Header list of 2dce.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 06-JAN-06 2DCE
TITLE SOLUTION STRUCTURE OF THE SWIRM DOMAIN OF HUMAN KIAA1915 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIAA1915 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SWIRM DOMAIN, RESIDUES 8-111;
COMPND 5 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: KIAA1915;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P041018-14;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SWIRM DOMAIN, KIAA1915, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT
KEYWDS 2 ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.YONEYAMA,N.TOCHIO,T.UMEHARA,S.KOSHIBA,M.INOUE,A.TANAKA,T.KIGAWA,
AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 5 09-MAR-22 2DCE 1 REMARK SEQADV
REVDAT 4 24-FEB-09 2DCE 1 VERSN
REVDAT 3 15-MAY-07 2DCE 3 ATOM
REVDAT 2 15-MAY-07 2DCE 1 JRNL
REVDAT 1 06-JUL-06 2DCE 0
JRNL AUTH M.YONEYAMA,N.TOCHIO,T.UMEHARA,S.KOSHIBA,M.INOUE,T.YABUKI,
JRNL AUTH 2 M.AOKI,E.SEKI,T.MATSUDA,S.WATANABE,Y.TOMO,Y.NISHIMURA,
JRNL AUTH 3 T.HARADA,T.TERADA,M.SHIROUZU,Y.HAYASHIZAKI,O.OHARA,A.TANAKA,
JRNL AUTH 4 T.KIGAWA,S.YOKOYAMA
JRNL TITL STRUCTURAL AND FUNCTIONAL DIFFERENCES OF SWIRM DOMAIN
JRNL TITL 2 SUBTYPES
JRNL REF J.MOL.BIOL. V. 369 222 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17428495
JRNL DOI 10.1016/J.JMB.2007.03.027
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DCE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000025248.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 320MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.17MM SWIRM DOMAIN U-15N,13C;
REMARK 210 20MM D-TRIS HCL; 300MM NACL; 1MM
REMARK 210 D-DTT; 0.02% NAN3; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9318, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS
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: 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 12 29.04 37.57
REMARK 500 1 LYS A 65 154.68 -40.55
REMARK 500 1 ALA A 99 -33.73 -34.00
REMARK 500 1 GLN A 106 42.80 -96.84
REMARK 500 2 SER A 6 97.78 -55.83
REMARK 500 2 HIS A 8 124.52 -37.52
REMARK 500 2 GLU A 40 -72.84 -59.70
REMARK 500 2 LYS A 65 155.05 -38.41
REMARK 500 2 LYS A 79 -66.76 -104.36
REMARK 500 2 ALA A 99 -34.62 -33.81
REMARK 500 2 GLU A 105 -35.04 -34.41
REMARK 500 2 GLN A 106 39.45 -83.09
REMARK 500 3 GLU A 9 128.54 -171.45
REMARK 500 3 GLU A 12 48.15 35.01
REMARK 500 3 LYS A 65 154.83 -36.40
REMARK 500 3 ASN A 80 46.00 -79.81
REMARK 500 3 GLN A 106 36.54 -95.47
REMARK 500 4 GLU A 11 73.03 -110.88
REMARK 500 4 LYS A 65 154.56 -43.51
REMARK 500 4 LEU A 78 45.31 71.74
REMARK 500 4 CYS A 81 -75.07 -63.16
REMARK 500 4 ALA A 99 -37.07 -34.09
REMARK 500 5 HIS A 8 42.88 -87.39
REMARK 500 5 GLU A 10 155.98 -43.14
REMARK 500 5 GLU A 30 -36.43 -38.05
REMARK 500 5 ARG A 42 155.44 -37.04
REMARK 500 5 ARG A 54 -70.02 -51.64
