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HEADER HYDROLASE 31-MAY-19 6RV7
TITLE CRYSTAL STRUCTURE OF GLUCURONOYL ESTERASE FROM CERRENA UNICOLOR
TITLE 2 INACTIVE S270A VARIANT IN 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;
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 6RV7 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. 1.73 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) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 99779
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 4947
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 49.3466 - 5.3733 0.99 3462 180 0.1540 0.1676
REMARK 3 2 5.3733 - 4.2657 0.99 3275 178 0.1247 0.1428
REMARK 3 3 4.2657 - 3.7267 0.99 3243 162 0.1305 0.1632
REMARK 3 4 3.7267 - 3.3861 1.00 3217 162 0.1481 0.1777
REMARK 3 5 3.3861 - 3.1434 1.00 3212 161 0.1658 0.1928
REMARK 3 6 3.1434 - 2.9581 1.00 3181 195 0.1760 0.2090
REMARK 3 7 2.9581 - 2.8100 1.00 3181 159 0.1767 0.1936
REMARK 3 8 2.8100 - 2.6877 1.00 3186 163 0.1709 0.2134
REMARK 3 9 2.6877 - 2.5842 1.00 3166 163 0.1671 0.1904
REMARK 3 10 2.5842 - 2.4950 1.00 3133 161 0.1614 0.1954
REMARK 3 11 2.4950 - 2.4170 1.00 3196 166 0.1673 0.1920
REMARK 3 12 2.4170 - 2.3479 1.00 3131 166 0.1651 0.1998
REMARK 3 13 2.3479 - 2.2861 1.00 3148 173 0.1656 0.1953
REMARK 3 14 2.2861 - 2.2303 1.00 3133 151 0.1758 0.2093
REMARK 3 15 2.2303 - 2.1796 1.00 3139 171 0.1667 0.1766
REMARK 3 16 2.1796 - 2.1333 1.00 3167 154 0.1669 0.1950
REMARK 3 17 2.1333 - 2.0906 1.00 3150 158 0.1655 0.1894
REMARK 3 18 2.0906 - 2.0511 1.00 3134 170 0.1796 0.2495
REMARK 3 19 2.0511 - 2.0145 1.00 3093 178 0.1789 0.2093
REMARK 3 20 2.0145 - 1.9803 1.00 3151 156 0.1792 0.2288
REMARK 3 21 1.9803 - 1.9484 1.00 3124 178 0.1851 0.2202
REMARK 3 22 1.9484 - 1.9184 1.00 3075 180 0.1954 0.2434
REMARK 3 23 1.9184 - 1.8902 1.00 3145 154 0.2076 0.2408
REMARK 3 24 1.8902 - 1.8636 1.00 3116 170 0.2079 0.2332
REMARK 3 25 1.8636 - 1.8384 1.00 3132 134 0.2123 0.2435
REMARK 3 26 1.8384 - 1.8145 1.00 3115 173 0.2165 0.2497
REMARK 3 27 1.8145 - 1.7918 1.00 3128 157 0.2264 0.2536
REMARK 3 28 1.7918 - 1.7703 1.00 3083 161 0.2335 0.2573
REMARK 3 29 1.7703 - 1.7497 1.00 3161 160 0.2435 0.2508
REMARK 3 30 1.7497 - 1.7300 1.00 3055 153 0.2545 0.2728
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) : 18.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.68
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 : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 80 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0270 4.2449 29.2613
REMARK 3 T TENSOR
REMARK 3 T11: 0.2472 T22: 0.1254
REMARK 3 T33: 0.1257 T12: -0.0266
REMARK 3 T13: -0.0196 T23: -0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 2.7479 L22: 3.0008
REMARK 3 L33: 2.7602 L12: -0.1504
REMARK 3 L13: 0.1500 L23: -1.0066
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: -0.2546 S13: 0.0108
REMARK 3 S21: 0.1991 S22: -0.0200 S23: 0.0268
REMARK 3 S31: -0.0596 S32: -0.0527 S33: -0.0166
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0801 5.3613 15.7469
REMARK 3 T TENSOR
REMARK 3 T11: 0.2009 T22: 0.0978
REMARK 3 T33: 0.1632 T12: -0.0048
REMARK 3 T13: 0.0386 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.4018 L22: 0.8789
REMARK 3 L33: 0.3849 L12: -0.1406
REMARK 3 L13: -0.0088 L23: 0.0479
REMARK 3 S TENSOR
REMARK 3 S11: -0.0052 S12: 0.0010 S13: -0.0525
REMARK 3 S21: 0.1398 S22: -0.0151 S23: 0.2255
