Header list of 2ct4.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 23-MAY-05 2CT4
TITLE SOLUTION STRUTCURE OF THE SH3 DOMAIN OF THE CDC42-INTERACTING PROTEIN
TITLE 2 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CDC42-INTERACTING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: THYROID RECEPTOR INTERACTING PROTEIN 10, TRIP-10;
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: TRIP10;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041213-01;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS CDC42-INTERACTING PROTEIN 4, THYROID RECEPTOR INTERACTING PROTEIN 10,
KEYWDS 2 SH3 DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.MIYAMOTO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CT4 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CT4 1 VERSN
REVDAT 1 23-NOV-05 2CT4 0
JRNL AUTH K.MIYAMOTO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUTCURE OF THE SH3 DOMAIN OF THE
JRNL TITL 2 CDC42-INTERACTING PROTEIN 4
JRNL REF TO BE PUBLISHED
JRNL REFN
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 2CT4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024593.
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 : 120
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.36MM SH3 DOMAIN U-13C,15N;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 D-DTT; 0.02% NAN3; 90%H2O, 10%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 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.925, 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 SER A 20 159.37 -44.83
REMARK 500 1 GLU A 21 49.16 -79.31
REMARK 500 1 GLU A 28 107.17 -54.63
REMARK 500 1 MET A 35 -59.44 -122.90
REMARK 500 1 TYR A 60 30.13 -96.43
REMARK 500 2 HIS A 15 108.08 -59.14
REMARK 500 2 SER A 19 43.73 -107.96
REMARK 500 2 GLU A 21 84.82 -65.93
REMARK 500 2 MET A 35 -53.42 -121.51
REMARK 500 3 THR A 23 179.68 -52.21
REMARK 500 4 SER A 19 43.39 74.11
REMARK 500 4 SER A 65 114.21 -166.85
REMARK 500 5 GLU A 28 109.07 -50.05
REMARK 500 6 SER A 6 97.49 -66.45
REMARK 500 6 GLU A 21 96.48 -35.24
REMARK 500 7 PRO A 67 0.33 -69.79
REMARK 500 7 SER A 68 99.41 -34.74
REMARK 500 8 SER A 20 117.62 -35.05
REMARK 500 8 GLU A 21 103.13 -39.74
REMARK 500 8 MET A 35 -66.17 -106.37
REMARK 500 8 SER A 69 42.53 37.71
REMARK 500 9 HIS A 15 103.81 -52.02
REMARK 500 9 SER A 20 141.72 -36.25
REMARK 500 9 GLU A 21 95.72 -53.51
REMARK 500 9 GLU A 50 39.04 -86.20
REMARK 500 9 SER A 68 155.06 -38.59
REMARK 500 10 HIS A 15 109.40 -48.96
REMARK 500 10 SER A 19 41.91 -86.94
REMARK 500 10 TYR A 60 31.24 -93.60
REMARK 500 11 SER A 5 42.76 70.07
REMARK 500 11 HIS A 15 108.76 -58.27
REMARK 500 11 SER A 20 -66.70 -107.05
REMARK 500 11 GLU A 21 105.57 -173.33
REMARK 500 11 THR A 23 171.89 -48.55
REMARK 500 11 THR A 64 150.64 -36.25
REMARK 500 12 SER A 3 43.01 37.02
REMARK 500 12 SER A 20 178.54 -49.16
REMARK 500 12 MET A 35 -67.54 -108.13
REMARK 500 12 SER A 68 101.24 -38.58
REMARK 500 13 SER A 20 171.60 -46.70
REMARK 500 13 MET A 35 -61.97 -120.12
REMARK 500 13 TYR A 60 30.83 -91.28
REMARK 500 14 SER A 6 85.93 -68.70
REMARK 500 14 HIS A 9 130.79 -39.12
REMARK 500 14 HIS A 15 103.58 -51.79
REMARK 500 14 SER A 20 147.67 -38.74
REMARK 500 14 GLU A 21 98.90 -57.00
REMARK 500 14 GLU A 28 106.97 -53.95
REMARK 500 15 SER A 20 170.74 -49.69
REMARK 500 15 GLU A 50 32.45 -92.10
REMARK 500
REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001002741.1 RELATED DB: TARGETDB
DBREF 2CT4 A 8 64 UNP Q15642 CIP4_HUMAN 487 543
SEQADV 2CT4 GLY A 1 UNP Q15642 CLONING ARTIFACT
SEQADV 2CT4 SER A 2 UNP Q15642 CLONING ARTIFACT
SEQADV 2CT4 SER A 3 UNP Q15642 CLONING ARTIFACT
SEQADV 2CT4 GLY A 4 UNP Q15642 CLONING ARTIFACT
SEQADV 2CT4 SER A 5 UNP Q15642 CLONING ARTIFACT
SEQADV 2CT4 SER A 6 UNP Q15642 CLONING ARTIFACT
SEQADV 2CT4 GLY A 7 UNP Q15642 CLONING ARTIFACT
SEQADV 2CT4 SER A 65 UNP Q15642 CLONING ARTIFACT
SEQADV 2CT4 GLY A 66 UNP Q15642 CLONING ARTIFACT
SEQADV 2CT4 PRO A 67 UNP Q15642 CLONING ARTIFACT
SEQADV 2CT4 SER A 68 UNP Q15642 CLONING ARTIFACT
SEQADV 2CT4 SER A 69 UNP Q15642 CLONING ARTIFACT
SEQADV 2CT4 GLY A 70 UNP Q15642 CLONING ARTIFACT
SEQRES 1 A 70 GLY SER SER GLY SER SER GLY GLY HIS CYS VAL ALA ILE
SEQRES 2 A 70 TYR HIS PHE GLU GLY SER SER GLU GLY THR ILE SER MET
SEQRES 3 A 70 ALA GLU GLY GLU ASP LEU SER LEU MET GLU GLU ASP LYS
SEQRES 4 A 70 GLY ASP GLY TRP THR ARG VAL ARG ARG LYS GLU GLY GLY
SEQRES 5 A 70 GLU GLY TYR VAL PRO THR SER TYR LEU ARG VAL THR SER
SEQRES 6 A 70 GLY PRO SER SER GLY
HELIX 1 1 THR A 58 TYR A 60 1 3
SHEET 1 A 5 GLU A 53 PRO A 57 0
SHEET 2 A 5 TRP A 43 ARG A 47 -1 N THR A 44 O VAL A 56
SHEET 3 A 5 ASP A 31 GLU A 36 -1 N SER A 33 O ARG A 47
SHEET 4 A 5 HIS A 9 ALA A 12 -1 N CYS A 10 O LEU A 32
SHEET 5 A 5 LEU A 61 VAL A 63 -1 O ARG A 62 N VAL A 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