Header list of 1tmw.pdb file
Complete list - v 10 2 Bytes
HEADER PROTEIN BINDING 11-JUN-04 1TMW
TITLE SOLUTION STRUCTURE OF HUMAN COACTOSIN LIKE PROTEIN D123N
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COACTOSIN-LIKE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: 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: PET22B(+)
KEYWDS COACTOSIN-LIKE PROTEIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.DAI,J.WU,Y.XU,Y.TANG,H.DING,Y.SHI
REVDAT 3 10-NOV-21 1TMW 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1TMW 1 VERSN
REVDAT 1 28-JUN-05 1TMW 0
JRNL AUTH H.DAI,J.WU,Y.XU,Y.TANG,H.DING,Y.SHI
JRNL TITL STUDY ON SOLUTION STRUCTURE AND ITS BINDING FUNCTION TO
JRNL TITL 2 F-ACTIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.2, MOLMOL 2K.2
REMARK 3 AUTHORS : F. DELAGLIO (NMRPIPE), KORADI (MOLMOL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TMW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022772.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 50MM NAH2PO4, 50MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5MM HUMAN COACTOSIN LIKE
REMARK 210 PROTEIN(D123N) U-15N, 13C; 50MM
REMARK 210 PHOSPHATE BUFFER, 50MM NACL; 90%
REMARK 210 H2O, 10% D2O; 1.5MM HUMAN
REMARK 210 COACTOSIN LIKE PROTEIN(D123N) U-
REMARK 210 15N; 50MM PHOSPHATE BUFFER, 50MM
REMARK 210 NACL; 90% H2O, 10% D2O; 1.5MM
REMARK 210 HUMAN COACTOSIN LIKE
REMARK 210 PROTEIN(D123N); 50MM PHOSPHATE
REMARK 210 BUFFER, 50MM NACL; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 2D NOESY; 3D
REMARK 210 CBCANH; 3D CBCA(CO)NH; 3D HNCO;
REMARK 210 3D HNCA; 3D HBHA(CBCACO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3, CNS 1.1, CSI 1.0,
REMARK 210 MOLMOL 2K.2
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
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 : 4
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 LEU A 143
REMARK 465 GLU A 144
REMARK 465 HIS A 145
REMARK 465 HIS A 146
REMARK 465 HIS A 147
REMARK 465 HIS A 148
REMARK 465 HIS A 149
REMARK 465 HIS A 150
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 SER A 34 37.38 -163.60
REMARK 500 1 GLU A 40 140.78 -34.73
REMARK 500 1 ASP A 55 41.17 -168.07
REMARK 500 1 VAL A 56 -172.61 174.97
REMARK 500 1 ASP A 68 79.78 -159.84
REMARK 500 1 MET A 70 -41.54 -148.09
REMARK 500 1 SER A 71 82.17 -158.50
REMARK 500 1 GLU A 84 -30.91 -30.35
REMARK 500 1 ASN A 85 36.64 -75.28
REMARK 500 1 ALA A 109 -54.90 -121.19
REMARK 500 1 TYR A 137 54.31 -92.65
REMARK 500 1 ALA A 139 -56.49 -147.62
REMARK 500 2 ASP A 19 98.74 -65.21
REMARK 500 2 SER A 34 -31.90 169.51
REMARK 500 2 GLU A 40 133.57 -27.46
REMARK 500 2 CYS A 52 81.58 -66.29
REMARK 500 2 ASP A 55 29.94 -158.85
REMARK 500 2 VAL A 56 158.67 173.87
REMARK 500 2 ALA A 69 17.15 -67.77
REMARK 500 2 GLU A 84 -68.54 7.56
REMARK 500 2 VAL A 86 100.19 -54.06
REMARK 500 2 ALA A 132 32.08 -98.25
