Header list of 1wyn.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 15-FEB-05 1WYN
TITLE SOLUTION STRUCTURE OF THE CH DOMAIN OF HUMAN CALPONIN-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALPONIN-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CH DOMAIN;
COMPND 5 SYNONYM: CALPONIN H2, SMOOTH MUSCLE, NEUTRAL CALPONIN;
COMPND 6 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: CNN2;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040607-10;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS CH DOMAIN, F-ACTIN BINDING, ALL ALPHA HELIX, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 3 STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WYN 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WYN 1 VERSN
REVDAT 1 15-AUG-05 1WYN 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE CH DOMAIN OF HUMAN CALPONIN-2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WYN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000024158.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.30MM CH DOMAIN U-15N,13C; 20MM
REMARK 210 D-TRIS-HCL(PH 7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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: 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 12 124.95 -35.17
REMARK 500 1 LYS A 40 -70.47 -66.67
REMARK 500 1 LEU A 48 -36.42 -34.20
REMARK 500 1 PRO A 57 3.62 -69.81
REMARK 500 1 SER A 59 -62.75 -101.22
REMARK 500 1 ARG A 65 44.28 -86.53
REMARK 500 1 MET A 67 38.66 -95.63
REMARK 500 1 ASN A 69 -72.41 -64.08
REMARK 500 1 ILE A 80 -70.75 -47.29
REMARK 500 1 GLU A 101 37.55 -99.55
REMARK 500 1 SER A 102 25.50 39.53
REMARK 500 1 ASN A 104 112.30 -175.19
REMARK 500 1 SER A 135 118.28 -160.53
REMARK 500 1 PRO A 143 97.61 -69.77
REMARK 500 2 LYS A 13 41.04 -84.80
REMARK 500 2 LYS A 43 -70.82 -37.64
REMARK 500 2 ASP A 44 -33.75 -34.75
REMARK 500 2 PRO A 57 3.34 -69.75
REMARK 500 2 SER A 59 -64.18 -101.38
REMARK 500 2 ARG A 65 42.14 -96.12
REMARK 500 2 MET A 67 43.49 -85.45
REMARK 500 2 SER A 102 25.19 39.98
REMARK 500 2 ASN A 104 113.39 -175.64
REMARK 500 2 THR A 121 -35.61 -37.29
REMARK 500 2 LEU A 124 107.18 -49.32
REMARK 500 3 LEU A 48 -39.93 -32.36
REMARK 500 3 PRO A 57 3.84 -69.80
REMARK 500 3 SER A 59 -67.32 -105.09
REMARK 500 3 ARG A 65 39.84 -94.13
REMARK 500 3 SER A 102 27.63 40.83
REMARK 500 3 ASN A 104 113.61 -175.52
REMARK 500 3 GLN A 125 76.72 -108.97
REMARK 500 3 SER A 141 -50.47 -123.74
REMARK 500 4 LYS A 13 -175.64 -175.54
REMARK 500 4 LYS A 43 -72.40 -36.14
REMARK 500 4 LEU A 48 -39.80 -33.08
REMARK 500 4 PRO A 57 79.98 -69.81
REMARK 500 4 SER A 59 -74.65 -86.20
REMARK 500 4 SER A 102 25.07 40.47
REMARK 500 4 ASN A 104 114.69 -175.12
REMARK 500 4 SER A 126 145.69 -38.84
REMARK 500 4 GLU A 139 46.17 72.60
REMARK 500 4 PRO A 143 1.60 -69.71
REMARK 500 5 LEU A 48 -35.55 -33.38
REMARK 500 5 ASN A 53 -39.47 -39.72
REMARK 500 5 PRO A 57 3.96 -69.70
REMARK 500 5 SER A 59 -65.54 -109.75
REMARK 500 5 ARG A 65 47.17 -87.24
REMARK 500 5 MET A 67 36.71 -94.99
REMARK 500 5 ASN A 69 -73.70 -63.65
REMARK 500
REMARK 500 THIS ENTRY HAS 249 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001001945.1 RELATED DB: TARGETDB
DBREF 1WYN A 8 140 UNP Q99439 CNN2_HUMAN 19 151
SEQADV 1WYN GLY A 1 UNP Q99439 CLONING ARTIFACT
SEQADV 1WYN SER A 2 UNP Q99439 CLONING ARTIFACT
SEQADV 1WYN SER A 3 UNP Q99439 CLONING ARTIFACT
SEQADV 1WYN GLY A 4 UNP Q99439 CLONING ARTIFACT
SEQADV 1WYN SER A 5 UNP Q99439 CLONING ARTIFACT
SEQADV 1WYN SER A 6 UNP Q99439 CLONING ARTIFACT
SEQADV 1WYN GLY A 7 UNP Q99439 CLONING ARTIFACT
SEQADV 1WYN SER A 141 UNP Q99439 CLONING ARTIFACT
SEQADV 1WYN GLY A 142 UNP Q99439 CLONING ARTIFACT
SEQADV 1WYN PRO A 143 UNP Q99439 CLONING ARTIFACT
SEQADV 1WYN SER A 144 UNP Q99439 CLONING ARTIFACT
SEQADV 1WYN SER A 145 UNP Q99439 CLONING ARTIFACT
SEQADV 1WYN GLY A 146 UNP Q99439 CLONING ARTIFACT
SEQRES 1 A 146 GLY SER SER GLY SER SER GLY ASN ARG LEU LEU SER LYS
SEQRES 2 A 146 TYR ASP PRO GLN LYS GLU ALA GLU LEU ARG THR TRP ILE
SEQRES 3 A 146 GLU GLY LEU THR GLY LEU SER ILE GLY PRO ASP PHE GLN
SEQRES 4 A 146 LYS GLY LEU LYS ASP GLY THR ILE LEU CYS THR LEU MET
SEQRES 5 A 146 ASN LYS LEU GLN PRO GLY SER VAL PRO LYS ILE ASN ARG
SEQRES 6 A 146 SER MET GLN ASN TRP HIS GLN LEU GLU ASN LEU SER ASN
SEQRES 7 A 146 PHE ILE LYS ALA MET VAL SER TYR GLY MET ASN PRO VAL
SEQRES 8 A 146 ASP LEU PHE GLU ALA ASN ASP LEU PHE GLU SER GLY ASN
SEQRES 9 A 146 MET THR GLN VAL GLN VAL SER LEU LEU ALA LEU ALA GLY
SEQRES 10 A 146 LYS ALA LYS THR LYS GLY LEU GLN SER GLY VAL ASP ILE
SEQRES 11 A 146 GLY VAL LYS TYR SER GLU LYS GLN GLU ARG SER GLY PRO
SEQRES 12 A 146 SER SER GLY
HELIX 1 1 GLN A 17 GLY A 31 1 15
HELIX 2 2 ASP A 37 ASP A 44 1 8
HELIX 3 3 THR A 46 GLN A 56 1 11
HELIX 4 4 GLN A 68 GLY A 87 1 20
HELIX 5 5 GLU A 95 GLU A 101 1 7
HELIX 6 6 MET A 105 LYS A 120 1 16
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