Header list of 1e3t.pdb file
Complete list - 25 20 Bytes
HEADER TRANSHYDROGENASE 22-JUN-00 1E3T
TITLE SOLUTION STRUCTURE OF THE NADP(H) BINDING COMPONENT (DIII)
TITLE 2 OF PROTON-TRANSLOCATING TRANSHYDROGENASE FROM
TITLE 3 RHODOSPIRILLUM RUBRUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE
COMPND 3 (SUBUNIT BETA);
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: NADP(H) BINDING DOMAIN;
COMPND 6 SYNONYM: DIII, NAD(P)(+) TRANSHYDROGENASE (B-SPECIFIC),
COMPND 7 PYRIDINE NUCLEOTIDE TRANSHYDROGENASE;
COMPND 8 EC: 1.6.1.1;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOSPIRILLUM RUBRUM;
SOURCE 3 ORGANISM_TAXID: 1085;
SOURCE 4 GENE: PNTB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11C
KEYWDS TRANSHYDROGENASE, MEMBRANE PROTEIN, PROTON TRANSLOCATION,
KEYWDS 2 NMR STRUCTURE, NUCLEOTIDE BINDING
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR M.JEEVES,K.J.SMITH,P.G.QUIRK,N.P.J.COTTON,J.B.JACKSON
REVDAT 2 24-FEB-09 1E3T 1 VERSN
REVDAT 1 03-OCT-00 1E3T 0
JRNL AUTH M.JEEVES,K.J.SMITH,P.G.QUIRK,N.P.J.COTTON,
JRNL AUTH 2 J.B.JACKSON
JRNL TITL SOLUTION STRUCTURE OF THE NADP(H)-BINDING
JRNL TITL 2 COMPONENT (DIII) OF PROTON-TRANSLOCATING
JRNL TITL 3 TRANSHYDROGENASE FROM RHODOSPIRILLUM RUBRUM
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1459 248 2000
JRNL REFN ISSN 0006-3002
JRNL PMID 11004437
JRNL DOI 10.1016/S0005-2728(00)00159-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE BBA REFERNCE CITED.
REMARK 4
REMARK 4 1E3T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUN-00.
REMARK 100 THE PDBE ID CODE IS EBI-5065.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 20 MM HEPES
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 13C; 15N RESOLVED
REMARK 210 NOESYS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : UNITY-PLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA IN XPLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : NULL
REMARK 210 CONFORMERS, SELECTION CRITERIA : AVERAGE OF 10 LOWEST
REMARK 210 ENERGY STRUCTURES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: AVERAGE STRUCTURE. THE STRUCTURE WAS DETERMINED
REMARK 210 USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON UNLABELLED,
REMARK 210 15N LABELLED AND 13C, 15N-LABELLED DIII.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 ARG A 3
REMARK 465 SER A 4
REMARK 465 ILE A 5
REMARK 465 PHE A 6
REMARK 465 ASN A 7
REMARK 465 VAL A 8
REMARK 465 ILE A 9
REMARK 465 LEU A 10
REMARK 465 GLY A 11
REMARK 465 GLY A 12
REMARK 465 PHE A 13
REMARK 465 GLY A 14
REMARK 465 SER A 15
REMARK 465 GLU A 16
REMARK 465 GLY A 17
REMARK 465 GLY A 18
REMARK 465 VAL A 19
REMARK 465 ALA A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 GLY A 23
REMARK 465 GLY A 24
REMARK 465 ALA A 25
REMARK 465 ALA A 26
REMARK 465 GLY A 27
REMARK 465 ASP A 28
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 ALA A 39 - H MET A 43 1.56
REMARK 500 O GLN A 61 - H ALA A 65 1.51
REMARK 500 O HIS A 85 - H VAL A 87 1.53
REMARK 500 HG22 VAL A 87 - H2D NAP A 755 1.56
REMARK 500 O PRO A 92 - H HIS A 94 1.58
REMARK 500 O HIS A 94 - H VAL A 97 1.37
REMARK 500 O VAL A 127 - O LEU A 161 2.13
REMARK 500 O LEU A 152 - N VAL A 154 2.19
REMARK 500 O GLY A 158 - HG1 THR A 184 1.51
REMARK 500 H PHE A 162 - O MET A 185 1.47
REMARK 500 O ASN A 182 - N THR A 184 2.15
REMARK 500 O ASP A 190 - H LYS A 193 1.52
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 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 SER A 30 -101.41 -137.63
REMARK 500 VAL A 31 36.13 -175.23
REMARK 500 SER A 35 -124.61 -81.16
REMARK 500 ALA A 40 -32.80 -38.05
REMARK 500 MET A 43 -72.69 -114.87
REMARK 500 ASN A 45 46.86 -167.23
REMARK 500 SER A 47 -45.51 -19.57
REMARK 500 VAL A 49 -157.30 -135.69
REMARK 500 ILE A 50 103.26 -162.35
