Header list of 1x67.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 17-MAY-05 1X67
TITLE SOLUTION STRUCTURE OF THE COFILIN HOMOLOGY DOMAIN OF HIP-55 (DREBRIN-
TITLE 2 LIKE PROTEIN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DREBRIN-LIKE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: COFILIN HOMOLOGY DOMAIN;
COMPND 5 SYNONYM: SH3 DOMAIN-CONTAINING PROTEIN 7, DREBRIN F, CERVICAL SH3P7,
COMPND 6 HPK1-INTERACTING PROTEIN OF 55 KDA, HIP-55, CERVICAL MUCIN-ASSOCIATED
COMPND 7 PROTEIN, PP5423;
COMPND 8 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: DBNL;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041129-01;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS CELL-FREE PROTEIN SYNTHESIS, ACTIN-BINDING PROTEIN, SH3P7, MABP1, T-
KEYWDS 2 CELL LYMPHOCYTE SIGNALING AND REGULATION, T-CELL ANTIGEN RECEPTOR
KEYWDS 3 REGULATION, HPK-1 ACTIVATION, C-JUN N-TERMINAL KINASE ACTIVATION,
KEYWDS 4 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 5 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 6 INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.K.GORONCY,T.KIGAWA,S.KOSHIBA,M.SATO,N.KOBAYASHI,N.TOCHIO,M.INOUE,
AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 02-MAR-22 1X67 1 REMARK SEQADV
REVDAT 3 02-FEB-10 1X67 1 JRNL
REVDAT 2 24-FEB-09 1X67 1 VERSN
REVDAT 1 17-NOV-05 1X67 0
JRNL AUTH A.K.GORONCY,S.KOSHIBA,N.TOCHIO,T.TOMIZAWA,M.SATO,M.INOUE,
JRNL AUTH 2 S.WATANABE,Y.HAYASHIZAKI,A.TANAKA,T.KIGAWA,S.YOKOYAMA
JRNL TITL NMR SOLUTION STRUCTURES OF ACTIN DEPOLYMERIZING FACTOR
JRNL TITL 2 HOMOLOGY DOMAINS.
JRNL REF PROTEIN SCI. V. 18 2384 2009
JRNL REFN ISSN 0961-8368
JRNL PMID 19768801
JRNL DOI 10.1002/PRO.248
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2
REMARK 3 AUTHORS : BRUKER (XWINNMR), PETER GUNTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X67 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024429.
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 : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.33MM COFILIN HOMOLOGY DOMAIN,
REMARK 210 20MM TRIS-HCL, 100MM NACL, 1MM D-
REMARK 210 DTT, 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.899A
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 : STRUCTURES WITH THE LEAST
REMARK 210 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 3 -56.64 -127.16
REMARK 500 1 SER A 5 -41.82 -169.87
REMARK 500 1 SER A 6 -52.00 -147.33
REMARK 500 1 MET A 8 111.36 64.83
REMARK 500 1 ASN A 15 42.20 -103.75
REMARK 500 1 THR A 33 112.96 -161.25
REMARK 500 1 ALA A 36 118.29 -169.35
REMARK 500 1 GLU A 41 -74.30 -84.13
REMARK 500 1 ASP A 46 98.87 -179.15
REMARK 500 1 ASN A 97 177.52 -59.55
REMARK 500 1 ALA A 118 103.23 -51.65
REMARK 500 1 ARG A 125 -42.53 -144.99
REMARK 500 1 VAL A 130 26.45 -150.57
REMARK 500 1 SER A 144 -45.95 -158.26
REMARK 500 1 SER A 145 127.39 -176.31
REMARK 500 2 SER A 2 -60.10 -175.31
REMARK 500 2 ASN A 15 42.68 -106.83
REMARK 500 2 THR A 33 109.20 -161.26
REMARK 500 2 ALA A 36 118.47 -170.67
REMARK 500 2 ASP A 46 93.68 -179.07
REMARK 500 2 ASN A 97 172.43 -53.68
REMARK 500 2 ALA A 118 103.15 -51.64
