Header list of 1h7j.pdb file
Complete list - 25 20 Bytes
HEADER ACYLTRANSFERASE 08-JUL-01 1H7J
TITLE SOLUTION STRUCTURE OF THE 26 AA PRESEQUENCE OF 5-ALAS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOLEVULINIC ACID SYNTHASE 2, ERYTHROID;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PRESEQUENCE RESIDUES 1-26;
COMPND 5 SYNONYM: AMINO LEVULINATE SYNTHASE, 5-AMINOLEVULINIC ACID
COMPND 6 SYNTHASE, DELTA-AMINOLEVULINATE SYNTHASE, DELTA-ALA
COMPND 7 SYNTHETASE;
COMPND 8 EC: 2.3.1.37
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 4 ORGANISM_TAXID: 10090
KEYWDS ACYLTRANSFERASE, ALAS, PRESEQUENCE, NMR STRUCTURE
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR B.J.GOODFELLOW,J.S.DIAS,G.C.FERREIRA,V.WRAY,P.HENKLEIN,
AUTHOR 2 A.L.MACEDO
REVDAT 2 24-FEB-09 1H7J 1 VERSN
REVDAT 1 18-OCT-01 1H7J 0
JRNL AUTH B.J.GOODFELLOW,J.S.DIAS,G.C.FERREIRA,P.HENKLEIN,
JRNL AUTH 2 V.WRAY,A.L.MACEDO
JRNL TITL THE SOLUTION STRUCTURE AND HEME BINDING OF THE
JRNL TITL 2 PRESEQUENCE OF MURINE 5-AMINOLEVULINATE SYNTHASE
JRNL REF FEBS LETT. V. 505 325 2001
JRNL REFN ISSN 0014-5793
JRNL PMID 11566198
JRNL DOI 10.1016/S0014-5793(01)02818-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H7J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUL-01.
REMARK 100 THE PDBE ID CODE IS EBI-8281.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY, COSY, TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: 150MS NOESY, 70MS TOCSY
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 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 1 VAL A 2 -157.62 -164.62
REMARK 500 1 LEU A 8 48.33 -91.31
REMARK 500 1 ARG A 9 -92.12 -58.60
REMARK 500 2 ALA A 3 59.42 -110.57
REMARK 500 2 ALA A 5 -45.24 -159.63
REMARK 500 2 MET A 6 40.32 -88.82
REMARK 500 2 LEU A 7 -47.72 -154.48
REMARK 500 2 PRO A 12 -84.28 -75.06
REMARK 500 2 LEU A 14 97.40 -178.94
REMARK 500 2 LYS A 24 52.37 -117.40
REMARK 500 3 ALA A 4 -48.22 -144.80
REMARK 500 3 MET A 6 -36.92 -37.77
REMARK 500 3 LEU A 7 -61.33 -94.73
REMARK 500 3 LEU A 8 64.81 38.54
REMARK 500 3 SER A 10 59.87 -176.72
REMARK 500 3 VAL A 13 -95.20 -125.32
REMARK 500 3 LYS A 24 78.36 -155.86
REMARK 500 4 ALA A 3 54.17 -141.09
REMARK 500 4 ALA A 4 -72.93 -64.25
REMARK 500 4 LEU A 8 49.46 -143.73
REMARK 500 4 SER A 10 28.00 43.48
REMARK 500 4 CYS A 11 88.90 46.96
REMARK 500 4 LEU A 14 -62.17 -173.35
REMARK 500 4 PRO A 18 -70.57 -75.05
REMARK 500 4 LEU A 21 -54.17 -136.50
REMARK 500 4 LYS A 24 83.60 -166.27
REMARK 500 5 VAL A 2 -157.58 -166.56
REMARK 500 5 ALA A 3 47.89 -106.41
REMARK 500 5 ALA A 4 58.96 -147.15
REMARK 500 5 ALA A 5 -47.09 -157.30
REMARK 500 5 MET A 6 38.77 -88.49
REMARK 500 5 LEU A 7 -47.15 -151.27
REMARK 500 5 LEU A 8 60.24 -117.90
REMARK 500 5 CYS A 11 65.06 39.18
REMARK 500 5 VAL A 13 -45.20 -158.89
REMARK 500 5 LEU A 14 -56.19 77.75
REMARK 500 5 SER A 15 -60.09 176.50
