Header list of 1boe.pdb file
Complete list - b 16 2 Bytes
HEADER HORMONE/GROWTH FACTOR 30-JUL-98 1BOE
TITLE STRUCTURE OF THE IGF BINDING DOMAIN OF THE INSULIN-LIKE GROWTH FACTOR-
TITLE 2 BINDING PROTEIN-5 (IGFBP-5): IMPLICATIONS FOR IGF AND IGF-I RECEPTOR
TITLE 3 INTERACTIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN-5
COMPND 3 (IGFBP-5));
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: BINDING DOMAIN;
COMPND 6 SYNONYM: MINI-IGFBP-5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS MINI-IGFBP-5, IGFBP-5, IGF, INSULIN-LIKE GROWTH FACTOR BINDING
KEYWDS 2 PROTEIN, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.KALUS,M.ZWECKSTETTER,C.RENNER,Y.SANCHEZ,J.GEORGESCU,M.GROL,
AUTHOR 2 D.DEMUTH,C.SCHUMACHERDONY,K.LANG,T.H.HOLAK
REVDAT 5 16-FEB-22 1BOE 1 REMARK
REVDAT 4 24-FEB-09 1BOE 1 VERSN
REVDAT 3 01-APR-03 1BOE 1 JRNL
REVDAT 2 22-DEC-99 1BOE 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 16-DEC-98 1BOE 0
JRNL AUTH W.KALUS,M.ZWECKSTETTER,C.RENNER,Y.SANCHEZ,J.GEORGESCU,
JRNL AUTH 2 M.GROL,D.DEMUTH,R.SCHUMACHER,C.DONY,K.LANG,T.A.HOLAK
JRNL TITL STRUCTURE OF THE IGF-BINDING DOMAIN OF THE INSULIN-LIKE
JRNL TITL 2 GROWTH FACTOR-BINDING PROTEIN-5 (IGFBP-5): IMPLICATIONS FOR
JRNL TITL 3 IGF AND IGF-I RECEPTOR INTERACTIONS.
JRNL REF EMBO J. V. 17 6558 1998
JRNL REFN ISSN 0261-4189
JRNL PMID 9822601
JRNL DOI 10.1093/EMBOJ/17.22.6558
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: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1BOE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008124.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR
REMARK 210 METHOD USED : SIMUALTED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 TYR A 59
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 H VAL A 22 O LEU A 46 1.54
REMARK 500 O GLY A 21 H THR A 24 1.58
REMARK 500 SG CYS A 27 SG CYS A 53 2.01
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 LEU A 14 172.62 -54.13
REMARK 500 1 ALA A 15 -154.63 -100.19
REMARK 500 1 CYS A 20 -152.46 -140.85
REMARK 500 1 THR A 24 -138.82 -98.52
REMARK 500 1 CYS A 27 163.57 -42.28
REMARK 500 1 ALA A 28 134.14 -29.17
REMARK 500 1 GLN A 29 -74.09 -34.33
REMARK 500 1 GLU A 39 -72.65 -87.20
REMARK 500 1 GLU A 40 -95.41 -166.87
REMARK 500 1 LYS A 41 59.26 -146.82
REMARK 500 1 LEU A 46 33.39 -86.34
REMARK 500 1 ASN A 55 152.96 -43.48
REMARK 500 1 GLU A 56 40.26 -86.87
REMARK 500 1 LYS A 57 -71.57 -91.43
REMARK 500 2 LEU A 14 170.98 -54.93
REMARK 500 2 ALA A 15 -166.97 -105.67
REMARK 500 2 CYS A 20 -151.43 -140.24
REMARK 500 2 THR A 24 -135.58 -98.61
REMARK 500 2 CYS A 27 163.85 -42.33
REMARK 500 2 ALA A 28 136.52 -29.27
REMARK 500 2 GLN A 29 -76.86 -33.79
REMARK 500 2 ARG A 36 176.62 -53.79
REMARK 500 2 GLN A 37 62.26 -156.77
REMARK 500 2 ASP A 38 -110.13 -133.08
REMARK 500 2 GLU A 40 -146.42 -107.18
REMARK 500 2 LYS A 41 77.94 -118.69
REMARK 500 2 HIS A 44 38.58 -170.49
REMARK 500 2 ALA A 45 -56.55 -140.93
REMARK 500 2 ARG A 50 17.32 -152.76
REMARK 500 2 GLU A 56 40.04 -86.73
REMARK 500 2 LYS A 57 -73.20 -101.47
REMARK 500 3 LEU A 14 179.06 -55.39
REMARK 500 3 ALA A 15 -148.03 -105.54
REMARK 500 3 CYS A 20 -149.66 -140.27
REMARK 500 3 THR A 24 -130.98 -98.43
REMARK 500 3 CYS A 27 163.28 -41.53
