Header list of 1rsf.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 09-DEC-03 1RSF
TITLE NMR STRUCTURE OF MONOMERIC CAR D1 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COXSACKIEVIRUS AND ADENOVIRUS RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: COXSACKIEVIRUS B-ADENOVIRUS RECEPTOR, HCAR, CVB3 BINDING
COMPND 5 PROTEIN;
COMPND 6 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: CXADR, CAR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS CAR, COXSACKIEVIRUS, ADENOVIRUS, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR S.JIANG,A.JACOBS,T.M.LAUE,M.CAFFREY
REVDAT 3 02-MAR-22 1RSF 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1RSF 1 VERSN
REVDAT 1 02-MAR-04 1RSF 0
JRNL AUTH S.JIANG,A.JACOBS,T.M.LAUE,M.CAFFREY
JRNL TITL SOLUTION STRUCTURE OF THE COXSACKIEVIRUS AND ADENOVIRUS
JRNL TITL 2 RECEPTOR DOMAIN 1.
JRNL REF BIOCHEMISTRY V. 43 1847 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 14967025
JRNL DOI 10.1021/BI035490X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : BRUNGER, A.T., ADAMS, P.D., CLORE, G.M., DELANO,
REMARK 3 W.L., GROS, P., ET AL. (CNS), BRUNGER, A.T., ADAMS,
REMARK 3 P.D., CLORE, G.M., DELANO, W.L., GROS, P., ET AL.
REMARK 3 (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RSF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021009.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : 100 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : U-15N; U-13C/U-15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCACB; CBCA(CO)NH; HN(CO)CA;
REMARK 210 HCCH-TOCSY; HCC(CO)NH; HNHA; 3D_
REMARK 210 15N-EDITED_NOESY; 3D_15N-EDITED_
REMARK 210 TOCSY; 2D_NOESY; 2D_TOCSY; 3D_
REMARK 210 13C-EDITED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 HD2 TYR A 74 HB ILE A 79 1.33
REMARK 500 O HIS A 92 H ASN A 106 1.57
REMARK 500 O LEU A 73 H TYR A 80 1.59
REMARK 500 O ARG A 90 O ASN A 106 2.19
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 THR A 24 82.88 43.12
REMARK 500 1 PRO A 25 -73.77 -78.36
REMARK 500 1 ASP A 49 73.69 -65.79
REMARK 500 1 ASP A 68 85.18 55.66
REMARK 500 1 ILE A 71 -41.38 -130.79
REMARK 500 1 ASP A 81 -53.47 -165.98
REMARK 500 1 ARG A 90 -50.97 -138.99
REMARK 500 1 LEU A 110 176.21 -45.45
REMARK 500 1 PRO A 126 50.04 -101.61
REMARK 500 1 PRO A 141 164.70 -46.85
REMARK 500 1 SER A 142 -79.59 -35.62
REMARK 500 2 THR A 24 83.24 41.75
REMARK 500 2 PRO A 25 -78.32 -78.72
REMARK 500 2 LYS A 33 153.32 -44.98
REMARK 500 2 ASP A 68 46.31 39.98
REMARK 500 2 ASP A 81 -56.48 -166.17
REMARK 500 2 ARG A 90 -49.26 -142.02
REMARK 500 2 THR A 94 36.03 -76.44
REMARK 500 2 LYS A 99 1.40 -65.80
REMARK 500 2 LEU A 110 175.84 -45.03
REMARK 500 2 PRO A 126 47.26 -100.68
REMARK 500 2 PRO A 141 -140.52 -14.72
REMARK 500 2 SER A 142 -51.87 -22.77
REMARK 500 3 THR A 24 82.52 40.28
REMARK 500 3 ILE A 71 -52.41 -134.06
REMARK 500 3 ASP A 81 -48.21 -166.07
REMARK 500 3 LEU A 87 38.01 -157.56
REMARK 500 3 ARG A 90 -48.13 -145.27
REMARK 500 3 THR A 94 32.94 -76.14
REMARK 500 3 LYS A 99 2.42 -62.99
REMARK 500 3 LEU A 110 89.72 -47.27
REMARK 500 3 PRO A 126 49.76 -100.62
REMARK 500 3 PRO A 141 -142.07 -51.52
REMARK 500 4 THR A 24 82.96 44.33
REMARK 500 4 PRO A 25 -86.19 -78.55
REMARK 500 4 ILE A 71 -52.19 -132.97
REMARK 500 4 ASP A 81 -52.19 -165.82
REMARK 500 4 ARG A 90 -47.92 -143.96
REMARK 500 4 LYS A 99 0.90 -63.21
