Header list of 1t5q.pdb file
Complete list - 2 20 Bytes
HEADER HORMONE/GROWTH FACTOR 05-MAY-04 1T5Q
TITLE SOLUTION STRUCTURE OF GIP(1-30)AMIDE IN TFE/WATER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GASTRIC INHIBITORY POLYPEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-30;
COMPND 5 SYNONYM: GIP, GLUCOSE-DEPENDENT INSULINOTROPIC POLYPEPTIDE;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED, THE SEQUENCE
SOURCE 4 OF THE PEPTIDE CAN BE NATURALLY FOUND IN HOMO SAPIENS (HUMAN)
KEYWDS GIP, MOLECULAR MODELLING, HELIX, DIABETES, OBESITY, HORMONE-GROWTH
KEYWDS 2 FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.ALANA,C.M.HEWAGE,J.P.G.MALTHOUSE,J.C.PARKER,V.A.GAULT,F.P.M.O'HARTE
REVDAT 3 02-MAR-22 1T5Q 1 REMARK
REVDAT 2 24-FEB-09 1T5Q 1 VERSN
REVDAT 1 16-NOV-04 1T5Q 0
JRNL AUTH I.ALANA,C.M.HEWAGE,J.P.G.MALTHOUSE,J.C.PARKER,V.A.GAULT,
JRNL AUTH 2 F.P.M.O'HARTE
JRNL TITL NMR STRUCTURE OF THE GLUCOSE-DEPENDENT INSULINOTROPIC
JRNL TITL 2 POLYPEPTIDE FRAGMENT, GIP(1-30)AMIDE.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 325 281 2004
JRNL REFN ISSN 0006-291X
JRNL PMID 15522230
JRNL DOI 10.1016/J.BBRC.2004.10.033
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, SYBYL 6.81
REMARK 3 AUTHORS : BRUKER (XWINNMR), TRIPOS (SYBYL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T5Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022345.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM GIP(1-30)AMIDE, 50% H2O, 50%
REMARK 210 D3-TFE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY; 1D
REMARK 210 VARIABLE TEMPERATURE; 1D D2O
REMARK 210 EXCHANGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, SYBYL 6.81, CYANA
REMARK 210 1.0.6
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING, CONJUGATE-
REMARK 210 GRADIENT MINIMISATION, POWELL
REMARK 210 MINIMISATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : CYANA TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THESE STRUCTURES WERE DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 2 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 3 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 4 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 5 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 6 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 8 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 12 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 13 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500 14 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 15 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 18 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 20 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
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 GLN A 29 45.69 -108.40
REMARK 500 2 GLN A 29 46.10 -109.38
REMARK 500 5 GLN A 29 53.69 -102.30
REMARK 500 6 GLN A 29 56.56 -107.33
REMARK 500 7 THR A 5 44.87 -107.24
REMARK 500 7 GLN A 29 74.43 -103.29
REMARK 500 8 ALA A 2 170.38 60.22
REMARK 500 9 ALA A 2 61.89 -153.83
REMARK 500 9 GLU A 3 84.22 -68.26
REMARK 500 9 GLN A 29 62.02 -104.56
REMARK 500 10 GLN A 29 67.52 -100.65
REMARK 500 12 THR A 5 46.33 -102.49
REMARK 500 14 GLU A 3 74.45 -69.22
REMARK 500 14 GLN A 29 46.45 -102.43
REMARK 500 15 GLN A 29 57.67 -100.80
REMARK 500 16 ALA A 2 59.48 -101.77
REMARK 500 16 THR A 5 43.32 -105.30
REMARK 500 16 GLN A 29 77.16 -106.58
REMARK 500 17 GLN A 29 71.61 -113.32
REMARK 500 18 ALA A 2 179.44 58.15
REMARK 500 18 GLN A 29 55.07 -103.27
REMARK 500 19 GLN A 29 50.56 -101.95
REMARK 500 20 ALA A 2 62.33 -109.28
REMARK 500 20 GLU A 3 81.96 -69.72
REMARK 500 20 THR A 5 49.94 -103.63
REMARK 500 20 GLN A 29 56.52 -100.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR
DBREF 1T5Q A 1 30 UNP P09681 GIP_HUMAN 52 81
SEQRES 1 A 30 TYR ALA GLU GLY THR PHE ILE SER ASP TYR SER ILE ALA
SEQRES 2 A 30 MET ASP LYS ILE HIS GLN GLN ASP PHE VAL ASN TRP LEU
SEQRES 3 A 30 LEU ALA GLN LYS
HELIX 1 1 PHE A 6 ALA A 28 1 23
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 - 2 20 Bytes