Header list of 1fge.pdb file
Complete list - 23 20 Bytes
HEADER BLOOD COAGULATION INHIBITOR 28-NOV-95 1FGE
TITLE EPIDERMAL GROWTH FACTOR (EGF) SUBDOMAIN OF HUMAN THROMBOMODULIN (NMR,
TITLE 2 14 STRUCTURES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBOMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL SUBDOMAIN, RESIDUES 407 - 426, OF 5TH EPIDERMAL
COMPND 5 GROWTH FACTOR (EGF);
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: NON-NATIVE DISULFIDE BOND BETWEEN THE FOURTH CYSTEINE
COMPND 9 (CYS 407) AND THE SIXTH CYSTEINE (CYS 421)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS BLOOD COAGULATION INHIBITOR, THROMBOMODULIN, EGF
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR R.HRABAL,E.A.KOMIVES,F.NI
REVDAT 3 23-FEB-22 1FGE 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1FGE 1 VERSN
REVDAT 1 20-JUN-96 1FGE 0
JRNL AUTH R.HRABAL,E.A.KOMIVES,F.NI
JRNL TITL STRUCTURAL RESILIENCY OF AN EGF-LIKE SUBDOMAIN BOUND TO ITS
JRNL TITL 2 TARGET PROTEIN, THROMBIN.
JRNL REF PROTEIN SCI. V. 5 195 1996
JRNL REFN ISSN 0961-8368
JRNL PMID 8745396
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 1FGE 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_1000173275.
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 : 14
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 1 ILE A 414 112.07 -170.10
REMARK 500 1 PHE A 419 147.15 77.11
REMARK 500 1 ILE A 420 -63.40 -138.85
REMARK 500 1 CYS A 421 98.90 177.68
REMARK 500 1 THR A 422 122.76 69.84
REMARK 500 1 ASP A 423 -53.48 -148.12
REMARK 500 1 ASP A 425 72.69 -112.30
REMARK 500 2 ILE A 414 105.15 -169.71
REMARK 500 2 PHE A 419 148.83 75.14
REMARK 500 2 ILE A 420 -59.89 -143.86
REMARK 500 2 CYS A 421 96.12 178.13
REMARK 500 2 THR A 422 122.66 70.21
REMARK 500 2 ASP A 423 -60.68 -145.75
REMARK 500 2 ASP A 425 62.12 -104.64
REMARK 500 3 GLU A 408 148.27 66.60
REMARK 500 3 ILE A 414 104.83 -171.10
REMARK 500 3 PHE A 419 147.25 75.03
REMARK 500 3 ILE A 420 -63.82 -142.18
REMARK 500 3 CYS A 421 105.94 -179.49
REMARK 500 3 THR A 422 116.53 67.16
REMARK 500 3 ASP A 423 -60.91 -149.76
REMARK 500 3 ASP A 425 65.63 -104.65
REMARK 500 4 GLU A 408 150.58 66.41
REMARK 500 4 ILE A 414 105.23 -171.68
REMARK 500 4 PHE A 419 147.64 73.05
REMARK 500 4 ILE A 420 -63.51 -143.10
REMARK 500 4 CYS A 421 101.19 -178.42
REMARK 500 4 THR A 422 118.61 70.02
REMARK 500 4 ASP A 423 -54.79 -148.28
REMARK 500 4 ASP A 425 71.28 -106.70
REMARK 500 5 ILE A 414 102.59 -172.38
REMARK 500 5 PHE A 419 147.62 73.72
REMARK 500 5 ILE A 420 -61.86 -143.77
REMARK 500 5 CYS A 421 110.88 179.50
REMARK 500 5 THR A 422 103.62 64.49
REMARK 500 5 ASP A 423 -37.13 -142.25
REMARK 500 6 GLU A 408 150.65 66.27
REMARK 500 6 ILE A 414 103.26 -170.60
REMARK 500 6 PHE A 419 147.92 71.82
REMARK 500 6 ILE A 420 -62.59 -143.13
REMARK 500 6 CYS A 421 112.68 178.48
REMARK 500 6 THR A 422 103.93 66.24
REMARK 500 6 ASP A 423 -39.20 -143.05
REMARK 500 7 GLU A 408 154.96 65.32
REMARK 500 7 ILE A 414 105.78 -172.35
REMARK 500 7 PHE A 419 148.11 70.88
REMARK 500 7 ILE A 420 -63.47 -143.78
REMARK 500 7 CYS A 421 101.27 -177.84
REMARK 500 7 THR A 422 118.48 70.85
REMARK 500 7 ASP A 423 -54.12 -147.84
REMARK 500
REMARK 500 THIS ENTRY HAS 99 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FGE A 407 426 UNP P07204 TRBM_HUMAN 425 444
SEQADV 1FGE ALA A 409 UNP P07204 CYS 427 CONFLICT
SEQRES 1 A 20 CYS GLU ALA PRO GLU GLY TYR ILE LEU ASP ASP GLY PHE
SEQRES 2 A 20 ILE CYS THR ASP ILE ASP GLU
SSBOND 1 CYS A 407 CYS A 421 1555 1555 2.02
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 - 23 20 Bytes