Header list of 1zr7.pdb file
Complete list - 2 20 Bytes
HEADER SIGNALING PROTEIN 19-MAY-05 1ZR7
TITLE SOLUTION STRUCTURE OF THE FIRST WW DOMAIN OF FBP11
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUNTINGTIN-INTERACTING PROTEIN HYPA/FBP11;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES IN DATABASE 150-177;
COMPND 5 SYNONYM: FORMIN BINDING PROTEIN 11 (FBP11)/HUNTINGTIN YEAST PARTNER A
COMPND 6 (HYPA);
COMPND 7 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: FBP11;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS BETA SHEET, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR Y.KATO,Y.HINO,M.TANOKURA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1ZR7 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1ZR7 1 VERSN
REVDAT 1 30-MAY-06 1ZR7 0
JRNL AUTH Y.KATO,Y.HINO,K.NAGATA,M.TANOKURA
JRNL TITL SOLUTION STRUCTURE AND BINDING SPECIFICITY OF FBP11/HYPA WW
JRNL TITL 2 DOMAIN AS GROUP-II/III
JRNL REF PROTEINS V. 63 227 2006
JRNL REFN ISSN 0887-3585
JRNL PMID 16463264
JRNL DOI 10.1002/PROT.20880
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0, CYANA 2.0
REMARK 3 AUTHORS : GUNTERT (CYANA), GUNTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZR7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000033024.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 0.175
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM FBP11 WW1 U-15N, 13C; 50MM
REMARK 210 PHOSPHATE BUFFER NA; 50MM NACL,
REMARK 210 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
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
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 11 23.22 -141.53
REMARK 500 1 ASP A 38 44.79 -108.16
REMARK 500 3 PRO A 37 79.10 -69.77
REMARK 500 3 ASP A 38 -73.92 -127.29
REMARK 500 5 PRO A 37 78.62 -69.73
REMARK 500 6 SER A 11 31.77 -142.98
REMARK 500 7 SER A 11 24.56 -151.15
REMARK 500 7 PRO A 37 83.29 -69.75
REMARK 500 10 PRO A 37 78.76 -69.76
REMARK 500 11 SER A 11 23.81 -143.97
REMARK 500 13 PRO A 37 80.60 -69.79
REMARK 500 14 SER A 11 26.18 -143.42
REMARK 500 15 PRO A 37 80.97 -69.78
REMARK 500 16 PRO A 37 79.46 -69.75
REMARK 500 18 PRO A 37 80.17 -69.77
REMARK 500 19 SER A 11 36.04 -141.06
REMARK 500 19 PRO A 37 79.48 -69.76
REMARK 500 20 ASP A 38 43.82 -100.22
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ZR7 A 12 39 GB 3341990 AAC27506 150 177
SEQADV 1ZR7 GLY A 10 GB 3341990 CLONING ARTIFACT
SEQADV 1ZR7 SER A 11 GB 3341990 CLONING ARTIFACT
SEQRES 1 A 30 GLY SER TRP THR GLU HIS LYS SER PRO ASP GLY ARG THR
SEQRES 2 A 30 TYR TYR TYR ASN THR GLU THR LYS GLN SER THR TRP GLU
SEQRES 3 A 30 LYS PRO ASP ASP
SHEET 1 A 3 TRP A 12 SER A 17 0
SHEET 2 A 3 ARG A 21 ASN A 26 -1 O TYR A 25 N THR A 13
SHEET 3 A 3 GLN A 31 THR A 33 -1 O THR A 33 N TYR A 24
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 - 2 20 Bytes