Header list of 1unc.pdb file
Complete list - r 25 2 Bytes
HEADER ACTIN BINDING 09-SEP-03 1UNC
TITLE SOLUTION STRUCTURE OF THE HUMAN VILLIN C-TERMINAL
TITLE 2 HEADPIECE SUBDOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VILLIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HEADPIECE SUBDOMAIN, RESIDUES 792-826;
COMPND 5 SYNONYM: VILLIN
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 ORGAN: INTESTINE;
SOURCE 7 TISSUE: BRUSH BORDER EPITHELIA;
SOURCE 8 CELL: BRUSH BORDER CELL
KEYWDS ACTIN BINDING, F-ACTIN BINDING, CYTOSKELETON, HEADPIECE
KEYWDS 2 SUBDOMAIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR W.VERMEULEN,M.VAN TROYS,P.VANHAESEBROUCK,M.VERSCHUEREN,
AUTHOR 2 F.FANT,C.AMPE,J.MARTINS,F.BORREMANS
REVDAT 2 24-FEB-09 1UNC 1 VERSN
REVDAT 1 15-JUL-04 1UNC 0
JRNL AUTH W.VERMEULEN,P.VANHAESEBROUCK,M.VAN TROYS,
JRNL AUTH 2 M.VERSCHUEREN,F.FANT,M.GOETHALS,C.AMPE,J.MARTINS,
JRNL AUTH 3 F.BORREMANS
JRNL TITL SOLUTION STRUCTURES OF THE C-TERMINAL HEADPIECE
JRNL TITL 2 SUBDOMAINS OF HUMAN VILLIN AND ADVILLIN,
JRNL TITL 3 EVALUATION OF HEADPIECE F-ACTIN-BINDING
JRNL TITL 4 REQUIREMENTS
JRNL REF PROTEIN SCI. V. 13 1276 2004
JRNL REFN ISSN 0961-8368
JRNL PMID 15096633
JRNL DOI 10.1110/PS.03518104
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : INSIGHT2
REMARK 3 AUTHORS : ACCELRYS
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: AMBER FORCEFIELD REFINEMENT USING
REMARK 3 SIMULATED ANNEALING
REMARK 4
REMARK 4 1UNC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-SEP-03.
REMARK 100 THE PDBE ID CODE IS EBI-13459.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 294
REMARK 210 PH : 4.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY, TOCSY, DQF-COSY,
REMARK 210 E.COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D-1H NMR
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HE2 PHE A 6 - HA PRO A 14 1.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 4 CD GLU A 4 OE2 0.111
REMARK 500 1 GLU A 31 CD GLU A 31 OE2 0.112
REMARK 500 2 GLU A 4 CD GLU A 4 OE2 0.111
REMARK 500 2 GLU A 31 CD GLU A 31 OE2 0.112
REMARK 500 3 GLU A 4 CD GLU A 4 OE2 0.112
REMARK 500 3 GLU A 31 CD GLU A 31 OE2 0.113
REMARK 500 4 GLU A 4 CD GLU A 4 OE2 0.112
REMARK 500 4 GLU A 31 CD GLU A 31 OE2 0.112
REMARK 500 5 GLU A 4 CD GLU A 4 OE2 0.112
REMARK 500 5 GLU A 31 CD GLU A 31 OE2 0.111
REMARK 500 6 GLU A 4 CD GLU A 4 OE2 0.112
REMARK 500 6 GLU A 31 CD GLU A 31 OE2 0.112
REMARK 500 7 GLU A 4 CD GLU A 4 OE2 0.112
REMARK 500 7 GLU A 31 CD GLU A 31 OE2 0.111
REMARK 500 8 GLU A 4 CD GLU A 4 OE2 0.110
REMARK 500 8 GLU A 31 CD GLU A 31 OE2 0.112
REMARK 500 9 GLU A 4 CD GLU A 4 OE2 0.113
REMARK 500 9 GLU A 31 CD GLU A 31 OE2 0.112
REMARK 500 10 GLU A 4 CD GLU A 4 OE2 0.113
REMARK 500 10 GLU A 31 CD GLU A 31 OE2 0.113
REMARK 500 11 GLU A 4 CD GLU A 4 OE2 0.111
REMARK 500 11 GLU A 31 CD GLU A 31 OE2 0.112
REMARK 500 12 GLU A 4 CD GLU A 4 OE2 0.113
