Header list of 2d89.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL PROTEIN, PROTEIN BINDING 02-DEC-05 2D89
TITLE SOLUTION STRUCTURE OF THE CH DOMAIN FROM HUMAN EH DOMAIN BINDING
TITLE 2 PROTEIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EHBP1 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CH DOMAIN;
COMPND 5 SYNONYM: EH DOMAIN BINDING PROTEIN 1;
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: EHBP1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050725-07;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ALL ALPHA, CALPONIN HOMOLOGY DOMAIN, ACTIN BINDING, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, STRUCTURAL PROTEIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2D89 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2D89 1 VERSN
REVDAT 1 02-JUN-06 2D89 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE CH DOMAIN FROM HUMAN EH DOMAIN
JRNL TITL 2 BINDING PROTEIN 1
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 2D89 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025110.
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 : 0.85MM CH DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 D2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 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 0.932, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR 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 LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 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 LEU A 15 -30.51 -37.57
REMARK 500 1 ASN A 24 46.13 -102.28
REMARK 500 1 ILE A 30 73.38 -64.96
REMARK 500 1 THR A 34 -60.81 -107.32
REMARK 500 1 SER A 36 -31.91 -37.34
REMARK 500 1 PRO A 62 3.26 -69.75
REMARK 500 1 ALA A 94 -66.75 -96.43
REMARK 500 1 PRO A 96 -178.53 -69.76
REMARK 500 1 SER A 114 153.04 -42.37
REMARK 500 2 PRO A 8 93.05 -69.76
REMARK 500 2 ALA A 10 93.54 -49.33
REMARK 500 2 SER A 11 42.97 39.07
REMARK 500 2 ASN A 24 47.37 -105.93
REMARK 500 2 ILE A 30 74.35 -68.84
REMARK 500 2 THR A 34 -71.63 -124.70
REMARK 500 2 PRO A 62 3.28 -69.79
REMARK 500 2 TYR A 73 -29.06 -38.22
REMARK 500 2 SER A 82 135.83 -37.38
REMARK 500 2 ASP A 97 99.93 -69.35
REMARK 500 2 THR A 100 -72.42 -58.60
REMARK 500 2 SER A 118 48.48 -79.02
REMARK 500 3 THR A 34 -73.31 -117.44
REMARK 500 3 PRO A 52 3.53 -69.79
REMARK 500 3 PRO A 62 2.97 -69.86
REMARK 500 3 ALA A 94 -65.42 -96.42
REMARK 500 3 TYR A 106 -37.26 -38.43
REMARK 500 4 THR A 34 -67.08 -131.59
REMARK 500 4 SER A 36 -27.72 -38.89
REMARK 500 4 PRO A 52 2.97 -69.77
REMARK 500 4 PRO A 62 3.29 -69.75
REMARK 500 4 ALA A 72 -71.60 -48.48
REMARK 500 4 PRO A 96 -170.18 -69.76
REMARK 500 5 ALA A 10 127.56 -174.32
REMARK 500 5 ASN A 24 56.89 -114.48
REMARK 500 5 THR A 34 -70.72 -126.76
REMARK 500 5 PRO A 52 3.29 -69.77
REMARK 500 5 PRO A 62 3.39 -69.75
REMARK 500 5 TYR A 73 -28.52 -37.83
REMARK 500 5 THR A 100 -73.09 -59.32
REMARK 500 5 SER A 114 129.04 -39.70
REMARK 500 5 PRO A 116 90.73 -69.78
REMARK 500 6 SER A 2 -55.18 -130.67
REMARK 500 6 ASN A 9 -74.82 -41.79
REMARK 500 6 ASN A 24 42.55 -102.74
REMARK 500 6 ILE A 30 56.74 -118.57
REMARK 500 6 THR A 34 -69.08 -134.50
REMARK 500 6 PRO A 52 0.58 -69.77
REMARK 500 6 PRO A 62 3.83 -69.74
REMARK 500 6 TYR A 73 -39.06 -37.85
REMARK 500 6 SER A 82 107.00 -47.94
REMARK 500
REMARK 500 THIS ENTRY HAS 186 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002100880.1 RELATED DB: TARGETDB
DBREF 2D89 A 8 113 GB 45501001 AAH67215 408 513
SEQADV 2D89 GLY A 1 GB 45501001 CLONING ARTIFACT
SEQADV 2D89 SER A 2 GB 45501001 CLONING ARTIFACT
SEQADV 2D89 SER A 3 GB 45501001 CLONING ARTIFACT
SEQADV 2D89 GLY A 4 GB 45501001 CLONING ARTIFACT
SEQADV 2D89 SER A 5 GB 45501001 CLONING ARTIFACT
SEQADV 2D89 SER A 6 GB 45501001 CLONING ARTIFACT
SEQADV 2D89 GLY A 7 GB 45501001 CLONING ARTIFACT
SEQADV 2D89 SER A 114 GB 45501001 CLONING ARTIFACT
SEQADV 2D89 GLY A 115 GB 45501001 CLONING ARTIFACT
SEQADV 2D89 PRO A 116 GB 45501001 CLONING ARTIFACT
SEQADV 2D89 SER A 117 GB 45501001 CLONING ARTIFACT
SEQADV 2D89 SER A 118 GB 45501001 CLONING ARTIFACT
SEQADV 2D89 GLY A 119 GB 45501001 CLONING ARTIFACT
SEQRES 1 A 119 GLY SER SER GLY SER SER GLY PRO ASN ALA SER GLN SER
SEQRES 2 A 119 LEU LEU VAL TRP CYS LYS GLU VAL THR LYS ASN TYR ARG
SEQRES 3 A 119 GLY VAL LYS ILE THR ASN PHE THR THR SER TRP ARG ASN
SEQRES 4 A 119 GLY LEU SER PHE CYS ALA ILE LEU HIS HIS PHE ARG PRO
SEQRES 5 A 119 ASP LEU ILE ASP TYR LYS SER LEU ASN PRO GLN ASP ILE
SEQRES 6 A 119 LYS GLU ASN ASN LYS LYS ALA TYR ASP GLY PHE ALA SER
SEQRES 7 A 119 ILE GLY ILE SER ARG LEU LEU GLU PRO SER ASP MET VAL
SEQRES 8 A 119 LEU LEU ALA ILE PRO ASP LYS LEU THR VAL MET THR TYR
SEQRES 9 A 119 LEU TYR GLN ILE ARG ALA HIS PHE SER SER GLY PRO SER
SEQRES 10 A 119 SER GLY
HELIX 1 1 ALA A 10 THR A 22 1 13
HELIX 2 2 THR A 34 ASN A 39 1 6
HELIX 3 3 GLY A 40 ARG A 51 1 12
HELIX 4 4 ASP A 56 LEU A 60 5 5
HELIX 5 5 ILE A 65 ALA A 77 1 13
HELIX 6 6 GLU A 86 LEU A 93 1 8
HELIX 7 7 ASP A 97 SER A 113 1 17
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