REMARK 500 MET A 57 -76.83 -10.66
REMARK 500 GLN A 61 -27.74 155.03
REMARK 500 ALA A 70 -8.33 -48.63
REMARK 500 VAL A 80 101.74 -168.68
REMARK 500 PRO A 86 41.78 -65.94
REMARK 500 VAL A 87 18.34 -165.65
REMARK 500 ARG A 90 -113.32 -83.69
REMARK 500 MET A 91 176.78 -53.66
REMARK 500 ALA A 102 -79.28 -79.93
REMARK 500 ASN A 103 -30.70 -178.21
REMARK 500 VAL A 104 155.46 -47.81
REMARK 500 GLU A 111 -89.80 -57.09
REMARK 500 LEU A 112 -79.59 -132.05
REMARK 500 VAL A 124 -169.62 -169.69
REMARK 500 ALA A 125 93.15 -172.74
REMARK 500 ASN A 131 -77.74 -156.58
REMARK 500 ASN A 135 91.27 -32.20
REMARK 500 PRO A 136 0.48 -69.44
REMARK 500 THR A 140 -62.18 -104.57
REMARK 500 SER A 144 157.35 -39.78
REMARK 500 ILE A 146 -159.45 -114.89
REMARK 500 MET A 149 -153.23 -176.71
REMARK 500 ILE A 151 -132.40 -55.11
REMARK 500 ASP A 153 70.37 -10.55
REMARK 500 LYS A 156 49.48 -82.09
REMARK 500 ARG A 165 -75.05 -54.10
REMARK 500 SER A 166 -70.24 -174.26
REMARK 500 VAL A 174 -140.82 -85.38
REMARK 500 GLU A 175 121.79 -36.13
REMARK 500 ASN A 176 36.42 -165.81
REMARK 500 LEU A 178 -29.12 -35.57
REMARK 500 PHE A 179 38.45 -77.69
REMARK 500 ASN A 182 132.88 -22.50
REMARK 500 ASN A 183 58.17 -14.15
REMARK 500 MET A 185 -143.15 -170.22
REMARK 500 MET A 194 -81.51 -62.33
REMARK 500 ILE A 198 -70.03 -76.31
REMARK 500 ALA A 201 58.52 -173.41
REMARK 500 MET A 202 -77.08 -51.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 29 0.30 SIDE CHAIN
REMARK 500 ARG A 67 0.31 SIDE CHAIN
REMARK 500 ARG A 90 0.32 SIDE CHAIN
REMARK 500 ARG A 165 0.15 SIDE CHAIN
REMARK 500 ARG A 181 0.16 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 755
DBREF 1E3T A 1 203 UNP Q59765 Q59765 262 464
SEQRES 1 A 203 MET ASN ARG SER ILE PHE ASN VAL ILE LEU GLY GLY PHE
SEQRES 2 A 203 GLY SER GLU GLY GLY VAL ALA ALA ALA GLY GLY ALA ALA
SEQRES 3 A 203 GLY ASP ARG SER VAL LYS ALA GLY SER ALA GLU ASP ALA
SEQRES 4 A 203 ALA PHE ILE MET LYS ASN ALA SER LYS VAL ILE ILE VAL
SEQRES 5 A 203 PRO GLY TYR GLY MET ALA VAL ALA GLN ALA GLN HIS ALA
SEQRES 6 A 203 LEU ARG GLU MET ALA ASP VAL LEU LYS LYS GLU GLY VAL
SEQRES 7 A 203 GLU VAL SER TYR ALA ILE HIS PRO VAL ALA GLY ARG MET
SEQRES 8 A 203 PRO GLY HIS MET ASN VAL LEU LEU ALA GLU ALA ASN VAL
SEQRES 9 A 203 PRO TYR ASP GLU VAL PHE GLU LEU GLU GLU ILE ASN SER
SEQRES 10 A 203 SER PHE GLN THR ALA ASP VAL ALA PHE VAL ILE GLY ALA
SEQRES 11 A 203 ASN ASP VAL THR ASN PRO ALA ALA LYS THR ASP PRO SER
SEQRES 12 A 203 SER PRO ILE TYR GLY MET PRO ILE LEU ASP VAL GLU LYS
SEQRES 13 A 203 ALA GLY THR VAL LEU PHE ILE LYS ARG SER MET ALA SER
SEQRES 14 A 203 GLY TYR ALA GLY VAL GLU ASN GLU LEU PHE PHE ARG ASN
SEQRES 15 A 203 ASN THR MET MET LEU PHE GLY ASP ALA LYS LYS MET THR
SEQRES 16 A 203 GLU GLN ILE VAL GLN ALA MET ASN
HET NAP A 755 73
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NAP PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 NAP C21 H28 N7 O17 P3
HELIX 1 1 ALA A 36 ILE A 42 1 7
HELIX 2 2 GLY A 56 ALA A 62 1 7
HELIX 3 3 ALA A 62 GLU A 76 1 15
HELIX 4 4 GLY A 93 ASN A 103 1 11
HELIX 5 5 GLU A 114 ALA A 122 1 9
HELIX 6 6 ALA A 137 THR A 140 1 4
HELIX 7 7 ALA A 191 GLN A 200 1 10
SHEET 1 A 6 GLU A 108 GLU A 111 0
SHEET 2 A 6 GLU A 79 HIS A 85 1 O ILE A 84 N PHE A 110
SHEET 3 A 6 LYS A 48 GLY A 54 1 O VAL A 49 N GLU A 79
SHEET 4 A 6 VAL A 124 GLY A 129 1 O ILE A 128 N GLY A 54
SHEET 5 A 6 GLY A 158 PHE A 162 1 O THR A 159 N ALA A 125
SHEET 6 A 6 ASN A 183 MET A 185 1 O MET A 185 N PHE A 162
SITE 1 AC1 18 TYR A 55 GLY A 56 VAL A 87 ALA A 88
SITE 2 AC1 18 GLY A 89 ARG A 90 MET A 91 PRO A 92
SITE 3 AC1 18 GLY A 129 ASN A 131 ASP A 132 VAL A 133
SITE 4 AC1 18 LYS A 164 ARG A 165 ALA A 168 SER A 169
SITE 5 AC1 18 GLY A 170 TYR A 171
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
Complete list - 25 20 Bytes