Header list of 1yka.pdb file
Complete list - r 2 2 Bytes
HEADER ELECTRON TRANSPORT 17-JAN-05 1YKA
TITLE SOLUTION STRUCTURE OF GRX4, A MONOTHIOL GLUTAREDOXIN FROM E. COLI.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOTHIOL GLUTAREDOXIN YDHD;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MONOTHIOL GLUTAREDOXIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: YDHD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)GRXA-GRXB-GRXC-;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-15B
KEYWDS MIXED ALPHA/BETA FOLD, THIOREDOXIN FOLD, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.FLADVAD,M.BELLANDA,A.P.FERNANDES,C.ANDRESEN,S.MAMMI,A.HOLMGREN,
AUTHOR 2 A.VLAMIS-GARDIKAS,M.SUNNERHAGEN
REVDAT 4 02-MAR-22 1YKA 1 REMARK
REVDAT 3 24-FEB-09 1YKA 1 VERSN
REVDAT 2 19-JUL-05 1YKA 1 JRNL
REVDAT 1 26-APR-05 1YKA 0
JRNL AUTH M.FLADVAD,M.BELLANDA,A.P.FERNANDES,S.MAMMI,
JRNL AUTH 2 A.VLAMIS-GARDIKAS,A.HOLMGREN,M.SUNNERHAGEN
JRNL TITL MOLECULAR MAPPING OF FUNCTIONALITIES IN THE SOLUTION
JRNL TITL 2 STRUCTURE OF REDUCED GRX4, A MONOTHIOL GLUTAREDOXIN FROM
JRNL TITL 3 ESCHERICHIA COLI.
JRNL REF J.BIOL.CHEM. V. 280 24553 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15840565
JRNL DOI 10.1074/JBC.M500679200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROSA 3.6, CNS 1.1
REMARK 3 AUTHORS : GUNTERT (PROSA), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 2703 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 77 J COUPLING DERIVED DIHEDRAL
REMARK 3 ANGLE RESTRAINTS, 164 BACKBONE TORSION ANGLE RESTRAINTS DERIVED
REMARK 3 FROM CHEMICAL SHIFTS
REMARK 4
REMARK 4 1YKA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031611.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 125MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM GRX4 U,15N,15N-13C; 5MM
REMARK 210 PHOPSPHATE, 125MM KCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D TOCSY; HNCA;
REMARK 210 DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.4, ARIA 1.2, CNS 1.1
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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 HB2 LYS A 22 HB2 LEU A 53 1.20
REMARK 500 HD3 LYS A 101 H GLU A 115 1.27
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 THR A 3 46.40 -72.97
REMARK 500 1 THR A 4 -46.05 -168.03
REMARK 500 1 PRO A 28 32.29 -74.41
REMARK 500 1 SER A 29 46.52 -165.07
REMARK 500 1 GLU A 45 -153.58 -100.36
REMARK 500 1 ILE A 52 -34.58 -146.68
REMARK 500 1 ASN A 67 -54.18 -174.73
REMARK 500 1 THR A 70 -127.73 -143.06
REMARK 500 1 CYS A 84 -70.76 -78.01
REMARK 500 1 LYS A 108 -147.32 -100.38
REMARK 500 1 SER A 109 -155.62 -74.45
REMARK 500 1 PRO A 112 47.31 -95.59
REMARK 500 2 LEU A 27 112.59 -161.42
REMARK 500 2 PRO A 28 14.30 -69.56
REMARK 500 2 SER A 29 47.14 -163.21
REMARK 500 2 GLU A 45 -152.12 -128.25
REMARK 500 2 ILE A 52 -37.05 -151.63
REMARK 500 2 ASN A 67 -54.97 -175.89
REMARK 500 2 THR A 70 -128.08 -143.19
REMARK 500 2 LYS A 108 -158.27 -91.94
REMARK 500 2 ASP A 113 -104.96 -120.69
