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HEADER HYDROLASE 27-MAY-19 6RTV
TITLE CRYSTAL STRUCTURE OF GLUCURONOYL ESTERASE FROM CERRENA UNICOLOR
TITLE 2 INACTIVE S270A VARIANT
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_COMMON: CANKER ROT FUNGUS;
SOURCE 4 ORGANISM_TAXID: 90312;
SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: X-33;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPICZ-ALPHA
KEYWDS CE15, ESTERASE, ALPHA/BETA-HYDROLASE, 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 6RTV 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. 1.46 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) : 1.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 163459
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 8194
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 44.4126 - 4.5350 1.00 5645 303 0.1570 0.1701
REMARK 3 2 4.5350 - 3.6001 1.00 5381 277 0.1421 0.1437
REMARK 3 3 3.6001 - 3.1452 1.00 5295 266 0.1632 0.1800
REMARK 3 4 3.1452 - 2.8577 1.00 5255 298 0.1763 0.1903
REMARK 3 5 2.8577 - 2.6529 1.00 5229 266 0.1728 0.1909
REMARK 3 6 2.6529 - 2.4965 1.00 5246 262 0.1704 0.1818
REMARK 3 7 2.4965 - 2.3715 1.00 5202 280 0.1722 0.1897
REMARK 3 8 2.3715 - 2.2682 1.00 5175 276 0.1760 0.1830
REMARK 3 9 2.2682 - 2.1809 1.00 5207 268 0.1796 0.2071
REMARK 3 10 2.1809 - 2.1057 1.00 5153 265 0.1657 0.1821
REMARK 3 11 2.1057 - 2.0398 1.00 5177 268 0.1888 0.2080
REMARK 3 12 2.0398 - 1.9815 1.00 5146 283 0.1805 0.2226
REMARK 3 13 1.9815 - 1.9293 1.00 5130 277 0.1868 0.2052
REMARK 3 14 1.9293 - 1.8823 1.00 5127 283 0.1831 0.2129
REMARK 3 15 1.8823 - 1.8395 1.00 5164 247 0.1841 0.1937
REMARK 3 16 1.8395 - 1.8003 1.00 5146 261 0.1890 0.2081
REMARK 3 17 1.8003 - 1.7643 1.00 5138 269 0.1972 0.2054
REMARK 3 18 1.7643 - 1.7310 1.00 5134 260 0.1960 0.2236
REMARK 3 19 1.7310 - 1.7001 1.00 5141 278 0.2014 0.2113
REMARK 3 20 1.7001 - 1.6713 1.00 5105 286 0.2137 0.2511
REMARK 3 21 1.6713 - 1.6443 1.00 5098 276 0.2184 0.2651
REMARK 3 22 1.6443 - 1.6190 1.00 5150 251 0.2077 0.2363
REMARK 3 23 1.6190 - 1.5952 1.00 5073 276 0.2107 0.2223
REMARK 3 24 1.5952 - 1.5727 1.00 5144 261 0.2207 0.2342
REMARK 3 25 1.5727 - 1.5515 1.00 5113 276 0.2277 0.2486
REMARK 3 26 1.5515 - 1.5313 1.00 5085 262 0.2387 0.2635
REMARK 3 27 1.5313 - 1.5122 1.00 5116 276 0.2505 0.2790
REMARK 3 28 1.5122 - 1.4940 1.00 5088 275 0.2615 0.2849
REMARK 3 29 1.4940 - 1.4766 1.00 5079 288 0.2719 0.3003
REMARK 3 30 1.4766 - 1.4600 1.00 5123 280 0.2887 0.2922
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.790
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.52
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.23
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 73 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.5103 47.9833 31.2723
REMARK 3 T TENSOR
REMARK 3 T11: 0.1052 T22: 0.0881
REMARK 3 T33: 0.0822 T12: -0.0068
REMARK 3 T13: -0.0192 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 2.1446 L22: 1.9418
REMARK 3 L33: 2.1578 L12: 0.3345
REMARK 3 L13: -0.0257 L23: -0.6157
REMARK 3 S TENSOR
REMARK 3 S11: 0.0242 S12: -0.2381 S13: 0.0449
REMARK 3 S21: 0.2125 S22: -0.0127 S23: 0.0376
REMARK 3 S31: -0.0617 S32: -0.0737 S33: -0.0415
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.3937 48.5009 15.4202
REMARK 3 T TENSOR
REMARK 3 T11: 0.1131 T22: 0.0757
REMARK 3 T33: 0.0972 T12: 0.0052
REMARK 3 T13: -0.0042 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.3367 L22: 0.3925
REMARK 3 L33: 0.2945 L12: -0.1024
REMARK 3 L13: -0.0492 L23: 0.0248
REMARK 3 S TENSOR
REMARK 3 S11: -0.0016 S12: 0.0141 S13: -0.0148
REMARK 3 S21: 0.0072 S22: -0.0020 S23: 0.0684
REMARK 3 S31: -0.0049 S32: -0.0192 S33: 0.0045
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 318 THROUGH 422 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.5236 40.6632 13.0068
REMARK 3 T TENSOR
REMARK 3 T11: 0.1021 T22: 0.0833
REMARK 3 T33: 0.0930 T12: 0.0123
REMARK 3 T13: -0.0064 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.3212 L22: 0.5525
REMARK 3 L33: 0.4872 L12: 0.0966
REMARK 3 L13: -0.0263 L23: -0.1864
REMARK 3 S TENSOR