REMARK 500 12 GLU A 31 CD GLU A 31 OE2 0.112
REMARK 500 13 GLU A 4 CD GLU A 4 OE2 0.113
REMARK 500 13 GLU A 31 CD GLU A 31 OE2 0.112
REMARK 500 14 GLU A 4 CD GLU A 4 OE2 0.112
REMARK 500 14 GLU A 31 CD GLU A 31 OE2 0.112
REMARK 500 15 GLU A 4 CD GLU A 4 OE2 0.112
REMARK 500 15 GLU A 31 CD GLU A 31 OE2 0.111
REMARK 500 16 GLU A 4 CD GLU A 4 OE2 0.112
REMARK 500 16 GLU A 31 CD GLU A 31 OE2 0.112
REMARK 500 17 GLU A 4 CD GLU A 4 OE2 0.111
REMARK 500 17 GLU A 31 CD GLU A 31 OE2 0.111
REMARK 500 18 GLU A 4 CD GLU A 4 OE2 0.112
REMARK 500 18 GLU A 31 CD GLU A 31 OE2 0.111
REMARK 500 19 GLU A 4 CD GLU A 4 OE2 0.112
REMARK 500 19 GLU A 31 CD GLU A 31 OE2 0.111
REMARK 500 20 GLU A 4 CD GLU A 4 OE2 0.111
REMARK 500 20 GLU A 31 CD GLU A 31 OE2 0.111
REMARK 500 21 GLU A 4 CD GLU A 4 OE2 0.111
REMARK 500 21 GLU A 31 CD GLU A 31 OE2 0.111
REMARK 500 22 GLU A 4 CD GLU A 4 OE2 0.111
REMARK 500 22 GLU A 31 CD GLU A 31 OE2 0.111
REMARK 500 23 GLU A 4 CD GLU A 4 OE2 0.113
REMARK 500 23 GLU A 31 CD GLU A 31 OE2 0.111
REMARK 500 24 GLU A 4 CD GLU A 4 OE2 0.110
REMARK 500 24 GLU A 31 CD GLU A 31 OE2 0.112
REMARK 500 25 GLU A 4 CD GLU A 4 OE2 0.111
REMARK 500 25 GLU A 31 CD GLU A 31 OE2 0.111
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 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 ALA A 9 36.42 -88.42
REMARK 500 2 ALA A 9 39.91 -85.87
REMARK 500 2 LEU A 34 -72.32 -72.19
REMARK 500 4 SER A 2 163.04 64.58
REMARK 500 10 SER A 2 120.10 59.51
REMARK 500 10 LEU A 34 -74.78 -68.55
REMARK 500 21 LEU A 34 -73.74 -81.01
REMARK 500 24 LEU A 34 -70.77 -77.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 PHE A 6 0.13 SIDE CHAIN
REMARK 500 3 PHE A 10 0.10 SIDE CHAIN
REMARK 500 4 PHE A 6 0.11 SIDE CHAIN
REMARK 500 7 PHE A 6 0.12 SIDE CHAIN
REMARK 500 8 PHE A 6 0.09 SIDE CHAIN
REMARK 500 9 PHE A 6 0.11 SIDE CHAIN
REMARK 500 10 PHE A 6 0.11 SIDE CHAIN
REMARK 500 11 PHE A 6 0.11 SIDE CHAIN
REMARK 500 12 PHE A 6 0.12 SIDE CHAIN
REMARK 500 13 PHE A 6 0.09 SIDE CHAIN
REMARK 500 15 PHE A 6 0.10 SIDE CHAIN
REMARK 500 16 PHE A 6 0.11 SIDE CHAIN
REMARK 500 17 PHE A 6 0.13 SIDE CHAIN
REMARK 500 18 PHE A 6 0.10 SIDE CHAIN
REMARK 500 19 PHE A 6 0.12 SIDE CHAIN
REMARK 500 20 PHE A 6 0.11 SIDE CHAIN
REMARK 500 21 PHE A 6 0.09 SIDE CHAIN
REMARK 500 24 PHE A 6 0.11 SIDE CHAIN
REMARK 500 25 PHE A 6 0.14 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1UNC A 0 0 PDB 1UNC 1UNC 0 0
DBREF 1UNC A 1 35 UNP P09327 VIL1_HUMAN 792 826
SEQRES 1 A 36 ACE LEU SER ILE GLU ASP PHE THR GLN ALA PHE GLY MET
SEQRES 2 A 36 THR PRO ALA ALA PHE SER ALA LEU PRO ARG TRP LYS GLN
SEQRES 3 A 36 GLN ASN LEU LYS LYS GLU LYS GLY LEU PHE
HET ACE A 0 6
HETNAM ACE ACETYL GROUP
FORMUL 2 ACE C2 H4 O
HELIX 1 1 SER A 2 ALA A 9 1 8
HELIX 2 2 THR A 13 LEU A 20 1 8
HELIX 3 3 PRO A 21 LYS A 32 1 12
LINK C ACE A 0 N LEU A 1 1555 1555 1.34
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 25 2 Bytes