Header list of 1b1a.pdb file
Complete list - 25 20 Bytes
HEADER ISOMERASE 19-NOV-98 1B1A
TITLE GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE MUTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: B12-BINDING SUBUNIT;
COMPND 5 SYNONYM: GLMS;
COMPND 6 EC: 5.4.99.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM COCHLEARIUM;
SOURCE 3 ORGANISM_TAXID: 1494;
SOURCE 4 ATCC: 17787;
SOURCE 5 GENE: GLMS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: MC4100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PJF 118 HE;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: POZ3;
SOURCE 12 EXPRESSION_SYSTEM_GENE: GLMS;
SOURCE 13 OTHER_DETAILS: DSM 1285
KEYWDS ISOMERASE, GLUTAMATE MUTASE, B12-BINDING SUBUNIT
EXPDTA SOLUTION NMR
AUTHOR B.HOFFMANN,R.KONRAT,H.BOTHE,W.BUCKEL,B.KRAEUTLER
REVDAT 4 24-NOV-10 1B1A 1 COMPND
REVDAT 3 24-FEB-09 1B1A 1 VERSN
REVDAT 2 01-APR-03 1B1A 1 JRNL
REVDAT 1 13-JUL-99 1B1A 0
JRNL AUTH B.HOFFMANN,R.KONRAT,H.BOTHE,W.BUCKEL,B.KRAUTLER
JRNL TITL STRUCTURE AND DYNAMICS OF THE B12-BINDING SUBUNIT OF
JRNL TITL 2 GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM.
JRNL REF EUR.J.BIOCHEM. V. 263 178 1999
JRNL REFN ISSN 0014-2956
JRNL PMID 10429202
JRNL DOI 10.1046/J.1432-1327.1999.00482.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH O.ZELDER,B.BEATRIX,W.BUCKEL
REMARK 1 TITL CLONING, SEQUENCING AND EXPRESSION IN ESCHERICHIA COLI OF
REMARK 1 TITL 2 THE GENE ENCODING COMPONENT S OF THE COENZYME B12-DEPENDENT
REMARK 1 TITL 3 GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM
REMARK 1 REF FEMS MICROBIOL.LETT. V. 118 15 1994
REMARK 1 REFN ISSN 0378-1097
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1B1A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 299
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 10MM K2HPO4/KH2PO4
REMARK 210 PRESSURE : ATMOSPHERIC ATM
REMARK 210 SAMPLE CONTENTS : 10% H2O/90% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 15N HSQC; 2D X-FILT NOESY; 2D
REMARK 210 NOESY; 2D TOCSY; 3D 15N NOESY-
REMARK 210 HSQC; 3D 15N TOCSY-HSQC; 3D HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, ANSIG, FELIX, X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 15
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: MEAN STRUCTURE
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 HH TYR A 117 HZ1 LYS A 132 1.49
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 LYS A 3 -169.75 -76.14
REMARK 500 VAL A 10 -106.06 64.09
REMARK 500 HIS A 16 -50.74 -134.25
REMARK 500 ALA A 17 41.37 -141.56
REMARK 500 VAL A 18 -51.74 -135.87
REMARK 500 ILE A 22 -41.58 -140.68
REMARK 500 LEU A 23 70.86 -108.67
REMARK 500 HIS A 25 -43.98 -145.88
REMARK 500 PHE A 27 -52.83 133.68
REMARK 500 THR A 28 -12.67 -155.62
REMARK 500 VAL A 39 164.42 -46.57
REMARK 500 THR A 53 56.08 -90.51
REMARK 500 LEU A 63 56.30 -108.82
REMARK 500 TYR A 64 95.57 66.32
REMARK 500 GLN A 66 172.73 92.31
REMARK 500 ILE A 69 -152.65 75.87
REMARK 500 CYS A 71 -67.67 -91.11
REMARK 500 GLU A 84 -98.98 -63.45
REMARK 500 ASN A 93 -179.88 67.97
REMARK 500 ILE A 94 -96.82 -134.61
REMARK 500 VAL A 96 -124.26 -93.34
REMARK 500 GLN A 99 27.98 -152.61
REMARK 500 HIS A 100 52.28 -160.09
REMARK 500 TRP A 101 -54.03 -172.95
REMARK 500 PRO A 102 105.60 -43.92
REMARK 500 TYR A 113 -25.45 -158.90
REMARK 500 ASP A 114 89.94 -53.20
REMARK 500 PRO A 119 113.66 -39.14
REMARK 500 PRO A 122 168.47 -49.71
REMARK 500 VAL A 125 -123.81 -42.62
REMARK 500 ILE A 127 -64.59 -90.21
REMARK 500 ILE A 136 50.64 -145.98
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1B1A A 1 137 UNP P80078 MAMA_CLOCO 1 137
SEQRES 1 A 137 MET GLU LYS LYS THR ILE VAL LEU GLY VAL ILE GLY SER
SEQRES 2 A 137 ASP CYS HIS ALA VAL GLY ASN LYS ILE LEU ASP HIS ALA
SEQRES 3 A 137 PHE THR ASN ALA GLY PHE ASN VAL VAL ASN ILE GLY VAL
SEQRES 4 A 137 LEU SER PRO GLN GLU VAL PHE ILE LYS ALA ALA ILE GLU
SEQRES 5 A 137 THR LYS ALA ASP ALA ILE LEU LEU SER SER LEU TYR GLY
SEQRES 6 A 137 GLN GLY GLU ILE ASP CYS LYS GLY LEU ARG GLN LYS CYS
SEQRES 7 A 137 ASP GLU ALA GLY LEU GLU GLY ILE LEU LEU TYR VAL GLY
SEQRES 8 A 137 GLY ASN ILE VAL VAL GLY LYS GLN HIS TRP PRO ASP VAL
SEQRES 9 A 137 GLU LYS ARG PHE LYS ASP MET GLY TYR ASP ARG VAL TYR
SEQRES 10 A 137 ALA PRO GLY THR PRO PRO GLU VAL GLY ILE ALA ASP LEU
SEQRES 11 A 137 LYS LYS ASP LEU ASN ILE GLU
HELIX 1 2 GLN A 43 GLU A 52 1 10
HELIX 2 3 ASP A 70 ALA A 81 1 12
HELIX 3 4 ASP A 103 MET A 111 1 9
HELIX 4 5 VAL A 125 ILE A 136 1 12
SHEET 1 S1 5 ASN A 33 ASN A 36 0
SHEET 2 S1 5 LYS A 4 LEU A 8 1
SHEET 3 S1 5 ASP A 56 LEU A 59 1
SHEET 4 S1 5 LEU A 87 GLY A 91 1
SHEET 5 S1 5 ARG A 115 ALA A 118 1
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