REMARK 3 S11: 0.0165 S12: 0.0178 S13: -0.0267
REMARK 3 S21: -0.0171 S22: -0.0347 S23: 0.0057
REMARK 3 S31: 0.0137 S32: 0.0115 S33: 0.0200
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 423 THROUGH 458 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.8628 31.9426 15.7426
REMARK 3 T TENSOR
REMARK 3 T11: 0.1241 T22: 0.0858
REMARK 3 T33: 0.1117 T12: 0.0225
REMARK 3 T13: -0.0032 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.7151 L22: 0.5870
REMARK 3 L33: 0.5110 L12: 0.3948
REMARK 3 L13: -0.0609 L23: -0.0168
REMARK 3 S TENSOR
REMARK 3 S11: 0.0151 S12: -0.0112 S13: -0.1143
REMARK 3 S21: 0.0123 S22: -0.0175 S23: -0.0323
REMARK 3 S31: 0.0230 S32: 0.0689 S33: 0.0151
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 73 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.1591 7.5557 36.0393
REMARK 3 T TENSOR
REMARK 3 T11: 0.1184 T22: 0.0991
REMARK 3 T33: 0.1290 T12: 0.0003
REMARK 3 T13: -0.0301 T23: -0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 2.5847 L22: 1.7404
REMARK 3 L33: 3.6083 L12: 0.2419
REMARK 3 L13: -0.8158 L23: 0.0574
REMARK 3 S TENSOR
REMARK 3 S11: 0.0610 S12: -0.2439 S13: 0.2313
REMARK 3 S21: 0.2055 S22: -0.0226 S23: 0.0212
REMARK 3 S31: -0.2143 S32: -0.0849 S33: -0.0398
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4640 10.2799 27.9169
REMARK 3 T TENSOR
REMARK 3 T11: 0.0884 T22: 0.0703
REMARK 3 T33: 0.1053 T12: 0.0032
REMARK 3 T13: 0.0160 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 1.2706 L22: 0.5556
REMARK 3 L33: 0.6194 L12: -0.4196
REMARK 3 L13: 0.3056 L23: -0.0351
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: -0.0484 S13: -0.0193
REMARK 3 S21: 0.0627 S22: -0.0069 S23: 0.0805
REMARK 3 S31: -0.0222 S32: -0.0726 S33: 0.0130
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9294 17.0291 19.2578
REMARK 3 T TENSOR
REMARK 3 T11: 0.0856 T22: 0.1139
REMARK 3 T33: 0.1252 T12: 0.0254
REMARK 3 T13: 0.0096 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 1.0896 L22: 7.1958
REMARK 3 L33: 3.9062 L12: 0.3609
REMARK 3 L13: 0.3965 L23: 3.9945
REMARK 3 S TENSOR
REMARK 3 S11: -0.0030 S12: -0.0072 S13: 0.0410
REMARK 3 S21: -0.3147 S22: 0.0853 S23: 0.0040
REMARK 3 S31: -0.2545 S32: -0.0958 S33: -0.0478
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 173 THROUGH 205 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0833 -1.9609 18.6389
REMARK 3 T TENSOR
REMARK 3 T11: 0.0966 T22: 0.1147
REMARK 3 T33: 0.1561 T12: -0.0248
REMARK 3 T13: 0.0043 T23: -0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 1.2970 L22: 0.8872
REMARK 3 L33: 2.4116 L12: -0.2930
REMARK 3 L13: -0.6243 L23: -0.0459
REMARK 3 S TENSOR
REMARK 3 S11: -0.0599 S12: 0.0351 S13: -0.1305
REMARK 3 S21: 0.0277 S22: -0.0510 S23: 0.2383
REMARK 3 S31: 0.2038 S32: -0.2733 S33: 0.0578
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 370 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.1226 6.6785 17.0615
REMARK 3 T TENSOR
REMARK 3 T11: 0.0962 T22: 0.0802
REMARK 3 T33: 0.0892 T12: 0.0028
REMARK 3 T13: -0.0019 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.5235 L22: 0.5420
REMARK 3 L33: 0.3815 L12: 0.0084
REMARK 3 L13: -0.0785 L23: -0.0173
REMARK 3 S TENSOR
REMARK 3 S11: 0.0065 S12: 0.0466 S13: 0.0377
REMARK 3 S21: -0.0084 S22: -0.0123 S23: 0.0354
REMARK 3 S31: -0.0225 S32: -0.0229 S33: 0.0061
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 371 THROUGH 458 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0833 -10.2075 21.0011
REMARK 3 T TENSOR
REMARK 3 T11: 0.1097 T22: 0.0573
REMARK 3 T33: 0.1065 T12: 0.0019
REMARK 3 T13: 0.0005 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 1.0166 L22: 0.5836
REMARK 3 L33: 0.9517 L12: 0.1419
REMARK 3 L13: -0.1898 L23: 0.1056
REMARK 3 S TENSOR
REMARK 3 S11: 0.0028 S12: 0.0018 S13: -0.0845
REMARK 3 S21: 0.0196 S22: -0.0197 S23: 0.0471
REMARK 3 S31: 0.0906 S32: -0.0108 S33: 0.0197
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 6RTV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1292102586.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-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 : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.3