REMARK 500 2 ARG A 125 -42.50 -143.39
REMARK 500 2 VAL A 130 26.50 -150.49
REMARK 500 2 SER A 141 99.61 -65.96
REMARK 500 3 SER A 2 176.78 59.88
REMARK 500 3 SER A 5 118.71 -167.94
REMARK 500 3 SER A 6 177.36 61.22
REMARK 500 3 ASN A 15 44.51 -104.66
REMARK 500 3 THR A 33 98.01 -161.22
REMARK 500 3 ALA A 36 123.75 -170.55
REMARK 500 3 ASN A 43 -35.46 -179.28
REMARK 500 3 ASP A 46 89.82 -174.43
REMARK 500 3 SER A 66 99.16 -69.96
REMARK 500 3 ASN A 97 178.63 -56.87
REMARK 500 3 ALA A 118 102.81 -52.26
REMARK 500 3 ARG A 125 -42.57 -146.01
REMARK 500 3 VAL A 130 26.17 -150.47
REMARK 500 3 PRO A 143 102.37 -51.58
REMARK 500 4 SER A 3 -73.99 -151.04
REMARK 500 4 SER A 5 -172.81 61.29
REMARK 500 4 ASN A 11 -62.76 -94.46
REMARK 500 4 ASN A 15 40.17 -103.76
REMARK 500 4 THR A 33 117.39 -161.20
REMARK 500 4 ALA A 36 121.16 -170.73
REMARK 500 4 ASN A 43 38.70 -99.94
REMARK 500 4 ASP A 46 100.77 -179.10
REMARK 500 4 SER A 66 96.68 -68.84
REMARK 500 4 LEU A 115 59.19 -98.44
REMARK 500 4 ALA A 118 103.14 -51.72
REMARK 500
REMARK 500 THIS ENTRY HAS 217 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002021501.1 RELATED DB: TARGETDB
DBREF 1X67 A 8 140 UNP Q9UJU6 DBNL_HUMAN 1 133
SEQADV 1X67 GLY A 1 UNP Q9UJU6 CLONING ARTIFACT
SEQADV 1X67 SER A 2 UNP Q9UJU6 CLONING ARTIFACT
SEQADV 1X67 SER A 3 UNP Q9UJU6 CLONING ARTIFACT
SEQADV 1X67 GLY A 4 UNP Q9UJU6 CLONING ARTIFACT
SEQADV 1X67 SER A 5 UNP Q9UJU6 CLONING ARTIFACT
SEQADV 1X67 SER A 6 UNP Q9UJU6 CLONING ARTIFACT
SEQADV 1X67 GLY A 7 UNP Q9UJU6 CLONING ARTIFACT
SEQADV 1X67 SER A 141 UNP Q9UJU6 CLONING ARTIFACT
SEQADV 1X67 GLY A 142 UNP Q9UJU6 CLONING ARTIFACT
SEQADV 1X67 PRO A 143 UNP Q9UJU6 CLONING ARTIFACT
SEQADV 1X67 SER A 144 UNP Q9UJU6 CLONING ARTIFACT
SEQADV 1X67 SER A 145 UNP Q9UJU6 CLONING ARTIFACT
SEQADV 1X67 GLY A 146 UNP Q9UJU6 CLONING ARTIFACT
SEQRES 1 A 146 GLY SER SER GLY SER SER GLY MET ALA ALA ASN LEU SER
SEQRES 2 A 146 ARG ASN GLY PRO ALA LEU GLN GLU ALA TYR VAL ARG VAL
SEQRES 3 A 146 VAL THR GLU LYS SER PRO THR ASP TRP ALA LEU PHE THR
SEQRES 4 A 146 TYR GLU GLY ASN SER ASN ASP ILE ARG VAL ALA GLY THR
SEQRES 5 A 146 GLY GLU GLY GLY LEU GLU GLU MET VAL GLU GLU LEU ASN
SEQRES 6 A 146 SER GLY LYS VAL MET TYR ALA PHE CYS ARG VAL LYS ASP
SEQRES 7 A 146 PRO ASN SER GLY LEU PRO LYS PHE VAL LEU ILE ASN TRP
SEQRES 8 A 146 THR GLY GLU GLY VAL ASN ASP VAL ARG LYS GLY ALA CYS
SEQRES 9 A 146 ALA SER HIS VAL SER THR MET ALA SER PHE LEU LYS GLY
SEQRES 10 A 146 ALA HIS VAL THR ILE ASN ALA ARG ALA GLU GLU ASP VAL
SEQRES 11 A 146 GLU PRO GLU CYS ILE MET GLU LYS VAL ALA SER GLY PRO
SEQRES 12 A 146 SER SER GLY
HELIX 1 1 ASN A 15 THR A 28 1 14
HELIX 2 2 GLY A 56 LEU A 64 1 9
HELIX 3 3 ASN A 97 LEU A 115 1 19
HELIX 4 4 ALA A 126 VAL A 130 5 5
HELIX 5 5 GLU A 131 SER A 141 1 11
SHEET 1 A 5 ILE A 47 GLY A 53 0
SHEET 2 A 5 TRP A 35 TYR A 40 -1 N LEU A 37 O GLY A 51
SHEET 3 A 5 VAL A 69 LYS A 77 -1 O PHE A 73 N ALA A 36
SHEET 4 A 5 PRO A 84 THR A 92 -1 O LYS A 85 N VAL A 76
SHEET 5 A 5 ALA A 118 ILE A 122 1 O ILE A 122 N LEU A 88
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