Header list of 1zv6.pdb file
Complete list - t 20 2 Bytes
HEADER PROTEIN BINDING 01-JUN-05 1ZV6
TITLE NMR STRUCTURE OF THE HUMAN DEMATIN HEADPIECE S74E MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPB49 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 316-383;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PD48
KEYWDS DEMATIN HEADPIECE, ACTIN BINDING DOMAIN, PHOSPHORYLATION, PROTEIN
KEYWDS 2 BINDING
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR Z.G.JIANG,C.J.MCKNIGHT
REVDAT 3 20-OCT-21 1ZV6 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1ZV6 1 VERSN
REVDAT 1 21-MAR-06 1ZV6 0
JRNL AUTH Z.G.JIANG,C.J.MCKNIGHT
JRNL TITL A PHOSPHORYLATION-INDUCED CONFORMATION CHANGE IN DEMATIN
JRNL TITL 2 HEADPIECE.
JRNL REF STRUCTURE V. 14 379 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16472756
JRNL DOI 10.1016/J.STR.2005.11.007
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : MOLMOL 2K.2, CNS 1.0
REMARK 3 AUTHORS : KORADI (MOLMOL), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1449 RESTRAINTS: 1289 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 142
REMARK 3 ARE DIHEDRAL ANGLE RESTRAINTS, AND 18 ARE DISTANCE RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1ZV6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033157.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 10 MM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM DHPS74E U-15N,13C U-15N; 1
REMARK 210 MM DHPS74E 10% 13C, U- 15N, 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; HNCA-J;
REMARK 210 HNCOCA; 2D NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHA; HNHB; 2D
REMARK 210 TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2004 VERSION, XWINNMR
REMARK 210 3.1, NMRVIEW 5.0.4.
REMARK 210 METHOD USED : DISTANCE GEOMETRY/SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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. MODEL 1 REPRESENTS MINIMIZED AVERAGE STRUCTURE.
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O LEU A 69 H ALA A 73 1.56
REMARK 500
REMARK 500 REMARK: NULL
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 VAL A 21 -68.84 -92.42
REMARK 500 1 ARG A 26 -72.87 -145.57
REMARK 500 1 LYS A 28 26.67 -73.68
REMARK 500 1 PRO A 30 -176.14 -57.82
REMARK 500 1 ARG A 37 43.03 -142.08
REMARK 500 1 GLU A 39 0.50 -69.55
REMARK 500 1 LEU A 61 -141.94 -79.40
REMARK 500 2 PRO A 15 166.60 -47.95
REMARK 500 2 VAL A 21 -67.42 -102.03
REMARK 500 2 THR A 27 -87.24 -50.70
REMARK 500 2 LYS A 28 23.13 48.34
REMARK 500 2 PRO A 30 -170.62 -54.11
REMARK 500 2 ARG A 37 36.73 -141.03
REMARK 500 2 LEU A 61 -145.89 -79.94
REMARK 500 3 PRO A 15 170.11 -52.00
REMARK 500 3 VAL A 21 -66.67 -100.87
REMARK 500 3 THR A 22 -64.83 -105.07
REMARK 500 3 ARG A 26 -46.64 -149.91
REMARK 500 3 THR A 27 20.62 -163.85
REMARK 500 3 LYS A 28 26.69 -70.41
