Header list of 1goe.pdb file
Complete list - t 21 2 Bytes
HEADER HORMONE 20-OCT-01 1GOE
TITLE MONITORING THE STRUCTURAL CONSEQUENCES OF PHE12-->D-PHE12
TITLE 2 AND LEU15-->AIB15 SUBSTITUTION IN H/R CORTICOTROPIN
TITLE 3 RELEASING HORMONE: IMPLICATIONS FOR DESIGN OF CRH
TITLE 4 ANTAGONISTS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CORTICOTROPIN RELEASING HORMONE;
COMPND 3 CHAIN: A;
COMPND 4 MUTATION: YES;
COMPND 5 OTHER_DETAILS: SYNTHETIC ANALOGUE WITH ISOLEUCINE-AMIDE
COMPND 6 C-TERMINUS
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 OTHER_DETAILS: SYNTHETIC ANALOGUE SYNTHESIZED THROUGH
SOURCE 7 SOLID PHASE SYNTHESIS USING FMOC/TBU SYNTHETIC PROTOCOLS.
SOURCE 8 NATIVE PHE12 AND LEU15 HAS BEEN SUBSTITUTED BY D-PHE AND
SOURCE 9 ALPHA-AMINOISOBUTYRIC ACID
KEYWDS HORMONE, CORTICOTROPIN RELEASING HORMONE, SYNTHETIC
KEYWDS 2 ANALOGUES, SOLID PHASE SYNTHESIS, NMR, SOLUTIONS STRUCTURE
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR G.A.SPYROULIAS,S.PAPAZACHARIAS,G.PAIRAS,P.CORDOPATIS
REVDAT 4 21-OCT-15 1GOE 1 SOURCE REMARK VERSN DBREF
REVDAT 4 2 SEQADV
REVDAT 3 24-FEB-09 1GOE 1 VERSN
REVDAT 2 12-DEC-02 1GOE 1 JRNL
REVDAT 1 31-OCT-01 1GOE 0
JRNL AUTH G.A.SPYROULIAS,S.PAPAZACHARIAS,G.PAIRAS,
JRNL AUTH 2 P.CORDOPATIS
JRNL TITL MONITORING THE STRUCTURAL CONSEQUENCES OF
JRNL TITL 2 PHE12-->D-PHE AND LEU15-->AIB SUBSTITUTION IN
JRNL TITL 3 HUMAN/RAT CORTICOTROPIN RELEASING HORMONE
JRNL REF EUR.J.BIOCHEM. V. 269 6009 2002
JRNL REFN ISSN 0014-2956
JRNL PMID 12473096
JRNL DOI 10.1046/J.1432-1033.2002.03278.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.ROMIER,J.M.BERNASSAU,C.CAMBILLAU,H.DARBON
REMARK 1 TITL SOLUTION STRUCTURE OF HUMAN CORTICOTROPIN
REMARK 1 TITL 2 RELEASING FACTOR BY 1H NMR AND DISTANCE GEOMETRY
REMARK 1 TITL 3 WITH RESTRAINED MOLECULAR DYNAMICS.
REMARK 1 REF PROTEIN ENG. V. 6 149 1993
REMARK 1 REFN ISSN 0269-2139
REMARK 1 PMID 8386360
REMARK 1 DOI 10.1093/PROTEIN/6.2.149
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 5.0
REMARK 3 AUTHORS : PETER KOLLMAN, DAVE CASE, KEN MERZ, THOMAS
REMARK 3 CHEATHAM, CARLOS SIMMERLING, TOM DARDEN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1GOE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-OCT-01.
REMARK 100 THE PDBE ID CODE IS EBI-8730.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 3.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 34% H2O / 66% TFE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA AND AMBER
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY
REMARK 210 SIMULATED ANNEALING IN TORSION
REMARK 210 ANGLE SPACE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 1H-1H
REMARK 210 DOUBLE-RESONANCE NMR SPECTROSCOPY. NMR-DERRIVED DISTANCE
REMARK 210 RESTRAINTS AND 3JHAHN COUPLING CONSTANTS AS WELL AS
REMARK 210 H-BOND CONSTRAINTS USED IN STRUCTURAL CALCULATION AND
REMARK 210 REFIMENT PROCEEDURE.
