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HEADER HYDROLASE 31-MAY-19 6RV9
TITLE CRYSTAL STRUCTURE OF GLUCURONOYL ESTERASE FROM CERRENA UNICOLOR
TITLE 2 INACTIVE S270A VARIANT IN COMPLEX WITH THE ALDOURONIC ACID XUXXR
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;
COMPND 7 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 6RV9 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. 1.64 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) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 116315
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 5754
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 44.5132 - 5.0934 0.99 4025 210 0.1668 0.1793
REMARK 3 2 5.0934 - 4.0437 0.98 3755 207 0.1411 0.1640
REMARK 3 3 4.0437 - 3.5327 0.98 3750 178 0.1545 0.1784
REMARK 3 4 3.5327 - 3.2098 0.99 3750 186 0.1776 0.2048
REMARK 3 5 3.2098 - 2.9798 0.99 3659 225 0.1923 0.2011
REMARK 3 6 2.9798 - 2.8042 0.99 3709 185 0.1900 0.2100
REMARK 3 7 2.8042 - 2.6638 1.00 3705 195 0.1902 0.2392
REMARK 3 8 2.6638 - 2.5478 1.00 3680 188 0.1915 0.2082
REMARK 3 9 2.5478 - 2.4497 1.00 3721 198 0.1880 0.2187
REMARK 3 10 2.4497 - 2.3652 1.00 3705 187 0.1868 0.2040
REMARK 3 11 2.3652 - 2.2913 1.00 3655 195 0.1901 0.2137
REMARK 3 12 2.2913 - 2.2258 1.00 3682 187 0.1902 0.2033
REMARK 3 13 2.2258 - 2.1672 1.00 3662 195 0.1928 0.2237
REMARK 3 14 2.1672 - 2.1143 1.00 3700 182 0.1939 0.2316
REMARK 3 15 2.1143 - 2.0662 1.00 3689 195 0.1934 0.2176
REMARK 3 16 2.0662 - 2.0223 1.00 3642 210 0.2035 0.2298
REMARK 3 17 2.0223 - 1.9818 1.00 3676 191 0.1996 0.2266
REMARK 3 18 1.9818 - 1.9444 1.00 3666 197 0.2048 0.2314
REMARK 3 19 1.9444 - 1.9097 1.00 3620 207 0.2085 0.2371
REMARK 3 20 1.9097 - 1.8773 1.00 3616 198 0.2122 0.2438
REMARK 3 21 1.8773 - 1.8470 1.00 3721 160 0.2218 0.2400
REMARK 3 22 1.8470 - 1.8186 1.00 3658 197 0.2241 0.2587
REMARK 3 23 1.8186 - 1.7919 1.00 3638 186 0.2261 0.2678
REMARK 3 24 1.7919 - 1.7666 1.00 3662 184 0.2399 0.2672
REMARK 3 25 1.7666 - 1.7428 1.00 3646 185 0.2498 0.2595
REMARK 3 26 1.7428 - 1.7201 1.00 3647 195 0.2544 0.2830
REMARK 3 27 1.7201 - 1.6986 1.00 3655 171 0.2611 0.3035
REMARK 3 28 1.6986 - 1.6782 1.00 3634 209 0.2764 0.3090
REMARK 3 29 1.6782 - 1.6586 0.99 3591 172 0.2955 0.3218
REMARK 3 30 1.6586 - 1.6400 0.99 3642 179 0.2999 0.3154
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.26
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.31
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 : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 98 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4321 7.8976 27.6269
REMARK 3 T TENSOR
REMARK 3 T11: 0.3828 T22: 0.2157
REMARK 3 T33: 0.1528 T12: -0.0097
REMARK 3 T13: -0.0258 T23: -0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 4.3117 L22: 4.3723
REMARK 3 L33: 6.0320 L12: 0.6427
REMARK 3 L13: -3.3285 L23: -0.2717
REMARK 3 S TENSOR
REMARK 3 S11: 0.1335 S12: -0.2926 S13: 0.1401
REMARK 3 S21: 0.1312 S22: -0.0721 S23: -0.0231
REMARK 3 S31: -0.4518 S32: 0.0217 S33: -0.0761
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 99 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0776 5.7202 27.7789
REMARK 3 T TENSOR
REMARK 3 T11: 0.3754 T22: 0.1546
REMARK 3 T33: 0.1728 T12: 0.0042
REMARK 3 T13: 0.0864 T23: -0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 3.0573 L22: 1.1688
REMARK 3 L33: 0.3645 L12: -0.9978
REMARK 3 L13: 0.4255 L23: -0.2810
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: -0.2162 S13: -0.1906
REMARK 3 S21: 0.3104 S22: 0.0179 S23: 0.1712
REMARK 3 S31: -0.0544 S32: -0.0289 S33: -0.0274
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 148 THROUGH 317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7244 5.3742 14.9236
REMARK 3 T TENSOR
REMARK 3 T11: 0.3355 T22: 0.1565
REMARK 3 T33: 0.2040 T12: 0.0161
REMARK 3 T13: 0.0812 T23: -0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 0.3975 L22: 1.0887
REMARK 3 L33: 0.2224 L12: 0.0319
REMARK 3 L13: 0.1889 L23: 0.0011
REMARK 3 S TENSOR
REMARK 3 S11: 0.0273 S12: 0.0305 S13: -0.0759
