Header list of 1d0w.pdb file
Complete list - 16 20 Bytes
HEADER NEUROPEPTIDE 14-SEP-99 1D0W TITLE SOLUTION STRUCTURE OF LACTAM-BRIDGED C-TERMINAL ANALOGUE-I OF TITLE 2 NEUROPEPTIDE Y COMPND MOL_ID: 1; COMPND 2 MOLECULE: C-TERMINAL ANALOGUE OF NEUROPEPTIDE Y, A POTENT Y2 RECEPTOR COMPND 3 AGONIST; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: C-TERMINAL ANALOGUE; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: SYNTHETIC WITH MUTATION: L24A, I28K, I31L, T32E, A COMPND 9 LACTAM-BRIDGE WAS INTRODUCED BETWEEN POSITIONS (28) AND (32) SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: CHEMICALLY SYNTHESIZED. KEYWDS LACTAM-BRIDGED, HELIX, NEUROPEPTIDE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.YAO,R.S.NORTON REVDAT 4 16-FEB-22 1D0W 1 REMARK LINK REVDAT 3 24-FEB-09 1D0W 1 VERSN REVDAT 2 29-MAR-05 1D0W 1 COMPND JRNL REMARK MASTER REVDAT 1 16-JUN-00 1D0W 0 JRNL AUTH S.YAO,M.A.SMITH-WHITE,E.K.POTTER,R.S.NORTON JRNL TITL STABILIZATION OF THE HELICAL STRUCTURE OF Y2-SELECTIVE JRNL TITL 2 ANALOGUES OF NEUROPEPTIDE Y BY LACTAM BRIDGES. JRNL REF J.MED.CHEM. V. 45 2310 2002 JRNL REFN ISSN 0022-2623 JRNL PMID 12014969 JRNL DOI 10.1021/JM010543Z REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.J.BARNHAM,F.CATALFAMO,P.K.PALLAGHY,G.J.HOWLETT,R.S.NORTON REMARK 1 TITL HELICAL STRUCTURE AND SELF-ASSOCIATION IN A 13-RESIDUE REMARK 1 TITL 2 NEUROPEPTIDE Y Y2 RECEPTOR AGONIST: RELATIONSHIP TO REMARK 1 TITL 3 BIOLOGICAL ACTIVITY REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH S.A.MONKS,G.KARAGIANIS,G.J.HOWLETT,R.S.NORTON REMARK 1 TITL SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y REMARK 1 REF J.BIOMOL.NMR V. 8 379 1996 REMARK 1 REFN ISSN 0925-2738 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XEASY 2.1, X-PLOR 3.85 REMARK 3 AUTHORS : BRUKER (XEASY), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS CALCULATED USING A REMARK 3 TOTAL OF 124 UPPER BOUND DISTANCE RESTRAINTS AND 8 BACKBONE REMARK 3 DIHEDRAL ANGLE CONSTRAINTS REMARK 4 REMARK 4 1D0W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-99. REMARK 100 THE DEPOSITION ID IS D_1000009695. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 3.5 MG IN 0.6 ML H2O CONTAINING REMARK 210 30% TFE-D3 (BY VOLUME) REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.3, X-PLOR 3.85 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY 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: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 1 HIS A 26 NE2 HIS A 26 CD2 -0.066 REMARK 500 3 HIS A 26 NE2 HIS A 26 CD2 -0.067 REMARK 500 4 HIS A 26 NE2 HIS A 26 CD2 -0.066 REMARK 500 5 HIS A 26 NE2 HIS A 26 CD2 -0.066 REMARK 500 6 HIS A 26 NE2 HIS A 26 CD2 -0.066 REMARK 500 7 HIS A 26 NE2 HIS A 26 CD2 -0.067 REMARK 500 8 HIS A 26 NE2 HIS A 26 CD2 -0.066 REMARK 500 9 HIS A 26 NE2 HIS A 26 CD2 -0.067 REMARK 500 11 HIS A 26 NE2 HIS A 26 CD2 -0.069 REMARK 500 12 HIS A 26 NE2 HIS A 26 CD2 -0.067 REMARK 500 13 HIS A 26 NE2 HIS A 26 CD2 -0.067 REMARK 500 14 HIS A 26 NE2 HIS A 26 CD2 -0.068 REMARK 500 15 HIS A 