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 163708
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460
REMARK 200 RESOLUTION RANGE LOW (A) : 49.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : 0.15800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.80
REMARK 200 R MERGE FOR SHELL (I) : 0.86400
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: 3PIC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.14
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 130.56350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 42.13650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.13650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 65.28175
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.13650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 42.13650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 195.84525
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 42.13650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.13650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.28175
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 42.13650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.13650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 195.84525
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 130.56350
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 898 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 97.81 -162.24
REMARK 500 ARG A 109 -34.00 -131.78
REMARK 500 GLU A 129 -18.51 -141.17
REMARK 500 SER A 162 -12.66 89.40
REMARK 500 GLN A 213 44.77 -150.82
REMARK 500 SER A 215 -170.37 -175.33
REMARK 500 ALA A 270 -129.89 62.99
REMARK 500 ASN A 325 -166.86 -161.32
REMARK 500 PRO A 343 35.32 -80.29
REMARK 500 SER A 370 66.14 63.85
REMARK 500 TRP A 449 -31.74 -134.88
REMARK 500 ASN B 92 96.06 -161.73
REMARK 500 GLN B 213 46.89 -144.53
REMARK 500 SER B 215 -173.49 -171.52
REMARK 500 ALA B 270 -131.17 62.53
REMARK 500 ASN B 325 -166.83 -160.06
REMARK 500 PRO B 343 35.03 -82.05
REMARK 500 SER B 370 65.79 66.92
REMARK 500 TRP B 449 -31.30 -137.02
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 507 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 259 O
REMARK 620 2 GOL B 505 O2 102.1
REMARK 620 3 GOL B 505 O3 169.9 68.8
REMARK 620 4 HOH B 812 O 97.2 160.8 92.0
REMARK 620 5 HOH B 800 O 91.4 93.4 93.4 87.2
REMARK 620 6 HOH B 798 O 85.5 91.2 90.4 89.3 174.9
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 EDO B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
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: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 501 bound
REMARK 800 to ASN B 104
DBREF1 6RTV A 79 458 UNP GCE_CERUI
DBREF2 6RTV A A0A0A7EQR3 95 474
DBREF1 6RTV B 79 458 UNP GCE_CERUI
DBREF2 6RTV B A0A0A7EQR3 95 474
SEQADV 6RTV GLU A 73 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV ALA A 74 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV GLU A 75 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV ALA A 76 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV GLU A 77 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV PHE A 78 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV ALA A 270 UNP A0A0A7EQR SER 286 ENGINEERED MUTATION
SEQADV 6RTV GLU A 459 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV ASN A 460 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV LEU A 461 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV TYR A 462 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV PHE A 463 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV GLN A 464 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV GLY A 465 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV VAL A 466 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV ASP A 467 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV HIS A 468 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV HIS A 469 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV HIS A 470 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV HIS A 471 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV HIS A 472 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV HIS A 473 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV GLU B 73 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV ALA B 74 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV GLU B 75 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV ALA B 76 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV GLU B 77 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV PHE B 78 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV ALA B 270 UNP A0A0A7EQR SER 286 ENGINEERED MUTATION
