HEADER STRUCTURAL PROTEIN 09-SEP-04 1XEC
TITLE DIMERIC BOVINE TISSUE-EXTRACTED DECORIN, CRYSTAL FORM 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DECORIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BONE PROTEOGLYCAN II; PG-S2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: SKIN;
SOURCE 6 OTHER_DETAILS: PROTEIN WAS EXTRACTED FROM CALF SKIN UNDER DENATURING
SOURCE 7 CONDITIONS AND REFOLDED
KEYWDS PROTEOGLYCAN; LEUCINE-RICH REPEAT, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.G.SCOTT,P.A.MCEWAN,C.M.DODD,E.M.BERGMANN,P.N.BISHOP,J.BELLA
REVDAT 6 23-AUG-23 1XEC 1 HETSYN
REVDAT 5 29-JUL-20 1XEC 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 13-JUL-11 1XEC 1 VERSN
REVDAT 3 24-FEB-09 1XEC 1 VERSN
REVDAT 2 09-NOV-04 1XEC 1 JRNL
REVDAT 1 02-NOV-04 1XEC 0
JRNL AUTH P.G.SCOTT,P.A.MCEWAN,C.M.DODD,E.M.BERGMANN,P.N.BISHOP,
JRNL AUTH 2 J.BELLA
JRNL TITL CRYSTAL STRUCTURE OF THE DIMERIC PROTEIN CORE OF DECORIN,
JRNL TITL 2 THE ARCHETYPAL SMALL LEUCINE-RICH REPEAT PROTEOGLYCAN
JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 15633 2004
JRNL REFN ISSN 0027-8424
JRNL PMID 15501918
JRNL DOI 10.1073/PNAS.0402976101
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.G.SCOTT,J.G.GROSSMANN,C.M.DODD,J.K.SHEEHAN,P.N.BISHOP
REMARK 1 TITL LIGHT AND X-RAY SCATTERING SHOW DECORIN TO BE A DIMER IN
REMARK 1 TITL 2 SOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 278 18353 2003
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1680211.910
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 36358
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) : 0.214
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3659
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4782
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 538
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4742
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 98
REMARK 3 SOLVENT ATOMS : 298
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 19.19000
REMARK 3 B22 (A**2) : -1.21000
REMARK 3 B33 (A**2) : -17.98000
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.33
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) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.43
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
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) : 1.500 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.510 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.590 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.970 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 29.51
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XEC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030266.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.75
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9780
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, TRUNCATE
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37599
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 19.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.19900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1XKU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
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: P 21 21 21
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
