Header list of 1y4e.pdb file
Complete list - r 2 2 Bytes
HEADER MEMBRANE PROTEIN 30-NOV-04 1Y4E TITLE NMR STRUCTURE OF TRANSMEMBRANE SEGMENT IV OF THE NHE1 ISOFORM OF THE TITLE 2 NA+/H+ EXCHANGER COMPND MOL_ID: 1; COMPND 2 MOLECULE: SODIUM/HYDROGEN EXCHANGER 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: TRANSMEMBRANE SEGMENT IV; COMPND 5 SYNONYM: NA+, /H+, EXCHANGER 1, NHE-1, NA+/H+ ANTIPORTER, AMILORIDE- COMPND 6 SENSITIVE, APNH; COMPND 7 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: SLC9A1, APNH1, NHE1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 (PLYSS); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: GEV-1 KEYWDS NHE1 ISOFORM, TRANSMEMBRANE, MEMBRANE PROTEIN EXPDTA SOLUTION NMR NUMMDL 100 AUTHOR E.R.SLEPKOV,J.K.RAINEY,X.LI,Y.LIU,D.A.LINDHOUT,B.D.SYKES,L.FLIEGEL REVDAT 4 02-MAR-22 1Y4E 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 1Y4E 1 VERSN REVDAT 2 10-MAY-05 1Y4E 1 JRNL REVDAT 1 01-FEB-05 1Y4E 0 JRNL AUTH E.R.SLEPKOV,J.K.RAINEY,X.LI,Y.LIU,F.J.CHENG,D.A.LINDHOUT, JRNL AUTH 2 B.D.SYKES,L.FLIEGEL JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF TRANSMEMBRANE JRNL TITL 2 SEGMENT IV OF THE NHE1 ISOFORM OF THE NA+/H+ EXCHANGER. JRNL REF J.BIOL.CHEM. V. 280 17863 2005 JRNL REFN ISSN 0021-9258 JRNL PMID 15677483 JRNL DOI 10.1074/JBC.M409608200 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.A.LINDHOUT,A.THIESSEN,D.SCHIEVE,B.D.SYKES REMARK 1 TITL HIGH-YIELD EXPRESSION OF ISOTOPICALLY LABELED PEPTIDES FOR REMARK 1 TITL 2 USE IN NMR STUDIES REMARK 1 REF PROTEIN SCI. V. 12 1786 2003 REMARK 1 REFN ISSN 0961-8368 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR VARIOUS, CNS 1.1 REMARK 3 AUTHORS : VARIAN INC. (VNMR), A.T.BRUNGER, P.D.ADAMS, REMARK 3 G.M.CLORE, W.L.DELANO, P.GROS, R.W.GROSSE- REMARK 3 KUNSTLEVE, J.-S.JIANG, J.KUSZEWSKI, M.NILGES, REMARK 3 N.S.PANNU, R.J.READ, L.M.RICE, T.SIMONSON, REMARK 3 G.L.WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 15 ROUNDS OF SIMULATED ANNEALING WERE REMARK 3 CARRIED OUT TO OPTIMIZE INCLUDED NOE CONTACTS AND LENGTHS, AS REMARK 3 WELL AS J-HNHA. FINALLY, HOMOSERINE LACTONE WAS INCLUDED. THE REMARK 3 ENSEMBLE OF STRUCTURES GIVEN IS SUPERPOSED OVER THE REGION I169- REMARK 3 F176. OTHER USEFUL SUPERPOSITIONS THAT SHOULD BE EXAMINED ARE REMARK 3 D159-L163 AND L165-P168. REMARK 4 REMARK 4 1Y4E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-04. REMARK 100 THE DEPOSITION ID IS D_1000031101. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2 MM TM IV, UNLABELLED; 1 MM REMARK 210 DSS, CDCL3:CD3OH:H2O (4:4:1 V:V: REMARK 210 V); 2 MM TM IV, U-15N; 1 MM DSS, REMARK 210 CDCL3:CD3OH:H2O (4:4:1 V:V:V) REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; REMARK 210 HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.3, SPARKY 3.109 AND REMARK 210 3.110, CNS 1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 100 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D REMARK 210 HOMONUCLEAR TECHNIQUES WITH THE EXCEPTION THAT HNHA J-COUPLING REMARK 210 CONSTANTS WERE INCORPORATED. 