Header list of 1wyp.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 15-FEB-05 1WYP TITLE SOLUTION STRUCTURE OF THE CH DOMAIN OF HUMAN CALPONIN 1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALPONIN 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CH DOMAIN; COMPND 5 SYNONYM: CALPONIN H1, SMOOTH MUSCLE, BASIC 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: CNN1; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040621-01; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS CH DOMAIN, F-ACTIN BINDING, ALL-ALPHA, STRUCTURAL GENOMICS, NPPSFA, KEYWDS 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL KEYWDS 3 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 1WYP 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WYP 1 VERSN REVDAT 1 15-AUG-05 1WYP 0 JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE CH DOMAIN OF HUMAN CALPONIN 1 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 1WYP 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_1000024160. 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 : 1.10MM 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 3 115.95 -169.21 REMARK 500 1 LYS A 13 175.43 -53.77 REMARK 500 1 ASN A 37 98.18 -53.51 REMARK 500 1 ASP A 44 -37.58 -35.45 REMARK 500 1 PRO A 57 90.86 -69.74 REMARK 500 1 LYS A 61 -71.95 -42.72 REMARK 500 1 ASN A 102 27.68 38.96 REMARK 500 1 PRO A 133 85.59 -69.73 REMARK 500 2 SER A 3 106.44 -168.11 REMARK 500 2 SER A 6 151.04 -38.86 REMARK 500 2 VAL A 29 -72.46 -76.59 REMARK 500 2 ASN A 36 -71.66 -36.76 REMARK 500 2 ASN A 37 101.42 -55.29 REMARK 500 2 PRO A 57 90.43 -69.80 REMARK 500 2 LYS A 61 -72.78 -45.82 REMARK 500 2 GLN A 68 131.51 -36.58 REMARK 500 2 THR A 111 -38.69 -33.72 REMARK 500 2 LEU A 113 -37.77 -38.06 REMARK 500 2 SER A 131 138.96 -34.79 REMARK 500 3 LYS A 9 137.59 -35.42 REMARK 500 3 LYS A 13 -63.84 -129.26 REMARK 500 3 ASN A 37 97.66 -58.03 REMARK 500 3 TYR A 86 -70.90 -48.78 REMARK 500 3 LYS A 89 158.68 -48.50 REMARK 500 3 ASN A 102 28.61 47.70 REMARK 500 3 VAL A 126 -68.57 -125.25 REMARK 500 4 VAL A 29 -70.01 -64.64 REMARK 500 4 ASN A 37 106.29 -58.54 REMARK 500 4 PRO A 57 86.43 -69.74 REMARK 500 4 LYS A 89 148.41 -38.98 REMARK 500 4 LYS A 125 99.59 -38.85 REMARK 500 4 VAL A 128 115.42 -36.98 REMARK 500 5 SER A 2 103.95 -36.99 REMARK 500 5 LYS A 9 45.48 -82.67 REMARK 500 5 TYR A 14 114.71 -36.30 REMARK 500 5 ASN A 36 -70.94 -49.14 REMARK 500 5 ASN A 37 100.68 -57.43 REMARK 500 5 MET A 39 -74.34 -51.73 REMARK 500 5 PRO A 57 81.58 -69.80 REMARK 500 5 SER A 66 -175.76 -171.36 REMARK 500 5 TRP A 70 -70.12 -38.71 REMARK 500 5 TYR A 86 -71.66 -46.29 REMARK 500 5 ASN A 127 30.44 -98.98 REMARK 500 5 SER A 135 91.85 -64.82 REMARK 500 6 ASN A 8 113.71 -168.55 REMARK 500 6 VAL A 29 -74.80 -74.25 REMARK 500 6 PHE A 38 -42.91 -130.55 REMARK 500 6 PRO A 57 1.23 -69.81 REMARK 500 6 SER A 59 -68.36 -106.89 REMARK 500 6 LYS A 61 -70.10 -50.15 REMARK 500 REMARK 500 THIS ENTRY HAS 218 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSS001003528.1 RELATED DB: TARGETDB DBREF 1WYP A 8 130 UNP P51911 CNN1_HUMAN 20 142 SEQADV 1WYP GLY A 1 UNP P51911 CLONING ARTIFACT SEQADV 1WYP SER A 2 UNP P51911 CLONING ARTIFACT SEQADV 1WYP SER A 3 UNP P51911 CLONING ARTIFACT SEQADV 1WYP GLY A 4 UNP P51911 CLONING ARTIFACT SEQADV 1WYP SER A 5 UNP P51911 CLONING ARTIFACT SEQADV 1WYP SER A 6 UNP P51911 CLONING ARTIFACT SEQADV 1WYP GLY A 7 UNP P51911 CLONING ARTIFACT SEQADV 1WYP SER A 131 UNP P51911 CLONING ARTIFACT SEQADV 1WYP GLY A 132 UNP P51911 CLONING ARTIFACT SEQADV 1WYP PRO A 133 UNP P51911 CLONING ARTIFACT SEQADV 1WYP SER A 134 UNP P51911 CLONING ARTIFACT SEQADV 1WYP SER A 135 UNP P51911 CLONING ARTIFACT SEQADV 1WYP GLY A 136 UNP P51911 CLONING ARTIFACT SEQRES 1 A 136 GLY SER SER GLY SER SER GLY ASN LYS LEU ALA GLN LYS SEQRES 2 A 136 TYR ASP HIS GLN ARG GLU GLN GLU LEU ARG GLU TRP ILE SEQRES 3 A 136 GLU GLY VAL THR GLY ARG ARG ILE GLY ASN ASN PHE MET SEQRES 4 A 136 ASP GLY LEU LYS ASP GLY ILE ILE LEU CYS GLU PHE ILE SEQRES 5 A 136 ASN LYS LEU GLN PRO GLY SER VAL LYS LYS ILE ASN GLU SEQRES 6 A 136 SER THR GLN ASN TRP HIS GLN LEU GLU ASN ILE GLY ASN SEQRES 7 A 136 PHE ILE LYS ALA ILE THR LYS TYR GLY VAL LYS PRO HIS SEQRES 8 A 136 ASP ILE PHE GLU ALA ASN ASP LEU PHE GLU ASN THR ASN SEQRES 9 A 136 HIS THR GLN VAL GLN SER THR LEU LEU ALA LEU ALA SER SEQRES 10 A 136 MET ALA LYS THR LYS GLY ASN LYS VAL ASN VAL GLY VAL SEQRES 11 A 136 SER GLY PRO SER SER GLY HELIX 1 1 ASP A 15 THR A 30 1 16 HELIX 2 2 MET A 39 ASP A 44 1 6 HELIX 3 3 GLY A 45 GLN A 56 1 12 HELIX 4 4 ASN A 69 GLY A 87 1 19 HELIX 5 5 LYS A 89 ILE A 93 5 5 HELIX 6 6 GLU A 95 GLU A 101 1 7 HELIX 7 7 HIS A 105 GLY A 123 1 19 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