REMARK 500 2 ALA A 135 26.46 -171.65
REMARK 500 2 ASN A 136 26.41 -164.68
REMARK 500 2 ALA A 139 -47.09 -166.11
REMARK 500 2 THR A 141 92.99 61.85
REMARK 500 3 ASP A 20 40.09 -97.70
REMARK 500 3 SER A 34 35.41 -160.27
REMARK 500 3 GLU A 40 136.25 -32.05
REMARK 500 3 VAL A 56 143.14 170.25
REMARK 500 3 ASP A 68 79.53 -155.22
REMARK 500 3 MET A 70 -37.69 -156.94
REMARK 500 3 SER A 71 79.04 -157.74
REMARK 500 3 GLU A 84 -40.31 -29.21
REMARK 500 3 ASN A 85 41.55 -72.27
REMARK 500 3 ALA A 139 -37.90 -149.99
REMARK 500 4 ASP A 20 19.67 53.51
REMARK 500 4 SER A 22 85.03 -64.70
REMARK 500 4 SER A 34 32.81 -155.45
REMARK 500 4 GLU A 40 140.81 -35.48
REMARK 500 4 ASP A 54 38.50 -87.40
REMARK 500 4 VAL A 56 157.30 169.48
REMARK 500 4 ALA A 69 49.85 31.39
REMARK 500 4 MET A 70 -36.71 -177.31
REMARK 500 4 GLU A 84 -51.38 -27.61
REMARK 500 4 ASN A 85 49.07 -71.41
REMARK 500 5 SER A 34 31.89 -150.13
REMARK 500 5 GLU A 40 141.06 -35.47
REMARK 500 5 VAL A 56 -175.09 -170.11
REMARK 500 5 ARG A 57 74.36 -169.39
REMARK 500
REMARK 500 THIS ENTRY HAS 237 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6071 RELATED DB: BMRB
DBREF 1TMW A 2 142 UNP Q14019 COTL1_HUMAN 2 142
SEQADV 1TMW ASN A 123 UNP Q14019 ASP 123 ENGINEERED MUTATION
SEQADV 1TMW LEU A 143 UNP Q14019 EXPRESSION TAG
SEQADV 1TMW GLU A 144 UNP Q14019 EXPRESSION TAG
SEQADV 1TMW HIS A 145 UNP Q14019 EXPRESSION TAG
SEQADV 1TMW HIS A 146 UNP Q14019 EXPRESSION TAG
SEQADV 1TMW HIS A 147 UNP Q14019 EXPRESSION TAG
SEQADV 1TMW HIS A 148 UNP Q14019 EXPRESSION TAG
SEQADV 1TMW HIS A 149 UNP Q14019 EXPRESSION TAG
SEQADV 1TMW HIS A 150 UNP Q14019 EXPRESSION TAG
SEQRES 1 A 149 ALA THR LYS ILE ASP LYS GLU ALA CYS ARG ALA ALA TYR
SEQRES 2 A 149 ASN LEU VAL ARG ASP ASP GLY SER ALA VAL ILE TRP VAL
SEQRES 3 A 149 THR PHE LYS TYR ASP GLY SER THR ILE VAL PRO GLY GLU
SEQRES 4 A 149 GLN GLY ALA GLU TYR GLN HIS PHE ILE GLN GLN CYS THR
SEQRES 5 A 149 ASP ASP VAL ARG LEU PHE ALA PHE VAL ARG PHE THR THR
SEQRES 6 A 149 GLY ASP ALA MET SER LYS ARG SER LYS PHE ALA LEU ILE
SEQRES 7 A 149 THR TRP ILE GLY GLU ASN VAL SER GLY LEU GLN ARG ALA
SEQRES 8 A 149 LYS THR GLY THR ASP LYS THR LEU VAL LYS GLU VAL VAL
SEQRES 9 A 149 GLN ASN PHE ALA LYS GLU PHE VAL ILE SER ASP ARG LYS
SEQRES 10 A 149 GLU LEU GLU GLU ASN PHE ILE LYS SER GLU LEU LYS LYS
SEQRES 11 A 149 ALA GLY GLY ALA ASN TYR ASP ALA GLN THR GLU LEU GLU
SEQRES 12 A 149 HIS HIS HIS HIS HIS HIS
HELIX 1 1 ASP A 6 ASP A 19 1 14
HELIX 2 2 TYR A 45 CYS A 52 1 8
HELIX 3 3 SER A 87 VAL A 105 1 19
HELIX 4 4 ASP A 116 GLU A 121 1 6
HELIX 5 5 GLU A 121 ALA A 132 1 12
SHEET 1 A 5 ILE A 36 GLY A 42 0
SHEET 2 A 5 TRP A 26 TYR A 31 -1 N THR A 28 O GLY A 39
SHEET 3 A 5 ARG A 57 THR A 65 -1 O PHE A 59 N PHE A 29
SHEET 4 A 5 SER A 74 ILE A 82 -1 O TRP A 81 N LEU A 58
SHEET 5 A 5 LYS A 110 ILE A 114 1 O LYS A 110 N LEU A 78
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 - v 10 2 Bytes