REMARK 500 4 LEU A 110 90.27 -42.86
REMARK 500 4 PRO A 126 50.47 -99.61
REMARK 500 4 SER A 142 -75.63 -39.91
REMARK 500 5 THR A 24 82.99 46.07
REMARK 500 5 PRO A 25 -77.39 -78.57
REMARK 500 5 LYS A 33 156.83 -42.88
REMARK 500 5 ASP A 81 -48.94 -165.82
REMARK 500 5 ARG A 90 -46.25 -145.96
REMARK 500 5 THR A 94 36.76 -73.03
REMARK 500 5 LYS A 99 1.47 -63.50
REMARK 500 5 LEU A 110 173.53 -46.19
REMARK 500
REMARK 500 THIS ENTRY HAS 289 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EAJ RELATED DB: PDB
REMARK 900 DIMERIC STRUCTURE OF THE COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR D1
REMARK 900 DOMAIN AT 1.35 ANGSTROM RESOLUTION
DBREF 1RSF A 21 144 UNP P78310 CXAR_HUMAN 21 144
SEQADV 1RSF GLY A 19 UNP P78310 CLONING ARTIFACT
SEQADV 1RSF SER A 20 UNP P78310 CLONING ARTIFACT
SEQRES 1 A 126 GLY SER SER ILE THR THR PRO GLU GLU MET ILE GLU LYS
SEQRES 2 A 126 ALA LYS GLY GLU THR ALA TYR LEU PRO CYS LYS PHE THR
SEQRES 3 A 126 LEU SER PRO GLU ASP GLN GLY PRO LEU ASP ILE GLU TRP
SEQRES 4 A 126 LEU ILE SER PRO ALA ASP ASN GLN LYS VAL ASP GLN VAL
SEQRES 5 A 126 ILE ILE LEU TYR SER GLY ASP LYS ILE TYR ASP ASP TYR
SEQRES 6 A 126 TYR PRO ASP LEU LYS GLY ARG VAL HIS PHE THR SER ASN
SEQRES 7 A 126 ASP LEU LYS SER GLY ASP ALA SER ILE ASN VAL THR ASN
SEQRES 8 A 126 LEU GLN LEU SER ASP ILE GLY THR TYR GLN CYS LYS VAL
SEQRES 9 A 126 LYS LYS ALA PRO GLY VAL ALA ASN LYS LYS ILE HIS LEU
SEQRES 10 A 126 VAL VAL LEU VAL LYS PRO SER GLY ALA
HELIX 1 1 ASP A 97 GLY A 101 5 5
HELIX 2 2 GLN A 111 ILE A 115 5 5
SHEET 1 A 2 ILE A 22 THR A 23 0
SHEET 2 A 2 LYS A 42 PHE A 43 -1 O LYS A 42 N THR A 23
SHEET 1 B 6 GLU A 26 ALA A 32 0
SHEET 2 B 6 GLY A 127 LEU A 138 1 O HIS A 134 N ILE A 29
SHEET 3 B 6 GLY A 116 LYS A 124 -1 N VAL A 122 O ALA A 129
SHEET 4 B 6 ILE A 55 SER A 60 -1 N GLU A 56 O LYS A 121
SHEET 5 B 6 GLN A 69 SER A 75 -1 O TYR A 74 N ILE A 55
SHEET 6 B 6 LYS A 78 TYR A 80 -1 O TYR A 80 N LEU A 73
SHEET 1 C 3 ALA A 37 LEU A 39 0
SHEET 2 C 3 ILE A 105 VAL A 107 -1 O VAL A 107 N ALA A 37
SHEET 3 C 3 HIS A 92 PHE A 93 -1 N HIS A 92 O ASN A 106
SSBOND 1 CYS A 41 CYS A 120 1555 1555 2.03
CISPEP 1 ALA A 125 PRO A 126 1 -0.63
CISPEP 2 ALA A 125 PRO A 126 2 -0.40
CISPEP 3 ALA A 125 PRO A 126 3 -0.54
CISPEP 4 ALA A 125 PRO A 126 4 -0.65
CISPEP 5 ALA A 125 PRO A 126 5 -1.07
CISPEP 6 ALA A 125 PRO A 126 6 -0.28
CISPEP 7 ALA A 125 PRO A 126 7 -0.76
CISPEP 8 ALA A 125 PRO A 126 8 -1.00
CISPEP 9 ALA A 125 PRO A 126 9 -0.95
CISPEP 10 ALA A 125 PRO A 126 10 -0.43
CISPEP 11 ALA A 125 PRO A 126 11 -0.67
CISPEP 12 ALA A 125 PRO A 126 12 -0.57
CISPEP 13 ALA A 125 PRO A 126 13 -0.87
CISPEP 14 ALA A 125 PRO A 126 14 -0.45
CISPEP 15 ALA A 125 PRO A 126 15 -0.26
CISPEP 16 ALA A 125 PRO A 126 16 -0.45
CISPEP 17 ALA A 125 PRO A 126 17 -1.01
CISPEP 18 ALA A 125 PRO A 126 18 -0.21
CISPEP 19 ALA A 125 PRO A 126 19 -1.02
CISPEP 20 ALA A 125 PRO A 126 20 -0.67
CISPEP 21 ALA A 125 PRO A 126 21 -0.61
CISPEP 22 ALA A 125 PRO A 126 22 -0.52
CISPEP 23 ALA A 125 PRO A 126 23 -0.70
CISPEP 24 ALA A 125 PRO A 126 24 -0.90
CISPEP 25 ALA A 125 PRO A 126 25 -0.61
CISPEP 26 ALA A 125 PRO A 126 26 -0.61
CISPEP 27 ALA A 125 PRO A 126 27 -0.72
CISPEP 28 ALA A 125 PRO A 126 28 -0.92
CISPEP 29 ALA A 125 PRO A 126 29 -0.42
CISPEP 30 ALA A 125 PRO A 126 30 -0.97
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
Complete list - r 2 2 Bytes