REMARK 500 5 LEU A 21 49.64 -91.27
REMARK 500 6 ALA A 3 58.37 -161.34
REMARK 500 6 PRO A 12 -72.25 -75.01
REMARK 500 6 LEU A 14 -67.53 -174.28
REMARK 500 6 SER A 15 -57.38 -173.72
REMARK 500 6 VAL A 25 -107.70 -105.72
REMARK 500 7 ALA A 4 29.85 40.45
REMARK 500 7 ALA A 5 -47.98 -160.31
REMARK 500 7 LEU A 8 81.82 51.25
REMARK 500 7 SER A 10 41.37 169.78
REMARK 500 7 CYS A 11 76.65 43.20
REMARK 500 7 LEU A 14 94.77 52.10
REMARK 500 7 VAL A 25 -107.93 -108.81
REMARK 500 8 VAL A 2 -157.61 -170.36
REMARK 500 8 ALA A 3 53.08 -98.22
REMARK 500 8 ALA A 4 59.81 -109.85
REMARK 500 8 ALA A 5 -43.71 -165.18
REMARK 500 8 MET A 6 37.26 -89.09
REMARK 500 8 LEU A 7 -48.64 -149.21
REMARK 500 8 LEU A 8 49.80 -105.69
REMARK 500 8 SER A 10 55.92 -140.46
REMARK 500 8 LEU A 14 89.73 56.74
REMARK 500 8 VAL A 25 -107.62 -105.51
REMARK 500 9 VAL A 2 -156.74 -95.77
REMARK 500 9 LEU A 8 46.44 -87.90
REMARK 500 9 CYS A 11 151.28 63.11
REMARK 500 9 SER A 15 158.67 58.68
REMARK 500 9 VAL A 25 -107.40 -103.29
REMARK 500 10 ALA A 3 60.15 -108.29
REMARK 500 10 LEU A 8 -52.22 -150.06
REMARK 500 10 LEU A 21 -67.04 -150.72
REMARK 500 10 LYS A 24 33.13 -96.53
REMARK 500 10 VAL A 25 -107.95 -123.12
REMARK 500 11 ALA A 3 68.65 -111.87
REMARK 500 11 ALA A 4 39.38 -159.41
REMARK 500 11 ALA A 5 -47.15 -133.75
REMARK 500 11 MET A 6 39.34 -88.38
REMARK 500 11 LEU A 7 -45.51 -160.36
REMARK 500 11 SER A 10 67.01 -169.01
REMARK 500 11 VAL A 13 -95.18 -140.64
REMARK 500 11 LEU A 14 -56.29 77.75
REMARK 500 11 VAL A 25 -107.33 -103.37
REMARK 500 12 ALA A 4 52.28 -177.24
REMARK 500 12 ALA A 5 -49.80 -172.41
REMARK 500 12 LEU A 8 44.10 -92.47
REMARK 500 12 LYS A 24 32.24 -99.64
REMARK 500 12 VAL A 25 -107.36 -103.41
REMARK 500 13 ALA A 4 55.02 178.62
REMARK 500 13 ALA A 5 -52.00 178.75
REMARK 500 13 LEU A 8 51.33 -100.28
REMARK 500 13 SER A 10 -58.51 -143.91
REMARK 500 13 LEU A 14 -53.48 -174.89
REMARK 500 13 SER A 15 136.04 -179.85
REMARK 500 13 PRO A 18 -70.36 -75.00
REMARK 500 13 VAL A 25 -107.89 -115.91
REMARK 500 14 ALA A 4 -47.41 -135.63
REMARK 500 14 ALA A 5 40.91 -91.26
REMARK 500 14 ARG A 9 38.53 -93.89
REMARK 500 14 CYS A 11 81.35 44.00
REMARK 500 14 LEU A 14 77.59 62.36
REMARK 500 14 PRO A 18 -70.34 -75.01
REMARK 500 14 LEU A 21 -58.34 -120.09
REMARK 500 14 LYS A 24 80.76 -159.86
REMARK 500 14 VAL A 25 -107.35 -103.32
REMARK 500 15 ALA A 4 -53.16 -126.95
REMARK 500 15 LEU A 8 56.40 -111.41
REMARK 500 15 SER A 10 24.19 48.11
REMARK 500 15 CYS A 11 151.02 63.30
REMARK 500 15 VAL A 13 -95.20 -136.65
REMARK 500 15 LEU A 21 -68.96 -124.51
REMARK 500 15 VAL A 25 -107.39 -103.41
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1H7J A 1 26 UNP Q64452 Q64452 1 26
SEQRES 1 A 26 MET VAL ALA ALA ALA MET LEU LEU ARG SER CYS PRO VAL
SEQRES 2 A 26 LEU SER GLN GLY PRO THR GLY LEU LEU GLY LYS VAL ALA
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 - 25 20 Bytes