Header list of 1bla.pdb file
Complete list - 3 20 Bytes
HEADER GROWTH FACTOR 20-MAY-96 1BLA
TITLE BASIC FIBROBLAST GROWTH FACTOR (FGF-2) MUTANT WITH CYS 78 REPLACED BY
TITLE 2 SER AND CYS 96 REPLACED BY SER, NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BASIC FIBROBLAST GROWTH FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FGF-2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CDNA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GROWTH FACTOR
EXPDTA SOLUTION NMR
AUTHOR R.POWERS,A.P.SEDDON,P.BOHLEN,F.J.MOY
REVDAT 3 03-NOV-21 1BLA 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1BLA 1 VERSN
REVDAT 1 08-NOV-96 1BLA 0
JRNL AUTH F.J.MOY,A.P.SEDDON,P.BOHLEN,R.POWERS
JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF BASIC FIBROBLAST
JRNL TITL 2 GROWTH FACTOR DETERMINED BY MULTIDIMENSIONAL HETERONUCLEAR
JRNL TITL 3 MAGNETIC RESONANCE SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 35 13552 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8885834
JRNL DOI 10.1021/BI961260P
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.J.MOY,A.P.SEDDON,E.B.CAMPBELL,P.BOHLEN,R.POWERS
REMARK 1 TITL 1H, 15N, 13C AND 13CO ASSIGNMENTS AND SECONDARY STRUCTURE
REMARK 1 TITL 2 DETERMINATION OF BASIC FIBROBLAST GROWTH FACTOR USING 3D
REMARK 1 TITL 3 HETERONUCLEAR NMR SPECTROSCOPY
REMARK 1 REF J.BIOMOL.NMR V. 6 245 1995
REMARK 1 REFN ISSN 0925-2738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BLA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171882.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
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: 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: 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 GLU A 5 -101.98 -84.90
REMARK 500 THR A 7 -175.10 49.19
REMARK 500 THR A 8 -79.01 -166.45
REMARK 500 LEU A 9 148.90 60.47
REMARK 500 LEU A 12 68.92 -162.45
REMARK 500 GLU A 14 86.63 55.15
REMARK 500 SER A 18 57.57 -91.73
REMARK 500 ALA A 20 -99.63 -152.86
REMARK 500 PHE A 21 70.54 -154.56
REMARK 500 PRO A 29 170.66 -56.97
REMARK 500 PRO A 58 2.44 -61.53
REMARK 500 GLU A 67 -86.51 -97.17
REMARK 500 SER A 109 49.47 -92.19
REMARK 500 ASN A 110 26.71 -151.42
REMARK 500 ASN A 111 -0.04 60.24
REMARK 500 ARG A 118 -76.28 -93.53
REMARK 500 THR A 121 0.84 -61.36
REMARK 500 LYS A 154 -81.14 -61.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BLD RELATED DB: PDB
REMARK 900 ENSEMBLE
DBREF 1BLA A 1 155 UNP P09038 FGF2_HUMAN 1 155
SEQADV 1BLA GLU A 3 UNP P09038 ALA 3 CONFLICT
SEQADV 1BLA GLU A 5 UNP P09038 SER 5 CONFLICT
SEQADV 1BLA SER A 78 UNP P09038 CYS 78 ENGINEERED MUTATION
SEQADV 1BLA SER A 96 UNP P09038 CYS 96 ENGINEERED MUTATION
SEQRES 1 A 155 MET ALA GLU GLY GLU ILE THR THR LEU PRO ALA LEU PRO
SEQRES 2 A 155 GLU ASP GLY GLY SER GLY ALA PHE PRO PRO GLY HIS PHE
SEQRES 3 A 155 LYS ASP PRO LYS ARG LEU TYR CYS LYS ASN GLY GLY PHE
SEQRES 4 A 155 PHE LEU ARG ILE HIS PRO ASP GLY ARG VAL ASP GLY VAL
SEQRES 5 A 155 ARG GLU LYS SER ASP PRO HIS ILE LYS LEU GLN LEU GLN
SEQRES 6 A 155 ALA GLU GLU ARG GLY VAL VAL SER ILE LYS GLY VAL SER
SEQRES 7 A 155 ALA ASN ARG TYR LEU ALA MET LYS GLU ASP GLY ARG LEU
SEQRES 8 A 155 LEU ALA SER LYS SER VAL THR ASP GLU CYS PHE PHE PHE
SEQRES 9 A 155 GLU ARG LEU GLU SER ASN ASN TYR ASN THR TYR ARG SER
SEQRES 10 A 155 ARG LYS TYR THR SER TRP TYR VAL ALA LEU LYS ARG THR
SEQRES 11 A 155 GLY GLN TYR LYS LEU GLY SER LYS THR GLY PRO GLY GLN
SEQRES 12 A 155 LYS ALA ILE LEU PHE LEU PRO MET SER ALA LYS SER
HELIX 1 1 PRO A 58 ILE A 60 5 3
HELIX 2 2 ASP A 99 CYS A 101 5 3
HELIX 3 3 LYS A 144 ILE A 146 5 3
SHEET 1 A 2 PHE A 40 ILE A 43 0
SHEET 2 A 2 VAL A 49 VAL A 52 -1 N VAL A 52 O PHE A 40
SHEET 1 B 2 LEU A 62 ALA A 66 0
SHEET 2 B 2 VAL A 72 GLY A 76 -1 N LYS A 75 O GLN A 63
SHEET 1 C 2 TYR A 82 MET A 85 0
SHEET 2 C 2 LEU A 91 SER A 94 -1 N SER A 94 O TYR A 82
SHEET 1 D 2 PHE A 103 LEU A 107 0
SHEET 2 D 2 ASN A 113 SER A 117 -1 N ARG A 116 O PHE A 104
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 - 3 20 Bytes