Header list of 2htg.pdb file
Complete list - r 9 2 Bytes
HEADER MEMBRANE PROTEIN 25-JUL-06 2HTG
TITLE STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF TM VII OF THE NHE1
TITLE 2 ISOFORM OF THE NA+/H+ EXCHANGER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NHE1 ISOFORM OF NA+/H+ EXCHANGER 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TRANSMEMBRANE SEGMENT VII;
COMPND 5 SYNONYM: SODIUM/HYDROGEN EXCHANGER 1; NHE-1; SOLUTE CARRIER FAMILY 9
COMPND 6 MEMBER 1; APNH;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHESIZED USING SOLID-PHASE CHEMICAL PEPTIDE
SOURCE 4 SYNTHESIS TECHNIQUES. ONE UNLABELED, ONE LABELED SAMPLE (15N LABELS
SOURCE 5 AT L254, L258, G261, L264, A268, AND L273)
KEYWDS MEMBRANE PROTEIN, TRANSMEMBRANE SEGMENT, HELIX-KINK-HELIX
EXPDTA SOLUTION NMR
NUMMDL 66
AUTHOR J.K.RAINEY,J.DING,C.XU,L.FLIEGEL,B.D.SYKES
REVDAT 4 09-MAR-22 2HTG 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2HTG 1 VERSN
REVDAT 2 28-NOV-06 2HTG 1 JRNL
REVDAT 1 08-AUG-06 2HTG 0
JRNL AUTH J.DING,J.K.RAINEY,C.XU,B.D.SYKES,L.FLIEGEL
JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF TRANSMEMBRANE
JRNL TITL 2 SEGMENT VII OF THE NA(+)/H(+) EXCHANGER ISOFORM 1
JRNL REF J.BIOL.CHEM. V. 281 29817 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16861220
JRNL DOI 10.1074/JBC.M606152200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BIOPACK, XPLOR-NIH 2.13
REMARK 3 AUTHORS : VARIAN (BIOPACK), SCHWIETERS ET AL. (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1311 UNIQUE NOE RESTRAINTS WERE USED;
REMARK 3 25 DIHEDRAL ANGLE RESTRAINTS. ALL INTER-RESIDUE RESTRAINTS WERE
REMARK 3 MADE AMBIGUOUS AND CALCULATIONS WERE CARRIED OUT USING 2
REMARK 3 IDENTICAL POLYPEPTIDE CHAINS
REMARK 4
REMARK 4 2HTG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000038740.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.8
REMARK 210 IONIC STRENGTH : ~ 75 MM NA+/DPC-
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : ~ 1 MM PEPTIDE SYNTHETIC SOURCE
REMARK 210 1 (UNLABELED), 90% H2O/10% D2O, ~
REMARK 210 75 MM DODECYLPHOSPHOCHOLINE,
REMARK 210 1.0 MM DSS; ~ 1 MM PEPTIDE
REMARK 210 SYNTHETIC SOURCE 2 (6 SPECIFIC
REMARK 210 15N LABELS), 90% H2O/10% D2O, ~
REMARK 210 75 MM DODECYLPHOSPHOCHOLINE, 1.0
REMARK 210 MM DSS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 13C-NATURAL
REMARK 210 ABUNDANCE HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2005.319.14.56, SPARKY
REMARK 210 3.110, XPLOR-NIH 2.13
REMARK 210 METHOD USED : SIMULATED ANNEALING; TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 120
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 66
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: 15N LABELS WERE USED TO ASSIST IN ASSIGNMENTS. 2D
REMARK 210 HOMONUCLEAR NOESY DATA FROM LABELED AND UNLABELED SAMPLES WERE
REMARK 210 POOLED FOR STRUCTURE CALCULATION.
