Header list of 1k37.pdb file
Complete list - 23 202 Bytes
HEADER HORMONE/GROWTH FACTOR 02-OCT-01 1K37 TITLE NMR STRUCTURE OF HUMAN EPIREGULIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: EPIREGULIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-46; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: AD494; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET32A KEYWDS EGF-LIKE FOLD, HORMONE-GROWTH FACTOR COMPLEX EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR K.SATO,K.MIURA,M.TADA,T.AIZAWA,K.MIYAMOTO,K.KAWANO REVDAT 4 23-FEB-22 1K37 1 REMARK REVDAT 3 24-FEB-09 1K37 1 VERSN REVDAT 2 17-FEB-04 1K37 1 JRNL REVDAT 1 30-SEP-03 1K37 0 JRNL AUTH K.SATO,T.NAKAMURA,M.MIZUGUCHI,K.MIURA,M.TADA,T.AIZAWA, JRNL AUTH 2 T.GOMI,K.MIYAMOTO,K.KAWANO JRNL TITL SOLUTION STRUCTURE OF EPIREGULIN AND THE EFFECT OF ITS JRNL TITL 2 C-TERMINAL DOMAIN FOR RECEPTOR BINDING AFFINITY JRNL REF FEBS LETT. V. 553 232 2003 JRNL REFN ISSN 0014-5793 JRNL PMID 14572630 JRNL DOI 10.1016/S0014-5793(03)01005-6 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 604 RESTRAINTS, 556 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 38 REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 10 DISTANCE RESTRAINTS FROM HYDROGEN REMARK 3 BONDS. REMARK 4 REMARK 4 1K37 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-OCT-01. REMARK 100 THE DEPOSITION ID IS D_1000014503. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303; 303 REMARK 210 PH : 3.4; 3.4 REMARK 210 IONIC STRENGTH : 0; 0 REMARK 210 PRESSURE : 1 ATM; 1 ATM REMARK 210 SAMPLE CONTENTS : 1.5MM EPIREGULIN, 90% H2O, 10% REMARK 210 D2O; 1.5MM EPIREGULIN, 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 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: 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 SER A 7 -166.29 -107.16 REMARK 500 ASP A 9 35.38 -95.08 REMARK 500 TYR A 13 -62.16 -158.65 REMARK 500 SER A 26 94.82 -28.55 REMARK 500 THR A 37 40.89 -108.92 REMARK 500 CYS A 41 82.75 32.65 REMARK 500 GLU A 42 -34.14 -143.85 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 ARG A 31 0.30 SIDE CHAIN REMARK 500 ARG A 40 0.25 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1K36 RELATED DB: PDB REMARK 900 1K36 IS 40 ENSEMBLE STRUCTURES OF EPIREGULIN DBREF 1K37 A 1 46 UNP O14944 EREG_HUMAN 63 108 SEQRES 1 A 46 VAL SER ILE THR LYS CYS SER SER ASP MET ASN GLY TYR SEQRES 2 A 46 CYS LEU HIS GLY GLN CYS ILE TYR LEU VAL ASP MET SER SEQRES 3 A 46 GLN ASN TYR CYS ARG CYS GLU VAL GLY TYR THR GLY VAL SEQRES 4 A 46 ARG CYS GLU HIS PHE PHE LEU HELIX 1 1 SER A 7 ASN A 11 5 5 SHEET 1 A 3 THR A 4 LYS A 5 0 SHEET 2 A 3 GLY A 17 LEU A 22 -1 O TYR A 21 N THR A 4 SHEET 3 A 3 GLN A 27 CYS A 32 -1 O TYR A 29 N ILE A 20 SSBOND 1 CYS A 6 CYS A 19 1555 1555 2.59 SSBOND 2 CYS A 14 CYS A 30 1555 1555 2.59 SSBOND 3 CYS A 32 CYS A 41 1555 1555 2.59 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
Complete list - 23 202 Bytes