Header list of 1yhp.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 10-JAN-05 1YHP
TITLE SOLUTION STRUCTURE OF CA2+-FREE DDCAD-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM-DEPENDENT CELL ADHESION MOLECULE-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DDCAD-1, GP24;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DICTYOSTELIUM DISCOIDEUM;
SOURCE 3 ORGANISM_TAXID: 44689;
SOURCE 4 GENE: CADA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-M
KEYWDS DDCAD-1, CELL ADHESION, CALCIUM
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR Z.LIN,H.B.HUANG,C.H.SIU,D.W.YANG
REVDAT 5 02-MAR-22 1YHP 1 REMARK
REVDAT 4 24-FEB-09 1YHP 1 VERSN
REVDAT 3 01-JAN-08 1YHP 1 JRNL
REVDAT 2 24-OCT-06 1YHP 1 JRNL REMARK
REVDAT 1 31-JAN-06 1YHP 0
JRNL AUTH Z.LIN,S.SRISKANTHADEVAN,H.B.HUANG,C.H.SIU,D.W.YANG
JRNL TITL SOLUTION STRUCTURES OF THE ADHESION MOLECULE DDCAD-1 REVEAL
JRNL TITL 2 NEW INSIGHTS INTO CA(2+)-DEPENDENT CELL-CELL ADHESION
JRNL REF NAT.STRUCT.MOL.BIOL. V. 13 1016 2006
JRNL REFN ISSN 1545-9993
JRNL PMID 17057715
JRNL DOI 10.1038/NSMB1162
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.LIN,H.B.HUANG,C.H.SIU,D.W.YANG
REMARK 1 TITL (1)H, (13)C AND (15)N RESONANCE ASSIGNMENTS OF CA(2+)-FREE
REMARK 1 TITL 2 DDCAD-1: A CA(2+)-DEPENDENT CELL-CELL ADHESION MOLECULE
REMARK 1 REF J.BIOMOL.NMR V. 30 375 2004
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 15756470
REMARK 1 DOI 10.1007/S10858-005-2336-5
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1.0.5, CYANA 1.0.5
REMARK 3 AUTHORS : PETER GUNTERT (CYANA), PETER GUNTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 4847 RESTRAINTS, 4481 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 212
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,154 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS
REMARK 4
REMARK 4 1YHP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031523.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 10MM PIPES, 0.05MM SODIUM AZIDE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8MM DDCAD-1 U-15N, 13C; 10MM
REMARK 210 PIPES BUFFER; 1MM EGTA, 1MM DTT,
REMARK 210 0.05MM SODIUM AZIDE, 90% H2O, 10%
REMARK 210 D2O; 0.8MM DDCAD-1 U-15N, 13C;
REMARK 210 10MM PIPES BUFFER; 1MM EGTA, 1MM
REMARK 210 DTT, 0.05MM SODIUM AZIDE, 99% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY;
REMARK 210 4D_13C/15N-SEPARATED_NOESY; 4D_
REMARK 210 13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1, NMRVIEW 5.04
