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HEADER STRUCTURAL PROTEIN 29-SEP-04 1XKU TITLE CRYSTAL STRUCTURE OF THE DIMERIC PROTEIN CORE OF DECORIN, TITLE 2 THE ARCHETYPAL SMALL LEUCINE-RICH REPEAT PROTEOGLYCAN COMPND MOL_ID: 1; COMPND 2 MOLECULE: DECORIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: BONE PROTEOGLYCAN II, PG-S2; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 GENE: DCN; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK 293A; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: ADENOVIRUS KEYWDS PROTEOGLYCAN, LEUCINE-RICH REPEAT EXPDTA X-RAY DIFFRACTION AUTHOR P.G.SCOTT,P.A.MCEWAN,C.M.DODD,E.M.BERGMANN,P.N.BISHOP, AUTHOR 2 J.BELLA REVDAT 2 09-NOV-04 1XKU 1 JRNL REVDAT 1 02-NOV-04 1XKU 0 JRNL AUTH P.G.SCOTT,P.A.MCEWAN,C.M.DODD,E.M.BERGMANN, JRNL AUTH 2 P.N.BISHOP,J.BELLA JRNL TITL CRYSTAL STRUCTURE OF THE DIMERIC PROTEIN CORE OF JRNL TITL 2 DECORIN, THE ARCHETYPAL SMALL LEUCINE-RICH REPEAT JRNL TITL 3 PROTEOGLYCAN JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 15633 2004 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH P.G.SCOTT,J.G.GROSSMANN,C.M.DODD,J.K.SHEEHAN, REMARK 1 AUTH 2 P.N.BISHOP REMARK 1 TITL LIGHT AND X-RAY SCATTERING SHOW DECORIN TO BE A REMARK 1 TITL 2 DIMER IN SOLUTION REMARK 1 REF J.BIOL.CHEM. V. 278 18353 2003 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. 2.15 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0003 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 3 NUMBER OF REFLECTIONS : 24591 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.191 REMARK 3 R VALUE (WORKING SET) : 0.190 REMARK 3 FREE R VALUE : 0.217 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1253 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.15 REMARK 3 BIN RESOLUTION RANGE LOW : 2.21 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1545 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.35 REMARK 3 BIN R VALUE (WORKING SET) : 0.2440 REMARK 3 BIN FREE R VALUE SET COUNT : 74 REMARK 3 BIN FREE R VALUE : 0.3370 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 2585 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 32.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.49 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.92000 REMARK 3 B22 (A**2) : 0.19000 REMARK 3 B33 (A**2) : -2.11000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.186 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.159 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.575 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2470 ; 0.021 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 1 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3352 ; 1.719 ; 1.991 REMARK 3 BOND ANGLES OTHERS (DEGREES): 2 ; 0.539 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 304 ; 5.519 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;43.917 ;25.600 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 442 ;15.199 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;14.684 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 393 ; 0.117 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1797 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1016 ; 0.214 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2 ; 0.287 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1624 ; 0.308 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 2 ; 0.239 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 150 ; 0.147 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 35 ; 0.250 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.132 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1587 ; 1.049 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1 ; 0.032 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2481 ; 1.632 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 990 ; 2.973 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 871 ; 4.702 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 22 A 200 REMARK 3 ORIGIN FOR THE GROUP (A): -11.9538 12.1333 36.2715 