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HEADER HYDROLASE 07-APR-98 2QWA TITLE THE X-RAY STRUCTURE OF A DRUG RESISTANT VARIANT R292K OF TITLE 2 TERN N9 INFLUENZA VIRUS NEURAMINIDASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURAMINIDASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 82 - 468; COMPND 5 SYNONYM: SIALIDASE; COMPND 6 EC: 3.2.1.18; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: INTEGRAL MEMBRANE PROTEIN, MEMBRANE BOUND COMPND 9 STALK CLEAVED BY PRONASE, RELEASING FULLY ACTIVE HEAD WITH COMPND 10 RESIDUES 82 - 468 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 STRAIN: A/TERN/AUSTRALIA/G70C/75; SOURCE 4 VARIANT: NEURAMINIDASE R292K MUTATION (N2-TOKYO/3/67 SOURCE 5 NUMBERING) KEYWDS NEURAMINIDASE, INFLUENZA PROTEIN, DRUG RESISTANT VARIANT, KEYWDS 2 GLYCOSYLATED PROTEIN, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR J.N.VARGHESE REVDAT 2 01-APR-03 2QWA 1 JRNL REVDAT 1 11-NOV-98 2QWA 0 JRNL AUTH J.N.VARGHESE,P.W.SMITH,S.L.SOLLIS,T.J.BLICK, JRNL AUTH 2 A.SAHASRABUDHE,J.L.MCKIMM-BRESCHKIN,P.M.COLMAN JRNL TITL DRUG DESIGN AGAINST A SHIFTING TARGET: A JRNL TITL 2 STRUCTURAL BASIS FOR RESISTANCE TO INHIBITORS IN A JRNL TITL 3 VARIANT OF INFLUENZA VIRUS NEURAMINIDASE. JRNL REF STRUCTURE V. 6 735 1998 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.L.MCKIMM-BRESCHKIN,A.SAHASRABUDHE,T.J.BLICK, REMARK 1 AUTH 2 M.MCDONALD,P.M.COLMAN,G.J.HART,R.C.BETHELL, REMARK 1 AUTH 3 J.N.VARGHESE REMARK 1 TITL MUTATIONS IN A CONSERVED RESIDUE IN THE INFLUENZA REMARK 1 TITL 2 VIRUS NEURAMINIDASE ACTIVE SITE DECREASES REMARK 1 TITL 3 SENSITIVITY TO NEU5AC2EN-DERIVED INHIBITORS REMARK 1 REF J.VIROL. V. 72 2456 1998 REMARK 1 REFN ASTM JOVIAM US ISSN 0022-538X REMARK 2 REMARK 2 RESOLUTION. 1.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.0 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.0 REMARK 3 NUMBER OF REFLECTIONS : 47115 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.171 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 15 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.76 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 46.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2459 REMARK 3 BIN R VALUE (WORKING SET) : 0.2450 REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3065 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 125 REMARK 3 SOLVENT ATOMS : 401 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.01 REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.013 REMARK 3 BOND ANGLES (DEGREES) : 1.82 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 2.500 ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.000 ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : 3.000 ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.500 ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : CHO.PAR REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : TOPCHO.PAR REMARK 3 TOPOLOGY FILE 3 : TOPHPEP REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 2 METAL IONS REMARK 4 REMARK 4 2QWA COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-JUL-1995 REMARK 200 TEMPERATURE (KELVIN) : 107.0 REMARK 200 PH : 5.90 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : MAC SCIENCE MULTI WAVELENGTH REMARK 200 SRA M18X REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : YALE MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : R-AXIS II REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS II REMARK 200 DATA SCALING SOFTWARE : PROTEIN V. 4 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51358 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700 REMARK 200 RESOLUTION RANGE LOW (A) : 100.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0 REMARK 200 DATA REDUNDANCY : 3.050 REMARK 200 R MERGE (I) : 0.07600 REMARK 200 R SYM (I) : 0.07400 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76 REMARK 200 COMPLETENESS FOR SHELL (%) : 46.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR 3.0 REMARK 200 STARTING MODEL: TERN N9 NEURAMINIDASE REMARK 200 REMARK 200 REMARK: THIS EXPERIMENT WAS CARRIED OUT TO DETERMINE THE REMARK 200 STRUCTURE OF DRUG RESISTANT VARIANT OF TERN N9 NEURAMINIDASE REMARK 200 GROWN IN PRESENCE OF THE ANTI-INFLUENZA CARBOXAMIDE DRUG 5-N- REMARK 200 ACETYL-4-GUANIDINO-6METHYL(PROPYL) CARBOXAMIDE-4,5-DIHYDRO- REMARK 200 2HPYRAN-2-CARBOXYLIC ACID. THE VARIANT HAS A SINGLE R292K REMARK 200 MUTATION WHICH WAS CONFIRMED BY THIS STRUCTURE. REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9M PHOSPHATE (PH 5.9) REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 Z,X,Y REMARK 290 6555 Z,-X,-Y REMARK 290 7555 -Z,-X,Y REMARK 290 8555 -Z,X,-Y REMARK 290 9555 Y,Z,X REMARK 290 10555 -Y,Z,-X REMARK 290 11555 Y,-Z,-X REMARK 290 12555 -Y,-Z,X REMARK 290 13555 Y,X,-Z REMARK 290 14555 -Y,-X,-Z REMARK 290 15555 Y,-X,Z REMARK 290 16555 -Y,X,Z REMARK 290 17555 X,Z,-Y REMARK 290 18555 -X,Z,Y REMARK 290 19555 -X,-Z,-Y REMARK 290 20555 X,-Z,Y REMARK 290 21555 Z,Y,-X REMARK 290 22555 Z,-Y,X REMARK 290 23555 -Z,Y,X REMARK 290 24555 -Z,-Y,-X REMARK 290 25555 1/2+X,1/2+Y,1/2+Z REMARK 290 26555 1/2-X,1/2-Y,1/2+Z REMARK 290 27555 1/2-X,1/2+Y,1/2-Z REMARK 290 28555 1/2+X,1/2-Y,1/2-Z REMARK 290 29555 1/2+Z,1/2+X,1/2+Y REMARK 290 30555 1/2+Z,1/2-X,1/2-Y REMARK 290 31555 1/2-Z,1/2-X,1/2+Y REMARK 290 32555 1/2-Z,1/2+X,1/2-Y REMARK 290 33555 1/2+Y,1/2+Z,1/2+X REMARK 290 34555 1/2-Y,1/2+Z,1/2-X REMARK 290 35555 1/2+Y,1/2-Z,1/2-X REMARK 290 36555 1/2-Y,1/2-Z,1/2+X REMARK 290 37555 1/2+Y,1/2+X,1/2-Z REMARK 290 38555 1/2-Y,1/2-X,1/2-Z REMARK 290 39555 1/2+Y,1/2-X,1/2+Z REMARK 290 40555 1/2-Y,1/2+X,1/2+Z REMARK 290 41555 1/2+X,1/2+Z,1/2-Y REMARK 290 42555 1/2-X,1/2+Z,1/2+Y REMARK 290 43555 1/2-X,1/2-Z,1/2-Y REMARK 290 44555 1/2+X,1/2-Z,1/2+Y REMARK 290 45555 1/2+Z,1/2+Y,1/2-X REMARK 290 46555 1/2+Z,1/2-Y,1/2+X REMARK 290 47555 1/2-Z,1/2+Y,1/2+X REMARK 290 48555 1/2-Z,1/2-Y,1/2-X 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 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 90.70000 REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 90.70000 REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 90.70000 REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 90.70000 REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 