Header list of 1a6x.pdb file
Complete list - b 16 2 Bytes
HEADER CARRIER PROTEIN 04-MAR-98 1A6X
TITLE STRUCTURE OF THE APO-BIOTIN CARBOXYL CARRIER PROTEIN (APO-BCCP87) OF
TITLE 2 ESCHERICHIA COLI ACETYL-COA CARBOXYLASE, NMR, 49 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APO-BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA
COMPND 3 CARBOXYLASE;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: CARBOXYL-TERMINAL FRAGMENT, RESIDUES 70 - 156;
COMPND 6 SYNONYM: APO-BCCP87;
COMPND 7 EC: 6.4.1.2;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI BL21(DE3);
SOURCE 3 ORGANISM_TAXID: 469008;
SOURCE 4 STRAIN: BL21 (DE3);
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTM53
KEYWDS ACETYL-COA CARBOXYLASE, BIOTIN CARBOXYL CARRIER PROTEIN, BACKBONE
KEYWDS 2 DYNAMICS, CARRIER PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 49
AUTHOR X.YAO,D.WEI,C.SODEN JUNIOR,M.F.SUMMERS,D.BECKETT
REVDAT 4 16-FEB-22 1A6X 1 REMARK
REVDAT 3 24-FEB-09 1A6X 1 VERSN
REVDAT 2 01-APR-03 1A6X 1 JRNL
REVDAT 1 14-OCT-98 1A6X 0
JRNL AUTH X.YAO,D.WEI,C.SODEN JR.,M.F.SUMMERS,D.BECKETT
JRNL TITL STRUCTURE OF THE CARBOXY-TERMINAL FRAGMENT OF THE APO-BIOTIN
JRNL TITL 2 CARBOXYL CARRIER SUBUNIT OF ESCHERICHIA COLI ACETYL-COA
JRNL TITL 3 CARBOXYLASE.
JRNL REF BIOCHEMISTRY V. 36 15089 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9398236
JRNL DOI 10.1021/BI971485F
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1A6X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170468.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; COSY; HSQC; NOESY
REMARK 210 -HSQC; TOCSY-HSQC AND T1; T2;
REMARK 210 NOE MEASUREMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : GE OMEGA PSG
REMARK 210 SPECTROMETER MANUFACTURER : GE
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 49
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 49
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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: 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 PHE A 91 H GLY A 143 1.53
REMARK 500 O THR A 134 H GLU A 156 1.56
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 ALA A 74 -62.06 71.46
REMARK 500 1 ALA A 76 -62.02 74.52
REMARK 500 1 GLU A 77 134.02 62.75
REMARK 500 1 ILE A 78 -48.03 -136.30
REMARK 500 1 SER A 79 116.87 62.76
REMARK 500 1 SER A 85 106.13 -39.98
REMARK 500 1 VAL A 111 108.59 -40.18
REMARK 500 1 CYS A 116 -172.70 175.91
REMARK 500 1 LYS A 131 103.43 177.75
REMARK 500 1 SER A 132 143.19 -39.13
REMARK 500 1 VAL A 135 160.57 -41.13
REMARK 500 1 LYS A 136 -49.10 -141.90
REMARK 500 1 ALA A 137 138.81 173.37
REMARK 500 1 ASP A 149 15.95 58.17
REMARK 500 1 LEU A 152 -77.49 -112.83
REMARK 500 2 GLU A 71 152.35 64.69
REMARK 500 2 ALA A 75 -61.12 -92.88
REMARK 500 2 ILE A 78 -70.27 -108.13
REMARK 500 2 SER A 79 42.95 179.88
REMARK 500 2 SER A 85 103.53 -44.52
REMARK 500 2 ASP A 98 52.91 -100.82
REMARK 500 2 VAL A 111 109.44 -40.30
REMARK 500 2 CYS A 116 -172.12 178.39
REMARK 500 2 LYS A 131 111.73 178.19
REMARK 500 2 SER A 132 160.73 -40.60
REMARK 500 2 VAL A 135 177.94 50.84
REMARK 500 2 LYS A 136 -47.66 -166.28
REMARK 500 2 ALA A 137 133.11 170.07
REMARK 500 2 LEU A 152 -77.48 -120.35
REMARK 500 3 ALA A 74 63.43 -157.47
REMARK 500 3 ALA A 76 170.25 63.26
REMARK 500 3 GLU A 77 90.88 -178.08
REMARK 500 3 ILE A 78 -66.88 69.07
REMARK 500 3 SER A 79 22.70 49.97
REMARK 500 3 SER A 85 103.75 -45.43
REMARK 500 3 VAL A 111 109.07 -40.34
REMARK 500 3 THR A 114 174.52 -49.43
REMARK 500 3 LEU A 115 -46.31 -137.75
REMARK 500 3 CYS A 116 -165.86 -178.47
REMARK 500 3 LYS A 131 96.08 175.57
REMARK 500 3 ALA A 137 133.21 168.56
REMARK 500 3 SER A 142 92.40 -64.05
REMARK 500 3 ASP A 149 -3.50 83.55
REMARK 500 3 LEU A 152 -80.98 -122.00
REMARK 500 4 ALA A 72 -54.47 168.01
REMARK 500 4 ALA A 74 91.21 45.13
REMARK 500 4 ALA A 75 -61.09 -124.24
REMARK 500 4 ALA A 76 106.82 -40.96
REMARK 500 4 GLU A 77 100.01 -178.25
REMARK 500 4 SER A 79 -82.44 72.35
REMARK 500
REMARK 500 THIS ENTRY HAS 807 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1A6X A 70 156 UNP P0ABD8 BCCP_ECOLI 70 156
SEQRES 1 A 87 MET GLU ALA PRO ALA ALA ALA GLU ILE SER GLY HIS ILE
SEQRES 2 A 87 VAL ARG SER PRO MET VAL GLY THR PHE TYR ARG THR PRO
SEQRES 3 A 87 SER PRO ASP ALA LYS ALA PHE ILE GLU VAL GLY GLN LYS
SEQRES 4 A 87 VAL ASN VAL GLY ASP THR LEU CYS ILE VAL GLU ALA MET
SEQRES 5 A 87 LYS MET MET ASN GLN ILE GLU ALA ASP LYS SER GLY THR
SEQRES 6 A 87 VAL LYS ALA ILE LEU VAL GLU SER GLY GLN PRO VAL GLU
SEQRES 7 A 87 PHE ASP GLU PRO LEU VAL VAL ILE GLU
SHEET 1 A 3 THR A 90 TYR A 92 0
SHEET 2 A 3 THR A 114 ALA A 120 -1 N GLU A 119 O THR A 90
SHEET 3 A 3 MET A 123 GLU A 128 -1 N ILE A 127 O LEU A 115
SHEET 1 B 2 VAL A 135 ILE A 138 0
SHEET 2 B 2 VAL A 153 ILE A 155 -1 N VAL A 154 O LYS A 136
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