REMARK 3 S31: -0.0039 S32: -0.0583 S33: 0.0159
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 318 THROUGH 422 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1014 -2.1837 12.7199
REMARK 3 T TENSOR
REMARK 3 T11: 0.2038 T22: 0.1129
REMARK 3 T33: 0.1620 T12: 0.0032
REMARK 3 T13: 0.0150 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.4848 L22: 0.4968
REMARK 3 L33: 0.6953 L12: 0.0940
REMARK 3 L13: 0.0187 L23: -0.2397
REMARK 3 S TENSOR
REMARK 3 S11: 0.0045 S12: 0.0584 S13: -0.0910
REMARK 3 S21: 0.0420 S22: -0.0341 S23: -0.0067
REMARK 3 S31: 0.0505 S32: 0.0322 S33: 0.0307
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 423 THROUGH 458 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5253 -10.9970 15.6093
REMARK 3 T TENSOR
REMARK 3 T11: 0.2328 T22: 0.1022
REMARK 3 T33: 0.1889 T12: 0.0342
REMARK 3 T13: 0.0125 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 1.0192 L22: 0.9443
REMARK 3 L33: 0.6252 L12: 0.5457
REMARK 3 L13: -0.1438 L23: -0.3629
REMARK 3 S TENSOR
REMARK 3 S11: -0.0166 S12: -0.0062 S13: -0.1565
REMARK 3 S21: 0.0651 S22: -0.0187 S23: -0.0205
REMARK 3 S31: 0.0887 S32: 0.0774 S33: 0.0557
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 80 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8345 -35.0570 31.3994
REMARK 3 T TENSOR
REMARK 3 T11: 0.2576 T22: 0.1637
REMARK 3 T33: 0.1883 T12: 0.0111
REMARK 3 T13: 0.0300 T23: -0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 2.4503 L22: 1.0229
REMARK 3 L33: 0.7904 L12: -0.6576
REMARK 3 L13: 0.6918 L23: -0.3743
REMARK 3 S TENSOR
REMARK 3 S11: -0.0590 S12: -0.2226 S13: 0.1346
REMARK 3 S21: 0.1719 S22: 0.0351 S23: 0.0804
REMARK 3 S31: -0.1410 S32: -0.1927 S33: 0.0325
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 205 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0547 -38.1101 21.2048
REMARK 3 T TENSOR
REMARK 3 T11: 0.1785 T22: 0.2894
REMARK 3 T33: 0.3477 T12: 0.0083
REMARK 3 T13: -0.0005 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 1.4074 L22: 1.6066
REMARK 3 L33: 3.7309 L12: -1.3652
REMARK 3 L13: -0.8756 L23: 1.0150
REMARK 3 S TENSOR
REMARK 3 S11: -0.0303 S12: -0.0035 S13: 0.1154
REMARK 3 S21: -0.0325 S22: 0.0496 S23: 0.2226
REMARK 3 S31: 0.0043 S32: -0.4194 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 317 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5822 -35.8289 18.8400
REMARK 3 T TENSOR
REMARK 3 T11: 0.1955 T22: 0.1533
REMARK 3 T33: 0.2161 T12: 0.0100
REMARK 3 T13: 0.0154 T23: -0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 1.7812 L22: 0.8923
REMARK 3 L33: 0.8852 L12: -0.2535
REMARK 3 L13: -0.2966 L23: -0.0296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0697 S12: -0.0038 S13: 0.0696
REMARK 3 S21: 0.0938 S22: 0.0301 S23: 0.2328
REMARK 3 S31: -0.0909 S32: -0.1768 S33: 0.0341
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 318 THROUGH 458 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2600 -47.7426 19.9899
REMARK 3 T TENSOR
REMARK 3 T11: 0.1674 T22: 0.1081
REMARK 3 T33: 0.1531 T12: -0.0032
REMARK 3 T13: 0.0294 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.7386 L22: 1.0765
REMARK 3 L33: 0.9191 L12: 0.0046
REMARK 3 L13: 0.0965 L23: 0.1243
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: -0.0161 S13: -0.0144
REMARK 3 S21: 0.1243 S22: -0.0147 S23: 0.1564
REMARK 3 S31: 0.0492 S32: -0.0749 S33: 0.0221
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 6RV7 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_1292102671.