90.70000 REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 90.70000 REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 90.70000 REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 90.70000 REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 90.70000 REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 90.70000 REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 90.70000 REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 90.70000 REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 90.70000 REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 90.70000 REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 90.70000 REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 90.70000 REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 90.70000 REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 90.70000 REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 90.70000 REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 90.70000 REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 90.70000 REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 90.70000 REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 90.70000 REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 90.70000 REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY1 37 0.000000 1.000000 0.000000 90.70000 REMARK 290 SMTRY2 37 1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY3 37 0.000000 0.000000 -1.000000 90.70000 REMARK 290 SMTRY1 38 0.000000 -1.000000 0.000000 90.70000 REMARK 290 SMTRY2 38 -1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY3 38 0.000000 0.000000 -1.000000 90.70000 REMARK 290 SMTRY1 39 0.000000 1.000000 0.000000 90.70000 REMARK 290 SMTRY2 39 -1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY3 39 0.000000 0.000000 1.000000 90.70000 REMARK 290 SMTRY1 40 0.000000 -1.000000 0.000000 90.70000 REMARK 290 SMTRY2 40 1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY3 40 0.000000 0.000000 1.000000 90.70000 REMARK 290 SMTRY1 41 1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY2 41 0.000000 0.000000 1.000000 90.70000 REMARK 290 SMTRY3 41 0.000000 -1.000000 0.000000 90.70000 REMARK 290 SMTRY1 42 -1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY2 42 0.000000 0.000000 1.000000 90.70000 REMARK 290 SMTRY3 42 0.000000 1.000000 0.000000 90.70000 REMARK 290 SMTRY1 43 -1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY2 43 0.000000 0.000000 -1.000000 90.70000 REMARK 290 SMTRY3 43 0.000000 -1.000000 0.000000 90.70000 REMARK 290 SMTRY1 44 1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY2 44 0.000000 0.000000 -1.000000 90.70000 REMARK 290 SMTRY3 44 0.000000 1.000000 0.000000 90.70000 REMARK 290 SMTRY1 45 0.000000 0.000000 1.000000 90.70000 REMARK 290 SMTRY2 45 0.000000 1.000000 0.000000 90.70000 REMARK 290 SMTRY3 45 -1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY1 46 0.000000 0.000000 1.000000 90.70000 REMARK 290 SMTRY2 46 0.000000 -1.000000 0.000000 90.70000 REMARK 290 SMTRY3 46 1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY1 47 0.000000 0.000000 -1.000000 90.70000 REMARK 