Header list of 1hze.pdb file
Complete list - 25 20 Bytes
HEADER TRANSFERASE 24-JAN-01 1HZE
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOFLAVIN SYNTHASE
TITLE 2 FROM E. COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOFLAVIN SYNTHASE ALPHA CHAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1-97;
COMPND 5 EC: 2.5.1.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GREEK-KEY-BARREL, TRANSFERASE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR V.TRUFFAULT,M.COLES,T.DIERCKS,K.ABELMANN,S.EBERHARDT,H.LUETTGEN,
AUTHOR 2 A.BACHER,H.KESSLER
REVDAT 4 13-JUL-11 1HZE 1 VERSN
REVDAT 3 24-FEB-09 1HZE 1 VERSN
REVDAT 2 01-APR-03 1HZE 1 JRNL
REVDAT 1 05-SEP-01 1HZE 0
JRNL AUTH V.TRUFFAULT,M.COLES,T.DIERCKS,K.ABELMANN,S.EBERHARDT,
JRNL AUTH 2 H.LUTTGEN,A.BACHER,H.KESSLER
JRNL TITL THE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF
JRNL TITL 2 RIBOFLAVIN SYNTHASE.
JRNL REF J.MOL.BIOL. V. 309 949 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11399071
JRNL DOI 10.1006/JMBI.2001.4683
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURES BASED ON 2569 NOE RESTRAINTS
REMARK 3 (353*2 INTRARES., 365*2 SEQUENTIAL, 159*2 MEDIUM-RANGE, 372*2 LONG-
REMARK 3 RANGE, 71 INTERMOLECULAR)
REMARK 3 56*2 DIHEDRAL RESTRAINTS,
REMARK 3 42*2 H-BONDS
REMARK 4
REMARK 4 1HZE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-01.
REMARK 100 THE RCSB ID CODE IS RCSB012713.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300; 300
REMARK 210 PH : 7.3; 7.3; 7.3
REMARK 210 IONIC STRENGTH : 50 MM; 50 MM; 50 MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM U-15N,13C ; EXCESS
REMARK 210 RIBOFLAVIN; 1 MM U-15N ; EXCESS
REMARK 210 RIBOFLAVIN; 1 MM U-15N ; EXCESS U
REMARK 210 -15N,13C RIBOFLAVIN 50 MM
REMARK 210 PHOSPHATE BUFFER 50 MM HCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; NCH-
REMARK 210 NOESY; CCH-NOESY; CNH-NOESY; 3D_
REMARK 210 15N-SEPARATED_NOESY; NNH-NOESY;
REMARK 210 2D 12C-FILTERED, 13C EDITED
REMARK 210 NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR, AURELIA, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 H ASN A 45 O ASN A 83 1.40
REMARK 500 H ASN B 45 O ASN B 83 1.40
REMARK 500 O HIS B 24 H PHE B 61 1.58
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 THR A 3 -38.04 -133.92
REMARK 500 ASN A 45 16.07 53.02
REMARK 500 ASN A 55 65.52 -105.55
REMARK 500 THR B 3 -38.05 -133.97
REMARK 500 ASN B 45 16.06 53.11
REMARK 500 ASN B 55 65.51 -105.59
