Header list of 1vii.pdb file
Complete list - 2 202 Bytes
HEADER ACTIN BINDING 15-JAN-97 1VII
TITLE THERMOSTABLE SUBDOMAIN FROM CHICKEN VILLIN HEADPIECE, NMR, MINIMIZED
TITLE 2 AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VILLIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THERMOSTABLE SUBDOMAIN;
COMPND 5 SYNONYM: HP-36, R42-76;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 ORGAN: INTESTINE;
SOURCE 6 TISSUE: EPITHELIUM;
SOURCE 7 CELL: EPITHELIAL;
SOURCE 8 CELLULAR_LOCATION: MICROVILLI;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 12 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PVHP42-76B
KEYWDS ACTIN BINDING, 3 HELIX MOTIF, THERMOSTABLE SUBDOMAIN
EXPDTA SOLUTION NMR
AUTHOR C.J.MCKNIGHT
REVDAT 4 02-MAR-22 1VII 1 REMARK
REVDAT 3 24-FEB-09 1VII 1 VERSN
REVDAT 2 01-APR-03 1VII 1 JRNL
REVDAT 1 12-AUG-97 1VII 0
JRNL AUTH C.J.MCKNIGHT,P.T.MATSUDAIRA,P.S.KIM
JRNL TITL NMR STRUCTURE OF THE 35-RESIDUE VILLIN HEADPIECE SUBDOMAIN.
JRNL REF NAT.STRUCT.BIOL. V. 4 180 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9164455
JRNL DOI 10.1038/NSB0397-180
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.J.MCKNIGHT,D.S.DOERING,P.T.MATSUDAIRA,P.S.KIM
REMARK 1 TITL A THERMOSTABLE 35-RESIDUE SUBDOMAIN WITHIN VILLIN HEADPIECE
REMARK 1 REF J.MOL.BIOL. V. 260 126 1996
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE X-PLOR (R6)1/6 NOE POTENTIAL WAS
REMARK 3 USED FOR NOE'S INVOLVING NON-STEREOSPECIFICALLY ASSIGNED METHYL,
REMARK 3 METHYLENE, AND AROMATIC PROTONS. NO ATTRACTIVE POTENTIALS WERE
REMARK 3 USED IN CALCULATING THE STRUCTURES. THE VAN DER WAALS CUTOFF
REMARK 3 USED FOR THE X-PLOR REPEL FUNCTION WAS 0.75 ANGSTROMS. AFTER
REMARK 3 DISTANCE GEOMETRY AND REGULARIZATION, EACH STRUCTURE WAS
REMARK 3 SUBJECTED TO ONE ROUND OF SIMULATED ANNEALING FROM 2000K TO 100K
REMARK 3 OVER 2000 STEPS. THIS IS THE AVERAGE OF 29 STRUCTURES MINIMIZED
REMARK 3 USING ONLY REPULSIVE POTENTIALS.
REMARK 4
REMARK 4 1VII COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177045.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 3.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; CLEANTOCSY; DQFCOSY;
REMARK 210 HSQC; ECOSY; HMQCJ
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATIONS > 0.4
REMARK 210 ANGSTROMS, NO ANGLE VIOLATION >
REMARK 210 5 DEG
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 LYS A 70 O LYS A 73 2.10
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 ASP A 44 -75.64 -33.48
REMARK 500 ALA A 49 39.36 -79.38
REMARK 500 VAL A 50 -78.92 -140.77
REMARK 500 PHE A 51 -72.80 -79.65
REMARK 500 MET A 53 -121.66 -90.62
REMARK 500 GLN A 66 -77.13 -68.88
REMARK 500 GLN A 67 -36.61 -37.79
REMARK 500 ASN A 68 -73.49 -67.77
REMARK 500 LYS A 70 -80.30 -71.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ABR
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: RESIDUES IMPLICATED IN ACTIN BINDING.
DBREF 1VII A 42 76 UNP P02640 VILI_CHICK 792 826
SEQRES 1 A 36 MET LEU SER ASP GLU ASP PHE LYS ALA VAL PHE GLY MET
SEQRES 2 A 36 THR ARG SER ALA PHE ALA ASN LEU PRO LEU TRP LYS GLN
SEQRES 3 A 36 GLN ASN LEU LYS LYS GLU LYS GLY LEU PHE
HELIX 1 1 ASP A 44 LYS A 48 1 5
HELIX 2 2 ARG A 55 PHE A 58 1 4
HELIX 3 3 LEU A 63 GLU A 72 1 10
SITE 1 ABR 7 LYS A 65 LYS A 70 LYS A 71 GLU A 72
SITE 2 ABR 7 LYS A 73 LEU A 75 PHE A 76
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
Complete list - 2 202 Bytes