Header list of 1de1.pdb file
Complete list - b 16 2 Bytes
HEADER ELECTRON TRANSPORT 12-NOV-99 1DE1
TITLE NMR STRUCTURES OF OXIDIZED BACTERIOPHAGE T4 GLUTAREDOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: OXIDIZED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE T4;
SOURCE 3 ORGANISM_TAXID: 10665;
SOURCE 4 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN BACTERIOPHAGE T4
KEYWDS GLUTAREDOXIN, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR Y.WANG,G.AMEGBEY,D.S.WISHART
REVDAT 5 16-FEB-22 1DE1 1 REMARK
REVDAT 4 24-FEB-09 1DE1 1 VERSN
REVDAT 3 30-MAR-04 1DE1 1 JRNL
REVDAT 2 30-JUN-00 1DE1 1 SOURCE EXPDTA
REVDAT 1 24-NOV-99 1DE1 0
JRNL AUTH Y.WANG,G.AMEGBEY,D.S.WISHART
JRNL TITL SOLUTION STRUCTURES OF REDUCED AND OXIDIZED BACTERIOPHAGE T4
JRNL TITL 2 GLUTAREDOXIN.
JRNL REF J.BIOMOL.NMR V. 29 85 2004
JRNL REFN ISSN 0925-2738
JRNL PMID 15017142
JRNL DOI 10.1023/B:JNMR.0000019506.30351.CA
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, X-PLOR 3.85
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER, A. T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 1050 DISTANCE, 188 DIHEDRAL ANGLE AND
REMARK 3 201 H
REMARK 3 CHEMICAL SHIFT CONSTRAINTS.
REMARK 4
REMARK 4 1DE1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000010006.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM T4 GLUTAREDOXIN; 50MM PH7.0
REMARK 210 PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY, TOCSY, DQF_COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.85
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY,TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 24
REMARK 210
REMARK 210 REMARK: THE STRUCTURES WERE DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES
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 ILE A 36 H ASP A 44 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
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 ASP A 8 -65.76 -107.80
REMARK 500 1 SER A 9 -32.53 168.79
REMARK 500 1 CYS A 14 115.36 -179.37
REMARK 500 1 LYS A 28 65.05 71.67
REMARK 500 1 ARG A 57 28.07 -150.64
REMARK 500 1 ASP A 58 -156.63 -121.70
REMARK 500 1 PHE A 79 -70.08 -79.66
REMARK 500 2 SER A 9 -13.76 83.81
REMARK 500 2 CYS A 14 88.93 -179.26
REMARK 500 2 LYS A 28 54.07 70.34
REMARK 500 2 PRO A 71 58.85 -63.74
REMARK 500 2 ASP A 72 29.74 90.49
REMARK 500 2 PHE A 79 -70.55 -70.79
REMARK 500 2 PHE A 86 -70.18 -87.87
REMARK 500 3 CYS A 14 108.09 -178.68
REMARK 500 3 PHE A 86 -70.74 -96.17
REMARK 500 4 ASP A 8 -76.21 -94.41
REMARK 500 4 SER A 9 -34.50 174.53
REMARK 500 4 LYS A 28 42.48 74.16
REMARK 500 4 ARG A 57 35.33 -95.51
REMARK 500 4 ASP A 58 -147.21 -120.88
REMARK 500 4 GLN A 60 98.21 -69.19
REMARK 500 4 SER A 74 152.76 179.92
REMARK 500 4 PHE A 79 -70.66 -71.56
REMARK 500 5 ASP A 8 -81.08 -72.15
REMARK 500 5 SER A 9 -41.91 174.12
REMARK 500 5 CYS A 14 73.82 -174.66
REMARK 500 5 LYS A 28 62.28 69.40
