Header list of 1ivz.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 02-APR-02 1IVZ
TITLE SOLUTION STRUCTURE OF THE SEA DOMAIN FROM MURINE HYPOTHETICAL PROTEIN
TITLE 2 HOMOLOGOUS TO HUMAN MUCIN 16
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN 1110008I14RIK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEA DOMAIN(RESIDUES 67-185);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P011109-16;
SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS STRUCTURAL GENOMICS, SEA DOMAIN, MUCIN 16, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.MAEDA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 23-FEB-22 1IVZ 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1IVZ 1 VERSN
REVDAT 2 04-MAY-04 1IVZ 1 JRNL
REVDAT 1 02-OCT-02 1IVZ 0
JRNL AUTH T.MAEDA,M.INOUE,S.KOSHIBA,T.YABUKI,M.AOKI,E.NUNOKAWA,E.SEKI,
JRNL AUTH 2 T.MATSUDA,Y.MOTODA,A.KOBAYASHI,F.HIROYASU,M.SHIROUZU,
JRNL AUTH 3 T.TERADA,N.HAYAMI,Y.ISHIZUKA,N.SHINYA,A.TATSUGUCHI,
JRNL AUTH 4 M.YOSHIDA,H.HIROTA,Y.MATSUO,K.TANI,T.ARAKAWA,P.CARNINCI,
JRNL AUTH 5 J.KAWAI,Y.HAYASHIZAKI,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SEA DOMAIN FROM THE MURINE
JRNL TITL 2 HOMOLOGUE OF OVARIAN CANCER ANTIGEN CA125 (MUC16)
JRNL REF J.BIOL.CHEM. V. 279 13174 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14764598
JRNL DOI 10.1074/JBC.M309417200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.8, CNS 1.0
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2533 RESTRAINTS, 2277 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 178 DIHEDRAL ANGLE RESTRAINTS, 78 DISTANCE
REMARK 3 CONSTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1IVZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000005323.
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 : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM PROTEIN U-15N, 13C; 20MM
REMARK 210 SODIUM PHOSPHATE BUFFER; 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% SODIUM
REMARK 210 AZIDE, 90%H2O, 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
REMARK 210 RESIDUES 1-7(GSSGSSG),127-132(SGPSSG) ARE CLONING ARTIFACTS.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 GLY A 132 O
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 SER A 2 99.24 60.47
REMARK 500 1 SER A 5 106.43 57.98
REMARK 500 1 SER A 6 31.15 -162.68
REMARK 500 1 SER A 9 -52.76 -154.21
REMARK 500 1 SER A 10 164.20 60.82
REMARK 500 1 SER A 11 159.71 60.81
REMARK 500 1 PHE A 18 113.12 -178.11
REMARK 500 1 LEU A 23 95.68 -169.94
REMARK 500 1 SER A 33 35.86 -93.01
REMARK 500 1 SER A 55 170.55 -59.02
REMARK 500 1 ILE A 57 46.13 -93.56
REMARK 500 1 SER A 59 -46.81 -152.72
REMARK 500 1 SER A 62 -73.82 -81.74
REMARK 500 1 ALA A 68 -165.74 -170.13
REMARK 500 1 ASN A 74 -66.73 69.13
REMARK 500 1 CYS A 85 75.14 -66.71
REMARK 500 1 THR A 111 -46.17 -137.42
REMARK 500 1 LEU A 114 -80.68 61.52
REMARK 500 1 PHE A 124 136.38 -173.96
REMARK 500 1 SER A 130 27.49 -157.44
REMARK 500 1 SER A 131 82.37 56.91
REMARK 500 2 SER A 2 -47.21 -158.44
REMARK 500 2 SER A 3 -47.19 -162.29
