Header list of 1sp7.pdb file
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HEADER STRUCTURAL PROTEIN 16-MAR-04 1SP7 TITLE STRUCTURE OF THE CYS-RICH C-TERMINAL DOMAIN OF HYDRA MINICOLLAGEN COMPND MOL_ID: 1; COMPND 2 MOLECULE: MINI-COLLAGEN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE SOURCE 4 OCCURS NATURALLY IN HYDRA SP. KEYWDS CYSTEINE-RICH, PROLINE-RICH, DISULFIDE BOND, STRUCTURAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR S.MEIER,D.HAUSSINGER,E.POKIDYSHEVA,H.P.BACHINGER,S.GRZESIEK REVDAT 4 02-MAR-22 1SP7 1 REMARK REVDAT 3 24-FEB-09 1SP7 1 VERSN REVDAT 2 13-JUL-04 1SP7 1 JRNL REVDAT 1 18-MAY-04 1SP7 0 JRNL AUTH S.MEIER,D.HAUSSINGER,E.POKIDYSHEVA,H.P.BACHINGER,S.GRZESIEK JRNL TITL DETERMINATION OF A HIGH-PRECISION NMR STRUCTURE OF THE JRNL TITL 2 MINICOLLAGEN CYSTEINE RICH DOMAIN FROM HYDRA AND JRNL TITL 3 CHARACTERIZATION OF ITS DISULFIDE BOND FORMATION. JRNL REF FEBS LETT. V. 569 112 2004 JRNL REFN ISSN 0014-5793 JRNL PMID 15225618 JRNL DOI 10.1016/J.FEBSLET.2004.05.034 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH E.POKIDYSHEVA,A.G.MILBRADT,S.MEIER,C.RENNER,D.HAUSSINGER, REMARK 1 AUTH 2 H.P.BACHINGER,L.MORODER,S.GRZESIEK,T.W.HOLSTEIN,S.OZBEK, REMARK 1 AUTH 3 J.ENGEL REMARK 1 TITL THE STRUCTURE OF THE CYS-RICH TERMINAL DOMAIN OF HYDRA REMARK 1 TITL 2 MINICOLLAGEN, WHICH IS INVOLVED IN DISULFIDE NETWORKS OF THE REMARK 1 TITL 3 NEMATOCYST WALL. REMARK 1 REF J.BIOL.CHEM. V. 279 30395 2004 REMARK 1 REFN ISSN 0021-9258 REMARK 1 PMID 15123641 REMARK 1 DOI 10.1074/JBC.M403734200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.0 REMARK 3 AUTHORS : BRUKER (XWINNMR), REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI, REMARK 3 NILGES,PANNU,READ,RICE,SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STANDARD CNS PROTOCOL REMARK 4 REMARK 4 1SP7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-04. REMARK 100 THE DEPOSITION ID IS D_1000021893. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 288 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : ~15 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 6 MM MCRD; 2 MM MCRD REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.1, PIPP 4.3.2, CNS 1.0 REMARK 210 METHOD USED : SIMULATED ANNEALING WITH TORSION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NATURAL ABUNDANCE SPECTRA FOR RDCS AND TALOS 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: 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 LYS A 22 81.54 -63.52 REMARK 500 2 ARG A 23 152.43 179.84 REMARK 500 3 ARG A 23 149.63 172.46 REMARK 500 5 LYS A 22 83.36 -55.10 REMARK 500 5 ARG A 23 147.24 -175.65 REMARK 500 6 LYS A 22 80.44 -58.30 REMARK 500 8 LYS A 22 81.36 -64.94 REMARK 500 9 LYS A 22 80.48 -68.63 REMARK 500 9 ARG A 23 150.15 179.95 REMARK 500 10 ARG A 23 169.18 176.53 REMARK 500 REMARK 500 REMARK: NULL DBREF 1SP7 A 1 24 UNP Q00484 Q00484_9CNID 126 149 SEQRES 1 A 24 PRO CYS PRO PRO VAL CYS VAL ALA GLN CYS VAL PRO THR SEQRES 2 A 24 CYS PRO GLN TYR CYS CYS PRO ALA LYS ARG LYS HELIX 1 1 PRO A 3 GLN A 9 1 7 SSBOND 1 CYS A 2 CYS A 18 1555 1555 2.02 SSBOND 2 CYS A 6 CYS A 14 1555 1555 2.01 SSBOND 3 CYS A 10 CYS A 19 1555 1555 2.03 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