REMARK 500 GLU B 93 47.87 -99.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RBF A 98
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RBF B 99
DBREF 1HZE A 1 97 UNP P29015 RISA_ECOLI 1 97
DBREF 1HZE B 1 97 UNP P29015 RISA_ECOLI 1 97
SEQRES 1 A 97 MET PHE THR GLY ILE VAL GLN GLY THR ALA LYS LEU VAL
SEQRES 2 A 97 SER ILE ASP GLU LYS PRO ASN PHE ARG THR HIS VAL VAL
SEQRES 3 A 97 GLU LEU PRO ASP HIS MET LEU ASP GLY LEU GLU THR GLY
SEQRES 4 A 97 ALA SER VAL ALA HIS ASN GLY CYS CYS LEU THR VAL THR
SEQRES 5 A 97 GLU ILE ASN GLY ASN HIS VAL SER PHE ASP LEU MET LYS
SEQRES 6 A 97 GLU THR LEU ARG ILE THR ASN LEU GLY ASP LEU LYS VAL
SEQRES 7 A 97 GLY ASP TRP VAL ASN VAL GLU ARG ALA ALA LYS PHE SER
SEQRES 8 A 97 ASP GLU ILE GLY GLY HIS
SEQRES 1 B 97 MET PHE THR GLY ILE VAL GLN GLY THR ALA LYS LEU VAL
SEQRES 2 B 97 SER ILE ASP GLU LYS PRO ASN PHE ARG THR HIS VAL VAL
SEQRES 3 B 97 GLU LEU PRO ASP HIS MET LEU ASP GLY LEU GLU THR GLY
SEQRES 4 B 97 ALA SER VAL ALA HIS ASN GLY CYS CYS LEU THR VAL THR
SEQRES 5 B 97 GLU ILE ASN GLY ASN HIS VAL SER PHE ASP LEU MET LYS
SEQRES 6 B 97 GLU THR LEU ARG ILE THR ASN LEU GLY ASP LEU LYS VAL
SEQRES 7 B 97 GLY ASP TRP VAL ASN VAL GLU ARG ALA ALA LYS PHE SER
SEQRES 8 B 97 ASP GLU ILE GLY GLY HIS
HET RBF A 98 47
HET RBF B 99 47
HETNAM RBF RIBOFLAVIN
HETSYN RBF RIBOFLAVINE; VITAMIN B2
FORMUL 3 RBF 2(C17 H20 N4 O6)
HELIX 1 1 PRO A 29 ASP A 34 1 6
HELIX 2 2 MET A 64 THR A 71 1 8
HELIX 3 3 ASN A 72 LEU A 76 5 5
HELIX 4 4 PRO B 29 ASP B 34 1 6
HELIX 5 5 MET B 64 THR B 71 1 8
HELIX 6 6 ASN B 72 LEU B 76 5 5
SHEET 1 A 7 GLY A 8 GLU A 17 0
SHEET 2 A 7 ARG A 22 GLU A 27 -1 N THR A 23 O ASP A 16
SHEET 3 A 7 HIS A 58 LEU A 63 -1 N VAL A 59 O VAL A 26
SHEET 4 A 7 CYS A 47 ASN A 55 -1 O THR A 50 N ASP A 62
SHEET 5 A 7 SER A 41 HIS A 44 -1 O VAL A 42 N LEU A 49
SHEET 6 A 7 TRP A 81 ALA A 87 -1 O GLU A 85 N ALA A 43
SHEET 7 A 7 GLY A 8 GLU A 17 -1 O GLY A 8 N VAL A 84
SHEET 1 B 7 GLY B 8 GLU B 17 0
SHEET 2 B 7 ARG B 22 GLU B 27 -1 N THR B 23 O ASP B 16
SHEET 3 B 7 HIS B 58 LEU B 63 -1 N VAL B 59 O VAL B 26
SHEET 4 B 7 CYS B 47 ASN B 55 -1 O THR B 50 N ASP B 62
SHEET 5 B 7 SER B 41 HIS B 44 -1 O VAL B 42 N LEU B 49
SHEET 6 B 7 TRP B 81 ALA B 87 -1 O GLU B 85 N ALA B 43
SHEET 7 B 7 GLY B 8 GLU B 17 -1 O GLY B 8 N VAL B 84
SITE 1 AC1 8 CYS A 48 LEU A 49 THR A 50 ASP A 62
SITE 2 AC1 8 LEU A 63 MET A 64 THR A 67 ILE B 5
SITE 1 AC2 8 ILE A 5 CYS B 48 LEU B 49 THR B 50
SITE 2 AC2 8 ASP B 62 LEU B 63 MET B 64 THR B 67
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