REMARK 3 S21: 0.1821 S22: -0.0552 S23: 0.2718
REMARK 3 S31: 0.0142 S32: -0.0478 S33: 0.0436
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 318 THROUGH 422 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2938 -1.7453 12.8197
REMARK 3 T TENSOR
REMARK 3 T11: 0.3088 T22: 0.1578
REMARK 3 T33: 0.1667 T12: 0.0299
REMARK 3 T13: 0.0450 T23: -0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 0.7878 L22: 0.7625
REMARK 3 L33: 0.6076 L12: 0.0656
REMARK 3 L13: 0.0587 L23: -0.2523
REMARK 3 S TENSOR
REMARK 3 S11: 0.0509 S12: 0.0963 S13: -0.1389
REMARK 3 S21: 0.0564 S22: -0.0834 S23: -0.0004
REMARK 3 S31: 0.0376 S32: 0.0448 S33: 0.0205
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 423 THROUGH 458 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6556 -10.4980 15.8817
REMARK 3 T TENSOR
REMARK 3 T11: 0.3604 T22: 0.1789
REMARK 3 T33: 0.2575 T12: 0.0457
REMARK 3 T13: 0.0458 T23: -0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 0.9869 L22: 0.8268
REMARK 3 L33: 0.4003 L12: 0.6087
REMARK 3 L13: 0.2170 L23: -0.2798
REMARK 3 S TENSOR
REMARK 3 S11: 0.0804 S12: 0.0501 S13: -0.2093
REMARK 3 S21: 0.0898 S22: -0.0486 S23: 0.0085
REMARK 3 S31: 0.1300 S32: 0.0744 S33: 0.0107
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 79 THROUGH 98 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2113 -34.1729 31.3530
REMARK 3 T TENSOR
REMARK 3 T11: 0.3929 T22: 0.2221
REMARK 3 T33: 0.2390 T12: -0.0309
REMARK 3 T13: 0.0279 T23: -0.0580
REMARK 3 L TENSOR
REMARK 3 L11: 2.7906 L22: 1.7139
REMARK 3 L33: 3.7334 L12: 0.1546
REMARK 3 L13: -1.4931 L23: -0.0390
REMARK 3 S TENSOR
REMARK 3 S11: 0.0846 S12: -0.4015 S13: 0.4040
REMARK 3 S21: 0.3293 S22: -0.0214 S23: 0.0629
REMARK 3 S31: -0.2389 S32: 0.1728 S33: -0.0608
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 99 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4142 -34.4435 30.7828
REMARK 3 T TENSOR
REMARK 3 T11: 0.3897 T22: 0.2367
REMARK 3 T33: 0.4139 T12: -0.0250
REMARK 3 T13: 0.1742 T23: -0.0980
REMARK 3 L TENSOR
REMARK 3 L11: 1.7526 L22: 1.2848
REMARK 3 L33: 0.5666 L12: -0.1178
REMARK 3 L13: 0.1931 L23: 0.0393
REMARK 3 S TENSOR
REMARK 3 S11: 0.0516 S12: -0.2124 S13: 0.1494
REMARK 3 S21: 0.3621 S22: -0.0973 S23: 0.5495
REMARK 3 S31: -0.0211 S32: -0.2311 S33: -0.0169
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 205 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.1654 -37.2047 19.5179
REMARK 3 T TENSOR
REMARK 3 T11: 0.2149 T22: 0.3743
REMARK 3 T33: 1.4105 T12: 0.0978
REMARK 3 T13: 0.2751 T23: -0.3983
REMARK 3 L TENSOR
REMARK 3 L11: 1.5903 L22: 0.9649
REMARK 3 L33: 0.9746 L12: -1.1960
REMARK 3 L13: -0.7752 L23: 0.8310
REMARK 3 S TENSOR
REMARK 3 S11: 0.2208 S12: -0.3059 S13: 0.3612
REMARK 3 S21: 0.1877 S22: -0.2870 S23: 0.8868
REMARK 3 S31: 0.1496 S32: -0.6517 S33: 0.7211
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 317 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7652 -34.9692 18.1204
REMARK 3 T TENSOR
REMARK 3 T11: 0.3002 T22: 0.2232
REMARK 3 T33: 0.5529 T12: 0.0173
REMARK 3 T13: 0.1447 T23: -0.1044
REMARK 3 L TENSOR
REMARK 3 L11: 0.9941 L22: 1.2427
REMARK 3 L33: 0.9902 L12: 0.3977
REMARK 3 L13: 0.2525 L23: 0.0694
REMARK 3 S TENSOR
REMARK 3 S11: -0.0628 S12: -0.0174 S13: 0.1458
REMARK 3 S21: 0.3412 S22: -0.1562 S23: 0.7850
REMARK 3 S31: -0.0217 S32: -0.2301 S33: 0.0277
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 318 THROUGH 458 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3224 -47.1196 19.6316
REMARK 3 T TENSOR
REMARK 3 T11: 0.3063 T22: 0.1836
REMARK 3 T33: 0.2637 T12: -0.0228
REMARK 3 T13: 0.1122 T23: -0.0541
REMARK 3 L TENSOR
REMARK 3 L11: 0.6357 L22: 1.3904
REMARK 3 L33: 0.9123 L12: 0.2218
REMARK 3 L13: 0.3009 L23: 0.4107
REMARK 3 S TENSOR
REMARK 3 S11: 0.0631 S12: -0.0523 S13: -0.0348
REMARK 3 S21: 0.3440 S22: -0.1847 S23: 0.4203
REMARK 3 S31: 0.1951 S32: -0.0843 S33: 0.0876
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 6RV9 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_1292102674.
