HEADER STRUCTURAL PROTEIN 28-JUL-04 1U5M
TITLE STRUCTURE OF A CHORDIN-LIKE CYSTEINE-RICH REPEAT (VWC MODULE) FROM
TITLE 2 COLLAGEN IIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA 1 TYPE II COLLAGEN ISOFORM 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXON2;
COMPND 5 SYNONYM: COLLAGEN II, ALPHA-1 POLYPEPTIDE; CARTILAGE COLLAGEN;
COMPND 6 CHONDROCALCIN, INCLUDED; COL11A3, FORMERLY;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: COL2A1;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICK9K-CRCOLIIA
KEYWDS 5 DISULFIDE BONDS, TWO SUB-DOMAIN ARCHITECTURE, BETA-SHEET,
KEYWDS 2 STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.M.O'LEARY,J.M.HAMILTON,C.M.DEANE,N.V.VALEYEV,L.J.SANDELL,
AUTHOR 2 A.K.DOWNING
REVDAT 4 20-OCT-21 1U5M 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1U5M 1 VERSN
REVDAT 2 17-JAN-06 1U5M 1 JRNL
REVDAT 1 05-OCT-04 1U5M 0
JRNL AUTH J.M.O'LEARY,J.M.HAMILTON,C.M.DEANE,N.V.VALEYEV,L.J.SANDELL,
JRNL AUTH 2 A.K.DOWNING
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF A PROTOTYPICAL
JRNL TITL 2 CHORDIN-LIKE CYSTEINE-RICH REPEAT (VON WILLEBRAND FACTOR
JRNL TITL 3 TYPE C MODULE) FROM COLLAGEN IIA
JRNL REF J.BIOL.CHEM. V. 279 53857 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15466413
JRNL DOI 10.1074/JBC.M409225200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.M.O'LEARY,C.M.RADCLIFFE,A.C.WILLIS,R.A.DWEK,P.M.RUDD,
REMARK 1 AUTH 2 A.K.DOWNING
REMARK 1 TITL IDENTIFICATION AND REMOVAL OF O-LINKED AND NON-COVALENTLY
REMARK 1 TITL 2 LINKED SUGARS FROM RECOMBINANT PROTEIN PRODUCED USING PICHIA
REMARK 1 TITL 3 PASTORIS
REMARK 1 REF PROTEIN EXPR.PURIF. 2004
REMARK 1 REFN ESSN 1096-0279
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1.0.6, CYANA 1.0.6
REMARK 3 AUTHORS : GUNTERT, P. (CYANA), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U5M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000023274.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 50 MM POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM U-15N EXON2; 50MM
REMARK 210 PHOSPHATE BUFFER; 0.02% NAN3; 90%
REMARK 210 H2O, 10% D2O; 0.8MM U-15N EXON2;
REMARK 210 50MM PHOSPHATE BUFFER; 0.02%
REMARK 210 NAN3; 99.9% D2O; 0.8MM U-15N,13C
REMARK 210 EXON2; 50MM PHOSPHATE BUFFER;
REMARK 210 0.02% NAN3; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HMQC-J;
REMARK 210 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : OMEGA
REMARK 210 SPECTROMETER MANUFACTURER : GE
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SEMI-AUTOMATED ASSIGNMENT AND
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 600
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1,2
REMARK 210
REMARK 210 REMARK: SEQUENTIAL ASSIGNMENTS WERE MADE USING TRIPLE RESONANCE
REMARK 210 TECHNIQUES. DISULFIDE BOND CONNECTIVITY WAS DETERMINED USING
REMARK 210 NOESY DATA ACQUIRED AT DIFFERENT TEMPERATURES.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
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 1 GLU A 3 86.89 49.85
REMARK 500 1 ALA A 7 150.02 60.87
REMARK 500 1 ASP A 47 -161.64 177.92
REMARK 500 1 LYS A 49 -78.07 -114.08