SEQADV 6RTV GLU B 459 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV ASN B 460 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV LEU B 461 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV TYR B 462 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV PHE B 463 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV GLN B 464 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV GLY B 465 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV VAL B 466 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV ASP B 467 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV HIS B 468 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV HIS B 469 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV HIS B 470 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV HIS B 471 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV HIS B 472 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RTV 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 EDO B 502 10
HET GOL B 503 14
HET GOL B 504 14
HET GOL B 505 14
HET GOL B 506 14
HET NA B 507 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
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 2(C2 H6 O2)
FORMUL 5 GOL 7(C3 H8 O3)
FORMUL 14 NA NA 1+
FORMUL 15 HOH *757(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 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 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 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 2.04
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 2.04
SSBOND 5 CYS B 269 CYS B 405 1555 1555 2.05
SSBOND 6 CYS B 301 CYS B 377 1555 1555 2.10
LINK ND2 ASN A 104 C1 NAG A 501 1555 1555 1.44
LINK ND2 ASN B 104 C1 NAG B 501 1555 1555 1.44
LINK O ILE B 259 NA NA B 507 1555 1555 2.30
LINK O2 GOL B 505 NA NA B 507 1555 1555 2.48
LINK O3 GOL B 505 NA NA B 507 1555 1555 2.46
LINK NA NA B 507 O HOH B 812 1555 1555 2.41
LINK NA NA B 507 O HOH B 800 1555 1555 2.48
LINK NA NA B 507 O HOH B 798 1555 1555 2.52
CISPEP 1 ALA A 354 PRO A 355 0 8.41
CISPEP 2 ALA B 354 PRO B 355 0 7.14
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 749 HOH A 765 HOH A 775
SITE 1 AC3 7 TYR A 91 THR A 101 PHE A 102 ALA A 103
SITE 2 AC3 7 ARG A 117 PRO A 343 HOH A 892
SITE 1 AC4 8 LYS A 136 PRO A 138 VAL A 139 VAL A 140
SITE 2 AC4 8 MET A 253 HOH A 766 HOH A 881 MET B 253
SITE 1 AC5 4 LYS B 274 GLN B 316 GLU B 324 TRP B 368
SITE 1 AC6 8 PHE B 282 GLU B 283 GLU B 284 ARG B 285
SITE 2 AC6 8 HOH B 679 HOH B 753 HOH B 763 HOH B 815
SITE 1 AC7 6 TYR B 91 THR B 101 PHE B 102 ALA B 103
SITE 2 AC7 6 ARG B 117 PRO B 343
SITE 1 AC8 9 GLU A 252 GLU B 252 PRO B 255 THR B 261
SITE 2 AC8 9 NA B 507 HOH B 622 HOH B 767 HOH B 781
SITE 3 AC8 9 HOH B 846
SITE 1 AC9 6 PRO B 413 GLN B 414 THR B 429 THR B 430
SITE 2 AC9 6 ASN B 431 HOH B 683
SITE 1 AD1 5 ILE B 259 GOL B 505 HOH B 798 HOH B 800
SITE 2 AD1 5 HOH B 812
SITE 1 AD2 14 GLU A 73 GLU A 75 CYS A 81 ALA A 83
SITE 2 AD2 14 ILE A 84 PHE A 102 ASN A 104 THR A 106
SITE 3 AD2 14 HOH A 611 HOH A 626 HOH A 763 HOH A 782
SITE 4 AD2 14 HOH A 800 ASN B 92
SITE 1 AD3 14 ASN A 92 GLU B 73 GLU B 75 CYS B 81
SITE 2 AD3 14 ILE B 84 PHE B 102 ASN B 104 THR B 106
SITE 3 AD3 14 HOH B 629 HOH B 634 HOH B 759 HOH B 772
SITE 4 AD3 14 HOH B 773 HOH B 803
CRYST1 84.273 84.273 261.127 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 0.011866 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011866 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003830 0.00000
TER 2976 THR A 458
TER 5938 THR B 458
MASTER 536 0 12 38 26 0 27 6 6654 2 166 62
END |