HEADER CELL ADHESION 16-JUN-03 1POZ
TITLE SOLUTION STRUCTURE OF THE HYALURONAN BINDING DOMAIN OF HUMAN CD44
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CD44 ANTIGEN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HYALURONAN BINDING DOMAIN;
COMPND 5 SYNONYM: PHAGOCYTIC GLYCOPROTEIN I, PGP-1, HUTCH-I, EXTRACELLULAR
COMPND 6 MATRIX RECEPTOR-III, ECMR-III, GP90 LYMPHOCYTE HOMING/ADHESION
COMPND 7 RECEPTOR, HERMES ANTIGEN, HYALURONATE RECEPTOR, HEPARAN SULFATE
COMPND 8 PROTEOGLYCAN, EPICAN, CDW44;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CD44;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET19B
KEYWDS HYALURONAN-BINDING DOMAIN, CARBOHYDRATE-BINDING DOMAIN, LINK MODULE,
KEYWDS 2 CELL ADHESION, GLYCOPROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.TERIETE,S.BANERJI,C.D.BLUNDELL,J.D.KAHMANN,A.R.PICKFORD,A.J.WRIGHT,
AUTHOR 2 I.D.CAMPBELL,D.G.JACKSON,A.J.DAY
REVDAT 3 27-OCT-21 1POZ 1 REMARK ATOM
REVDAT 2 24-FEB-09 1POZ 1 VERSN
REVDAT 1 16-MAR-04 1POZ 0
JRNL AUTH P.TERIETE,S.BANERJI,M.NOBLE,C.D.BLUNDELL,A.J.WRIGHT,
JRNL AUTH 2 A.R.PICKFORD,E.LOWE,D.J.MAHONEY,M.I.TAMMI,J.D.KAHMANN,
JRNL AUTH 3 I.D.CAMPBELL,A.J.DAY,D.G.JACKSON
JRNL TITL STRUCTURE OF THE REGULATORY HYALURONAN BINDING DOMAIN IN THE
JRNL TITL 2 INFLAMMATORY LEUKOCYTE HOMING RECEPTOR CD44.
JRNL REF MOL.CELL V. 13 483 2004
JRNL REFN ISSN 1097-2765
JRNL PMID 14992719
JRNL DOI 10.1016/S1097-2765(04)00080-2
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.STAMENKOVIC,M.AMIOT,J.M.PESANDO,B.SEED
REMARK 1 TITL A LYMPHOCYTE MOLECULE IMPLICATED IN LYMPH NODE HOMING IS A
REMARK 1 TITL 2 MEMBER OF THE CARTILAGE LINK PROTEIN FAMILY.
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 56 1057 1989
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/0092-8674(89)90638-7
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.A GOLDSTIEN,D.F.H.ZHOU,L.J.PICKER,C.N.MINTY,R.F.BARGATZE,
REMARK 1 AUTH 2 J.F.DIN,E.C.BUTCHER
REMARK 1 TITL A HUMAN LYMPHOCYTE HOMING RECEPTOR, THE HERMES ANTIGEN, IS
REMARK 1 TITL 2 RELATED TO CARTILAGE PROTEOGLYCAN CORE AND LINK PROTEINS.
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 56 1063 1989
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/0092-8674(89)90639-9
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.ARUFFO,I.STAMENKOVIC,M.MELNICK,C.B.UNDERHILL,B.SEED
REMARK 1 TITL CD44 IS THE PRINCIPAL CELL SURFACE RECEPTOR FOR HYALURONATE.
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 61 1303 1990
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/0092-8674(90)90694-A
REMARK 1 REFERENCE 4
REMARK 1 AUTH R.J.PEACH,D.HOLLENBAUGH,I.STAMENKOVIC,A.ARUFFO
REMARK 1 TITL IDENTIFICATION OF HYALURONIC ACID BINDING SITES IN THE
REMARK 1 TITL 2 EXTRACELLULAR DOMAIN OF CD44.