290 SMTRY2 47 0.000000 1.000000 0.000000 90.70000 REMARK 290 SMTRY3 47 1.000000 0.000000 0.000000 90.70000 REMARK 290 SMTRY1 48 0.000000 0.000000 -1.000000 90.70000 REMARK 290 SMTRY2 48 0.000000 -1.000000 0.000000 90.70000 REMARK 290 SMTRY3 48 -1.000000 0.000000 0.000000 90.70000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 3 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT2 4 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 4 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 CA CA 989 LIES ON A SPECIAL POSITION. REMARK 375 HOH 28Q LIES ON A SPECIAL POSITION. REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH 43R O HOH 47R 31555 0.23 REMARK 500 O HOH 67R O HOH 72R 48555 0.44 REMARK 500 O HOH 4Q O HOH 5Q 48555 0.55 REMARK 500 O HOH 22N O HOH 22N 48555 0.71 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ASN A 294 CG ASN A 294 OD1 0.100 REMARK 500 MET A 310 SD MET A 310 CE -0.083 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLN A 226 N - CA - C ANGL. DEV. = 12.6 DEGREES REMARK 500 ASN A 299 N - CA - C ANGL. DEV. =-12.0 DEGREES REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 801K DISTANCE = 5.27 ANGSTROMS REMARK 525 HOH 863K DISTANCE = 15.20 ANGSTROMS REMARK 525 HOH 119L DISTANCE = 6.14 ANGSTROMS DBREF 2QWA A 82 468 UNP P03472 NRAM_IATRA 83 470 SEQADV 2QWA LYS A 292 UNP P03472 ARG 294 ENGINEERED SEQRES 1 A 388 ARG ASP PHE ASN ASN LEU THR LYS GLY LEU CYS THR ILE SEQRES 2 A 388 ASN SER TRP HIS ILE TYR GLY LYS ASP ASN ALA VAL ARG SEQRES 3 A 388 ILE GLY GLU ASP SER ASP VAL LEU VAL THR ARG GLU PRO SEQRES 4 A 388 TYR VAL SER CYS ASP PRO ASP GLU CYS ARG PHE TYR ALA SEQRES 5 A 388 LEU SER GLN GLY THR THR ILE ARG GLY LYS HIS SER ASN SEQRES 6 A 388 GLY THR ILE HIS ASP ARG SER GLN TYR ARG ALA LEU ILE SEQRES 7 A 388 SER TRP PRO LEU SER SER PRO PRO THR VAL TYR ASN SER SEQRES 8 A 388 ARG VAL GLU CYS ILE GLY TRP SER SER THR SER CYS HIS SEQRES 9 A 388 ASP GLY LYS THR ARG MET SER ILE CYS ILE SER GLY PRO SEQRES 10 A 388 ASN ASN ASN ALA SER ALA VAL ILE TRP TYR ASN ARG ARG SEQRES 11 A 388 PRO VAL THR GLU ILE ASN THR TRP ALA ARG ASN ILE LEU SEQRES 12 A 388 ARG THR GLN GLU SER GLU CYS VAL CYS HIS ASN GLY VAL SEQRES 13 A 388 CYS PRO VAL VAL PHE THR ASP GLY SER ALA THR GLY PRO SEQRES 14 A 388 ALA GLU THR ARG ILE TYR TYR PHE LYS GLU GLY LYS ILE SEQRES 15 A 388 LEU LYS TRP GLU PRO LEU ALA GLY THR ALA LYS HIS ILE SEQRES 16 A 388 GLU GLU CYS SER CYS TYR GLY GLU ARG ALA GLU ILE THR SEQRES 17 A 388 CYS THR CYS LYS ASP ASN TRP GLN GLY SER ASN ARG PRO SEQRES 18 A 388 VAL ILE ARG ILE ASP PRO VAL ALA MET THR HIS THR SER SEQRES 19 A 388 GLN TYR ILE CYS SER PRO VAL LEU THR ASP ASN PRO ARG SEQRES 20 A 388 PRO ASN ASP PRO THR VAL GLY LYS CYS ASN ASP PRO TYR SEQRES 21 A 388 PRO GLY ASN ASN ASN ASN GLY VAL LYS GLY PHE SER TYR SEQRES 22 A 388 LEU ASP GLY VAL ASN THR TRP LEU GLY ARG THR ILE SER SEQRES 23 A 388 ILE ALA SER ARG SER GLY TYR GLU MET LEU LYS VAL PRO SEQRES 24 A 388 ASN ALA LEU THR ASP ASP LYS SER LYS PRO THR GLN GLY SEQRES 25 A 388 GLN THR ILE VAL LEU ASN THR ASP TRP SER GLY TYR SER SEQRES 26 A 388 GLY SER PHE MET ASP TYR TRP ALA GLU GLY GLU