Header list of 1dwm.pdb file
Complete list - r 25 2 Bytes
HEADER SERINE PROTEINASE INHIBITOR 08-DEC-99 1DWM
TITLE SOLUTION STRUCTURE OF LINUM USITATISSINUM TRYPSIN INHIBITOR
TITLE 2 (LUTI)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LINUM USITATISSINUM TRYPSIN INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LUTI
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LINUM USITATISSIMUM;
SOURCE 3 ORGANISM_COMMON: FLAX;
SOURCE 4 ORGANISM_TAXID: 4006;
SOURCE 5 ORGAN: SEED
KEYWDS SERINE PROTEINASE INHIBITOR, TRYPSIN INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.CIERPICKI,J.OTLEWSKI
REVDAT 4 24-FEB-09 1DWM 1 VERSN
REVDAT 3 27-FEB-04 1DWM 1 HET SSBOND LINK ATOM
REVDAT 3 2 TER CONECT
REVDAT 2 05-MAR-01 1DWM 1 JRNL ATOM
REVDAT 1 17-DEC-99 1DWM 0
JRNL AUTH T.CIERPICKI,J.OTLEWSKI
JRNL TITL DETERMINATION OF A HIGH PRECISION STRUCTURE OF A
JRNL TITL 2 NOVEL PROTEIN, LINUM USITATISSIMUM TRYPSIN
JRNL TITL 3 INHIBITOR (LUTI), USING COMPUTER-AIDED ASSIGNMENT
JRNL TITL 4 OF NOESY CROSS-PEAKS
JRNL REF J.MOL.BIOL. V. 302 1179 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 11183783
JRNL DOI 10.1006/JMBI.2000.4116
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DWM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-DEC-99.
REMARK 100 THE PDBE ID CODE IS EBI-4395.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 4.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 10% H2O/90% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY, TOCSY, DQF-COSY,
REMARK 210 1H-15N HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500
REMARK 210 SPECTROMETER MODEL : UNITY PLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, SPARKY, DYANA,
REMARK 210 CNS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210 AND LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED BASING ON 1760
REMARK 210 EXPERIMENTAL RESTRAINTS DERIVED FROM TWO DIMENSIONAL 1H
REMARK 210 NMR EXPERIMENTS. NOESY CROSSPEAKS WERE ASSIGNED
REMARK 210 AUTOMATICALY USING NOAH/DYANA PROGRAM. STRUCTURE
REMARK 210 REFINEMENT WAS ACCOMPLISHED IN CNS.
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: 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 MET A 20 - HG1 THR A 24 1.57
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 1 ARG A 2 70.91 -152.67
REMARK 500 1 ARG A 3 88.91 -151.12
REMARK 500 1 ALA A 42 81.85 -66.86
REMARK 500 1 ASP A 46 171.95 -52.04
REMARK 500 1 ILE A 68 106.31 -39.34
REMARK 500 2 ARG A 3 89.23 -151.35
REMARK 500 2 TRP A 10 74.93 -111.40
REMARK 500 2 ASP A 46 161.12 -47.25
REMARK 500 2 ILE A 68 109.34 -47.51
REMARK 500 3 ARG A 2 80.11 58.87
REMARK 500 3 ARG A 3 98.13 -174.42
REMARK 500 3 TRP A 10 67.46 -113.39
REMARK 500 3 PRO A 66 97.49 -58.86
REMARK 500 4 ARG A 2 72.62 -156.96
REMARK 500 4 ARG A 3 74.36 -101.52
REMARK 500 4 LYS A 7 143.52 -33.23
REMARK 500 4 TRP A 10 74.81 -108.79
REMARK 500 4 SER A 41 -178.09 -68.09
REMARK 500 4 ASP A 46 159.36 -45.95
REMARK 500 5 ARG A 2 52.50 -103.22
REMARK 500 5 ARG A 3 84.24 -153.68
REMARK 500 5 TRP A 10 74.36 -109.52
REMARK 500 5 ARG A 30 1.88 -63.70
REMARK 500 5 PRO A 66 99.84 -60.32
REMARK 500 6 ARG A 2 73.77 -154.94
REMARK 500 6 TRP A 10 67.35 -116.71
REMARK 500 6 ASN A 29 78.18 -119.44
REMARK 500 6 ALA A 42 81.14 -62.54
REMARK 500 6 ASP A 46 152.65 -37.74