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 26.35050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.85600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.47600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.85600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.35050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.47600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 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 ASP B 1
REMARK 465 GLU B 2
REMARK 465 ALA B 3
REMARK 465 SER B 4
REMARK 465 GLY B 5
REMARK 465 ILE B 6
REMARK 465 GLY B 7
REMARK 465 PRO B 8
REMARK 465 GLU B 9
REMARK 465 GLU B 10
REMARK 465 HIS B 11
REMARK 465 PHE B 12
REMARK 465 PRO B 13
REMARK 465 GLU B 14
REMARK 465 VAL B 15
REMARK 465 PRO B 16
REMARK 465 GLU B 17
REMARK 465 ILE B 18
REMARK 465 GLU B 19
REMARK 465 PRO B 20
REMARK 465 MET B 21
REMARK 465 GLY B 327
REMARK 465 ASN B 328
REMARK 465 TYR B 329
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS B 29 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 28 -17.57 89.36
REMARK 500 ASN A 62 -162.80 -127.23
REMARK 500 LEU A 75 55.48 -110.24
REMARK 500 ASN A 86 -152.75 -124.09
REMARK 500 ASN A 110 -155.74 -137.65
REMARK 500 LYS A 118 70.51 50.47
REMARK 500 ASN A 131 -152.05 -128.38
REMARK 500 PRO A 156 41.20 -83.38
REMARK 500 THR A 181 -160.05 -122.02
REMARK 500 ASN A 202 -142.19 -105.01
REMARK 500 ASN A 226 -160.01 -123.80
REMARK 500 ASN A 250 -151.53 -133.05
REMARK 500 PRO A 286 -52.13 -20.33
REMARK 500 ARG B 28 -20.08 89.57
REMARK 500 ASP B 71 -36.12 -38.72
REMARK 500 LEU B 75 44.22 -107.66
REMARK 500 ASN B 86 -162.25 -126.09
REMARK 500 LYS B 109 60.17 63.16
REMARK 500 LYS B 121 -7.84 -59.33
REMARK 500 ASN B 131 -148.55 -126.45
REMARK 500 LEU B 157 133.70 -32.68
REMARK 500 PRO B 187 152.41 -47.43
REMARK 500 ASN B 202 -145.54 -105.32
REMARK 500 ASN B 226 -155.77 -130.07
REMARK 500 ASN B 250 -150.96 -127.78
REMARK 500 THR B 290 -9.12 -58.70
REMARK 500 VAL B 320 65.09 -107.11
REMARK 500 ARG B 321 -50.69 -15.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XKU RELATED DB: PDB
REMARK 900 DIMERIC RECOMBINANT BOVINE DECORIN
REMARK 900 RELATED ID: 1XCD RELATED DB: PDB
REMARK 900 DIMERIC TISSUE-EXTRACTED BOVINE DECORIN, CRYSTAL FORM 1
DBREF 1XEC A 1 329 UNP P21793 PGS2_BOVIN 31 359
DBREF 1XEC B 1 329 UNP P21793 PGS2_BOVIN 31 359
SEQADV 1XEC VAL A 253 UNP P21793 ALA 283 SEE REMARK 999
SEQADV 1XEC LEU A 259 UNP P21793 VAL 289 SEE REMARK 999
SEQADV 1XEC VAL B 253 UNP P21793 ALA 283 SEE REMARK 999
SEQADV 1XEC LEU B 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
SEQRES 1 B 329 ASP GLU ALA SER GLY ILE GLY PRO GLU GLU HIS PHE PRO
SEQRES 2 B 329 GLU VAL PRO GLU ILE GLU PRO MET GLY PRO VAL CYS PRO
SEQRES 3 B 329 PHE ARG CYS GLN CYS HIS LEU ARG VAL VAL GLN CYS SER
SEQRES 4 B 329 ASP LEU GLY LEU GLU LYS VAL PRO LYS ASP LEU PRO PRO
SEQRES 5 B 329 ASP THR ALA LEU LEU ASP LEU GLN ASN ASN LYS ILE THR
SEQRES 6 B 329 GLU ILE LYS ASP GLY ASP PHE LYS ASN LEU LYS ASN LEU
SEQRES 7 B 329 HIS THR LEU ILE LEU ILE ASN ASN LYS ILE SER LYS ILE
SEQRES 8 B 329 SER PRO GLY ALA PHE ALA PRO LEU VAL LYS LEU GLU ARG
SEQRES 9 B 329 LEU TYR LEU SER LYS ASN GLN LEU LYS GLU LEU PRO GLU
SEQRES 10 B 329 LYS MET PRO LYS THR LEU GLN GLU LEU ARG VAL HIS GLU
SEQRES 11 B 329 ASN GLU ILE THR LYS VAL ARG LYS SER VAL PHE ASN GLY
SEQRES 12 B 329 LEU ASN GLN MET ILE VAL VAL GLU LEU GLY THR ASN PRO
SEQRES 13 B 329 LEU LYS SER SER GLY ILE GLU ASN GLY ALA PHE GLN GLY
SEQRES 14 B 329 MET LYS LYS LEU SER TYR ILE ARG ILE ALA ASP THR ASN
