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HEADER STRUCTURAL PROTEIN 01-SEP-04 1XCD TITLE DIMERIC BOVINE TISSUE-EXTRACTED DECORIN, CRYSTAL FORM 1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: DECORIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: BONE PROTEOGLYCAN II, PG-S2 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 OTHER_DETAILS: EXTRACTED FROM CALF SKIN UNDER DENATURING SOURCE 5 CONDITIONS AND REFOLDED KEYWDS LEUCINE-RICH REPEAT, PROTEOGLYCAN 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 1XCD 1 JRNL REVDAT 1 02-NOV-04 1XCD 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. 2.31 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.31 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.14 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1988687.570 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 19940 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 SET) : 0.222 REMARK 3 FREE R VALUE : 0.257 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1897 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.31 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.45 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.50 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5898 REMARK 3 BIN R VALUE (WORKING SET) : 0.2820 REMARK 3 BIN FREE R VALUE : 0.3570 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 319 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2371 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 58 REMARK 3 SOLVENT ATOMS : 129 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 35.60 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 13.95000 REMARK 3 B22 (A**2) : -3.97000 REMARK 3 B33 (A**2) : -9.98000 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 COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26 REMARK 3 ESD FROM SIGMAA (A) : 0.19 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.30 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.80 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.91 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.440 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.440 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.230 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.390 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.31 REMARK 3 BSOL : 33.72 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : TMN.PARAM REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : TMN.TOP REMARK 3 TOPOLOGY FILE 3 : CARBOHYDRATE.TOP REMARK 3 TOPOLOGY FILE 4 : WATER.TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED REMARK 4 REMARK 4 1XCD 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 RCSB030198. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-NOV-2001 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) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : YALE MIRRORS REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC Q210 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20012 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.310 REMARK 200 RESOLUTION RANGE LOW (A) : 55.900 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04400 REMARK 200 FOR THE DATA SET : 11.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7 REMARK 200 DATA REDUNDANCY IN SHELL : 4.10 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.21200 REMARK 200 FOR SHELL : 3.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS 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 (%): 59.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, TRIS, BETA-OCTYL-D- REMARK 280 GLUCOSIDE, SODIUM AZIDE, PH 7.75, VAPOR DIFFUSION, HANGING REMARK 280 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 64.76000 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 64.76000 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 27.69000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.05500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 27.69000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.05500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.76000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 