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 : 99913
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730
REMARK 200 RESOLUTION RANGE LOW (A) : 49.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.11900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 1.27600
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 (%): 54.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M PHOSPHATE-CITRATE PH 4.2, 0.1 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 130.19000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 42.39050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.39050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 65.09500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.39050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 42.39050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 195.28500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 42.39050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.39050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.09500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 42.39050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.39050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 195.28500
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 130.19000
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 835 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 GLY A 79
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 GLY B 79
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 98.57 -162.71
REMARK 500 ARG A 109 -34.30 -131.02
REMARK 500 SER A 162 -9.93 88.08
REMARK 500 GLN A 213 46.75 -151.64
REMARK 500 SER A 215 -173.60 -173.44
REMARK 500 ALA A 270 -129.07 62.47
REMARK 500 ASN A 325 -167.09 -163.21
REMARK 500 PRO A 343 35.48 -84.39
REMARK 500 SER A 370 62.62 64.03
REMARK 500 SER A 427 49.38 -84.19
REMARK 500 PHE A 433 89.46 -154.55
REMARK 500 TRP A 449 -38.16 -133.65
REMARK 500 ASN B 92 97.38 -160.25
REMARK 500 GLN B 213 48.24 -150.49
REMARK 500 ALA B 270 -123.34 61.60
REMARK 500 ASN B 325 -167.20 -162.05
REMARK 500 PRO B 343 31.30 -81.05
REMARK 500 SER B 370 67.37 64.74
REMARK 500 TRP B 449 -38.57 -133.13
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 residue BXP A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
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: AC4
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: AC5
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
DBREF1 6RV7 A 79 458 UNP GCE_CERUI
DBREF2 6RV7 A A0A0A7EQR3 95 474
DBREF1 6RV7 B 79 458 UNP GCE_CERUI
DBREF2 6RV7 B A0A0A7EQR3 95 474
SEQADV 6RV7 GLU A 73 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 ALA A 74 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 GLU A 75 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 ALA A 76 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 GLU A 77 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 PHE A 78 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 ALA A 270 UNP A0A0A7EQR SER 286 ENGINEERED MUTATION
SEQADV 6RV7 GLU A 459 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 ASN A 460 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 LEU A 461 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 TYR A 462 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 PHE A 463 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 GLN A 464 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 GLY A 465 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 VAL A 466 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 ASP A 467 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 HIS A 468 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 HIS A 469 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 HIS A 470 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 HIS A 471 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 HIS A 472 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 HIS A 473 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 GLU B 73 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 ALA B 74 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 GLU B 75 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 ALA B 76 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 GLU B 77 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 PHE B 78 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 ALA B 270 UNP A0A0A7EQR SER 286 ENGINEERED MUTATION
SEQADV 6RV7 GLU B 459 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 ASN B 460 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 LEU B 461 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 TYR B 462 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 PHE B 463 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 GLN B 464 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 GLY B 465 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 VAL B 466 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 ASP B 467 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 HIS B 468 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 HIS B 469 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 HIS B 470 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 HIS B 471 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 HIS B 472 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RV7 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 BXP A 503 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 23
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM EDO 1,2-ETHANEDIOL
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 BXP C10 H18 O9
FORMUL 7 XYL C5 H12 O5
FORMUL 7 XYP 2(C5 H10 O5)
FORMUL 7 GCV C7 H12 O7
FORMUL 8 HOH *518(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 THR A 254 1 20
HELIX 6 AA6 PRO A 255 ALA A 257 5 3
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 LEU A 185
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 LEU B 185
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 2.10
SSBOND 4 CYS B 81 CYS B 116 1555 1555 2.05
SSBOND 5 CYS B 269 CYS B 405 1555 1555 2.07
SSBOND 6 CYS B 301 CYS B 377 1555 1555 2.10
LINK ND2 ASN A 104 C1 NAG A 501 1555 1555 1.45
LINK ND2 ASN B 104 C1 NAG B 501 1555 1555 1.47
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 505 1555 1555 1.41
CISPEP 1 ALA A 354 PRO A 355 0 6.55
CISPEP 2 ALA B 354 PRO B 355 0 7.68
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 8 CYS A 81 ALA A 83 PHE A 102 ASN A 104
SITE 2 AC3 8 THR A 106 HOH A 603 HOH A 613 ASN B 92
SITE 1 AC4 9 ASN A 92 CYS B 81 ALA B 83 PHE B 102
SITE 2 AC4 9 ASN B 104 THR B 106 HOH B 634 HOH B 643
SITE 3 AC4 9 HOH B 741
SITE 1 AC5 13 ALA B 270 ARG B 271 LYS B 274 GLN B 316
SITE 2 AC5 13 GLU B 320 GLU B 324 TRP B 368 LEU B 369
SITE 3 AC5 13 HIS B 404 HOH B 660 HOH B 675 HOH B 697
SITE 4 AC5 13 HOH B 742
CRYST1 84.781 84.781 260.380 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 0.011795 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011795 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003841 0.00000
TER 2895 THR A 458
TER 5782 THR B 458
MASTER 484 0 8 36 26 0 11 6 6324 2 167 62
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