REMARK 500 2 SER A 9 72.09 59.96
REMARK 500 2 SER A 10 31.45 -99.70
REMARK 500 2 PHE A 18 113.10 -176.61
REMARK 500 2 THR A 21 30.05 -97.74
REMARK 500 2 ALA A 30 30.22 -95.74
REMARK 500 2 GLN A 31 106.33 -163.03
REMARK 500 2 PRO A 32 64.22 -67.76
REMARK 500 2 SER A 33 31.33 -165.37
REMARK 500 2 ILE A 57 46.15 -94.38
REMARK 500 2 LYS A 58 43.52 -94.52
REMARK 500 2 SER A 59 -46.67 -136.20
REMARK 500 2 SER A 62 -70.23 -101.74
REMARK 500 2 ALA A 68 -177.26 -175.99
REMARK 500 2 CYS A 85 78.56 -65.43
REMARK 500 2 ARG A 93 71.89 61.58
REMARK 500 2 HIS A 108 70.20 52.32
REMARK 500 2 LEU A 114 -78.84 61.84
REMARK 500 2 ASN A 115 38.15 -141.90
REMARK 500 2 SER A 127 103.79 -56.80
REMARK 500 2 SER A 130 -40.32 -176.31
REMARK 500 2 SER A 131 -168.69 -62.98
REMARK 500 3 SER A 11 161.71 60.76
REMARK 500 3 PHE A 18 116.86 -177.03
REMARK 500 3 ILE A 57 45.82 -93.62
REMARK 500 3 SER A 59 -47.72 -153.13
REMARK 500 3 ASP A 63 -179.08 -177.09
REMARK 500 3 ASN A 77 18.25 -142.91
REMARK 500
REMARK 500 THIS ENTRY HAS 357 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007010579.1 RELATED DB: TARGETDB
DBREF 1IVZ A 8 126 UNP Q9D1H1 Q9D1H1_MOUSE 67 185
SEQADV 1IVZ GLY A 1 UNP Q9D1H1 CLONING ARTIFACT
SEQADV 1IVZ SER A 2 UNP Q9D1H1 CLONING ARTIFACT
SEQADV 1IVZ SER A 3 UNP Q9D1H1 CLONING ARTIFACT
SEQADV 1IVZ GLY A 4 UNP Q9D1H1 CLONING ARTIFACT
SEQADV 1IVZ SER A 5 UNP Q9D1H1 CLONING ARTIFACT
SEQADV 1IVZ SER A 6 UNP Q9D1H1 CLONING ARTIFACT
SEQADV 1IVZ GLY A 7 UNP Q9D1H1 CLONING ARTIFACT
SEQADV 1IVZ SER A 127 UNP Q9D1H1 CLONING ARTIFACT
SEQADV 1IVZ GLY A 128 UNP Q9D1H1 CLONING ARTIFACT
SEQADV 1IVZ PRO A 129 UNP Q9D1H1 CLONING ARTIFACT
SEQADV 1IVZ SER A 130 UNP Q9D1H1 CLONING ARTIFACT
SEQADV 1IVZ SER A 131 UNP Q9D1H1 CLONING ARTIFACT
SEQADV 1IVZ GLY A 132 UNP Q9D1H1 CLONING ARTIFACT
SEQRES 1 A 132 GLY SER SER GLY SER SER GLY SER SER SER SER GLN HIS
SEQRES 2 A 132 PHE ASN LEU ASN PHE THR ILE THR ASN LEU PRO TYR SER
SEQRES 3 A 132 GLN ASP ILE ALA GLN PRO SER THR THR LYS TYR GLN GLN
SEQRES 4 A 132 THR LYS ARG SER ILE GLU ASN ALA LEU ASN GLN LEU PHE
SEQRES 5 A 132 ARG ASN SER SER ILE LYS SER TYR PHE SER ASP CYS GLN
SEQRES 6 A 132 VAL LEU ALA PHE ARG SER VAL SER ASN ASN ASN ASN HIS
SEQRES 7 A 132 THR GLY VAL ASP SER LEU CYS ASN PHE SER PRO LEU ALA
SEQRES 8 A 132 ARG ARG VAL ASP ARG VAL ALA ILE TYR GLU GLU PHE LEU
SEQRES 9 A 132 ARG MET THR HIS ASN GLY THR GLN LEU LEU ASN PHE THR
SEQRES 10 A 132 LEU ASP ARG LYS SER VAL PHE VAL ASP SER GLY PRO SER
SEQRES 11 A 132 SER GLY
HELIX 1 1 SER A 26 GLN A 31 1 6
HELIX 2 2 THR A 34 SER A 55 1 22
HELIX 3 3 ASP A 95 THR A 107 1 13
SHEET 1 A 6 PHE A 124 SER A 127 0
SHEET 2 A 6 HIS A 13 THR A 19 -1 N ASN A 15 O ASP A 126
SHEET 3 A 6 GLY A 80 PHE A 87 -1 O VAL A 81 N PHE A 18
SHEET 4 A 6 PHE A 61 CYS A 64 -1 N SER A 62 O ASN A 86
SHEET 5 A 6 GLY A 80 PHE A 87 -1 N ASN A 86 O ASP A 63
SHEET 6 A 6 ALA A 68 ARG A 70 -1 O ALA A 68 N ASP A 82
SHEET 1 B 2 GLN A 112 LEU A 113 0
SHEET 2 B 2 PHE A 116 THR A 117 -1 O PHE A 116 N LEU A 113
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 - b 23 2 Bytes