27.69000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 62.05500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.76000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 27.69000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 62.05500 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 64.76000 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 500 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 ND2 ASN A 85 O HOH 544 2.08 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 GLY A 22 N GLY A 22 CA 0.044 REMARK 500 ILE A 84 CG1 ILE A 84 CD1 0.039 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 ASP A 71 N - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 ASN A 85 CB - CA - C ANGL. DEV. = 9.3 DEGREES REMARK 500 GLN A 168 CB - CA - C ANGL. DEV. = 9.4 DEGREES REMARK 500 ILE A 178 N - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 LEU A 199 CA - CB - CG ANGL. DEV. = 8.8 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1XKU RELATED DB: PDB REMARK 900 DIMERIC RECOMBINANT BOVINE DECORIN REMARK 900 RELATED ID: 1XEC RELATED DB: PDB REMARK 900 DIMERIC BOVINE TISSUE-EXTRACTED DECORIN, CRYSTAL FORM 2 DBREF 1XCD A 1 329 UNP P21793 PGS2_BOVIN 31 359 SEQADV 1XCD VAL A 253 UNP P21793 ALA 283 SEE REMARK 999 SEQADV 1XCD LEU A 259 UNP P21793 VAL 289 SEE REMARK 999 SEQRES 1 A 329 ASP GLU ALA SER GLY ILE GLY PRO GLU GLU HIS PHE PRO SEQRES 2 A 329 GLU VAL PRO GLU ILE GLU PRO MET GLY PRO VAL CYS PRO SEQRES 3 A 329 PHE ARG CYS GLN CYS HIS LEU ARG VAL VAL GLN CYS SER SEQRES 4 A 329 ASP LEU GLY LEU GLU LYS VAL PRO LYS ASP LEU PRO PRO SEQRES 5 A 329 ASP THR ALA LEU LEU ASP LEU GLN ASN ASN LYS ILE THR SEQRES 6 A 329 GLU ILE LYS ASP GLY ASP PHE LYS ASN LEU LYS ASN LEU SEQRES 7 A 329 HIS THR LEU ILE LEU ILE ASN ASN LYS ILE SER LYS ILE SEQRES 8 A 329 SER PRO GLY ALA PHE ALA PRO LEU VAL LYS LEU GLU ARG SEQRES 9 A 329 LEU TYR LEU SER LYS ASN GLN LEU LYS GLU LEU PRO GLU SEQRES 10 A 329 LYS MET PRO LYS THR LEU GLN GLU LEU ARG VAL HIS GLU SEQRES 11 A 329 ASN GLU ILE THR LYS VAL ARG LYS SER VAL PHE ASN GLY SEQRES 12 A 329 LEU ASN GLN MET ILE VAL VAL GLU LEU GLY THR ASN PRO SEQRES 13 A 329 LEU LYS SER SER GLY ILE GLU ASN GLY ALA PHE GLN GLY SEQRES 14 A 329 MET LYS LYS LEU SER TYR ILE ARG ILE ALA ASP THR ASN SEQRES 15 A 329 ILE THR THR ILE PRO GLN GLY LEU PRO PRO SER LEU THR SEQRES 16 A 329 GLU LEU HIS LEU ASP GLY ASN LYS ILE THR LYS VAL ASP SEQRES 17 A 329 ALA ALA SER LEU LYS GLY LEU ASN ASN LEU ALA LYS LEU SEQRES 18 A 329 GLY LEU SER PHE ASN SER ILE SER ALA VAL ASP ASN GLY SEQRES 19 A 329 SER LEU ALA ASN THR PRO HIS LEU ARG GLU LEU HIS LEU SEQRES 20 A 329 ASN ASN ASN LYS LEU VAL LYS VAL PRO GLY GLY LEU ALA SEQRES 21 A 329 ASP HIS LYS TYR ILE GLN VAL VAL TYR LEU HIS ASN ASN SEQRES 22 A 329 ASN ILE SER ALA ILE GLY SER ASN ASP PHE CYS PRO PRO SEQRES 23 A 329 GLY TYR ASN THR LYS LYS ALA SER TYR SER GLY VAL SER SEQRES 24 A 329 LEU PHE SER ASN PRO VAL GLN TYR TRP GLU ILE GLN PRO SEQRES 25 A 329 SER THR PHE ARG CYS VAL TYR VAL ARG ALA ALA VAL GLN SEQRES 26 A 329 LEU GLY ASN TYR MODRES 1XCD ASN A 182 ASN GLYCOSYLATION SITE MODRES 1XCD ASN A 233 ASN GLYCOSYLATION SITE MODRES 1XCD ASN A 274 ASN GLYCOSYLATION SITE HET NAG 400 14 HET NAG 401 14 HET NAG 402 14 HET TRS 700 8 HET TRS 701 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 2(C4 H12 N O3 1+) FORMUL 7 HOH *129(H2 O) HELIX 1 1 ARG A 137 ASN A 142 5 6 HELIX 2 2 LYS A 158 ILE A 162 5 5 HELIX 3 3 SER A 235 THR A 239 5 5 HELIX 4 4 GLN A 306 ILE A 310 5 5 HELIX 5 5 GLN A 311 ARG A 316 5 6 SHEET 1 A14 GLN A 30 CYS A 31 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 GLU A 244 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 GLU A 66 ILE A 67 0 SHEET 2 B 2 LYS A 90 ILE A 91 1 O LYS A 90 N ILE A 67 SHEET 1 C 2 LYS A 206 VAL A 207 0 SHEET 2 C 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 400 LINK ND2 ASN A 233 C1 NAG 401 LINK ND2 ASN A 274 C1 NAG 402 CRYST1 55.380 124.110 129.520 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 0.018057 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008057 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007721 0.00000