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 : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.3
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116474
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 49.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.95000
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 (%): 54.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M PHOSPHATE-CITRATE PH 4.2, 0.2 M
REMARK 280 KCL, 20% W/V PEG8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 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 130.86600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 42.24050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.24050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 65.43300
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.24050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 42.24050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 196.29900
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 42.24050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.24050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.43300
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 42.24050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.24050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 196.29900
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 130.86600
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 838 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 73
REMARK 465 ALA A 74
REMARK 465 GLU A 75
REMARK 465 ALA A 76
REMARK 465 GLU A 77
REMARK 465 PHE A 78
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 73
REMARK 465 ALA B 74
REMARK 465 GLU B 75
REMARK 465 ALA B 76
REMARK 465 GLU B 77
REMARK 465 PHE B 78
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 99.26 -160.62
REMARK 500 ARG A 109 -34.19 -131.57
REMARK 500 SER A 162 -10.97 85.84
REMARK 500 GLN A 213 47.80 -152.78
REMARK 500 SER A 215 -173.04 -171.07
REMARK 500 ALA A 270 -129.63 64.49
REMARK 500 ASN A 325 -167.38 -160.54
REMARK 500 PRO A 343 33.51 -81.77
REMARK 500 SER A 370 65.89 64.34
REMARK 500 SER A 427 49.77 -82.52
REMARK 500 TRP A 449 -37.17 -133.51
REMARK 500 ASN B 92 97.07 -163.84
REMARK 500 GLN B 213 46.96 -148.15
REMARK 500 ALA B 270 -126.97 63.51
REMARK 500 PRO B 343 32.36 -82.25
REMARK 500 SER B 370 63.59 66.38
REMARK 500 CYS B 405 -0.65 74.32
REMARK 500 TRP B 449 -39.18 -136.88
REMARK 500
REMARK 500 REMARK: NULL
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 Mono-Saccharide NAG A 501 bound
REMARK 800 to ASN A 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
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: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues XYL B
REMARK 800 502 through GCV B 506
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
REMARK 900 RELATED ID: 6RV8 RELATED DB: PDB
DBREF1 6RV9 A 79 458 UNP GCE_CERUI
DBREF2 6RV9 A A0A0A7EQR3 95 474
DBREF1 6RV9 B 79 458 UNP GCE_CERUI
DBREF2 6RV9 B A0A0A7EQR3 95 474
SEQADV 6RV9 GLU A 73 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 ALA A 74 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 GLU A 75 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 ALA A 76 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 GLU A 77 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 PHE A 78 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 ALA A 270 UNP A0A0A7EQR SER 286 ENGINEERED MUTATION
SEQADV 6RV9 GLU A 459 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 ASN A 460 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 LEU A 461 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 TYR A 462 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 PHE A 463 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 GLN A 464 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 GLY A 465 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 VAL A 466 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 ASP A 467 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 HIS A 468 