REMARK 500 3 SER A 2 -125.35 -79.12
REMARK 500 3 THR A 3 -24.18 74.17
REMARK 500 3 PRO A 28 26.30 -74.99
REMARK 500 3 SER A 29 49.86 -164.33
REMARK 500 3 CYS A 30 61.03 -67.06
REMARK 500 3 GLU A 45 -154.62 -97.37
REMARK 500 3 ILE A 52 -37.32 -149.68
REMARK 500 3 ASN A 67 -55.40 -174.99
REMARK 500 3 THR A 70 -124.38 -142.44
REMARK 500 3 SER A 109 -140.10 -84.73
REMARK 500 3 GLU A 110 45.55 -72.77
REMARK 500 3 ASP A 113 -124.95 -84.01
REMARK 500 4 SER A 2 -41.42 70.82
REMARK 500 4 MET A 21 -154.05 -148.10
REMARK 500 4 LEU A 27 116.67 -160.46
REMARK 500 4 PRO A 28 31.43 -72.94
REMARK 500 4 SER A 29 51.82 -169.61
REMARK 500 4 GLU A 45 -154.68 -99.95
REMARK 500 4 ILE A 52 -33.93 -143.50
REMARK 500 4 ASN A 67 -55.02 -174.82
REMARK 500 4 THR A 70 -128.13 -143.07
REMARK 500 4 LYS A 108 -149.91 -89.58
REMARK 500 4 SER A 109 -148.36 -82.84
REMARK 500 4 PRO A 112 49.81 -99.70
REMARK 500 5 THR A 3 -121.48 53.09
REMARK 500 5 THR A 4 132.50 75.18
REMARK 500 5 PRO A 28 20.37 -71.99
REMARK 500 5 SER A 29 52.35 -161.97
REMARK 500 5 GLU A 45 -151.85 -115.09
REMARK 500
REMARK 500 THIS ENTRY HAS 229 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 18 ALA A 60 10.70
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1YKA A 1 115 UNP P0AC69 YDHD_ECOLI 1 115
SEQRES 1 A 115 MET SER THR THR ILE GLU LYS ILE GLN ARG GLN ILE ALA
SEQRES 2 A 115 GLU ASN PRO ILE LEU LEU TYR MET LYS GLY SER PRO LYS
SEQRES 3 A 115 LEU PRO SER CYS GLY PHE SER ALA GLN ALA VAL GLN ALA
SEQRES 4 A 115 LEU ALA ALA CYS GLY GLU ARG PHE ALA TYR VAL ASP ILE
SEQRES 5 A 115 LEU GLN ASN PRO ASP ILE ARG ALA GLU LEU PRO LYS TYR
SEQRES 6 A 115 ALA ASN TRP PRO THR PHE PRO GLN LEU TRP VAL ASP GLY
SEQRES 7 A 115 GLU LEU VAL GLY GLY CYS ASP ILE VAL ILE GLU MET TYR
SEQRES 8 A 115 GLN ARG GLY GLU LEU GLN GLN LEU ILE LYS GLU THR ALA
SEQRES 9 A 115 ALA LYS TYR LYS SER GLU GLU PRO ASP ALA GLU
HELIX 1 1 THR A 4 ASN A 15 1 12
HELIX 2 2 PHE A 32 GLY A 44 1 13
HELIX 3 3 ASN A 55 ASN A 67 1 13
HELIX 4 4 CYS A 84 GLY A 94 1 11
HELIX 5 5 GLY A 94 LYS A 108 1 15
SHEET 1 A 4 ALA A 48 ASP A 51 0
SHEET 2 A 4 ILE A 17 MET A 21 1 N LEU A 19 O VAL A 50
SHEET 3 A 4 GLN A 73 VAL A 76 -1 O TRP A 75 N LEU A 18
SHEET 4 A 4 GLU A 79 LEU A 80 -1 O GLU A 79 N VAL A 76
CISPEP 1 PHE A 71 PRO A 72 1 -0.84
CISPEP 2 PHE A 71 PRO A 72 2 -1.78
CISPEP 3 PHE A 71 PRO A 72 3 -1.30
CISPEP 4 PHE A 71 PRO A 72 4 -0.89
CISPEP 5 PHE A 71 PRO A 72 5 -0.69
CISPEP 6 PHE A 71 PRO A 72 6 -2.66
CISPEP 7 PHE A 71 PRO A 72 7 -1.06
CISPEP 8 PHE A 71 PRO A 72 8 -1.88
CISPEP 9 PHE A 71 PRO A 72 9 -1.79
CISPEP 10 PHE A 71 PRO A 72 10 -2.06
CISPEP 11 PHE A 71 PRO A 72 11 -1.19
CISPEP 12 PHE A 71 PRO A 72 12 -0.42
CISPEP 13 PHE A 71 PRO A 72 13 -0.91
CISPEP 14 PHE A 71 PRO A 72 14 -2.03
CISPEP 15 PHE A 71 PRO A 72 15 -1.12
CISPEP 16 PHE A 71 PRO A 72 16 -0.64
CISPEP 17 PHE A 71 PRO A 72 17 -1.50
CISPEP 18 PHE A 71 PRO A 72 18 -1.24
CISPEP 19 PHE A 71 PRO A 72 19 -1.31
CISPEP 20 PHE A 71 PRO A 72 20 -1.42
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 2 2 Bytes