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 THR A 270 H TYR A 274 1.43
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 ILE A 251 14.58 -145.63
REMARK 500 1 LEU A 254 -12.71 -45.98
REMARK 500 1 HIS A 256 -82.88 -85.26
REMARK 500 1 PHE A 260 -19.90 -42.07
REMARK 500 1 GLU A 262 -86.83 -42.35
REMARK 500 1 TYR A 274 -81.09 -90.81
REMARK 500 2 VAL A 259 -71.27 -55.49
REMARK 500 2 PHE A 260 -76.67 -83.21
REMARK 500 2 SER A 263 0.76 -63.40
REMARK 500 2 ASN A 266 -80.26 -88.27
REMARK 500 2 THR A 270 -69.56 -94.83
REMARK 500 2 VAL A 272 -18.22 -44.27
REMARK 500 2 LEU A 273 -74.23 -100.71
REMARK 500 2 TYR A 274 -83.31 -49.57
REMARK 500 3 GLU A 253 2.25 -69.08
REMARK 500 3 LEU A 254 -9.91 -51.31
REMARK 500 3 HIS A 256 -83.30 -82.00
REMARK 500 3 VAL A 259 -75.71 -58.60
REMARK 500 3 VAL A 271 -69.84 -102.39
REMARK 500 3 LEU A 273 -77.22 -93.78
REMARK 500 4 LEU A 254 -13.14 -44.80
REMARK 500 4 HIS A 256 -74.71 -95.57
REMARK 500 4 ILE A 257 -35.70 -39.02
REMARK 500 4 LEU A 258 -27.61 -37.38
REMARK 500 4 PHE A 260 -80.53 -51.18
REMARK 500 5 PHE A 260 -8.00 -54.50
REMARK 500 5 SER A 263 -7.56 -54.11
REMARK 500 5 ASN A 266 0.75 -69.66
REMARK 500 6 ILE A 251 -134.49 59.70
REMARK 500 6 GLU A 253 1.07 -63.98
REMARK 500 6 LEU A 254 -10.77 -49.57
REMARK 500 6 LEU A 258 -35.17 -39.53
REMARK 500 6 VAL A 259 -71.31 -41.60
REMARK 500 6 SER A 263 -81.80 -44.44
REMARK 500 6 ALA A 268 -66.04 -92.09
REMARK 500 6 LEU A 273 -67.33 -100.28
REMARK 500 6 TYR A 274 -88.25 -58.17
REMARK 500 7 LEU A 254 -15.68 -45.28
REMARK 500 7 HIS A 256 -80.11 -80.99
REMARK 500 7 VAL A 259 0.18 -60.93
REMARK 500 7 VAL A 271 -17.94 -45.06
REMARK 500 8 ILE A 251 -40.18 64.60
REMARK 500 8 ASN A 252 -60.02 -92.38
REMARK 500 8 LEU A 254 -16.42 -42.34
REMARK 500 8 HIS A 256 -79.63 -91.34
REMARK 500 8 ILE A 257 -32.97 -39.84
REMARK 500 8 VAL A 259 -84.31 -56.79
REMARK 500 8 VAL A 269 -19.97 -49.72
REMARK 500 8 VAL A 271 -69.74 -121.09
REMARK 500 8 VAL A 272 -18.00 -44.11
REMARK 500
REMARK 500 THIS ENTRY HAS 396 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 277
DBREF 2HTG A 250 274 UNP P19634 SL9A1_HUMAN 250 274
SEQADV 2HTG LYS A 275 UNP P19634 CLONING ARTIFACT
SEQADV 2HTG LYS A 276 UNP P19634 CLONING ARTIFACT
SEQRES 1 A 28 HIS ILE ASN GLU LEU LEU HIS ILE LEU VAL PHE GLY GLU
SEQRES 2 A 28 SER LEU LEU ASN ASP ALA VAL THR VAL VAL LEU TYR LYS
SEQRES 3 A 28 LYS NH2
HET NH2 A 277 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 LEU A 255 PHE A 260 1 6
LINK C LYS A 276 N NH2 A 277 1555 1555 1.31
SITE 1 AC1 2 LYS A 275 LYS A 276
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 9 2 Bytes