Header list of 2fmc.pdb file
Complete list - r 9 2 Bytes
HEADER SURFACE ACTIVE PROTEIN 09-JAN-06 2FMC
TITLE SOLUTION STRUCTURE OF THE CLASS I HYDROPHOBIN EAS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROPHOBIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RODLET PROTEIN, CLOCK-CONTROLLED GENE PROTEIN 2, BLUE LIGHT-
COMPND 5 INDUCED PROTEIN 7, EAS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEUROSPORA CRASSA;
SOURCE 3 ORGANISM_TAXID: 5141;
SOURCE 4 TISSUE: SPORES
KEYWDS BETA BARREL, FLEXIBLE LOOP, DISULPHIDE BONDS, SURFACE ACTIVE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.H.KWAN
REVDAT 3 09-MAR-22 2FMC 1 REMARK
REVDAT 2 24-FEB-09 2FMC 1 VERSN
REVDAT 1 28-MAR-06 2FMC 0
JRNL AUTH A.H.KWAN,R.D.WINEFIELD,M.SUNDE,J.M.MATTHEWS,R.G.HAVERKAMP,
JRNL AUTH 2 M.D.TEMPLETON,J.P.MACKAY
JRNL TITL STRUCTURAL BASIS FOR RODLET ASSEMBLY IN FUNGAL HYDROPHOBINS
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 3621 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16537446
JRNL DOI 10.1073/PNAS.0505704103
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, ARIA 1.2
REMARK 3 AUTHORS : BRUKER (XWINNMR), LINGE ET AL (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON: 1623 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 90 DIHEDRAL ANGLE RESTRAINTS,10
REMARK 3 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 2FMC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000036048.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 280
REMARK 210 PH : 4.5; 4.5
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM EAS; U-15N 0.2MM EAS; 20MM
REMARK 210 SODIUM ACETATE; U-15N,13C 0.5MM
REMARK 210 EAS; 20MM SODIUM ACETATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 15N-HSQC; 3D_15N-SEPARATED_NOESY;
REMARK 210 HNHA; 3D_13C-SEPARATED_NOESY;
REMARK 210 13C-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, ARIA 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
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: OTHER STANDARD TRIPLE RESONANCE NMR EXPTS WERE ALSO
REMARK 210 COLLECTED, INCLUDING: HNCO, HNCA, HNCACB, CBCA(CO)NH, HCCH-TOCSY
REMARK 210 ETC
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 HZ2 LYS A 15 OD1 ASP A 63 1.57
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 ILE A 11 -87.25 -87.83
REMARK 500 1 SER A 23 -78.91 -160.46
REMARK 500 1 SER A 40 -80.28 -123.75
REMARK 500 2 ILE A 11 -109.99 -84.03
REMARK 500 2 MET A 22 -89.31 -88.65
REMARK 500 2 LEU A 32 -35.15 -147.68
REMARK 500 2 LEU A 39 -1.71 -142.75
REMARK 500 2 SER A 40 -34.92 -140.35
REMARK 500 2 VAL A 49 95.37 -63.67
REMARK 500 3 THR A 8 -100.89 -125.14
REMARK 500 3 ILE A 11 -135.84 -119.20
