
SITE 3 AD2 14 THR B 106 HOH B 625 HOH B 655 HOH B 739
SITE 4 AD2 14 HOH B 799 HOH B 815
SITE 1 AD3 12 ALA B 270 ARG B 271 LYS B 274 GLN B 316
SITE 2 AD3 12 GLU B 324 TRP B 368 LEU B 369 HIS B 404
SITE 3 AD3 12 HOH B 667 HOH B 735 HOH B 864 HOH B 888
CRYST1 84.240 84.240 260.815 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 0.011871 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011871 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003834 0.00000
TER 2991 THR A 458
TER 5956 THR B 458
MASTER 557 0 14 38 26 0 29 6 6659 2 214 62
END |