Header list of 1xy4.pdb file
Complete list - 25 20 Bytes
HEADER HORMONE/GROWTH FACTOR 09-NOV-04 1XY4 TITLE NMR STRCUTRE OF SST1-SELECTIVE SOMATOSTATIN (SRIF) ANALOG 1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SST1-SELECTIVE SOMATOSATIN ANALOG; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SRIF; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: PEPTIDE SYNTHESISED USING SOLID PHASE APPROACH EITHER SOURCE 4 MANUALLY OR ON A CS-BIOPEPTIDE SYNTHESIZER MODEL CS536 KEYWDS GAMMA TURN, HORMONE-GROWTH FACTOR COMPLEX EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR C.R.R.GRACE,L.DURRER,S.C.KOERBER,J.ERCHEGYI,J.C.REUBI,J.E.RIVIER, AUTHOR 2 R.RIEK REVDAT 3 28-SEP-11 1XY4 1 HETATM VERSN REVDAT 2 24-FEB-09 1XY4 1 VERSN REVDAT 1 15-FEB-05 1XY4 0 JRNL AUTH C.R.R.GRACE,L.DURRER,S.C.KOERBER,J.ERCHEGYI,J.C.REUBI, JRNL AUTH 2 J.E.RIVIER,R.RIEK JRNL TITL SOMATOSTATIN RECEPTOR 1 SELECTIVE ANALOGUES: 4. JRNL TITL 2 THREE-DIMENSIONAL CONSENSUS STRUCTURE BY NMR JRNL REF J.MED.CHEM. V. 48 523 2005 JRNL REFN ISSN 0022-2623 JRNL PMID 15658866 JRNL DOI 10.1021/JM049518U REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.0.6 REMARK 3 AUTHORS : PETER GUNTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 151 REMARK 3 DISTANCE RESTRAINTS, 36 ANGLE RESTRAINTS REMARK 4 REMARK 4 1XY4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-04. REMARK 100 THE RCSB ID CODE IS RCSB030899. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2.5 MM OF THE PEPTIDE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.0.6 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR REMARK 210 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-10 REMARK 470 RES CSSEQI ATOMS REMARK 470 GLU A 4 OE2 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 HG1 THR A 8 H PHE A 9 0.93 REMARK 500 CD GLU A 4 HZ3 LYS A 10 1.41 REMARK 500 OE1 GLU A 4 HZ3 LYS A 10 1.46 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 PHE A 5 -151.80 37.73 REMARK 500 1 DTR A 6 72.19 -68.73 REMARK 500 1 IAM A 7 50.52 38.39 REMARK 500 1 THR A 8 -135.54 -132.08 REMARK 500 1 PHE A 9 170.06 -44.08 REMARK 500 2 PHE A 5 -148.86 35.44 REMARK 500 2 DTR A 6 76.07 -66.76 REMARK 500 2 IAM A 7 44.81 35.52 REMARK 500 2 THR A 8 -135.91 -129.73 REMARK 500 2 PHE A 9 171.87 -45.05 REMARK 500 3 PHE A 5 -162.53 40.94 REMARK 500 3 DTR A 6 81.49 -62.82 REMARK 500 3 IAM A 7 50.95 32.93 REMARK 500 3 THR A 8 -150.26 -135.56 REMARK 500 3 PHE A 9 156.97 -43.45 REMARK 500 3 SER A 11 -81.53 -107.69 REMARK 500 4 PHE A 5 -160.30 42.38 REMARK 500 4 DTR A 6 79.67 -63.56 REMARK 500 4 IAM A 7 54.38 31.45 REMARK 500 4 THR A 8 -142.57 -133.59 REMARK 500 4 PHE A 9 173.77 -51.32 REMARK 500 5 PHE A 5 -155.15 39.77 REMARK 500 5 DTR A 6 77.14 -65.02 REMARK 500 5 IAM A 7 54.29 32.61 REMARK 500 5 THR A 8 -136.99 -131.21 REMARK 500 6 PHE A 5 -161.02 39.78 REMARK 500 6 DTR A 6 83.83 -58.87 REMARK 500 6 IAM A 7 54.25 26.97 REMARK 500 6 THR A 8 -139.59 -134.14 REMARK 500 7 PHE A 5 -153.51 44.39 REMARK 500 7 DTR A 6 68.55 -68.46 REMARK 500 7 THR A 8 -138.84 -129.57 REMARK 500 8 PHE A 5 -159.10 43.34 REMARK 500 8 DTR A 6 83.28 -61.82 REMARK 500 8 IAM A 7 54.07 28.58 REMARK 500 8 THR A 8 -141.11 -134.66 REMARK 500 8 PHE A 9 175.30 -53.84 REMARK 500 9 PHE A 5 -152.72 44.18 REMARK 500 9 DTR A 6 69.46 -67.42 REMARK 500 9 THR A 8 -140.30 -130.31 REMARK 500 10 PHE A 5 -157.59 37.28 REMARK 500 10 DTR A 6 80.49 -60.01 REMARK 500 10 IAM A 7 52.58 30.73 REMARK 500 10 THR A 8 -138.64 -137.48 REMARK 500 10 PHE A 9 169.28 -43.90 REMARK 500 10 SER A 11 53.47 -142.48 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 DTR A 6 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1XXZ RELATED DB: PDB REMARK 900 RELATED ID: 1XY5 RELATED DB: PDB REMARK 900 RELATED ID: 1XY6 RELATED DB: PDB REMARK 900 RELATED ID: 1XY8 RELATED DB: PDB REMARK 900 RELATED ID: 1XY9 RELATED DB: PDB DBREF 1XY4 A 1 12 PDB 1XY4 1XY4 1 12 SEQRES 1 A 12 TYR CYS LYS GLU PHE DTR IAM THR PHE LYS SER CYS MODRES 1XY4 IAM A 7 ALA 4-[(ISOPROPYLAMINO)METHYL]PHENYLALANINE HET DTR A 6 24 HET IAM A 7 34 HETNAM DTR D-TRYPTOPHAN HETNAM IAM 4-[(ISOPROPYLAMINO)METHYL]PHENYLALANINE FORMUL 1 DTR C11 H12 N2 O2 FORMUL 1 IAM C13 H20 N2 O2 SSBOND 1 CYS A 2 CYS A 12 1555 1555 2.01 LINK C PHE A 5 N DTR A 6 1555 1555 1.33 LINK C DTR A 6 N IAM A 7 1555 1555 1.33 LINK C IAM A 7 N THR A 8 1555 1555 1.33 LINK CD GLU A 4 NZ LYS A 10 1555 1555 1.89 SITE 1 AC1 4 GLU A 4 PHE A 5 IAM A 7 THR A 8 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 - 25 20 Bytes