REMARK 500 1 CYS A 51 -153.17 44.25
REMARK 500 1 LEU A 52 -71.14 -137.08
REMARK 500 1 PHE A 58 -95.82 56.26
REMARK 500 1 GLU A 60 -147.66 -128.58
REMARK 500 1 ASP A 68 -50.88 -174.86
REMARK 500 1 ALA A 70 74.96 60.52
REMARK 500 2 SER A 9 153.99 179.98
REMARK 500 2 ASN A 18 -170.43 -54.70
REMARK 500 2 CYS A 28 -36.95 -169.22
REMARK 500 2 ASP A 50 -33.28 166.77
REMARK 500 2 CYS A 51 166.23 64.51
REMARK 500 2 LEU A 52 -96.74 -49.46
REMARK 500 2 PHE A 58 44.59 36.31
REMARK 500 2 GLU A 60 -77.57 -137.55
REMARK 500 2 CYS A 61 -38.03 -178.28
REMARK 500 2 ALA A 67 -150.96 -68.34
REMARK 500 2 ALA A 70 173.91 56.59
REMARK 500 2 ALA A 72 -59.92 74.94
REMARK 500 3 VAL A 2 134.54 -173.32
REMARK 500 3 ASN A 18 -177.86 -59.80
REMARK 500 3 ILE A 43 98.95 -69.31
REMARK 500 3 GLU A 46 105.81 -56.47
REMARK 500 3 VAL A 48 140.80 65.00
REMARK 500 3 LYS A 49 46.45 -94.75
REMARK 500 3 ASP A 50 27.49 -145.49
REMARK 500 3 LEU A 52 -90.11 -69.81
REMARK 500 3 PHE A 58 43.80 36.85
REMARK 500 3 GLU A 60 -135.62 -136.22
REMARK 500 3 ALA A 67 53.19 -145.33
REMARK 500 3 ASP A 68 49.09 -161.87
REMARK 500 3 ALA A 71 -62.37 -163.52
REMARK 500 4 GLU A 3 -60.26 -145.12
REMARK 500 4 PHE A 4 90.52 50.24
REMARK 500 4 ASN A 18 175.58 -56.15
REMARK 500 4 ASP A 47 33.39 -168.45
REMARK 500 4 LYS A 49 -77.62 -111.12
REMARK 500 4 ASP A 50 55.45 -147.73
REMARK 500 4 CYS A 51 163.25 -48.37
REMARK 500 4 LEU A 52 -76.27 -50.26
REMARK 500 4 GLU A 60 -149.76 -141.35
REMARK 500 4 ALA A 67 75.94 -101.90
REMARK 500 4 ASP A 68 -49.25 -154.83
REMARK 500 5 PHE A 4 94.09 51.13
REMARK 500 5 SER A 9 157.24 62.72
REMARK 500 5 ASP A 47 89.09 -152.79
REMARK 500 5 VAL A 48 149.34 66.35
REMARK 500
REMARK 500 THIS ENTRY HAS 249 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FBR RELATED DB: PDB
REMARK 900 PAIR OF FIBRONECTIN TYPE I DOMAINS
DBREF 1U5M A 1 73 UNP P02458 CO2A1_HUMAN 25 97
SEQADV 1U5M TYR A 1 UNP P02458 GLY 25 CLONING ARTIFACT
SEQADV 1U5M VAL A 2 UNP P02458 GLN 26 CLONING ARTIFACT
SEQADV 1U5M GLU A 3 UNP P02458 ASP 27 CLONING ARTIFACT
SEQADV 1U5M PHE A 4 UNP P02458 VAL 28 CLONING ARTIFACT
SEQADV 1U5M ALA A 67 UNP P02458 THR 91 ENGINEERED MUTATION
SEQADV 1U5M ALA A 71 UNP P02458 THR 95 ENGINEERED MUTATION
SEQADV 1U5M ALA A 73 UNP P02458 SER 97 ENGINEERED MUTATION
SEQRES 1 A 73 TYR VAL GLU PHE GLN GLU ALA GLY SER CYS VAL GLN ASP
SEQRES 2 A 73 GLY GLN ARG TYR ASN ASP LYS ASP VAL TRP LYS PRO GLU
SEQRES 3 A 73 PRO CYS ARG ILE CYS VAL CYS ASP THR GLY THR VAL LEU
SEQRES 4 A 73 CYS ASP ASP ILE ILE CYS GLU ASP VAL LYS ASP CYS LEU
SEQRES 5 A 73 SER PRO GLU ILE PRO PHE GLY GLU CYS CYS PRO ILE CYS
SEQRES 6 A 73 PRO ALA ASP LEU ALA ALA ALA ALA
SHEET 1 A 2 CYS A 10 VAL A 11 0
SHEET 2 A 2 ARG A 16 TYR A 17 -1 O TYR A 17 N CYS A 10
SHEET 1 B 3 VAL A 22 TRP A 23 0
SHEET 2 B 3 ARG A 29 ASP A 34 -1 O CYS A 31 N TRP A 23
SHEET 3 B 3 THR A 37 ASP A 42 -1 O LEU A 39 N VAL A 32
SSBOND 1 CYS A 10 CYS A 33 1555 1555 2.00
SSBOND 2 CYS A 28 CYS A 61 1555 1555 1.99
SSBOND 3 CYS A 31 CYS A 40 1555 1555 2.00
SSBOND 4 CYS A 45 CYS A 62 1555 1555 2.05
SSBOND 5 CYS A 51 CYS A 65 1555 1555 2.15
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