CYS TYR SEQRES 27 A 388 ARG ALA CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG PRO SEQRES 28 A 388 LYS GLU ASP LYS VAL TRP TRP THR SER ASN SER ILE VAL SEQRES 29 A 388 SER MET CYS SER SER THR GLU PHE LEU GLY GLN TRP ASP SEQRES 30 A 388 TRP PRO ASP GLY ALA LYS ILE GLU TYR PHE LEU MODRES ASN A 200 ASN GLYCOSYLATION SITE MODRES ASN A 86 ASN GLYCOSYLATION SITE MODRES ASN A 146 ASN GLYCOSYLATION SITE MODRES 2QWA ASN A 200 ASN GLYCOSYLATION SITE MODRES 2QWA ASN A 86 ASN GLYCOSYLATION SITE MODRES 2QWA ASN A 146 ASN GLYCOSYLATION SITE HET NAG 200A 14 HET NAG 200B 14 HET BMA 200C 11 HET MAN 200D 11 HET MAN 200E 11 HET MAN 200F 11 HET MAN 200G 11 HET NAG 86A 14 HET NAG 86B 14 HET NAG 146A 14 HET CA 999 1 HET CA 989 1 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM CA CALCIUM ION HETSYN NAG NAG FORMUL 2 NAG 5(C8 H15 N O6) FORMUL 2 BMA C6 H12 O6 FORMUL 2 MAN 4(C6 H12 O6) FORMUL 5 CA 2(CA 2+) FORMUL 7 HOH *399(H2 O) HELIX 1 1 ALA A 105 ASP A 111 1 7 HELIX 2 2 LYS A 143 SER A 145 5 3 HELIX 3 3 ILE A 464 TYR A 466 5 3 SHEET 1 A 4 TYR A 121 ASP A 125 0 SHEET 2 A 4 GLU A 128 SER A 135 -1 N TYR A 132 O TYR A 121 SHEET 3 A 4 ALA A 157 PRO A 162 -1 N TRP A 161 O PHE A 131 SHEET 4 A 4 ARG A 172 ILE A 176 -1 N CYS A 175 O LEU A 158 SHEET 1 B 4 SER A 179 HIS A 184 0 SHEET 2 B 4 ARG A 189 SER A 195 -1 N ILE A 194 O SER A 179 SHEET 3 B 4 SER A 202 TYR A 207 -1 N TRP A 206 O SER A 191 SHEET 4 B 4 ARG A 210 ASN A 216 -1 N ILE A 215 O ALA A 203 SHEET 1 C 4 VAL A 231 HIS A 233 0 SHEET 2 C 4 VAL A 236 ASP A 243 -1 N PRO A 238 O VAL A 231 SHEET 3 C 4 GLU A 251 LYS A 258 -1 N PHE A 257 O CYS A 237 SHEET 4 C 4 LYS A 261 PRO A 267 -1 N GLU A 266 O ILE A 254 SHEET 1 D 4 SER A 279 GLU A 283 0 SHEET 2 D 4 GLU A 286 THR A 290 -1 N THR A 290 O SER A 279 SHEET 3 D 4 PRO A 301 ASP A 306 -1 N ILE A 305 O ILE A 287 SHEET 4 D 4 THR A 311 TYR A 316 -1 N GLN A 315 O VAL A 302 SHEET 1 E 3 TRP A 361 ARG A 364 0 SHEET 2 E 3 TYR A 374 LYS A 378 -1 N LEU A 377 O LEU A 362 SHEET 3 E 3 GLN A 392 VAL A 398 -1 N VAL A 398 O TYR A 374 SHEET 1 F 4 SER A 407 MET A 411 0 SHEET 2 F 4 ALA A 420 GLY A 429 -1 N TYR A 423 O GLY A 408 SHEET 3 F 4 THR A 439 SER A 449 -1 N MET A 446 O PHE A 422 SHEET 4 F 4 SER A 96 LYS A 102 -1 N GLY A 101 O SER A 445 SSBOND 1 CYS A 92 CYS A 417 SSBOND 2 CYS A 124 CYS A 129 SSBOND 3 CYS A 175 CYS A 193 SSBOND 4 CYS A 183 CYS A 230 SSBOND 5 CYS A 232 CYS A 237 SSBOND 6 CYS A 278 CYS A 291 SSBOND 7 CYS A 280 CYS A 289 SSBOND 8 CYS A 318 CYS A 337 SSBOND 9 CYS A 421 CYS A 447 LINK ND2 ASN A 86 C1 NAG 86A LINK ND2 ASN A 146 C1 NAG 146A LINK ND2 ASN A 200 C1 NAG 200A LINK O4 NAG 200A C1 NAG 200B LINK O4 NAG 200B C1 BMA 200C LINK O3 BMA 200C C1 MAN 200D LINK O6 BMA 200C C1 MAN 200G LINK O2 MAN 200D C1 MAN 200E LINK O2 MAN 200E C1 MAN 200F LINK O4 NAG 86A C1 NAG 86B CISPEP 1 ASN A 325 PRO A 326 0 -9.04 CISPEP 2 ARG A 430 PRO A 431 0 4.09 CRYST1 181.400 181.400 181.400 90.00 90.00 90.00 I 4 3 2 48 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 0.005513 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005513 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005513 0.00000