SEQRES 15 B 329 ILE THR THR ILE PRO GLN GLY LEU PRO PRO SER LEU THR
SEQRES 16 B 329 GLU LEU HIS LEU ASP GLY ASN LYS ILE THR LYS VAL ASP
SEQRES 17 B 329 ALA ALA SER LEU LYS GLY LEU ASN ASN LEU ALA LYS LEU
SEQRES 18 B 329 GLY LEU SER PHE ASN SER ILE SER ALA VAL ASP ASN GLY
SEQRES 19 B 329 SER LEU ALA ASN THR PRO HIS LEU ARG GLU LEU HIS LEU
SEQRES 20 B 329 ASN ASN ASN LYS LEU VAL LYS VAL PRO GLY GLY LEU ALA
SEQRES 21 B 329 ASP HIS LYS TYR ILE GLN VAL VAL TYR LEU HIS ASN ASN
SEQRES 22 B 329 ASN ILE SER ALA ILE GLY SER ASN ASP PHE CYS PRO PRO
SEQRES 23 B 329 GLY TYR ASN THR LYS LYS ALA SER TYR SER GLY VAL SER
SEQRES 24 B 329 LEU PHE SER ASN PRO VAL GLN TYR TRP GLU ILE GLN PRO
SEQRES 25 B 329 SER THR PHE ARG CYS VAL TYR VAL ARG ALA ALA VAL GLN
SEQRES 26 B 329 LEU GLY ASN TYR
MODRES 1XEC ASN A 182 ASN GLYCOSYLATION SITE
MODRES 1XEC ASN A 233 ASN GLYCOSYLATION SITE
MODRES 1XEC ASN A 274 ASN GLYCOSYLATION SITE
MODRES 1XEC ASN B 182 ASN GLYCOSYLATION SITE
MODRES 1XEC ASN B 274 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET NAG A 401 14
HET NAG A 402 14
HET NAG B 403 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 3 NAG 7(C8 H15 N O6)
FORMUL 8 HOH *298(H2 O)
HELIX 1 1 ARG A 137 PHE A 141 5 5
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
HELIX 6 6 VAL A 320 ALA A 322 5 3
HELIX 7 7 ARG B 137 PHE B 141 5 5
HELIX 8 8 LYS B 158 ILE B 162 5 5
HELIX 9 9 ASP B 208 LYS B 213 1 6
HELIX 10 10 SER B 235 THR B 239 5 5
HELIX 11 11 GLN B 306 ILE B 310 5 5
HELIX 12 12 GLN B 311 ARG B 316 5 6
HELIX 13 13 VAL B 320 ALA B 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 ARG A 127 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 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
SHEET 1 D14 GLN B 30 HIS B 32 0
SHEET 2 D14 VAL B 35 GLN B 37 -1 O GLN B 37 N GLN B 30
SHEET 3 D14 LEU B 56 ASP B 58 1 O ASP B 58 N VAL B 36
SHEET 4 D14 THR B 80 ILE B 82 1 O ILE B 82 N LEU B 57
SHEET 5 D14 ARG B 104 TYR B 106 1 O TYR B 106 N LEU B 81
SHEET 6 D14 GLU B 125 ARG B 127 1 O GLU B 125 N LEU B 105
SHEET 7 D14 VAL B 149 GLU B 151 1 O GLU B 151 N LEU B 126
SHEET 8 D14 TYR B 175 ARG B 177 1 O ARG B 177 N VAL B 150
SHEET 9 D14 GLU B 196 HIS B 198 1 O HIS B 198 N ILE B 176
SHEET 10 D14 LYS B 220 GLY B 222 1 O GLY B 222 N LEU B 197
SHEET 11 D14 GLU B 244 HIS B 246 1 O GLU B 244 N LEU B 221
SHEET 12 D14 VAL B 267 TYR B 269 1 O VAL B 267 N LEU B 245
SHEET 13 D14 GLY B 297 SER B 299 1 O GLY B 297 N VAL B 268
SHEET 14 D14 VAL B 324 GLN B 325 1 O GLN B 325 N VAL B 298
SHEET 1 E 2 LYS B 206 VAL B 207 0
SHEET 2 E 2 ALA B 230 VAL B 231 1 O ALA B 230 N VAL B 207
SSBOND 1 CYS A 25 CYS A 31 1555 1555 2.05
SSBOND 2 CYS A 29 CYS A 38 1555 1555 2.05
SSBOND 3 CYS A 284 CYS A 317 1555 1555 2.04
SSBOND 4 CYS B 25 CYS B 31 1555 1555 2.05
SSBOND 5 CYS B 29 CYS B 38 1555 1555 2.06
SSBOND 6 CYS B 284 CYS B 317 1555 1555 2.04
LINK ND2 ASN A 182 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN A 233 C1 NAG A 401 1555 1555 1.45
LINK ND2 ASN A 274 C1 NAG A 402 1555 1555 1.46
LINK ND2 ASN B 182 C1 NAG B 403 1555 1555 1.45
LINK ND2 ASN B 274 C1 NAG D 1 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.39
CRYST1 52.701 120.952 129.712 90.00 90.00 90.00 P 21 21 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 0.018975 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008268 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007709 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
