Header list of 1ak6.pdb file
Complete list - 16 20 Bytes
HEADER ACTIN-BINDING PROTEIN 29-MAY-97 1AK6
TITLE DESTRIN, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DESTRIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: HUMAN, PIG;
SOURCE 4 ORGANISM_TAXID: 9606,9823;
SOURCE 5 STRAIN: ,;
SOURCE 6 CELLULAR_LOCATION: CYTOPLASM AND NUCLEUS;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKID-W
KEYWDS ACTIN DEPOLYMERIZATION FACTOR, ACTIN-BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR H.HATANAKA,K.MORIYAMA,K.OGURA,S.ICHIKAWA,I.YAHARA,F.INAGAKI
REVDAT 3 16-FEB-22 1AK6 1 REMARK
REVDAT 2 24-FEB-09 1AK6 1 VERSN
REVDAT 1 12-NOV-97 1AK6 0
JRNL AUTH H.HATANAKA,K.OGURA,K.MORIYAMA,S.ICHIKAWA,I.YAHARA,F.INAGAKI
JRNL TITL TERTIARY STRUCTURE OF DESTRIN AND STRUCTURAL SIMILARITY
JRNL TITL 2 BETWEEN TWO ACTIN-REGULATING PROTEIN FAMILIES.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 85 1047 1996
JRNL REFN ISSN 0092-8674
JRNL PMID 8674111
JRNL DOI 10.1016/S0092-8674(00)81305-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1AK6 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_1000170917.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; HN(CO)CA; HNCA; CBCACONH;
REMARK 210 CBCANH; HBHA(CO)NH; HN(CA)HA;
REMARK 210 C(CO)NH; HC(C)H-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS 600
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST FNOE+FREPEL
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 HA PRO A 26 HB ILE A 29 1.34
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 SER A -3 34.66 -93.51
REMARK 500 ASN A 0 -36.30 -141.76
REMARK 500 ALA A 2 43.03 -102.57
REMARK 500 SER A 3 99.59 47.48
REMARK 500 VAL A 5 -158.68 -58.08
REMARK 500 GLN A 6 17.60 -151.68
REMARK 500 VAL A 7 176.89 50.36
REMARK 500 ASP A 9 -39.47 83.80
REMARK 500 LYS A 19 -83.04 -44.84
REMARK 500 VAL A 20 -114.79 -146.98
REMARK 500 LYS A 22 89.96 -52.16
REMARK 500 CYS A 23 86.70 -159.58
REMARK 500 SER A 24 -64.22 -16.11
REMARK 500 GLU A 28 -31.97 -147.30
REMARK 500 LYS A 33 113.14 65.90
REMARK 500 LYS A 34 -52.76 -132.82
REMARK 500 CYS A 39 33.18 170.53
REMARK 500 LEU A 40 120.70 80.25
REMARK 500 SER A 41 -156.91 -52.74
REMARK 500 ASP A 43 -15.23 83.74
REMARK 500 LYS A 44 95.26 80.01
REMARK 500 LYS A 45 -112.07 -161.91
REMARK 500 CYS A 46 126.56 -27.83
REMARK 500 ILE A 48 134.81 -170.83
REMARK 500 VAL A 49 92.58 -68.16
REMARK 500 GLU A 50 84.64 -155.00
REMARK 500 GLU A 51 -29.80 -179.05
REMARK 500 LYS A 53 -138.71 -135.22
REMARK 500 GLU A 54 139.05 75.43
REMARK 500 VAL A 57 -56.28 76.67
REMARK 500 VAL A 60 93.22 -33.46
REMARK 500 VAL A 62 -91.13 -114.01
REMARK 500 ILE A 64 -165.98 -121.90
REMARK 500 THR A 65 26.50 -164.60
REMARK 500 ASP A 66 -15.49 98.57
REMARK 500 PRO A 67 -118.52 -76.47
REMARK 500 PHE A 68 -32.47 -168.70
REMARK 500 PRO A 76 -164.25 -79.83
REMARK 500 ARG A 81 168.73 161.27
REMARK 500 ASP A 86 99.78 -46.15
REMARK 500 GLU A 90 -142.33 -77.36
REMARK 500 THR A 91 -179.87 157.21
REMARK 500 SER A 94 -176.28 100.90
REMARK 500 ARG A 95 99.87 -42.42
REMARK 500 LEU A 99 174.01 -47.08
REMARK 500 LEU A 103 47.10 -86.86
REMARK 500 TRP A 104 97.46 -40.48
REMARK 500 ALA A 109 169.81 -42.42
REMARK 500 ASP A 122 -40.12 179.01
REMARK 500 PHE A 128 36.57 -97.17
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
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 ARG A 13 0.26 SIDE CHAIN
REMARK 500 ARG A 21 0.30 SIDE CHAIN
REMARK 500 ARG A 32 0.10 SIDE CHAIN
REMARK 500 ARG A 81 0.32 SIDE CHAIN
REMARK 500 ARG A 145 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AK7 RELATED DB: PDB
DBREF 1AK6 A 2 165 UNP P60982 DEST_PIG 2 165
SEQRES 1 A 174 THR MET ILE THR PRO SER SER GLY ASN SER ALA SER GLY
SEQRES 2 A 174 VAL GLN VAL ALA ASP GLU VAL CYS ARG ILE PHE TYR ASP
SEQRES 3 A 174 MET LYS VAL ARG LYS CYS SER THR PRO GLU GLU ILE LYS
SEQRES 4 A 174 LYS ARG LYS LYS ALA VAL ILE PHE CYS LEU SER ALA ASP
SEQRES 5 A 174 LYS LYS CYS ILE ILE VAL GLU GLU GLY LYS GLU ILE LEU
SEQRES 6 A 174 VAL GLY ASP VAL GLY VAL THR ILE THR ASP PRO PHE LYS
SEQRES 7 A 174 HIS PHE VAL GLY MET LEU PRO GLU LYS ASP CYS ARG TYR
SEQRES 8 A 174 ALA LEU TYR ASP ALA SER PHE GLU THR LYS GLU SER ARG
SEQRES 9 A 174 LYS GLU GLU LEU MET PHE PHE LEU TRP ALA PRO GLU LEU
SEQRES 10 A 174 ALA PRO LEU LYS SER LYS MET ILE TYR ALA SER SER LYS
SEQRES 11 A 174 ASP ALA ILE LYS LYS LYS PHE GLN GLY ILE LYS HIS GLU
SEQRES 12 A 174 CYS GLN ALA ASN GLY PRO GLU ASP LEU ASN ARG ALA CYS
SEQRES 13 A 174 ILE ALA GLU LYS LEU GLY GLY SER LEU ILE VAL ALA PHE
SEQRES 14 A 174 GLU GLY CYS PRO VAL
HELIX 1 H1 ASP A 9 ASP A 17 1 9
HELIX 2 H2 PRO A 26 LYS A 30 1 5
HELIX 3 H3 VAL A 57 VAL A 60 1 4
HELIX 4 H4 PHE A 68 LEU A 75 1 8
HELIX 5 H5 LEU A 111 PHE A 128 1 18
HELIX 6 H6 ARG A 145 GLY A 154 1 10
SHEET 1 S1 4 HIS A 133 ASN A 138 0
SHEET 2 S1 4 GLU A 97 PRO A 106 1 O PHE A 101 N CYS A 135
SHEET 3 S1 4 TYR A 82 GLU A 90 -1 O ALA A 83 N PHE A 102
SHEET 4 S1 4 ALA A 35 CYS A 39 -1 O VAL A 36 N LEU A 84
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 - 16 20 Bytes