Header list of 2b4n.pdb file
Complete list - r 9 2 Bytes
HEADER HORMONE/GROWTH FACTOR 26-SEP-05 2B4N
TITLE SOLUTION STRUCTURE OF GLUCOSE-DEPENDENT INSULINOTROPIC POLYPEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GASTRIC INHIBITORY POLYPEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 52-93;
COMPND 5 SYNONYM: GIP, GLUCOSE-DEPENDENT INSULINOTROPIC POLYPEPTIDE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS GIP, MOLECULAR MODELLING, HELIX, DIABETES, OBESITY, HORMONE-GROWTH
KEYWDS 2 FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.ALANA,C.M.HEWAGE,F.P.M.O'HARTE,J.P.G.MALTHOUSE
REVDAT 4 09-MAR-22 2B4N 1 REMARK
REVDAT 3 24-FEB-09 2B4N 1 VERSN
REVDAT 2 20-JUN-06 2B4N 1 JRNL
REVDAT 1 02-MAY-06 2B4N 0
JRNL AUTH I.ALANA,J.C.PARKER,V.A.GAULT,P.R.FLATT,F.P.O'HARTE,
JRNL AUTH 2 J.P.MALTHOUSE,C.M.HEWAGE
JRNL TITL NMR AND ALANINE SCAN STUDIES OF GLUCOSE-DEPENDENT
JRNL TITL 2 INSULINOTROPIC POLYPEPTIDE IN WATER.
JRNL REF J.BIOL.CHEM. V. 281 16370 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16621806
JRNL DOI 10.1074/JBC.M510414200
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, INC. (SYBYL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2B4N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034669.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM GIP, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 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, SPARKY 3.110, 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 : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS 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: 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
REMARK 500 REMARK: NULL
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 1 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 1 TRP A 36 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 2 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500 2 TRP A 36 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 3 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500 3 TRP A 36 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 4 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 4 TRP A 36 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 5 SER A 8 N - CA - CB ANGL. DEV. = 9.1 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 6 TRP A 36 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 7 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 8 TRP A 36 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 9 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 9 TRP A 36 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 10 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 10 TRP A 36 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500 11 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500 11 TRP A 36 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 12 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 12 TRP A 36 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 13 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 16 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 17 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 17 TRP A 36 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 18 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 19 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500 19 TRP A 36 CE2 - CD2 - CG ANGL. DEV. = -4.8 DEGREES
REMARK 500 20 TRP A 25 CE2 - CD2 - CG ANGL. DEV. = -5.0 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 SER A 8 55.52 -99.07
REMARK 500 1 SER A 11 -62.17 -153.40
REMARK 500 1 ALA A 13 -61.34 -155.56
REMARK 500 1 LYS A 32 79.22 60.56
REMARK 500 1 LYS A 33 49.51 -145.84
REMARK 500 1 TRP A 36 89.64 -68.60
REMARK 500 1 LYS A 37 72.87 57.96
REMARK 500 1 ASN A 39 91.33 69.80
REMARK 500 1 ILE A 40 70.84 63.78
REMARK 500 2 ALA A 2 56.33 -145.49
REMARK 500 2 THR A 5 59.37 -91.60
REMARK 500 2 PHE A 6 -56.89 -169.99
REMARK 500 2 SER A 8 52.84 -152.64
REMARK 500 2 ASP A 9 -74.24 60.65
REMARK 500 2 ALA A 13 -53.65 166.86
REMARK 500 2 ASN A 34 60.42 -156.58
REMARK 500 2 ASP A 35 50.61 -144.54
REMARK 500 2 HIS A 38 48.07 -99.58
REMARK 500 2 ASN A 39 53.32 -145.93
REMARK 500 3 ALA A 2 159.63 63.79
REMARK 500 3 PHE A 6 -63.52 -179.26
REMARK 500 3 SER A 8 58.19 -157.50
REMARK 500 3 ALA A 13 -55.93 -170.18
REMARK 500 3 LYS A 30 -60.39 -155.03
REMARK 500 3 LYS A 33 53.23 -156.91
REMARK 500 3 ASN A 34 53.51 -100.71
REMARK 500 3 ASP A 35 61.54 -164.24
REMARK 500 3 LYS A 37 58.70 -150.10
REMARK 500 3 ASN A 39 54.19 -143.59
REMARK 500 4 PHE A 6 49.08 -148.51
REMARK 500 4 SER A 8 52.23 -103.92
REMARK 500 4 ASP A 9 53.92 36.98
REMARK 500 4 ALA A 13 -56.14 -168.79
REMARK 500 4 GLN A 29 49.08 -103.26
REMARK 500 4 LYS A 30 -67.68 -141.30
REMARK 500 4 LYS A 32 102.84 -164.25
REMARK 500 4 ASP A 35 53.48 -99.46
REMARK 500 4 ILE A 40 164.29 68.06
REMARK 500 5 THR A 5 -77.59 -143.65
REMARK 500 5 SER A 8 143.69 131.58
REMARK 500 5 ASP A 9 64.03 -153.05
REMARK 500 5 ALA A 13 -55.13 -176.58
REMARK 500 5 ASN A 34 49.61 -104.25
REMARK 500 5 ASP A 35 57.14 -169.99
REMARK 500 5 LYS A 37 74.56 55.93
REMARK 500 5 HIS A 38 51.75 -118.84
REMARK 500 5 ASN A 39 58.49 -159.04
REMARK 500 6 ALA A 2 53.67 -153.86
REMARK 500 6 SER A 8 66.82 -151.57
REMARK 500 6 ASP A 9 -57.71 -168.80
REMARK 500
REMARK 500 THIS ENTRY HAS 172 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 TYR A 10 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR
DBREF 2B4N A 1 42 UNP P09681 GIP_HUMAN 52 93
SEQRES 1 A 42 TYR ALA GLU GLY THR PHE ILE SER ASP TYR SER ILE ALA
SEQRES 2 A 42 MET ASP LYS ILE HIS GLN GLN ASP PHE VAL ASN TRP LEU
SEQRES 3 A 42 LEU ALA GLN LYS GLY LYS LYS ASN ASP TRP LYS HIS ASN
SEQRES 4 A 42 ILE THR GLN
HELIX 1 1 SER A 11 GLN A 29 1 19
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