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 HIS A 469 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 HIS A 470 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 HIS A 471 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 HIS A 472 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 HIS A 473 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 GLU B 73 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 ALA B 74 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 GLU B 75 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 ALA B 76 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 GLU B 77 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 PHE B 78 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 ALA B 270 UNP A0A0A7EQR SER 286 ENGINEERED MUTATION
SEQADV 6RV9 GLU B 459 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 ASN B 460 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 LEU B 461 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 TYR B 462 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 PHE B 463 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 GLN B 464 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 GLY B 465 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 VAL B 466 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 ASP B 467 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 HIS B 468 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 HIS B 469 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 HIS B 470 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 HIS B 471 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 HIS B 472 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV9 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 NAG B 501 14
HET XYL B 502 21
HET XYP B 503 17
HET XYP B 504 16
HET XYP B 505 18
HET GCV B 506 23
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM XYL D-XYLITOL
HETNAM XYP BETA-D-XYLOPYRANOSE
HETNAM GCV 4-O-METHYL-ALPHA-D-GLUCURONIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 EDO C2 H6 O2
FORMUL 6 XYL C5 H12 O5
FORMUL 6 XYP 3(C5 H10 O5)
FORMUL 6 GCV C7 H12 O7
FORMUL 7 HOH *527(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 ALA 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 THR B 110 GLU B 129 1 20
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 ALA 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 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 156 N THR B 141
SHEET 3 AA3 3 GLN B 163 PHE B 167 -1 O ILE B 165 N ALA B 157
SHEET 1 AA410 VAL B 139 SER B 147 0
SHEET 2 AA410 THR B 150 SER B 160 -1 O THR B 156 N THR B 141
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 GLN B 292 N GLY B 268
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 2.09
SSBOND 4 CYS B 81 CYS B 116 1555 1555 2.04
SSBOND 5 CYS B 269 CYS B 405 1555 1555 2.06
SSBOND 6 CYS B 301 CYS B 377 1555 1555 2.11
LINK ND2 ASN A 104 C1 NAG A 501 1555 1555 1.42
LINK ND2 ASN B 104 C1 NAG B 501 1555 1555 1.45
LINK O4 XYL B 502 C1B XYP B 503 1555 1555 1.40
LINK O4B XYP B 503 C1B XYP B 504 1555 1555 1.37
LINK O2B XYP B 504 C1 GCV B 506 1555 1555 1.45
LINK O4B XYP B 504 C1B XYP B 505 1555 1555 1.38
CISPEP 1 ALA A 354 PRO A 355 0 8.42
CISPEP 2 ALA B 354 PRO B 355 0 4.09
SITE 1 AC1 4 LYS A 274 GLN A 316 GLU A 324 TRP A 368
SITE 1 AC2 9 CYS A 81 ALA A 83 PHE A 102 ASN A 104
SITE 2 AC2 9 THR A 106 HOH A 663 HOH A 713 HOH A 819
SITE 3 AC2 9 ASN B 92
SITE 1 AC3 8 ASN A 92 CYS B 81 PHE B 102 ASN B 104
SITE 2 AC3 8 THR B 106 HOH B 625 HOH B 630 HOH B 682
SITE 1 AC4 13 ALA B 270 ARG B 271 LYS B 274 GLN B 316
SITE 2 AC4 13 GLU B 320 GLU B 324 TRP B 368 LEU B 369
SITE 3 AC4 13 HIS B 404 HOH B 612 HOH B 639 HOH B 645
SITE 4 AC4 13 HOH B 749
CRYST1 84.481 84.481 261.732 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 0.011837 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011837 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003821 0.00000
TER 2873 THR A 458
TER 5740 THR B 458
MASTER 509 0 8 36 26 0 10 6 6331 2 147 62
END |