REMARK 500 3 PRO A 30 -174.36 -60.34
REMARK 500 3 LEU A 61 -145.11 -80.07
REMARK 500 4 PRO A 15 166.94 -46.67
REMARK 500 4 VAL A 21 -67.78 -102.13
REMARK 500 4 ARG A 26 -158.00 -137.57
REMARK 500 4 LYS A 28 25.48 39.55
REMARK 500 4 PRO A 30 -173.00 -56.00
REMARK 500 4 ARG A 37 50.23 -143.33
REMARK 500 4 ALA A 52 -3.02 80.90
REMARK 500 4 LEU A 61 -144.31 -84.84
REMARK 500 5 PRO A 15 170.70 -51.17
REMARK 500 5 VAL A 21 -67.63 -102.41
REMARK 500 5 ARG A 26 -158.53 -138.23
REMARK 500 5 LYS A 28 25.23 39.65
REMARK 500 5 PRO A 30 -171.36 -56.10
REMARK 500 5 ARG A 37 44.43 -145.82
REMARK 500 5 ALA A 52 -3.07 90.32
REMARK 500 5 LEU A 61 -141.60 -80.92
REMARK 500 6 PRO A 15 170.92 -51.06
REMARK 500 6 VAL A 21 -65.91 -102.40
REMARK 500 6 ARG A 26 -53.33 -132.93
REMARK 500 6 THR A 27 -57.17 -150.29
REMARK 500 6 LYS A 28 23.22 41.88
REMARK 500 6 PRO A 30 -173.68 -55.38
REMARK 500 6 ARG A 37 41.91 -147.20
REMARK 500 6 GLU A 39 7.07 -68.31
REMARK 500 6 LEU A 61 -141.51 -80.63
REMARK 500 7 VAL A 21 -67.62 -102.19
REMARK 500 7 THR A 22 -61.76 -105.88
REMARK 500 7 ASN A 23 -33.38 -33.80
REMARK 500
REMARK 500 THIS ENTRY HAS 166 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QZP RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE HUMAN DEMATIN HEADPIECE DOMAIN
REMARK 900 RELATED ID: 1QQV RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN
REMARK 900 RELATED ID: 1VII RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE THERMOSTABLE, 35-RESIDUE SUBDOMAIN FROM
REMARK 900 CHICKEN VILLIN HEADPIECE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE DHPS74E CONSTRUCT SPANS RESIDUES 316 TO 383 OF THE 48
REMARK 999 KDA FORM OF HUMAN DEMATIN, WITH SER74 REPLACED BY GLU.
REMARK 999 TO FACILITATE THE COMPARISON WITH OTHER HEADPIECE DOMAINS,
REMARK 999 WE USE THE NUMBERING SCHEME FROM VARDAR ET AL., 1999,
REMARK 999 J.MOLEC.BIOL., 294, 1299-1310, SUCH THAT THE N-TERMINAL
REMARK 999 PROLINE OF DHP IS RESIDUE 9, AND C-TERMINAL PHENYLALANINE
REMARK 999 IS RESIDUE 76. THE FINAL RESIDUE (F76) IS THE NATURAL
REMARK 999 C-TERMINAL RESIDUE OF DEMATIN.
DBREF 1ZV6 A 9 76 GB 31127246 AAH52805 316 383
SEQADV 1ZV6 GLU A 74 GB 31127246 SER 381 ENGINEERED MUTATION
SEQRES 1 A 68 PRO GLY LEU GLN ILE TYR PRO TYR GLU MET LEU VAL VAL
SEQRES 2 A 68 THR ASN LYS GLY ARG THR LYS LEU PRO PRO GLY VAL ASP
SEQRES 3 A 68 ARG MET ARG LEU GLU ARG HIS LEU SER ALA GLU ASP PHE
SEQRES 4 A 68 SER ARG VAL PHE ALA MET SER PRO GLU GLU PHE GLY LYS
SEQRES 5 A 68 LEU ALA LEU TRP LYS ARG ASN GLU LEU LYS LYS LYS ALA
SEQRES 6 A 68 GLU LEU PHE
HELIX 1 1 TYR A 16 VAL A 20 5 5
HELIX 2 2 ASP A 34 MET A 36 5 3
HELIX 3 3 ARG A 37 LEU A 42 1 6
HELIX 4 4 SER A 43 PHE A 51 1 9
HELIX 5 5 SER A 54 LEU A 61 1 8
HELIX 6 6 ALA A 62 ALA A 73 1 12
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
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