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 LEU A 156 98.79 -165.35 REMARK 500 1 GLN A 157 -31.35 -172.09 REMARK 500 1 ASP A 159 -59.47 73.48 REMARK 500 1 VAL A 160 -44.55 87.73 REMARK 500 1 PHE A 164 -70.91 -76.71 REMARK 500 1 PRO A 168 39.90 -80.98 REMARK 500 1 ILE A 169 -71.24 -79.13 REMARK 500 1 ALA A 173 -71.10 -71.75 REMARK 500 1 TYR A 175 -61.90 69.74 REMARK 500 1 ARG A 180 57.76 -148.83 REMARK 500 2 GLN A 157 46.84 -168.97 REMARK 500 2 SER A 158 56.30 -164.66 REMARK 500 2 ASP A 159 -51.54 78.88 REMARK 500 2 VAL A 160 -54.06 71.14 REMARK 500 2 PHE A 162 11.88 -160.93 REMARK 500 2 LEU A 166 41.81 -158.10 REMARK 500 2 TYR A 175 -25.73 76.02 REMARK 500 2 PRO A 178 90.95 -48.75 REMARK 500 3 GLN A 157 -55.07 -170.53 REMARK 500 3 ASP A 159 -47.00 72.74 REMARK 500 3 VAL A 160 -52.52 90.17 REMARK 500 3 PHE A 161 32.99 -78.53 REMARK 500 3 PHE A 162 -14.23 -169.41 REMARK 500 3 LEU A 165 -30.79 86.57 REMARK 500 3 ALA A 173 -70.36 -71.67 REMARK 500 3 TYR A 175 -20.14 79.15 REMARK 500 3 PHE A 176 46.52 -94.83 REMARK 500 4 LEU A 156 -76.53 -164.35 REMARK 500 4 GLN A 157 -5.67 80.92 REMARK 500 4 SER A 158 -47.18 76.38 REMARK 500 4 VAL A 160 -50.60 66.94 REMARK 500 4 PHE A 164 -71.74 -75.32 REMARK 500 4 LEU A 166 110.93 -160.79 REMARK 500 4 ASP A 172 13.84 -152.40 REMARK 500 4 TYR A 175 -45.88 73.63 REMARK 500 4 PRO A 178 60.83 -68.33 REMARK 500 4 ARG A 180 32.38 -87.30 REMARK 500 5 GLN A 157 -39.58 -170.87 REMARK 500 5 ASP A 159 -62.18 78.12 REMARK 500 5 VAL A 160 -47.87 82.01 REMARK 500 5 PHE A 162 8.26 -166.23 REMARK 500 5 PHE A 164 -1.74 59.42 REMARK 500 5 LEU A 166 56.77 -164.47 REMARK 500 5 PRO A 167 105.82 -51.28 REMARK 500 5 ILE A 169 -108.75 -72.72 REMARK 500 5 ILE A 170 -64.65 24.19 REMARK 500 5 TYR A 175 -48.11 70.90 REMARK 500 5 PRO A 178 86.24 -50.52 REMARK 500 5 LEU A 179 -60.29 -93.81 REMARK 500 6 SER A 158 38.61 -163.46 REMARK 500 REMARK 500 THIS ENTRY HAS 954 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1Y4E A 155 180 UNP P19634 SL9A1_HUMAN 155 180 SEQADV 1Y4E HSL A 181 UNP P19634 INSERTION SEQRES 1 A 27 PHE LEU GLN SER ASP VAL PHE PHE LEU PHE LEU LEU PRO SEQRES 2 A 27 PRO ILE ILE LEU ASP ALA GLY TYR PHE LEU PRO LEU ARG SEQRES 3 A 27 HSL MODRES 1Y4E HSL A 181 SER HOMOSERINE LACTONE HET HSL A 181 13 HETNAM HSL HOMOSERINE LACTONE FORMUL 1 HSL C4 H7 N O2 HELIX 1 1 PHE A 161 LEU A 166 1 6 HELIX 2 2 ILE A 170 TYR A 175 1 6 HELIX 3 3 PHE A 176 HSL A 181 5 6 LINK C ARG A 180 N HSL A 181 1555 1555 1.38 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