REMARK 500 3 ALA A 28 135.64 -28.78
REMARK 500 3 GLN A 29 -75.37 -33.90
REMARK 500 3 GLU A 40 40.09 -83.77
REMARK 500 3 LYS A 41 65.16 166.96
REMARK 500 3 HIS A 44 40.82 -172.82
REMARK 500 3 ALA A 45 -51.16 -141.22
REMARK 500 3 GLU A 56 40.46 -88.87
REMARK 500 3 LYS A 57 -67.31 -100.65
REMARK 500 4 LEU A 14 170.86 -54.93
REMARK 500 4 ALA A 15 -155.12 -104.95
REMARK 500 4 CYS A 20 -146.43 -141.52
REMARK 500 4 THR A 24 -130.35 -98.19
REMARK 500 4 CYS A 27 163.03 -41.22
REMARK 500 4 ALA A 28 135.44 -28.61
REMARK 500
REMARK 500 THIS ENTRY HAS 296 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 32 0.32 SIDE CHAIN
REMARK 500 1 ARG A 36 0.26 SIDE CHAIN
REMARK 500 1 ARG A 50 0.27 SIDE CHAIN
REMARK 500 2 ARG A 26 0.24 SIDE CHAIN
REMARK 500 2 ARG A 32 0.32 SIDE CHAIN
REMARK 500 2 ARG A 36 0.32 SIDE CHAIN
REMARK 500 2 ARG A 50 0.27 SIDE CHAIN
REMARK 500 3 ARG A 26 0.31 SIDE CHAIN
REMARK 500 3 ARG A 32 0.31 SIDE CHAIN
REMARK 500 3 ARG A 36 0.28 SIDE CHAIN
REMARK 500 3 ARG A 50 0.23 SIDE CHAIN
REMARK 500 4 ARG A 26 0.31 SIDE CHAIN
REMARK 500 4 ARG A 32 0.26 SIDE CHAIN
REMARK 500 4 ARG A 36 0.29 SIDE CHAIN
REMARK 500 4 ARG A 50 0.29 SIDE CHAIN
REMARK 500 5 ARG A 26 0.24 SIDE CHAIN
REMARK 500 5 ARG A 32 0.21 SIDE CHAIN
REMARK 500 5 ARG A 36 0.19 SIDE CHAIN
REMARK 500 5 ARG A 50 0.29 SIDE CHAIN
REMARK 500 6 ARG A 26 0.31 SIDE CHAIN
REMARK 500 6 ARG A 32 0.32 SIDE CHAIN
REMARK 500 6 ARG A 36 0.30 SIDE CHAIN
REMARK 500 6 ARG A 50 0.31 SIDE CHAIN
REMARK 500 7 ARG A 26 0.12 SIDE CHAIN
REMARK 500 7 ARG A 32 0.15 SIDE CHAIN
REMARK 500 7 ARG A 36 0.31 SIDE CHAIN
REMARK 500 7 ARG A 50 0.26 SIDE CHAIN
REMARK 500 8 ARG A 26 0.30 SIDE CHAIN
REMARK 500 8 ARG A 32 0.26 SIDE CHAIN
REMARK 500 8 ARG A 36 0.29 SIDE CHAIN
REMARK 500 8 ARG A 50 0.16 SIDE CHAIN
REMARK 500 9 ARG A 26 0.22 SIDE CHAIN
REMARK 500 9 ARG A 32 0.27 SIDE CHAIN
REMARK 500 9 ARG A 36 0.25 SIDE CHAIN
REMARK 500 9 ARG A 50 0.24 SIDE CHAIN
REMARK 500 10 ARG A 26 0.21 SIDE CHAIN
REMARK 500 10 ARG A 32 0.29 SIDE CHAIN
REMARK 500 10 ARG A 36 0.26 SIDE CHAIN
REMARK 500 10 ARG A 50 0.31 SIDE CHAIN
REMARK 500 11 ARG A 26 0.27 SIDE CHAIN
REMARK 500 11 ARG A 32 0.29 SIDE CHAIN
REMARK 500 11 ARG A 36 0.17 SIDE CHAIN
REMARK 500 11 ARG A 50 0.23 SIDE CHAIN
REMARK 500 12 ARG A 26 0.29 SIDE CHAIN
REMARK 500 12 ARG A 32 0.24 SIDE CHAIN
REMARK 500 12 ARG A 36 0.25 SIDE CHAIN
REMARK 500 12 ARG A 50 0.14 SIDE CHAIN
REMARK 500 13 ARG A 26 0.31 SIDE CHAIN
REMARK 500 13 ARG A 32 0.11 SIDE CHAIN
REMARK 500 13 ARG A 50 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 77 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: IBS
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: HYDROPHOBIC BINDING SITE TO IGF
DBREF 1BOE A 13 59 UNP P24593 IBP5_HUMAN 60 106
SEQRES 1 A 47 ALA LEU ALA GLU GLY GLN SER CYS GLY VAL TYR THR GLU
SEQRES 2 A 47 ARG CYS ALA GLN GLY LEU ARG CYS LEU PRO ARG GLN ASP
SEQRES 3 A 47 GLU GLU LYS PRO LEU HIS ALA LEU LEU HIS GLY ARG GLY
SEQRES 4 A 47 VAL CYS LEU ASN GLU LYS SER TYR
SHEET 1 A 2 LEU A 31 LEU A 34 0
SHEET 2 A 2 VAL A 52 ASN A 55 -1 N LEU A 54 O ARG A 32
SSBOND 1 CYS A 20 CYS A 33 1555 1555 2.02
SITE 1 IBS 3 VAL A 22 LEU A 46 LEU A 47
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