REMARK 3 T TENSOR REMARK 3 T11: -0.1527 T22: -0.0084 REMARK 3 T33: -0.0113 T12: -0.0007 REMARK 3 T13: 0.0069 T23: -0.0448 REMARK 3 L TENSOR REMARK 3 L11: 0.6519 L22: 1.1294 REMARK 3 L33: 4.3774 L12: 0.0091 REMARK 3 L13: -0.2295 L23: 0.0189 REMARK 3 S TENSOR REMARK 3 S11: -0.0643 S12: 0.0574 S13: 0.0165 REMARK 3 S21: 0.0220 S22: -0.0576 S23: 0.2674 REMARK 3 S31: 0.0796 S32: -0.7408 S33: 0.1219 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 201 A 326 REMARK 3 ORIGIN FOR THE GROUP (A): 2.0981 16.0869 68.3309 REMARK 3 T TENSOR REMARK 3 T11: 0.1729 T22: -0.0781 REMARK 3 T33: -0.0174 T12: -0.0325 REMARK 3 T13: -0.0327 T23: -0.0467 REMARK 3 L TENSOR REMARK 3 L11: 1.2581 L22: 3.4785 REMARK 3 L33: 3.9797 L12: 0.2958 REMARK 3 L13: 0.6580 L23: -1.0147 REMARK 3 S TENSOR REMARK 3 S11: -0.0568 S12: -0.1930 S13: 0.0746 REMARK 3 S21: 0.7388 S22: -0.1487 S23: -0.2582 REMARK 3 S31: -0.4300 S32: 0.0983 S33: 0.2056 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1XKU 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 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB030469. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-JAN-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.75 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RU-H3R REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : OSMIC REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24593 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150 REMARK 200 RESOLUTION RANGE LOW (A) : 33.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 200 DATA REDUNDANCY : 10.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04800 REMARK 200 FOR THE DATA SET : 8.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7 REMARK 200 DATA REDUNDANCY IN SHELL : 8.20 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.36700 REMARK 200 FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIR/AS REMARK 200 SOFTWARE USED: SHARP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, TRIS, OCTYL-BETA-D- REMARK 280 GLUCOPYRANOSIDE, SODIUM AZIDE, PH 7.75, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 -X,Y,1/2-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 1/2+X,1/2+Y,Z REMARK 290 6555 1/2-X,1/2-Y,1/2+Z REMARK 290 7555 1/2-X,1/2+Y,1/2-Z REMARK 290 8555 1/2+X,1/2-Y,-Z 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 64.80450 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 64.80450 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 1.000000 0.000000 0.000000 27.89000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.07250 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 27.89000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.07250 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.80450 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 27.89000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 62.07250 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.80450 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 27.89000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 62.07250 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 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 64.80450 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 803 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 ASP A 1 REMARK 465 GLU A 2 REMARK 465 ALA A 3 REMARK 465 SER A 4 REMARK 465 GLY A 5 REMARK 465 ILE A 6 REMARK 465 GLY A 7 REMARK 465 PRO A 8 REMARK 465 GLU A 9 REMARK 465 GLU A 10 REMARK 465 HIS A 11 REMARK 465 PHE A 12 REMARK 465 PRO A 13 REMARK 465 GLU A 14 REMARK 465 VAL A 15 REMARK 465 PRO A 16 REMARK 465 GLU A 17 REMARK 465 ILE A 18 REMARK 465 GLU A 19 REMARK 465 PRO A 20 REMARK 465 MET A 21 REMARK 465 GLY A 327 REMARK 465 ASN A 328 REMARK 465 TYR A 329 REMARK 465 LYS A 330 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 GLN A 60 CB GLN A 60 CG -0.130 REMARK 500 ILE A 148 CB ILE A 148 CG2 0.156 REMARK 500 GLU A 309 CD GLU A 309 OE1 0.162 REMARK 500 GLU A 309 CD GLU A 309 OE2 0.226 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1XCD