Header list of 1wgp.pdb file
Complete list - r 2 2 Bytes
HEADER MEMBRANE PROTEIN 28-MAY-04 1WGP TITLE SOLUTION STRUCTURE OF THE CNMP-BINDING DOMAIN FROM ARABIDOPSIS TITLE 2 THALIANA CYCLIC NUCLEOTIDE-REGULATED ION CHANNEL COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROBABLE CYCLIC NUCLEOTIDE-GATED ION CHANNEL 6; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CNMP BINDING DOMAIN; COMPND 5 SYNONYM: CYCLIC NUCLEOTIDE-REGULATED ION CHANNEL, ATCNGC6, CYCLIC COMPND 6 NUCLEOTIDE- AND CALMODULIN-REGULATED ION CHANNEL 6; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 3 ORGANISM_COMMON: THALE CRESS; SOURCE 4 ORGANISM_TAXID: 3702; SOURCE 5 GENE: RIKEN RAFL05-10-A11; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021218-34; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS CYCLIC NUCLEOTIDE MONOPHOSPHATE, CNMP, CNMP-BINDING, STRUCTURAL KEYWDS 2 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, KEYWDS 3 MEMBRANE PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR E.CHIKAYAMA,N.NAMEKI,T.KIGAWA,S.KOSHIBA,M.INOUE,T.TOMIZAWA, AUTHOR 2 N.KOBAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS AUTHOR 3 INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WGP 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WGP 1 VERSN REVDAT 1 28-NOV-04 1WGP 0 JRNL AUTH E.CHIKAYAMA,N.NAMEKI,T.KIGAWA,S.KOSHIBA,M.INOUE,T.TOMIZAWA, JRNL AUTH 2 N.KOBAYASHI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE CNMP-BINDING DOMAIN FROM JRNL TITL 2 ARABIDOPSIS THALIANA CYCLIC NUCLEOTIDE-REGULATED ION CHANNEL 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 1WGP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023560. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.5 REMARK 210 IONIC STRENGTH : 220MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.66MM CNMP-BINDING DOMAIN U REMARK 210 -15N, 13C; 20MM D-TRIS-HCL(PH REMARK 210 7.5); 200MM NACL; 1MM D-DTT; REMARK 210 0.02% NAN3; 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 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 0.901, CYANA 2.0.17 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY, TARGET REMARK 210 FUNCTION 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 O LYS A 123 H SER A 127 1.52 REMARK 500 O ASP A 23 H GLU A 27 1.53 REMARK 500 O LEU A 22 H CYS A 26 1.58 REMARK 500 H MET A 50 O LEU A 117 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 SER A 2 -58.31 -150.06 REMARK 500 1 SER A 3 97.40 67.27 REMARK 500 1 VAL A 8 43.67 33.69 REMARK 500 1 LYS A 37 35.05 70.68 REMARK 500 1 ARG A 55 109.02 -169.63 REMARK 500 1 THR A 63 -51.02 -122.56 REMARK 500 1 SER A 68 93.90 53.34 REMARK 500 1 TYR A 71 98.53 48.25 REMARK 500 1 SER A 97 65.66 -113.00 REMARK 500 1 ASN A 98 169.85 61.98 REMARK 500 1 ARG A 130 86.24 40.99 REMARK 500 1 SER A 132 -56.40 -141.22 REMARK 500 1 SER A 135 87.22 39.15 REMARK 500 2 SER A 2 79.78 -172.81 REMARK 500 2 SER A 3 -58.50 -158.59 REMARK 500 2 SER A 6 139.02 68.17 REMARK 500 2 ARG A 55 119.35 -175.80 REMARK 500 2 PHE A 70 99.81 49.48 REMARK 500 2 SER A 97 157.55 -39.42 REMARK 500 2 ASN A 98 175.36 -53.00 REMARK 500 2 LEU A 99 156.98 -45.50 REMARK 500 2 ASP A 120 -71.18 -41.28 REMARK 500 2 ARG A 130 89.24 44.37 REMARK 500 2 SER A 135 -58.37 -153.14 REMARK 500 3 SER A 5 -64.63 -152.11 REMARK 500 3 SER A 6 132.28 165.63 REMARK 500 3 LEU A 29 126.33 -39.97 REMARK 500 3 THR A 63 55.75 -172.80 REMARK 500 3 ARG A 67 -54.45 -177.89 REMARK 500 3 LEU A 99 156.83 -47.67 REMARK 500 3 ARG A 130 84.43 42.78 REMARK 500 3 SER A 132 129.35 64.02 REMARK 500 3 SER A 136 -60.31 -105.56 REMARK 500 4 SER A 6 91.87 65.29 REMARK 500 4 VAL A 8 54.78 -107.67 REMARK 500 4 ARG A 10 64.69 -166.61 REMARK 500 4 LEU A 29 119.38 -38.07 REMARK 500 4 ARG A 55 117.13 -172.69 REMARK 500 4 THR A 63 -51.47 -122.25 REMARK 500 4 ARG A 67 -54.80 -147.98 REMARK 500 4 SER A 97 -50.72 -138.99 REMARK 500 4 LEU A 99 157.49 -47.56 REMARK 500 4 ARG A 130 128.35 -39.22 REMARK 500 4 ARG A 131 102.93 -178.01 REMARK 500 4 SER A 132 93.00 178.87 REMARK 500 4 SER A 136 -60.41 -96.54 REMARK 500 5 SER A 2 -58.27 -149.11 REMARK 500 5 VAL A 8 173.06 -49.62 REMARK 500 5 ARG A 9 135.27 79.15 REMARK 500 5 MET A 17 161.53 -48.61 REMARK 500 REMARK 500 THIS ENTRY HAS 245 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: ATR001011378.1 RELATED DB: TARGETDB DBREF 1WGP A 8 131 UNP O82226 CNGC6_ARATH 509 632 SEQADV 1WGP GLY A 1 UNP O82226 CLONING ARTIFACT SEQADV 1WGP SER A 2 UNP O82226 CLONING ARTIFACT SEQADV 1WGP SER A 3 UNP O82226 CLONING ARTIFACT SEQADV 1WGP GLY A 4 UNP O82226 CLONING ARTIFACT SEQADV 1WGP SER A 5 UNP O82226 CLONING ARTIFACT SEQADV 1WGP SER A 6 UNP O82226 CLONING ARTIFACT SEQADV 1WGP GLY A 7 UNP O82226 CLONING ARTIFACT SEQADV 1WGP SER A 132 UNP O82226 CLONING ARTIFACT SEQADV 1WGP GLY A 133 UNP O82226 CLONING ARTIFACT SEQADV 1WGP PRO A 134 UNP O82226 CLONING ARTIFACT SEQADV 1WGP SER A 135 UNP O82226 CLONING ARTIFACT SEQADV 1WGP SER A 136 UNP O82226 CLONING ARTIFACT SEQADV 1WGP GLY A 137 UNP O82226 CLONING ARTIFACT SEQRES 1 A 137 GLY SER SER GLY SER SER GLY VAL ARG ARG VAL PRO LEU SEQRES 2 A 137 PHE GLU ASN MET ASP GLU ARG LEU LEU ASP ALA ILE CYS SEQRES 3 A 137 GLU ARG LEU LYS PRO CYS LEU PHE THR GLU LYS SER TYR SEQRES 4 A 137 LEU VAL ARG GLU GLY ASP PRO VAL ASN GLU MET LEU PHE SEQRES 5 A 137 ILE ILE ARG GLY ARG LEU GLU SER VAL THR THR ASP GLY SEQRES 6 A 137 GLY ARG SER GLY PHE TYR ASN ARG SER LEU LEU LYS GLU SEQRES 7 A 137 GLY ASP PHE CYS GLY ASP GLU LEU LEU THR TRP ALA LEU SEQRES 8 A 137 ASP PRO LYS SER GLY SER ASN LEU PRO SER SER THR ARG SEQRES 9 A 137 THR VAL LYS ALA LEU THR GLU VAL GLU ALA PHE ALA LEU SEQRES 10 A 137 ILE ALA ASP GLU LEU LYS PHE VAL ALA SER GLN PHE ARG SEQRES 11 A 137 ARG SER GLY PRO SER SER GLY HELIX 1 1 PRO A 12 ASN A 16 5 5 HELIX 2 2 ASP A 18 LEU A 29 1 12 HELIX 3 3 ASP A 84 ASP A 92 1 9 HELIX 4 4 ALA A 119 ARG A 130 1 12 SHEET 1 A 4 SER A 38 VAL A 41 0 SHEET 2 A 4 THR A 105 ALA A 108 -1 SHEET 3 A 4 LEU A 58 THR A 62 -1 SHEET 4 A 4 ASN A 72 LEU A 76 -1 SHEET 1 B 4 PHE A 81 CYS A 82 0 SHEET 2 B 4 GLU A 49 ARG A 55 -1 SHEET 3 B 4 VAL A 112 ILE A 118 -1 SHEET 4 B 4 LYS A 30 PHE A 34 -1 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