Header list of 1r5s.pdb file
Complete list - r 2 2 Bytes
HEADER MEMBRANE PROTEIN 13-OCT-03 1R5S TITLE CONNEXIN 43 CARBOXYL TERMINAL DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: GAP JUNCTION ALPHA-1 PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CARBOXYL TERMINAL DOMAIN; COMPND 5 SYNONYM: CONNEXIN 43, CX43, GAP JUNCTION 43 KDA HEART PROTEIN; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 GENE: GJA1 OR CXN-43; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CX43CT, MEMBRANE PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR P.L.SORGEN,H.S.DUFFY,D.MARIO,P.SAHOO,W.COOMBS,M.DELMAR,D.C.SPRAY REVDAT 4 02-MAR-22 1R5S 1 REMARK SEQADV REVDAT 3 24-FEB-09 1R5S 1 VERSN REVDAT 2 18-JAN-05 1R5S 1 JRNL REVDAT 1 26-OCT-04 1R5S 0 JRNL AUTH P.L.SORGEN,H.S.DUFFY,P.SAHOO,W.COOMBS,M.DELMAR,D.C.SPRAY JRNL TITL STRUCTURAL CHANGES IN THE CARBOXYL TERMINUS OF THE GAP JRNL TITL 2 JUNCTION PROTEIN CONNEXIN43 INDICATES SIGNALING BETWEEN JRNL TITL 3 BINDING DOMAINS FOR C-SRC AND ZONULA OCCLUDENS-1 JRNL REF J.BIOL.CHEM. V. 279 54695 2004 JRNL REFN ISSN 0021-9258 JRNL PMID 15492000 JRNL DOI 10.1074/JBC.M409552200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1, CNS 1.1 REMARK 3 AUTHORS : BRUNGER, ET AL. (CNS), BRUNGER, ET AL. (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1R5S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-03. REMARK 100 THE DEPOSITION ID IS D_1000020472. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 280 REMARK 210 PH : 5.8 REMARK 210 IONIC STRENGTH : PBS REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.5MM CX43CT U-15N,13C, PBS 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 : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 7.2 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 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: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D REMARK 210 HOMONUCLEAR TECHNIQUES 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 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 PRO A 6 49.80 -79.02 REMARK 500 1 CYS A 10 91.95 52.44 REMARK 500 1 SER A 12 159.14 63.76 REMARK 500 1 LYS A 14 -62.00 -152.55 REMARK 500 1 TYR A 15 -67.95 -124.39 REMARK 500 1 ALA A 16 -34.76 -179.60 REMARK 500 1 ASN A 19 -77.05 69.74 REMARK 500 1 THR A 25 75.53 -59.13 REMARK 500 1 PRO A 27 -158.57 -57.34 REMARK 500 1 LEU A 28 -49.85 -130.98 REMARK 500 1 SER A 29 -46.97 179.21 REMARK 500 1 PRO A 30 43.50 -76.34 REMARK 500 1 PRO A 34 87.16 -49.76 REMARK 500 1 TYR A 36 77.76 -113.12 REMARK 500 1 LYS A 37 -38.28 -178.02 REMARK 500 1 LEU A 38 -81.34 62.87 REMARK 500 1 VAL A 39 -58.80 -140.04 REMARK 500 1 ASN A 44 -49.12 83.25 REMARK 500 1 SER A 46 -16.68 83.00 REMARK 500 1 SER A 47 71.87 51.38 REMARK 500 1 CYS A 48 -47.95 -152.02 REMARK 500 1 ARG A 49 66.99 -105.17 REMARK 500 1 TYR A 51 101.57 60.51 REMARK 500 1 ALA A 55 -66.48 69.30 REMARK 500 1 SER A 56 -59.36 96.85 REMARK 500 1 GLU A 57 87.27 179.87 REMARK 500 1 ALA A 61 107.20 74.84 REMARK 500 1 TYR A 63 -27.83 68.50 REMARK 500 1 SER A 64 42.54 72.78 REMARK 500 1 ALA A 65 27.20 -157.26 REMARK 500 1 ILE A 77 112.19 60.10 REMARK 500 1 SER A 78 -37.26 -175.71 REMARK 500 1 ASN A 79 79.09 -119.34 REMARK 500 1 SER A 80 48.92 -101.18 REMARK 500 1 HIS A 81 -45.31 -178.28 REMARK 500 1 ALA A 82 27.89 45.64 REMARK 500 1 PHE A 85 -63.60 -159.18 REMARK 500 1 ASP A 89 50.83 -90.98 REMARK 500 1 ASP A 90 41.28 -152.07 REMARK 500 1 ASN A 91 -46.94 -130.50 REMARK 500 1 GLN A 92 -71.91 -70.44 REMARK 500 1 LEU A 103 -48.72 -175.82 REMARK 500 1 ALA A 107 49.10 -167.72 REMARK 500 1 VAL A 109 49.71 -146.62 REMARK 500 1 ARG A 112 -57.55 104.25 REMARK 500 1 SER A 114 -4.08 69.21 REMARK 500 1 ARG A 116 -164.82 -79.74 REMARK 500 1 PRO A 125 -150.68 -67.89 REMARK 500 1 ARG A 126 -50.85 -148.07 REMARK 500 1 ASP A 128 -37.00 169.19 REMARK 500 REMARK 500 THIS ENTRY HAS 439 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5431 RELATED DB: BMRB REMARK 900 CONNEXIN 43 CARBOXYL TERMINAL DOMAIN ASSIGNMENTS DBREF 1R5S A 5 132 UNP P08050 CXA1_RAT 254 381 SEQADV 1R5S GLY A 1 UNP P08050 LINKER SEQADV 1R5S PRO A 2 UNP P08050 LINKER SEQADV 1R5S LEU A 3 UNP P08050 LINKER SEQADV 1R5S GLY A 4 UNP P08050 LINKER SEQRES 1 A 132 GLY PRO LEU GLY SER PRO SER LYS ASP CYS GLY SER PRO SEQRES 2 A 132 LYS TYR ALA TYR PHE ASN GLY CYS SER SER PRO THR ALA SEQRES 3 A 132 PRO LEU SER PRO MET SER PRO PRO GLY TYR LYS LEU VAL SEQRES 4 A 132 THR GLY ASP ARG ASN ASN SER SER CYS ARG ASN TYR ASN SEQRES 5 A 132 LYS GLN ALA SER GLU GLN ASN TRP ALA ASN TYR SER ALA SEQRES 6 A 132 GLU GLN ASN ARG MET GLY GLN ALA GLY SER THR ILE SER SEQRES 7 A 132 ASN SER HIS ALA GLN PRO PHE ASP PHE PRO ASP ASP ASN SEQRES 8 A 132 GLN ASN ALA LYS LYS VAL ALA ALA GLY HIS GLU LEU GLN SEQRES 9 A 132 PRO LEU ALA ILE VAL ASP GLN ARG PRO SER SER ARG ALA SEQRES 10 A 132 SER SER ARG ALA SER SER ARG PRO ARG PRO ASP ASP LEU SEQRES 11 A 132 GLU ILE HELIX 1 1 GLU A 66 THR A 76 1 11 HELIX 2 2 ASN A 91 ALA A 99 1 9 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