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: 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 2 TYR A 115 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 9 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.6 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 1 PHE A 12 48.73 -93.78
REMARK 500 1 ASN A 15 40.14 72.56
REMARK 500 1 MET A 42 -31.46 -149.65
REMARK 500 1 SER A 48 -25.68 -168.17
REMARK 500 1 ILE A 60 51.31 -147.68
REMARK 500 1 ASP A 61 -31.64 -177.48
REMARK 500 1 SER A 75 169.33 179.37
REMARK 500 1 LEU A 80 26.04 -140.30
REMARK 500 1 ASN A 84 39.97 82.29
REMARK 500 1 SER A 87 -35.96 -144.58
REMARK 500 1 PRO A 93 32.00 -78.95
REMARK 500 1 ASN A 106 103.08 -58.96
REMARK 500 1 VAL A 108 -35.78 -143.82
REMARK 500 1 ALA A 112 -44.38 69.93
REMARK 500 1 TYR A 122 98.96 -33.90
REMARK 500 1 GLN A 123 51.12 39.68
REMARK 500 1 ASP A 134 55.16 -95.56
REMARK 500 1 PHE A 135 93.10 60.33
REMARK 500 1 LEU A 143 -175.42 55.21
REMARK 500 1 ASN A 168 76.52 -150.12
REMARK 500 1 THR A 178 -40.22 -130.08
REMARK 500 1 THR A 179 30.03 -149.22
REMARK 500 1 THR A 190 -43.14 -145.12
REMARK 500 1 ASN A 194 -32.41 -148.31
REMARK 500 1 THR A 203 12.68 53.66
REMARK 500 1 GLU A 212 57.44 -150.48
REMARK 500 2 PHE A 12 43.12 -78.17
REMARK 500 2 ASN A 33 2.23 -67.61
REMARK 500 2 PHE A 41 31.19 -67.00
REMARK 500 2 SER A 48 -22.63 -156.47
REMARK 500 2 GLU A 56 -63.02 -95.27
REMARK 500 2 ILE A 60 45.72 -142.40
REMARK 500 2 ASP A 61 -26.00 -169.82
REMARK 500 2 SER A 87 -63.77 -125.25
REMARK 500 2 SER A 110 -42.82 65.72
REMARK 500 2 ALA A 112 176.11 50.69
REMARK 500 2 SER A 114 30.58 -140.78
REMARK 500 2 TYR A 122 106.43 -42.46
REMARK 500 2 ASP A 125 109.67 -55.23
REMARK 500 2 ASP A 131 108.36 -51.94
REMARK 500 2 PHE A 135 90.49 63.37
REMARK 500 2 ASP A 147 0.09 -69.60
REMARK 500 2 THR A 161 133.77 -39.79
REMARK 500 2 THR A 179 28.52 -156.28
REMARK 500 2 THR A 190 -47.54 -142.91
REMARK 500 2 PRO A 192 -96.87 -78.36
REMARK 500 2 LYS A 193 -36.36 -179.68
REMARK 500 3 MET A 42 -73.76 -62.45
REMARK 500 3 SER A 48 -21.86 -166.95
REMARK 500 3 SER A 75 158.36 176.05
REMARK 500
REMARK 500 THIS ENTRY HAS 204 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 3 TYR A 23 0.07 SIDE CHAIN
REMARK 500 9 TYR A 23 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6159 RELATED DB: BMRB
REMARK 900 1H, 13C AND 15N RESONANCE ASSIGNMENTS OF CA2+-FREE DDCAD-1
DBREF 1YHP A 2 213 UNP P54657 CAD1_DICDI 2 213
SEQRES 1 A 212 SER VAL ASP ALA ASN LYS VAL LYS PHE PHE PHE GLY LYS
SEQRES 2 A 212 ASN CYS THR GLY GLU SER PHE GLU TYR ASN LYS GLY GLU
SEQRES 3 A 212 THR VAL ARG PHE ASN ASN GLY ASP LYS TRP ASN ASP LYS
SEQRES 4 A 212 PHE MET SER CYS LEU VAL GLY SER ASN VAL ARG CYS ASN