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 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 GLU A 2 -56.61 -153.03
REMARK 500 1 GLU A 17 -61.26 -121.41
REMARK 500 2 GLU A 2 -63.41 -143.62
REMARK 500 2 GLU A 17 -61.25 -122.80
REMARK 500 3 GLU A 2 -71.68 -155.01
REMARK 500 3 GLU A 17 -61.54 -122.37
REMARK 500 4 ARG A 16 4.76 -69.85
REMARK 500 5 GLU A 17 -63.95 -92.78
REMARK 500 6 GLU A 17 -63.71 -126.30
REMARK 500 7 GLU A 17 -65.75 -99.52
REMARK 500 10 GLU A 2 -50.67 -152.96
REMARK 500 13 GLU A 2 -85.65 -83.40
REMARK 500 13 GLU A 17 -61.78 -109.68
REMARK 500 16 GLU A 17 -62.54 -120.05
REMARK 500 17 GLU A 17 -60.22 -123.58
REMARK 500 18 GLU A 2 -53.60 -137.30
REMARK 500 20 GLU A 17 -62.47 -121.28
REMARK 500 21 GLU A 17 -64.06 -102.51
REMARK 500 22 GLU A 17 -64.47 -121.72
REMARK 500 28 LEU A 19 -46.27 -132.20
REMARK 500 31 GLU A 2 -59.98 -125.90
REMARK 500 32 GLU A 2 15.36 -141.41
REMARK 500 32 ARG A 16 1.68 -68.23
REMARK 500 34 GLU A 17 -65.30 -121.07
REMARK 500 36 GLU A 3 -61.16 -100.07
REMARK 500 38 GLU A 17 -62.22 -121.83
REMARK 500 39 ARG A 16 21.14 -77.78
REMARK 500 39 GLU A 17 -62.72 -124.64
REMARK 500 40 GLU A 17 -63.85 -125.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 NH2 A 42
DBREF 1GOE A 1 41 UNP P06850 CRF_HUMAN 154 194
SEQADV 1GOE DPN A 12 UNP P06850 PHE 165 ENGINEERED MUTATION
SEQADV 1GOE AIB A 15 UNP P06850 LEU 168 ENGINEERED MUTATION
SEQADV 1GOE NH2 A 42 UNP P06850 AMIDATION
SEQRES 1 A 42 SER GLU GLU PRO PRO ILE SER LEU ASP LEU THR DPN HIS
SEQRES 2 A 42 LEU AIB ARG GLU VAL LEU GLU MET ALA ARG ALA GLU GLN
SEQRES 3 A 42 LEU ALA GLN GLN ALA HIS SER ASN ARG LYS LEU MET GLU
SEQRES 4 A 42 ILE ILE NH2
HET DPN A 12 20
HET AIB A 15 13
HET NH2 A 42 3
HETNAM DPN D-PHENYLALANINE
HETNAM AIB ALPHA-AMINOISOBUTYRIC ACID
HETNAM NH2 AMINO GROUP
FORMUL 1 DPN C9 H11 N O2
FORMUL 1 AIB C4 H9 N O2
FORMUL 2 NH2 H2 N
HELIX 1 1 ILE A 6 VAL A 18 1 13
HELIX 2 2 GLU A 20 ILE A 40 1 21
LINK C THR A 11 N DPN A 12 1555 1555 1.34
LINK C DPN A 12 N HIS A 13 1555 1555 1.33
LINK C LEU A 14 N AIB A 15 1555 1555 1.34
LINK C AIB A 15 N ARG A 16 1555 1555 1.34
LINK C ILE A 41 N NH2 A 42 1555 1555 1.33
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 - t 21 2 Bytes