REMARK 500 6 PRO A 66 98.32 -56.92
REMARK 500 7 TRP A 10 74.88 -113.52
REMARK 500 7 SER A 41 -173.93 -65.73
REMARK 500 7 ASP A 46 155.00 -45.52
REMARK 500 7 ILE A 68 103.54 -44.11
REMARK 500 8 ARG A 2 75.30 -158.38
REMARK 500 8 ARG A 3 94.83 -174.40
REMARK 500 8 TRP A 10 74.16 -119.49
REMARK 500 8 ARG A 30 1.88 -64.62
REMARK 500 8 SER A 41 -174.24 -66.01
REMARK 500 8 PRO A 66 103.39 -58.06
REMARK 500 8 ILE A 68 107.40 -41.81
REMARK 500 9 ARG A 2 61.84 -154.69
REMARK 500 9 SER A 41 -164.23 -72.76
REMARK 500 10 ARG A 2 77.87 -159.47
REMARK 500 10 ARG A 3 83.28 46.82
REMARK 500 10 TRP A 10 74.14 -108.65
REMARK 500 10 SER A 41 -166.09 -68.69
REMARK 500 10 ILE A 68 116.43 -38.28
REMARK 500 11 ARG A 2 59.28 -113.85
REMARK 500 11 ARG A 3 81.31 53.73
REMARK 500 11 ASN A 29 79.48 -118.73
REMARK 500 11 SER A 41 -162.38 -70.46
REMARK 500 11 ILE A 68 116.52 -36.63
REMARK 500 12 ARG A 2 64.14 -155.58
REMARK 500 12 TRP A 10 73.95 -108.00
REMARK 500 12 PRO A 66 99.04 -59.42
REMARK 500 13 ARG A 2 78.50 51.21
REMARK 500 13 ARG A 3 105.24 -164.79
REMARK 500 13 TRP A 10 73.11 -110.86
REMARK 500 13 SER A 41 -167.72 -66.44
REMARK 500 13 ASP A 46 159.56 -46.48
REMARK 500 13 PRO A 66 95.46 -54.47
REMARK 500 13 ILE A 68 109.39 -44.23
REMARK 500 14 ARG A 2 68.16 -168.20
REMARK 500 14 TRP A 10 70.06 -114.82
REMARK 500 14 SER A 41 -178.00 -61.43
REMARK 500 14 PRO A 66 100.30 -59.05
REMARK 500 14 ILE A 68 109.92 -47.71
REMARK 500 15 ARG A 2 60.86 -106.69
REMARK 500 15 ARG A 3 97.57 53.28
REMARK 500 15 TRP A 10 72.13 -119.45
REMARK 500 15 SER A 41 -167.68 -67.61
REMARK 500 16 ARG A 3 98.98 -161.54
REMARK 500 16 TRP A 10 72.85 -115.48
REMARK 500 16 ASP A 46 163.34 -41.88
REMARK 500 16 PRO A 66 90.82 -60.81
REMARK 500 17 ARG A 2 81.90 51.64
REMARK 500 17 ARG A 3 94.17 -167.19
REMARK 500 17 TRP A 10 69.89 -112.62
REMARK 500 17 SER A 41 -166.58 -68.27
REMARK 500 18 ARG A 2 78.16 57.97
REMARK 500 18 ARG A 3 67.63 -160.99
REMARK 500 18 TRP A 10 68.93 -110.34
REMARK 500 18 ARG A 30 0.97 -62.58
REMARK 500 18 SER A 41 -176.01 -67.62
REMARK 500 18 PRO A 66 89.29 -65.69
REMARK 500 19 ARG A 2 84.66 -160.46
REMARK 500 19 ARG A 3 77.34 -154.01
REMARK 500 19 TRP A 10 73.48 -112.52
REMARK 500 19 SER A 41 -179.32 -67.62
REMARK 500 19 ASP A 46 160.84 -44.81
REMARK 500 19 PRO A 66 92.17 -57.75
REMARK 500 20 ARG A 3 90.65 55.77
REMARK 500 20 TRP A 10 68.15 -119.73
REMARK 500 20 SER A 41 -177.22 -69.71
REMARK 500 20 PRO A 66 99.86 -57.91
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.
DBREF 1DWM A 0 69 PDB 1DWM 1DWM 0 69
SEQRES 1 A 70 ACE SER ARG ARG CYS PRO GLY LYS ASN ALA TRP PRO GLU
SEQRES 2 A 70 LEU VAL GLY LYS SER GLY ASN MET ALA ALA ALA THR VAL
SEQRES 3 A 70 GLU ARG GLU ASN ARG ASN VAL HIS ALA ILE VAL LEU LYS
SEQRES 4 A 70 GLU GLY SER ALA MET THR LYS ASP PHE ARG CYS ASP ARG
SEQRES 5 A 70 VAL TRP VAL ILE VAL ASN ASP HIS GLY VAL VAL THR SER
SEQRES 6 A 70 VAL PRO HIS ILE THR
HET ACE A 0 6
HETNAM ACE ACETYL GROUP
FORMUL 2 ACE C2 H4 O
HELIX 1 H1 TRP A 10 LEU A 13 5 4
HELIX 2 H2 GLY A 18 GLU A 28 1 11
SHEET 1 S1 1 HIS A 33 LYS A 38 0
SHEET 1 S2 1 ARG A 51 VAL A 56 1 N VAL A 56 O HIS A 33
SSBOND 1 CYS A 4 CYS A 49 1555 1555 2.03
LINK C ACE A 0 N SER A 1 1555 1555 1.33
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 25 2 Bytes