REMARK 500 3 ASP A 12 -165.32 -79.79
REMARK 500 3 SER A 23 30.19 -80.21
REMARK 500 3 ALA A 56 -168.78 -124.45
REMARK 500 3 ASP A 63 169.08 175.39
REMARK 500 4 CYS A 9 27.42 -155.82
REMARK 500 4 ASP A 12 -149.94 -90.88
REMARK 500 4 LEU A 31 -137.65 -106.30
REMARK 500 4 CYS A 45 -176.80 65.38
REMARK 500 4 THR A 66 -120.70 -101.00
REMARK 500 4 ASN A 79 50.91 -95.35
REMARK 500 5 THR A 8 -70.66 -157.54
REMARK 500 5 CYS A 9 42.68 -159.69
REMARK 500 5 ILE A 11 -92.73 -80.47
REMARK 500 5 LEU A 34 66.52 63.57
REMARK 500 5 SER A 40 -68.65 -145.53
REMARK 500 5 ALA A 41 108.10 -163.70
REMARK 500 5 ALA A 56 -113.24 -149.17
REMARK 500 5 ASN A 67 55.62 -92.86
REMARK 500 6 ASN A 7 54.72 -108.72
REMARK 500 6 THR A 8 -74.32 -72.91
REMARK 500 6 ASP A 13 99.24 -63.91
REMARK 500 6 SER A 23 49.38 -86.23
REMARK 500 6 ALA A 26 85.95 -68.85
REMARK 500 6 LEU A 31 -121.46 -138.64
REMARK 500 6 LEU A 39 -4.25 -144.28
REMARK 500 6 ALA A 56 -152.26 -158.32
REMARK 500 6 ASN A 70 -161.03 -124.57
REMARK 500 6 PHE A 72 -158.88 -157.28
REMARK 500 6 ALA A 78 -102.28 21.25
REMARK 500 7 ASN A 7 41.59 -101.31
REMARK 500 7 ILE A 11 -133.07 -113.43
REMARK 500 7 ASP A 13 80.24 46.79
REMARK 500 7 ALA A 26 -65.13 -149.54
REMARK 500 7 ALA A 56 -123.80 -125.39
REMARK 500 8 ASP A 12 -85.00 -18.68
REMARK 500 8 ALA A 26 50.21 -108.15
REMARK 500 8 ASP A 64 -72.66 -79.33
REMARK 500 8 VAL A 65 94.19 47.79
REMARK 500 8 ASN A 67 59.84 -119.86
REMARK 500
REMARK 500 THIS ENTRY HAS 125 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R2M RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION STRUCTURE OF THE CLASS II HYDROPHOBIN HFBII
DBREF 2FMC A 1 82 UNP Q04571 RODL_NEUCR 27 108
SEQRES 1 A 82 ALA THR THR ILE GLY PRO ASN THR CYS SER ILE ASP ASP
SEQRES 2 A 82 TYR LYS PRO TYR CYS CYS GLN SER MET SER GLY PRO ALA
SEQRES 3 A 82 GLY SER PRO GLY LEU LEU ASN LEU ILE PRO VAL ASP LEU
SEQRES 4 A 82 SER ALA SER LEU GLY CYS VAL VAL GLY VAL ILE GLY SER
SEQRES 5 A 82 GLN CYS GLY ALA SER VAL LYS CYS CYS LYS ASP ASP VAL
SEQRES 6 A 82 THR ASN THR GLY ASN SER PHE LEU ILE ILE ASN ALA ALA
SEQRES 7 A 82 ASN CYS VAL ALA
SHEET 1 A 2 THR A 2 THR A 3 0
SHEET 2 A 2 GLN A 53 CYS A 54 -1 O CYS A 54 N THR A 2
SHEET 1 B 4 VAL A 46 VAL A 47 0
SHEET 2 B 4 LYS A 15 CYS A 19 -1 N CYS A 18 O VAL A 46
SHEET 3 B 4 SER A 57 LYS A 62 -1 O LYS A 59 N TYR A 17
SHEET 4 B 4 ASN A 79 VAL A 81 -1 O ASN A 79 N LYS A 62
SHEET 1 C 2 LEU A 43 GLY A 44 0
SHEET 2 C 2 ILE A 74 ILE A 75 -1 O ILE A 75 N LEU A 43
SSBOND 1 CYS A 9 CYS A 60 1555 1555 2.03
SSBOND 2 CYS A 18 CYS A 54 1555 1555 2.04
SSBOND 3 CYS A 19 CYS A 45 1555 1555 2.03
SSBOND 4 CYS A 61 CYS A 80 1555 1555 2.03
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 9 2 Bytes