REMARK 500 5 LYS A 65 154.47 -39.38
REMARK 500 5 PRO A 76 1.33 -69.76
REMARK 500 5 LYS A 79 -74.58 -98.12
REMARK 500 5 CYS A 81 50.42 -106.25
REMARK 500 5 VAL A 84 -36.89 -35.83
REMARK 500 5 ALA A 107 164.54 -45.08
REMARK 500 6 SER A 2 44.56 38.99
REMARK 500 6 HIS A 8 39.13 -89.95
REMARK 500 6 GLU A 29 -32.60 -34.73
REMARK 500 6 ARG A 42 -178.97 -66.23
REMARK 500 6 GLN A 43 -70.39 -95.22
REMARK 500 6 LYS A 65 154.31 -44.04
REMARK 500 6 LEU A 78 69.23 -106.90
REMARK 500 6 ASN A 80 -72.53 -40.83
REMARK 500 6 ALA A 99 -33.65 -35.01
REMARK 500 7 ARG A 54 -70.69 -51.88
REMARK 500 7 LYS A 65 154.86 -35.99
REMARK 500 7 LYS A 79 -66.04 -99.80
REMARK 500 7 ALA A 99 -36.73 -33.77
REMARK 500 7 GLN A 106 44.07 -98.06
REMARK 500 8 SER A 2 140.90 -170.48
REMARK 500 8 GLU A 10 157.24 -48.12
REMARK 500 8 GLU A 11 53.31 -90.37
REMARK 500
REMARK 500 THIS ENTRY HAS 136 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002101882.2 RELATED DB: TARGETDB
DBREF 2DCE A 8 111 UNP Q5VVJ2 MYSM1_HUMAN 367 470
SEQADV 2DCE GLY A 1 UNP Q5VVJ2 CLONING ARTIFACT
SEQADV 2DCE SER A 2 UNP Q5VVJ2 CLONING ARTIFACT
SEQADV 2DCE SER A 3 UNP Q5VVJ2 CLONING ARTIFACT
SEQADV 2DCE GLY A 4 UNP Q5VVJ2 CLONING ARTIFACT
SEQADV 2DCE SER A 5 UNP Q5VVJ2 CLONING ARTIFACT
SEQADV 2DCE SER A 6 UNP Q5VVJ2 CLONING ARTIFACT
SEQADV 2DCE GLY A 7 UNP Q5VVJ2 CLONING ARTIFACT
SEQRES 1 A 111 GLY SER SER GLY SER SER GLY HIS GLU GLU GLU GLU LEU
SEQRES 2 A 111 LYS PRO PRO GLU GLN GLU ILE GLU ILE ASP ARG ASN ILE
SEQRES 3 A 111 ILE GLN GLU GLU GLU LYS GLN ALA ILE PRO GLU PHE PHE
SEQRES 4 A 111 GLU GLY ARG GLN ALA LYS THR PRO GLU ARG TYR LEU LYS
SEQRES 5 A 111 ILE ARG ASN TYR ILE LEU ASP GLN TRP GLU ILE CYS LYS
SEQRES 6 A 111 PRO LYS TYR LEU ASN LYS THR SER VAL ARG PRO GLY LEU
SEQRES 7 A 111 LYS ASN CYS GLY ASP VAL ASN CYS ILE GLY ARG ILE HIS
SEQRES 8 A 111 THR TYR LEU GLU LEU ILE GLY ALA ILE ASN PHE GLY CYS
SEQRES 9 A 111 GLU GLN ALA VAL TYR ASN ARG
HELIX 1 1 GLN A 28 GLN A 33 1 6
HELIX 2 2 ILE A 35 GLU A 40 5 6
HELIX 3 3 THR A 46 LYS A 65 1 20
HELIX 4 4 ASN A 70 VAL A 74 5 5
HELIX 5 5 ASP A 83 GLY A 98 1 16
CISPEP 1 LYS A 65 PRO A 66 1 -0.06
CISPEP 2 LYS A 65 PRO A 66 2 -0.04
CISPEP 3 LYS A 65 PRO A 66 3 -0.12
CISPEP 4 LYS A 65 PRO A 66 4 -0.18
CISPEP 5 LYS A 65 PRO A 66 5 -0.07
CISPEP 6 LYS A 65 PRO A 66 6 -0.04
CISPEP 7 LYS A 65 PRO A 66 7 -0.11
CISPEP 8 LYS A 65 PRO A 66 8 -0.07
CISPEP 9 LYS A 65 PRO A 66 9 -0.18
CISPEP 10 LYS A 65 PRO A 66 10 -0.10
CISPEP 11 LYS A 65 PRO A 66 11 -0.06
CISPEP 12 LYS A 65 PRO A 66 12 -0.10
CISPEP 13 LYS A 65 PRO A 66 13 -0.12
CISPEP 14 LYS A 65 PRO A 66 14 -0.11
CISPEP 15 LYS A 65 PRO A 66 15 -0.14
CISPEP 16 LYS A 65 PRO A 66 16 -0.06
CISPEP 17 LYS A 65 PRO A 66 17 -0.10
CISPEP 18 LYS A 65 PRO A 66 18 -0.09
CISPEP 19 LYS A 65 PRO A 66 19 -0.13
CISPEP 20 LYS A 65 PRO A 66 20 -0.11
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 9 2 Bytes