26 NE2 HIS A 26 CD2 -0.066 REMARK 500 18 HIS A 26 NE2 HIS A 26 CD2 -0.067 REMARK 500 19 HIS A 26 NE2 HIS A 26 CD2 -0.066 REMARK 500 20 HIS A 26 NE2 HIS A 26 CD2 -0.068 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 4 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 9 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 12 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 19 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 20 TYR A 36 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 20 TYR A 36 CB - CG - CD1 ANGL. DEV. = 3.7 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 HIS A 26 47.52 -107.86 REMARK 500 1 TYR A 27 -65.02 -135.39 REMARK 500 2 HIS A 26 63.84 -117.68 REMARK 500 2 LEU A 30 -62.84 -102.47 REMARK 500 2 GLN A 34 -36.80 -35.96 REMARK 500 2 ARG A 35 51.85 -101.93 REMARK 500 3 TYR A 27 -60.24 -132.94 REMARK 500 3 LEU A 30 -61.19 -100.93 REMARK 500 3 GLN A 34 33.89 -87.94 REMARK 500 4 HIS A 26 41.14 -108.23 REMARK 500 4 LEU A 30 -67.00 -102.93 REMARK 500 5 ARG A 25 -49.44 -22.05 REMARK 500 5 TYR A 27 -67.36 -100.54 REMARK 500 5 ASN A 29 -11.22 -47.04 REMARK 500 5 LEU A 30 -62.70 -101.00 REMARK 500 5 GLU A 32 34.24 -99.92 REMARK 500 5 GLN A 34 -53.02 -24.38 REMARK 500 6 ARG A 25 -62.48 -101.20 REMARK 500 6 HIS A 26 68.52 -109.15 REMARK 500 6 TYR A 27 -74.80 -110.46 REMARK 500 7 TYR A 27 -66.16 -125.93 REMARK 500 7 LEU A 30 -60.03 -101.01 REMARK 500 7 GLN A 34 -71.55 -25.20 REMARK 500 8 ARG A 25 -79.55 -111.68 REMARK 500 8 HIS A 26 55.40 -91.99 REMARK 500 8 ASN A 29 13.55 -47.27 REMARK 500 8 GLU A 32 30.79 -97.12 REMARK 500 9 HIS A 26 64.65 -3.18 REMARK 500 9 TYR A 27 -59.75 -127.98 REMARK 500 9 ASN A 29 -37.96 -36.76 REMARK 500 9 ARG A 35 50.01 -95.24 REMARK 500 10 ARG A 25 -67.31 -98.12 REMARK 500 10 ASN A 29 11.14 -46.50 REMARK 500 10 GLN A 34 -68.15 -100.81 REMARK 500 11 TYR A 27 -59.00 -17.07 REMARK 500 12 ARG A 25 -53.68 -23.94 REMARK 500 12 TYR A 27 -62.93 -123.47 REMARK 500 12 ASN A 29 25.48 -65.92 REMARK 500 12 LEU A 30 -60.35 -101.12 REMARK 500 12 ARG A 35 41.45 -109.09 REMARK 500 13 ARG A 25 -57.61 15.13 REMARK 500 13 TYR A 27 -63.38 -105.96 REMARK 500 13 ASN A 29 14.67 -62.16 REMARK 500 13 ARG A 33 -61.37 -100.77 REMARK 500 13 GLN A 34 -55.20 -19.34 REMARK 500 13 ARG A 35 43.14 -148.76 REMARK 500 14 HIS A 26 40.74 -93.84 REMARK 500 14 ASN A 29 -14.96 -47.85 REMARK 500 14 GLN A 34 -34.95 -20.06 REMARK 500 15 ASN A 29 0.18 -64.16 REMARK 500 REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 37 DBREF 1D0W A 24 37 PDB 1D0W 1D0W 24 37 SEQRES 1 A 14 AYA ARG HIS TYR LYS ASN LEU LEU GLU ARG GLN ARG TYR SEQRES 2 A 14 NH2 MODRES 1D0W AYA A 24 ALA N-ACETYLALANINE HET AYA A 24 16 HET NH2 A 37 3 HETNAM AYA N-ACETYLALANINE HETNAM NH2 AMINO GROUP FORMUL 1 AYA C5 H9 N O3 FORMUL 1 NH2 H2 N HELIX 1 1 TYR A 27 GLU A 32 1 6 LINK C AYA A 24 N ARG A 25 1555 1555 1.31 LINK NZ LYS A 28 CD GLU A 32 1555 1555 1.31 LINK C TYR A 36 N NH2 A 37 1555 1555 1.30 SITE 1 AC1 2 ARG A 35 TYR A 36 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 - 16 20 Bytes