Header list of 2h3t.pdb file
Complete list - 9 20 Bytes
HEADER DE NOVO PROTEIN 23-MAY-06 2H3T TITLE TRANS-(4-AMINOMETHYL)PHENYLAZOBENZOIC ACID-APP BOUND TO DPC MICELLES COMPND MOL_ID: 1; COMPND 2 MOLECULE: PANCREATIC HORMONE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PANCREATIC HORMONE, RESIDUES 1-9; COMPND 5 SYNONYM: PANCREATIC POLYPEPTIDE, APP; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: PANCREATIC HORMONE; COMPND 9 CHAIN: B; COMPND 10 FRAGMENT: PANCREATIC HORMONE, RESIDUES 11-34; COMPND 11 SYNONYM: PANCREATIC POLYPEPTIDE, APP; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: SYNTHESIZED BY SOLID-PHASE PEPTIDE SYNTHESIS, SOURCE 4 DERIVATIVCE OF AVIAN PP; RESIDUES 10-12 OF AVIAN PANCREATIC SOURCE 5 POLYPPETIDE (APP) ARE REPLACED BY TRANS-(4-AMINOMETHYL) SOURCE 6 PHENYLAZOBENZOIC ACID-APP.; SOURCE 7 MOL_ID: 2; SOURCE 8 SYNTHETIC: YES; SOURCE 9 OTHER_DETAILS: SYNTHESIZED BY SOLID-PHASE PEPTIDE SYNTHESIS, SOURCE 10 DERIVATIVCE OF AVIAN PP; RESIDUES 10-12 OF AVIAN PANCREATIC SOURCE 11 POLYPPETIDE (APP) ARE REPLACED BY TRANS-(4-AMINOMETHYL) SOURCE 12 PHENYLAZOBENZOIC ACID-APP. KEYWDS PHOTOSWITCH, PP FOLDING, DE NOVO PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.JURT,A.AEMISSEGGER,P.GUENTERT,O.ZERBE,D.HILVERT REVDAT 4 09-MAR-22 2H3T 1 REMARK LINK REVDAT 3 24-FEB-09 2H3T 1 VERSN REVDAT 2 03-OCT-06 2H3T 1 JRNL REVDAT 1 12-SEP-06 2H3T 0 JRNL AUTH S.JURT,A.AEMISSEGGER,P.GUENTERT,O.ZERBE,D.HILVERT JRNL TITL A PHOTOSWITCHABLE MINIPROTEIN BASED ON THE SEQUENCE OF AVIAN JRNL TITL 2 PANCREATIC POLYPEPTIDE JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 45 6297 2006 JRNL REFN ESSN 0570-0833 JRNL PMID 16933352 JRNL DOI 10.1002/ANIE.200602084 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 2.2.2 REMARK 3 AUTHORS : GUENTERT, P. ET AL. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2H3T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-06. REMARK 100 THE DEPOSITION ID IS D_1000037894. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 0.0 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM PEPTIDE; 300MM DPC; 50MM MES REMARK 210 BUFFER(PH 6.0); 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; 2D TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CYANA 2.2.2 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 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 VAL B 12 -39.81 -131.93 REMARK 500 1 HIS B 32 48.42 -105.97 REMARK 500 1 ARG B 33 27.91 47.09 REMARK 500 2 GLN A 4 61.67 -154.79 REMARK 500 2 ASP B 14 -51.29 -120.99 REMARK 500 2 HIS B 32 44.78 -99.53 REMARK 500 3 PRO A 2 68.52 -68.36 REMARK 500 3 TYR A 7 73.74 59.70 REMARK 500 3 VAL B 12 -58.74 -130.07 REMARK 500 3 TYR B 19 -46.87 -132.97 REMARK 500 4 GLN A 4 69.03 37.03 REMARK 500 4 VAL B 12 -70.18 -112.02 REMARK 500 4 ARG B 33 33.59 -166.89 REMARK 500 5 VAL B 28 -42.78 -135.03 REMARK 500 5 ARG B 33 15.16 -155.91 