REMARK 500 5 ARG A 57 30.87 -150.53
REMARK 500 5 ASP A 58 -151.34 -121.00
REMARK 500 5 PHE A 86 -69.80 -90.65
REMARK 500 6 SER A 9 -33.15 166.73
REMARK 500 6 CYS A 14 108.32 -172.14
REMARK 500 6 PHE A 43 170.29 -59.40
REMARK 500 6 SER A 74 113.08 -167.64
REMARK 500 6 PHE A 86 -70.38 -87.64
REMARK 500 7 CYS A 14 123.78 -175.61
REMARK 500 7 LYS A 28 61.14 67.08
REMARK 500 7 ARG A 57 31.35 -93.90
REMARK 500 7 ASP A 58 -153.46 -121.15
REMARK 500 7 PHE A 86 -70.34 -87.97
REMARK 500 8 CYS A 14 113.70 -167.92
REMARK 500 8 LYS A 28 60.99 68.39
REMARK 500 8 PHE A 79 -70.03 -71.28
REMARK 500 8 PHE A 86 -70.37 -95.62
REMARK 500 9 CYS A 14 119.00 -175.04
REMARK 500 9 LYS A 40 -8.00 -58.79
REMARK 500 9 ARG A 57 -167.60 -125.25
REMARK 500 9 PHE A 79 -70.20 -74.36
REMARK 500 10 CYS A 14 111.65 -175.95
REMARK 500
REMARK 500 THIS ENTRY HAS 213 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DE2 RELATED DB: PDB
REMARK 900 REDUCED BACTERIOPHAGE T4 GLUTAREDOXIN
DBREF 1DE1 A 1 87 UNP P00276 GLRX_BPT4 1 87
SEQRES 1 A 87 MET PHE LYS VAL TYR GLY TYR ASP SER ASN ILE HIS LYS
SEQRES 2 A 87 CYS VAL TYR CYS ASP ASN ALA LYS ARG LEU LEU THR VAL
SEQRES 3 A 87 LYS LYS GLN PRO PHE GLU PHE ILE ASN ILE MET PRO GLU
SEQRES 4 A 87 LYS GLY VAL PHE ASP ASP GLU LYS ILE ALA GLU LEU LEU
SEQRES 5 A 87 THR LYS LEU GLY ARG ASP THR GLN ILE GLY LEU THR MET
SEQRES 6 A 87 PRO GLN VAL PHE ALA PRO ASP GLY SER HIS ILE GLY GLY
SEQRES 7 A 87 PHE ASP GLN LEU ARG GLU TYR PHE LYS
HELIX 1 1 VAL A 15 LYS A 28 1 14
HELIX 2 2 ASP A 44 GLY A 56 1 13
HELIX 3 3 GLY A 78 LYS A 87 1 10
SHEET 1 A 4 PHE A 31 ASN A 35 0
SHEET 2 A 4 PHE A 2 GLY A 6 1 O PHE A 2 N GLU A 32
SHEET 3 A 4 GLN A 67 ALA A 70 -1 N GLN A 67 O TYR A 5
SHEET 4 A 4 SER A 74 GLY A 77 -1 O SER A 74 N ALA A 70
SSBOND 1 CYS A 14 CYS A 17 1555 1555 2.03
CISPEP 1 MET A 65 PRO A 66 1 0.53
CISPEP 2 MET A 65 PRO A 66 2 0.39
CISPEP 3 MET A 65 PRO A 66 3 0.60
CISPEP 4 MET A 65 PRO A 66 4 0.31
CISPEP 5 MET A 65 PRO A 66 5 0.25
CISPEP 6 MET A 65 PRO A 66 6 0.31
CISPEP 7 MET A 65 PRO A 66 7 0.39
CISPEP 8 MET A 65 PRO A 66 8 0.37
CISPEP 9 MET A 65 PRO A 66 9 0.26
CISPEP 10 MET A 65 PRO A 66 10 0.51
CISPEP 11 MET A 65 PRO A 66 11 0.56
CISPEP 12 MET A 65 PRO A 66 12 0.31
CISPEP 13 MET A 65 PRO A 66 13 0.56
CISPEP 14 MET A 65 PRO A 66 14 0.41
CISPEP 15 MET A 65 PRO A 66 15 0.67
CISPEP 16 MET A 65 PRO A 66 16 0.42
CISPEP 17 MET A 65 PRO A 66 17 0.46
CISPEP 18 MET A 65 PRO A 66 18 0.29
CISPEP 19 MET A 65 PRO A 66 19 0.50
CISPEP 20 MET A 65 PRO A 66 20 0.34
CISPEP 21 MET A 65 PRO A 66 21 0.29
CISPEP 22 MET A 65 PRO A 66 22 0.18
CISPEP 23 MET A 65 PRO A 66 23 0.20
CISPEP 24 MET A 65 PRO A 66 24 0.56
CISPEP 25 MET A 65 PRO A 66 25 0.32
CISPEP 26 MET A 65 PRO A 66 26 0.51
CISPEP 27 MET A 65 PRO A 66 27 0.61
CISPEP 28 MET A 65 PRO A 66 28 0.40
CISPEP 29 MET A 65 PRO A 66 29 0.26
CISPEP 30 MET A 65 PRO A 66 30 0.52
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 - b 16 2 Bytes