REMARK 1 REF J.CELL BIOL. V. 122 257 1993
REMARK 1 REFN ISSN 0021-9525
REMARK 1 DOI 10.1083/JCB.122.1.257
REMARK 1 REFERENCE 5
REMARK 1 AUTH D.KOHDA,C.J.MORTON,A.A.PARKAR,H.HATANAKA,F.M.INAGAKI,
REMARK 1 AUTH 2 I.D.CAMPBELL,A.J.DAY
REMARK 1 TITL SOLUTION STRUCTURE OF THE LINK MODULE: A HYALURONAN-BINDING
REMARK 1 TITL 2 DOMAIN INVOLVED IN EXTRACELLULAR MATRIX STABILITY AND CELL
REMARK 1 TITL 3 MIGRATION
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 86 767 1996
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/S0092-8674(00)80151-8
REMARK 1 REFERENCE 6
REMARK 1 AUTH J.BAJORATH,B.GREENFIELD,S.B.MUNRO,A.J.DAY,A.ARUFFO
REMARK 1 TITL IDENTIFICATION OF CD44 RESIDUES IMPORTANT FOR HYALURONAN
REMARK 1 TITL 2 BINDING AND DELINEATION OF THE BINDING SITE
REMARK 1 REF J.BIOL.CHEM. V. 273 338 1998
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.273.1.338
REMARK 1 REFERENCE 7
REMARK 1 AUTH N.M.ENGLISH,J.F.LESLEY,R.HYMAN
REMARK 1 TITL SITE-SPECIFIC DE-N-GLYCOSYLATION OF CD44 CAN ACTIVATE
REMARK 1 TITL 2 HYALURONAN BINDING, AND CD44 ACTIVATION STATES SHOW DISTINCT
REMARK 1 TITL 3 THRESHOLD DENSITIES FOR HYALURONAN BINDING
REMARK 1 REF CANCER RES. V. 58 3736 1998
REMARK 1 REFN ISSN 0008-5472
REMARK 1 REFERENCE 8
REMARK 1 AUTH S.BANERJI,A.J.DAY,J.D.KAHMANN,D.G.JACKSON
REMARK 1 TITL CHARACTERIZATION OF A FUNCTIONAL HYALURONAN-BINDING DOMAIN
REMARK 1 TITL 2 FROM THE HUMAN CD44 MOLECULE EXPRESSED IN ESCHERICHIA COLI
REMARK 1 REF PROTEIN EXPR.PURIF. V. 14 371 1998
REMARK 1 REFN ISSN 1046-5928
REMARK 1 DOI 10.1006/PREP.1998.0971
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, SOPHIE 1.0
REMARK 3 AUTHORS : BRUNGER, A.T. (CNS), PICKFORD, A.R. (SOPHIE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE CALCULATED FROM 2271
REMARK 3 RESTRAINTS, 2168 ARE NOE BASED, 47 DIHEDRAL CONSTRAINTS AND 56
REMARK 3 DISTANCE RESTRAINTS FROM HYDROGEN BONDS
REMARK 4
REMARK 4 1POZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019467.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : <5MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM [U-13C; U-15N] PROTEIN, 95%
REMARK 210 H2O/5% D2O; 1 MM [U-15N] PROTEIN,
REMARK 210 95% H2O/5% D2O; 1 MM [U-15N]
REMARK 210 PROTEIN, 100% D2O; 1 MM PROTEIN,
REMARK 210 95% H2O/5% D2O; 1 MM PROTEIN,
REMARK 210 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D
REMARK 210 NOESY; 2D TOCSY; HMQC-J; CBCA(CO)
REMARK 210 NH; NH-EXCHANGE HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : OMEGA
REMARK 210 SPECTROMETER MANUFACTURER : GE
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2.3, SOPHIE 1.0, SPARKY
REMARK 210 2.0, XEASY 3.13
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS SIMULATED
REMARK 210 ANNEALING REFINEMENT BY
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY,TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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 HE2 HIS A 35 HB3 ASP A 115 1.28
REMARK 500 HA3 GLY A 80 HE1 TYR A 117 1.33
REMARK 500 HD1 HIS A 35 HG23 THR A 76 1.34
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 ASN A 25 105.81 -160.07
REMARK 500 1 CYS A 28 167.85 154.75
REMARK 500 1 ALA A 31 28.05 48.80
REMARK 500 1 ASN A 39 35.19 29.01
REMARK 500 1 ARG A 41 87.39 28.95
REMARK 500 1 TYR A 42 -6.41 80.66
REMARK 500 1 ALA A 49 -71.20 -48.64
REMARK 500 1 PHE A 56 56.93 -107.18
REMARK 500 1 ASN A 57 83.15 34.40
REMARK 500 1 LEU A 60 147.48 -36.74
REMARK 500 1 PRO A 61 83.58 -59.63
REMARK 500 1 CYS A 77 15.63 56.24