SEQRES 5 A 212 ILE TRP GLU HIS ASN GLU ILE ASP THR PRO THR PRO GLY
SEQRES 6 A 212 LYS PHE GLN GLU LEU ALA GLN GLY SER THR ASN ASN ASP
SEQRES 7 A 212 LEU THR SER ILE ASN GLY LEU SER LYS PHE GLN VAL LEU
SEQRES 8 A 212 PRO GLY ALA PHE GLN TRP ALA VAL ASP VAL LYS ILE VAL
SEQRES 9 A 212 ASN LYS VAL ASN SER THR ALA GLY SER TYR GLU MET THR
SEQRES 10 A 212 ILE THR PRO TYR GLN VAL ASP LYS VAL ALA CYS LYS ASP
SEQRES 11 A 212 GLY ASP ASP PHE VAL GLN LEU PRO ILE PRO LYS LEU THR
SEQRES 12 A 212 PRO PRO ASP SER GLU ILE VAL SER HIS LEU THR VAL ARG
SEQRES 13 A 212 GLN THR HIS THR PRO TYR ASP TYR VAL VAL ASN GLY SER
SEQRES 14 A 212 VAL TYR PHE LYS TYR SER PRO THR THR GLY GLN VAL THR
SEQRES 15 A 212 VAL ILE LYS LYS ASP GLU THR PHE PRO LYS ASN MET THR
SEQRES 16 A 212 VAL THR GLN ASP ASP ASN THR SER PHE ILE PHE ASN LEU
SEQRES 17 A 212 ASN SER GLU LYS
HELIX 1 1 ASP A 35 LYS A 40 1 6
HELIX 2 2 LEU A 80 ASN A 84 5 5
SHEET 1 A 4 SER A 20 TYR A 23 0
SHEET 2 A 4 VAL A 8 PHE A 11 -1 N VAL A 8 O TYR A 23
SHEET 3 A 4 SER A 43 VAL A 46 -1 O LEU A 45 N LYS A 9
SHEET 4 A 4 SER A 75 ASN A 77 -1 O ASN A 77 N CYS A 44
SHEET 1 B 4 GLU A 27 ARG A 30 0
SHEET 2 B 4 LYS A 88 LEU A 92 -1 O VAL A 91 N GLU A 27
SHEET 3 B 4 ARG A 51 TRP A 55 -1 N TRP A 55 O LYS A 88
SHEET 4 B 4 PHE A 68 LEU A 71 -1 O GLN A 69 N ILE A 54
SHEET 1 C 4 VAL A 136 ILE A 140 0
SHEET 2 C 4 TRP A 98 ASN A 106 -1 N VAL A 100 O LEU A 138
SHEET 3 C 4 SER A 204 LEU A 209 1 O PHE A 207 N LYS A 103
SHEET 4 C 4 MET A 195 ASP A 201 -1 N THR A 196 O ASN A 208
SHEET 1 D 5 VAL A 127 LYS A 130 0
SHEET 2 D 5 TYR A 115 PRO A 121 -1 N MET A 117 O CYS A 129
SHEET 3 D 5 ILE A 150 GLN A 158 -1 O THR A 155 N THR A 118
SHEET 4 D 5 TYR A 165 SER A 176 -1 O GLY A 169 N LEU A 154
SHEET 5 D 5 GLN A 181 ILE A 185 -1 O GLN A 181 N SER A 176
CISPEP 1 THR A 144 PRO A 145 1 -9.83
CISPEP 2 THR A 161 PRO A 162 1 5.50
CISPEP 3 THR A 144 PRO A 145 2 -6.85
CISPEP 4 THR A 161 PRO A 162 2 3.84
CISPEP 5 THR A 144 PRO A 145 3 -6.47
CISPEP 6 THR A 161 PRO A 162 3 -7.36
CISPEP 7 THR A 144 PRO A 145 4 -5.76
CISPEP 8 THR A 161 PRO A 162 4 3.80
CISPEP 9 THR A 144 PRO A 145 5 -4.63
CISPEP 10 THR A 161 PRO A 162 5 -9.03
CISPEP 11 THR A 144 PRO A 145 6 -3.53
CISPEP 12 THR A 161 PRO A 162 6 -9.57
CISPEP 13 THR A 144 PRO A 145 7 -7.58
CISPEP 14 THR A 161 PRO A 162 7 3.86
CISPEP 15 THR A 144 PRO A 145 8 -7.45
CISPEP 16 THR A 161 PRO A 162 8 -5.04
CISPEP 17 THR A 144 PRO A 145 9 -5.94
CISPEP 18 THR A 161 PRO A 162 9 1.02
CISPEP 19 THR A 144 PRO A 145 10 -5.61
CISPEP 20 THR A 161 PRO A 162 10 2.90
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