Header list of 1q8x.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 22-AUG-03 1Q8X
TITLE NMR STRUCTURE OF HUMAN COFILIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COFILIN, NON-MUSCLE ISOFORM;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 18 KDA PHOSPHOPROTEIN, P18;
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 GENE: CFL1 OR CFL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL27(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMW172
KEYWDS ADF/COFILIN, CHEMICAL SHIFT PERTURBATION, ACTIN CYTOSKELETON, G-ACTIN
KEYWDS 2 BINDING, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.J.POPE,K.M.ZIERLER-GOULD,R.KUHNE,A.G.WEEDS,L.J.BALL
REVDAT 3 02-MAR-22 1Q8X 1 REMARK
REVDAT 2 24-FEB-09 1Q8X 1 VERSN
REVDAT 1 06-JUL-04 1Q8X 0
JRNL AUTH B.J.POPE,K.M.ZIERLER-GOULD,R.KUHNE,A.G.WEEDS,L.J.BALL
JRNL TITL THE SOLUTION STRUCTURE OF HUMAN COFILIN: RATIONALIZING ACTIN
JRNL TITL 2 BINDING AND PH SENSITIVITY
JRNL REF J.BIOL.CHEM. V. 279 4840 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14627701
JRNL DOI 10.1074/JBC.M310148200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.3, CYANA 1.1
REMARK 3 AUTHORS : BRUKER AG (XWINNMR), GUENTHERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Q8X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000020064.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 1; 1
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8 MM COFILIN U-15N,13C; 10MM
REMARK 210 PHOSPHATE BUFFER; 90% H2O, 10%
REMARK 210 D2O; 1 MM COFILIN U-15N, 10MM
REMARK 210 PHOSPHATE BUFFER; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY; 2D
REMARK 210 TOCSY; DQF-COSY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 1.3, AZARA 2.1, ANSIG
REMARK 210 3.3, CYANA 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: 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 H PHE A 38 O TYR A 82 1.58
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 ALA A 2 36.28 -158.79
REMARK 500 1 VAL A 5 122.58 -174.37
REMARK 500 1 ASP A 9 -53.35 69.49
REMARK 500 1 LYS A 22 89.30 -57.57
REMARK 500 1 SER A 24 -78.47 -176.94
REMARK 500 1 GLU A 28 -45.89 -143.23
REMARK 500 1 LYS A 31 37.89 -95.20
REMARK 500 1 LYS A 44 32.10 70.86
REMARK 500 1 LYS A 45 28.89 -166.15
REMARK 500 1 LYS A 53 38.15 -144.09
REMARK 500 1 PHE A 71 -83.73 -60.79
REMARK 500 1 PRO A 76 172.82 -47.40
REMARK 500 1 LEU A 84 77.01 -105.25
REMARK 500 1 THR A 91 -176.47 -63.01
REMARK 500 1 GLU A 93 -60.37 -170.60
REMARK 500 1 PHE A 101 79.85 -106.63
REMARK 500 1 ILE A 102 89.71 -57.27
REMARK 500 1 PHE A 103 88.48 -68.62
REMARK 500 1 SER A 113 35.91 -161.72
REMARK 500 1 LYS A 114 -47.74 -144.14
REMARK 500 1 ILE A 116 -70.57 -78.94
REMARK 500 1 THR A 129 71.60 65.00
REMARK 500 1 LYS A 132 -81.45 -48.57