REMARK 500 1 GLU A 83 -33.74 -39.50
REMARK 500 1 HIS A 85 144.02 -174.66
REMARK 500 1 ARG A 90 58.87 -171.03
REMARK 500 1 ILE A 96 -34.58 -163.63
REMARK 500 1 CYS A 97 -75.35 -70.52
REMARK 500 1 ALA A 98 -81.11 -66.58
REMARK 500 1 ALA A 99 -76.96 -158.77
REMARK 500 1 ASN A 100 -61.56 -135.05
REMARK 500 1 VAL A 104 49.53 36.28
REMARK 500 1 THR A 108 55.14 -159.87
REMARK 500 1 SER A 109 -155.74 -142.23
REMARK 500 1 SER A 112 -102.00 -172.77
REMARK 500 1 GLN A 113 -169.29 -164.81
REMARK 500 1 TYR A 114 -161.51 -163.38
REMARK 500 1 CYS A 118 121.88 -170.80
REMARK 500 1 SER A 122 -76.89 -45.76
REMARK 500 1 PRO A 124 -175.30 -67.69
REMARK 500 1 PRO A 125 76.76 -58.62
REMARK 500 1 SER A 131 89.30 -55.02
REMARK 500 1 VAL A 132 -88.28 -44.01
REMARK 500 1 THR A 133 8.31 48.01
REMARK 500 1 ASP A 134 -79.34 -88.09
REMARK 500 1 PRO A 136 2.34 -57.45
REMARK 500 1 ALA A 138 -154.46 -109.37
REMARK 500 1 ARG A 150 -76.39 28.05
REMARK 500 1 ASP A 151 16.53 -156.91
REMARK 500 1 TYR A 161 -30.33 -173.43
REMARK 500 1 ILE A 168 -74.23 -102.54
REMARK 500 1 SER A 171 -77.61 -94.83
REMARK 500 1 ASP A 175 98.35 -164.54
REMARK 500 2 ASN A 25 102.15 -160.02
REMARK 500 2 CYS A 28 175.85 127.49
REMARK 500 2 ARG A 29 79.15 -109.05
REMARK 500 2 ALA A 31 -13.52 71.55
REMARK 500 2 ASN A 39 95.87 -46.86
REMARK 500 2 ARG A 41 -154.81 -68.38
REMARK 500 2 TYR A 42 -5.16 159.85
REMARK 500 2 SER A 45 -165.33 -115.00
REMARK 500
REMARK 500 THIS ENTRY HAS 831 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1O7B RELATED DB: PDB
REMARK 900 LINK MODULE OF THE HUMAN TSG-6
REMARK 900 RELATED ID: 1O7C RELATED DB: PDB
REMARK 900 CONFORMATION OF THE BOUND LINK MODULE OF THE HUMAN TSG-6 TO A
REMARK 900 HYALURONIC ACID OCTAMER.
DBREF 1POZ A 20 178 UNP Q16208 CD44_HUMAN 20 178
SEQRES 1 A 159 ALA GLN ILE ASP LEU ASN ILE THR CYS ARG PHE ALA GLY
SEQRES 2 A 159 VAL PHE HIS VAL GLU LYS ASN GLY ARG TYR SER ILE SER
SEQRES 3 A 159 ARG THR GLU ALA ALA ASP LEU CYS LYS ALA PHE ASN SER
SEQRES 4 A 159 THR LEU PRO THR MET ALA GLN MET GLU LYS ALA LEU SER
SEQRES 5 A 159 ILE GLY PHE GLU THR CYS ARG TYR GLY PHE ILE GLU GLY
SEQRES 6 A 159 HIS VAL VAL ILE PRO ARG ILE HIS PRO ASN SER ILE CYS
SEQRES 7 A 159 ALA ALA ASN ASN THR GLY VAL TYR ILE LEU THR SER ASN
SEQRES 8 A 159 THR SER GLN TYR ASP THR TYR CYS PHE ASN ALA SER ALA
SEQRES 9 A 159 PRO PRO GLU GLU ASP CYS THR SER VAL THR ASP LEU PRO
SEQRES 10 A 159 ASN ALA PHE ASP GLY PRO ILE THR ILE THR ILE VAL ASN
SEQRES 11 A 159 ARG ASP GLY THR ARG TYR VAL GLN LYS GLY GLU TYR ARG
SEQRES 12 A 159 THR ASN PRO GLU ASP ILE TYR PRO SER ASN PRO THR ASP
SEQRES 13 A 159 ASP ASP VAL
HELIX 1 1 SER A 45 PHE A 56 1 12
HELIX 2 2 THR A 62 ILE A 72 1 11
HELIX 3 3 ASN A 164 ILE A 168 5 5
SHEET 1 A 3 GLN A 21 ASP A 23 0
SHEET 2 A 3 PHE A 139 ASN A 149 1 O THR A 144 N ILE A 22
SHEET 3 A 3 THR A 153 TYR A 155 -1 O TYR A 155 N ILE A 147
SHEET 1 B 3 GLN A 21 ASP A 23 0
SHEET 2 B 3 PHE A 139 ASN A 149 1 O THR A 144 N ILE A 22
SHEET 3 B 3 LYS A 158 GLU A 160 -1 O GLY A 159 N ILE A 143
SHEET 1 C 2 ARG A 29 PHE A 30 0
SHEET 2 C 2 VAL A 33 PHE A 34 -1 O VAL A 33 N PHE A 30
SHEET 1 D 2 SER A 58 THR A 59 0
SHEET 2 D 2 PHE A 119 ASN A 120 -1 O PHE A 119 N THR A 59
SHEET 1 E 3 VAL A 86 VAL A 87 0
SHEET 2 E 3 GLY A 80 PHE A 81 -1 N GLY A 80 O VAL A 87
SHEET 3 E 3 ASP A 115 THR A 116 1 O ASP A 115 N PHE A 81
SSBOND 1 CYS A 28 CYS A 129 1555 1555 2.03
SSBOND 2 CYS A 53 CYS A 118 1555 1555 2.03
SSBOND 3 CYS A 77 CYS A 97 1555 1555 2.03
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