REMARK 500 6 GLN A 4 86.26 60.40 REMARK 500 6 TYR A 7 57.41 -152.63 REMARK 500 6 HIS B 32 42.87 -96.71 REMARK 500 7 GLN A 4 159.09 62.54 REMARK 500 7 TYR A 7 55.45 -140.36 REMARK 500 7 VAL B 28 -55.01 -134.34 REMARK 500 7 ARG B 33 83.54 69.72 REMARK 500 8 GLN A 4 154.18 77.17 REMARK 500 8 TYR A 7 63.18 39.18 REMARK 500 8 VAL B 28 -36.61 -137.32 REMARK 500 8 ARG B 33 72.42 -178.16 REMARK 500 9 PRO A 2 92.83 -65.53 REMARK 500 9 VAL B 12 -51.15 -128.32 REMARK 500 9 TYR B 25 0.43 -66.93 REMARK 500 9 LEU B 26 -63.55 -106.32 REMARK 500 9 ARG B 33 14.26 -145.23 REMARK 500 10 VAL B 28 -64.85 -124.47 REMARK 500 10 ARG B 33 61.09 61.99 REMARK 500 11 GLN A 4 157.63 63.22 REMARK 500 11 PRO A 5 -177.23 -69.31 REMARK 500 11 LEU B 26 -64.02 -101.61 REMARK 500 11 ARG B 33 80.84 65.62 REMARK 500 12 ARG B 33 64.05 68.58 REMARK 500 13 HIS B 32 40.51 -95.81 REMARK 500 14 GLN A 4 60.44 36.17 REMARK 500 14 VAL B 12 -54.56 -128.41 REMARK 500 14 ARG B 33 67.34 -172.65 REMARK 500 15 VAL B 12 -64.84 -132.05 REMARK 500 15 ARG B 33 30.76 -162.75 REMARK 500 16 HIS B 32 50.47 -104.65 REMARK 500 17 GLN A 4 60.53 -159.20 REMARK 500 17 TYR A 7 64.60 38.24 REMARK 500 17 VAL B 12 -59.01 -129.70 REMARK 500 17 ARG B 33 21.40 -160.92 REMARK 500 18 VAL B 12 -57.17 -129.35 REMARK 500 REMARK 500 THIS ENTRY HAS 56 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 3 TYR B 19 0.12 SIDE CHAIN REMARK 500 4 ASP B 14 0.08 SIDE CHAIN REMARK 500 4 TYR B 34 0.07 SIDE CHAIN REMARK 500 8 ASP B 14 0.09 SIDE CHAIN REMARK 500 9 TYR B 19 0.08 SIDE CHAIN REMARK 500 12 ASP B 21 0.08 SIDE CHAIN REMARK 500 16 ASP B 14 0.09 SIDE CHAIN REMARK 500 19 ASP B 21 0.08 SIDE CHAIN REMARK 500 19 TYR B 34 0.07 SIDE CHAIN REMARK 500 20 GLU B 13 0.07 SIDE CHAIN 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 EAB A 10 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2H3S RELATED DB: PDB REMARK 900 THE SAME PEPTIDE CONTAINING CIS INSTEAD OF TRANS-4- REMARK 900 AMINOMETHYLPHENYLAZOBENZOIC ACID IN PRESENCE OF DPC MICELLES REMARK 900 RELATED ID: 2H4B RELATED DB: PDB REMARK 900 THE SAME PEPTIDE CONTAINING CIS INSTEAD OF TRANS-4- REMARK 900 AMINOMETHYLPHENYLAZOBENZOIC ACID IN PLAIN WATER DBREF 2H3T A 1 9 UNP P68249 PAHO_MELGA 1 9 DBREF 2H3T B 11 34 UNP P68249 PAHO_MELGA 13 36 SEQRES 1 A 9 GLY PRO SER GLN PRO THR TYR PRO GLY SEQRES 1 B 25 PRO VAL GLU ASP LEU ILE ARG PHE TYR ASN ASP LEU GLN SEQRES 2 B 25 GLN TYR LEU ASN VAL VAL THR ARG HIS ARG TYR NH2 HET NH2 B 35 3 HET EAB A 10 32 HETNAM NH2 AMINO GROUP HETNAM EAB (3-{(E)-[3-(AMINOMETHYL)PHENYL]DIAZENYL}PHENYL)ACETIC HETNAM 2 EAB ACID FORMUL 2 NH2 H2 N FORMUL 3 EAB C15 H15 N3 O2 HELIX 1 1 VAL B 12 VAL B 28 1 17 LINK C GLY A 9 N EAB A 10 1555 1555 1.33 LINK C EAB A 10 N PRO B 11 1555 1555 1.35 LINK C TYR B 34 N NH2 B 35 1555 1555 1.33 SITE 1 AC1 4 PRO A 8 GLY A 9 PRO B 11 VAL B 12 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 - 9 20 Bytes