REMARK 500 1 LEU A 135 92.94 -165.69
REMARK 500 1 LYS A 144 34.62 -97.78
REMARK 500 1 GLU A 162 34.20 168.20
REMARK 500 1 LYS A 164 -59.84 172.79
REMARK 500 2 VAL A 7 159.98 -49.78
REMARK 500 2 ASP A 9 -58.11 70.19
REMARK 500 2 ARG A 21 166.90 57.48
REMARK 500 2 SER A 23 -167.93 -161.86
REMARK 500 2 SER A 24 -78.03 -174.61
REMARK 500 2 GLU A 28 -45.86 -143.61
REMARK 500 2 ARG A 32 -167.01 -61.34
REMARK 500 2 SER A 41 -175.51 -59.05
REMARK 500 2 LYS A 44 34.41 70.65
REMARK 500 2 LYS A 45 29.09 -173.48
REMARK 500 2 GLU A 51 -45.07 -136.31
REMARK 500 2 GLN A 62 -78.20 -120.53
REMARK 500 2 PHE A 71 -79.54 -58.32
REMARK 500 2 PRO A 76 167.19 -47.86
REMARK 500 2 ALA A 83 128.63 -178.51
REMARK 500 2 ALA A 87 85.64 -56.65
REMARK 500 2 SER A 94 -169.42 -178.52
REMARK 500 2 ILE A 102 93.04 -58.01
REMARK 500 2 GLU A 107 63.70 -69.37
REMARK 500 2 SER A 108 -24.35 -166.36
REMARK 500 2 SER A 113 36.58 -159.85
REMARK 500 2 LYS A 114 -45.48 -145.72
REMARK 500 2 TYR A 117 -59.49 -123.88
REMARK 500
REMARK 500 THIS ENTRY HAS 599 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Q8G RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN COFILIN
DBREF 1Q8X A 1 166 UNP P23528 COF1_HUMAN 1 166
SEQRES 1 A 166 MET ALA SER GLY VAL ALA VAL SER ASP GLY VAL ILE LYS
SEQRES 2 A 166 VAL PHE ASN ASP MET LYS VAL ARG LYS SER SER THR PRO
SEQRES 3 A 166 GLU GLU VAL LYS LYS ARG LYS LYS ALA VAL LEU PHE CYS
SEQRES 4 A 166 LEU SER GLU ASP LYS LYS ASN ILE ILE LEU GLU GLU GLY
SEQRES 5 A 166 LYS GLU ILE LEU VAL GLY ASP VAL GLY GLN THR VAL ASP
SEQRES 6 A 166 ASP PRO TYR ALA THR PHE VAL LYS MET LEU PRO ASP LYS
SEQRES 7 A 166 ASP CYS ARG TYR ALA LEU TYR ASP ALA THR TYR GLU THR
SEQRES 8 A 166 LYS GLU SER LYS LYS GLU ASP LEU VAL PHE ILE PHE TRP
SEQRES 9 A 166 ALA PRO GLU SER ALA PRO LEU LYS SER LYS MET ILE TYR
SEQRES 10 A 166 ALA SER SER LYS ASP ALA ILE LYS LYS LYS LEU THR GLY
SEQRES 11 A 166 ILE LYS HIS GLU LEU GLN ALA ASN CYS TYR GLU GLU VAL
SEQRES 12 A 166 LYS ASP ARG CYS THR LEU ALA GLU LYS LEU GLY GLY SER
SEQRES 13 A 166 ALA VAL ILE SER LEU GLU GLY LYS PRO LEU
HELIX 1 1 ASP A 9 VAL A 20 1 12
HELIX 2 2 GLU A 28 LYS A 31 5 4
HELIX 3 3 GLY A 58 GLN A 62 5 5
HELIX 4 4 ASP A 66 MET A 74 1 9
HELIX 5 5 PRO A 110 SER A 113 5 4
HELIX 6 6 LYS A 114 THR A 129 1 16
HELIX 7 7 CYS A 139 LYS A 144 1 6
HELIX 8 8 ASP A 145 ALA A 150 1 6
SHEET 1 A 2 LYS A 33 LEU A 40 0
SHEET 2 A 2 ILE A 47 LEU A 56 -1 O ILE A 55 N ALA A 35
SHEET 1 B 3 ARG A 81 ALA A 83 0
SHEET 2 B 3 LYS A 95 TRP A 104 -1 O ILE A 102 N ALA A 83
SHEET 3 B 3 ASP A 86 GLU A 90 -1 N TYR A 89 O LYS A 96
SHEET 1 C 3 ARG A 81 ALA A 83 0
SHEET 2 C 3 LYS A 95 TRP A 104 -1 O ILE A 102 N ALA A 83
SHEET 3 C 3 HIS A 133 GLU A 134 1 O HIS A 133 N PHE A 101
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 2 2 Bytes