RELATED DB: PDB REMARK 900 DIMERIC BOVINE TISSUE-EXTRACTED DECORIN, CRYSTAL FORM 1 REMARK 900 RELATED ID: 1XEC RELATED DB: PDB REMARK 900 DIMERIC BOVINE TISSUE-EXTRACTED DECORIN, CRYSTAL FORM 2 DBREF 1XKU A 1 330 UNP P21793 PGS2_BOVIN 31 360 SEQADV 1XKU VAL A 253 UNP P21793 ALA 283 SEE REMARK 999 SEQADV 1XKU LEU A 259 UNP P21793 VAL 289 SEE REMARK 999 SEQRES 1 A 330 ASP GLU ALA SER GLY ILE GLY PRO GLU GLU HIS PHE PRO SEQRES 2 A 330 GLU VAL PRO GLU ILE GLU PRO MET GLY PRO VAL CYS PRO SEQRES 3 A 330 PHE ARG CYS GLN CYS HIS LEU ARG VAL VAL GLN CYS SER SEQRES 4 A 330 ASP LEU GLY LEU GLU LYS VAL PRO LYS ASP LEU PRO PRO SEQRES 5 A 330 ASP THR ALA LEU LEU ASP LEU GLN ASN ASN LYS ILE THR SEQRES 6 A 330 GLU ILE LYS ASP GLY ASP PHE LYS ASN LEU LYS ASN LEU SEQRES 7 A 330 HIS THR LEU ILE LEU ILE ASN ASN LYS ILE SER LYS ILE SEQRES 8 A 330 SER PRO GLY ALA PHE ALA PRO LEU VAL LYS LEU GLU ARG SEQRES 9 A 330 LEU TYR LEU SER LYS ASN GLN LEU LYS GLU LEU PRO GLU SEQRES 10 A 330 LYS MET PRO LYS THR LEU GLN GLU LEU ARG VAL HIS GLU SEQRES 11 A 330 ASN GLU ILE THR LYS VAL ARG LYS SER VAL PHE ASN GLY SEQRES 12 A 330 LEU ASN GLN MET ILE VAL VAL GLU LEU GLY THR ASN PRO SEQRES 13 A 330 LEU LYS SER SER GLY ILE GLU ASN GLY ALA PHE GLN GLY SEQRES 14 A 330 MET LYS LYS LEU SER TYR ILE ARG ILE ALA ASP THR ASN SEQRES 15 A 330 ILE THR THR ILE PRO GLN GLY LEU PRO PRO SER LEU THR SEQRES 16 A 330 GLU LEU HIS LEU ASP GLY ASN LYS ILE THR LYS VAL ASP SEQRES 17 A 330 ALA ALA SER LEU LYS GLY LEU ASN ASN LEU ALA LYS LEU SEQRES 18 A 330 GLY LEU SER PHE ASN SER ILE SER ALA VAL ASP ASN GLY SEQRES 19 A 330 SER LEU ALA ASN THR PRO HIS LEU ARG GLU LEU HIS LEU SEQRES 20 A 330 ASN ASN ASN LYS LEU VAL LYS VAL PRO GLY GLY LEU ALA SEQRES 21 A 330 ASP HIS LYS TYR ILE GLN VAL VAL TYR LEU HIS ASN ASN SEQRES 22 A 330 ASN ILE SER ALA ILE GLY SER ASN ASP PHE CYS PRO PRO SEQRES 23 A 330 GLY TYR ASN THR LYS LYS ALA SER TYR SER GLY VAL SER SEQRES 24 A 330 LEU PHE SER ASN PRO VAL GLN TYR TRP GLU ILE GLN PRO SEQRES 25 A 330 SER THR PHE ARG CYS VAL TYR VAL ARG ALA ALA VAL GLN SEQRES 26 A 330 LEU GLY ASN TYR LYS MODRES 1XKU ASN A 182 ASN GLYCOSYLATION SITE MODRES 1XKU ASN A 233 ASN GLYCOSYLATION SITE MODRES 1XKU ASN A 274 ASN GLYCOSYLATION SITE HET NAG 800 14 HET NAG 801 14 HET NAG 802 14 HET TRS 968 8 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL HETSYN NAG NAG HETSYN TRS TRIS BUFFER FORMUL 2 NAG 3(C8 H15 N O6) FORMUL 5 TRS C4 H12 N O3 1+ FORMUL 6 HOH *164(H2 O) HELIX 1 1 ARG A 137 ASN A 142 1 6 HELIX 2 2 LYS A 158 ILE A 162 5 5 HELIX 3 3 GLY A 165 MET A 170 5 6 HELIX 4 4 ALA A 209 LYS A 213 5 5 HELIX 5 5 SER A 235 THR A 239 5 5 HELIX 6 6 GLN A 306 ILE A 310 5 5 HELIX 7 7 GLN A 311 ARG A 316 5 6 HELIX 8 8 VAL A 320 ALA A 322 5 3 SHEET 1 A14 GLN A 30 HIS A 32 0 SHEET 2 A14 VAL A 35 GLN A 37 -1 O GLN A 37 N GLN A 30 SHEET 3 A14 LEU A 56 ASP A 58 1 O ASP A 58 N VAL A 36 SHEET 4 A14 THR A 80 ILE A 82 1 O ILE A 82 N LEU A 57 SHEET 5 A14 ARG A 104 TYR A 106 1 O TYR A 106 N LEU A 81 SHEET 6 A14 GLU A 125 ARG A 127 1 O GLU A 125 N LEU A 105 SHEET 7 A14 VAL A 149 GLU A 151 1 O GLU A 151 N LEU A 126 SHEET 8 A14 TYR A 175 ARG A 177 1 O ARG A 177 N VAL A 150 SHEET 9 A14 GLU A 196 HIS A 198 1 O HIS A 198 N ILE A 176 SHEET 10 A14 LYS A 220 GLY A 222 1 O GLY A 222 N LEU A 197 SHEET 11 A14 GLU A 244 HIS A 246 1 O HIS A 246 N LEU A 221 SHEET 12 A14 VAL A 267 TYR A 269 1 O VAL A 267 N LEU A 245 SHEET 13 A14 GLY A 297 SER A 299 1 O GLY A 297 N VAL A 268 SHEET 14 A14 VAL A 324 GLN A 325 1 O GLN A 325 N VAL A 298 SHEET 1 B 2 LYS A 206 VAL A 207 0 SHEET 2 B 2 ALA A 230 VAL A 231 1 O ALA A 230 N VAL A 207 SSBOND 1 CYS A 25 CYS A 31 SSBOND 2 CYS A 29 CYS A 38 SSBOND 3 CYS A 284 CYS A 317 LINK ND2 ASN A 182 C1 NAG 800 LINK ND2 ASN A 233 C1 NAG 801 LINK ND2 ASN A 274 C1 NAG 802 CRYST1 55.780 124.145 129.609 90.00 90.00 90.00 C 2 2 21 8 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 0.017928 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008055 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007716 0.00000