Header list of 1ssl.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 24-MAR-04 1SSL TITLE SOLUTION STRUCTURE OF THE PSI DOMAIN FROM THE MET RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEPATOCYTE GROWTH FACTOR RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PSI DOMAIN (RESIDUES 519-562); COMPND 5 SYNONYM: MET PROTO-ONCOGENE TYROSINE KINASE, C-MET, HGF RECEPTOR, COMPND 6 HGF-SF RECEPTOR; COMPND 7 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: ORIGAMI (NOVAGEN); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET32A KEYWDS CYSTEINE KNOT, STRUCTURAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR G.KOZLOV,A.PERREAULT,J.D.SCHRAG,M.CYGLER,K.GEHRING,I.EKIEL REVDAT 3 02-MAR-22 1SSL 1 REMARK SEQADV REVDAT 2 24-FEB-09 1SSL 1 VERSN REVDAT 1 12-OCT-04 1SSL 0 JRNL AUTH G.KOZLOV,A.PERREAULT,J.D.SCHRAG,M.PARK,M.CYGLER,K.GEHRING, JRNL AUTH 2 I.EKIEL JRNL TITL INSIGHTS INTO FUNCTION OF PSI DOMAINS FROM STRUCTURE OF THE JRNL TITL 2 MET RECEPTOR PSI DOMAIN. JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 321 234 2004 JRNL REFN ISSN 0006-291X JRNL PMID 15358240 JRNL DOI 10.1016/J.BBRC.2004.06.132 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.1, XPLOR-NIH 2.9.2 REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), CLORE (XPLOR-NIH) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 492 RESTRAINTS, 407 ARE NOE- REMARK 3 DERIVED REMARK 3 DISTANCE CONSTRAINTS, 66 DIHEDRAL ANGLE RESTRAINTS, 19 DISTANCE REMARK 3 RESTRAINTS REMARK 3 FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1SSL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-04. REMARK 100 THE DEPOSITION ID IS D_1000021968. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 283 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 0.15M NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM PSI, 50MM PHOSPHATE BUFFER, REMARK 210 0.15M NAC, 90%H2O, 10%D2O; 1MM REMARK 210 PSI, 50MM PHOSPHATE BUFFER, REMARK 210 0.15M NACL, 100%D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.1, XEASY 1.3.13, CYANA REMARK 210 1.0.6 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: THE STRUCTURE WAS DETERMINED USING 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: 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 OD1 ASP A 29 H LYS A 30 1.60 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 28 10.46 46.43 REMARK 500 1 ASP A 29 -80.80 169.37 REMARK 500 1 ILE A 46 -48.23 -144.88 REMARK 500 2 PHE A 9 155.47 -44.96 REMARK 500 2 GLN A 10 -87.89 -70.17 REMARK 500 2 GLN A 23 -34.49 -147.09 REMARK 500 2 HIS A 28 17.41 45.49 REMARK 500 2 ASP A 29 -84.72 170.97 REMARK 500 2 ILE A 46 -72.91 -150.50 REMARK 500 3 SER A 2 86.02 -66.04 REMARK 500 3 ALA A 3 -40.67 179.99 REMARK 500 3 GLN A 10 -87.68 -75.00 REMARK 500 3 SER A 11 -145.34 -98.47 REMARK 500 3 VAL A 22 -167.32 -128.89 REMARK 500 3 GLN A 23 -35.87 -143.56 REMARK 500 3 HIS A 28 -1.04 54.75 REMARK 500 3 ASP A 29 -67.76 169.78 REMARK 500 3 SER A 39 -165.30 -128.96 REMARK 500 3 ILE A 46 -42.64 -150.14 REMARK 500 4 ALA A 3 -99.38 -130.77 REMARK 500 4 MET A 4 79.51 -176.21 REMARK 500 4 PHE A 9 161.89 -45.52 REMARK 500 4 GLN A 10 -70.09 -78.57 REMARK 500 4 SER A 11 -169.67 -117.31 REMARK 500 4 ALA A 18 54.63 -144.21 REMARK 500 4 GLN A 23 -31.17 -150.15 REMARK 500 4 HIS A 28 20.59 44.30 REMARK 500 4 ASP A 29 -88.53 172.97 REMARK 500 4 SER A 34 -33.99 -36.64 REMARK 500 4 CYS A 37 56.64 -94.58 REMARK 500 4 ILE A 46 -47.46 -150.18 REMARK 500 5 SER A 2 -175.09 54.21 REMARK 500 5 GLN A 10 -69.57 -92.68 REMARK 500 5 ALA A 18 57.11 -143.79 REMARK 500 5 HIS A 28 20.72 39.74 REMARK 500 5 ASP A 29 -81.84 169.62 REMARK 500 5 ILE A 46 -37.67 -148.55 REMARK 500 6 ALA A 3 107.62 58.35 REMARK 500 6 PHE A 9 -174.64 -51.35 REMARK 500 6 GLN A 10 -69.59 -97.30 REMARK 500 6 SER A 11 -147.65 -119.59 REMARK 500 6 GLN A 23 -47.67 -138.02 REMARK 500 6 HIS A 28 -4.27 59.24 REMARK 500 6 ASP A 29 -64.25 170.46 REMARK 500 6 SER A 34 -28.23 -38.02 REMARK 500 6 GLN A 44 23.45 -145.98 REMARK 500 6 ILE A 46 -36.40 -150.70 REMARK 500 7 SER A 2 -109.83 -116.79 REMARK 500 7 ALA A 3 -64.34 172.43 REMARK 500 7 PHE A 9 -169.03 -52.84 REMARK 500 REMARK 500 THIS ENTRY HAS 155 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 1 ARG A 7 0.32 SIDE CHAIN REMARK 500 1 ARG A 33 0.31 SIDE CHAIN REMARK 500 2 ARG A 7 0.23 SIDE CHAIN REMARK 500 2 ARG A 33 0.31 SIDE CHAIN REMARK 500 3 ARG A 7 0.21 SIDE CHAIN REMARK 500 3 ARG A 33 0.12 SIDE CHAIN REMARK 500 4 ARG A 7 0.30 SIDE CHAIN REMARK 500 4 ARG A 33 0.32 SIDE CHAIN REMARK 500 5 ARG A 7 0.26 SIDE CHAIN REMARK 500 6 ARG A 7 0.24 SIDE CHAIN REMARK 500 6 ARG A 33 0.32 SIDE CHAIN REMARK 500 7 ARG A 7 0.32 SIDE CHAIN REMARK 500 7 ARG A 33 0.32 SIDE CHAIN REMARK 500 8 ARG A 7 0.31 SIDE CHAIN REMARK 500 8 ARG A 33 0.31 SIDE CHAIN REMARK 500 9 ARG A 7 0.26 SIDE CHAIN REMARK 500 9 ARG A 33 0.31 SIDE CHAIN REMARK 500 10 ARG A 7 0.25 SIDE CHAIN REMARK 500 10 ARG A 33 0.31 SIDE CHAIN REMARK 500 11 ARG A 7 0.08 SIDE CHAIN REMARK 500 11 ARG A 33 0.28 SIDE CHAIN REMARK 500 12 ARG A 7 0.23 SIDE CHAIN REMARK 500 12 ARG A 33 0.31 SIDE CHAIN REMARK 500 13 ARG A 7 0.16 SIDE CHAIN REMARK 500 13 ARG A 33 0.24 SIDE CHAIN REMARK 500 14 ARG A 7 0.25 SIDE CHAIN REMARK 500 14 ARG A 33 0.32 SIDE CHAIN REMARK 500 15 ARG A 7 0.31 SIDE CHAIN REMARK 500 15 ARG A 33 0.28 SIDE CHAIN REMARK 500 16 ARG A 7 0.26 SIDE CHAIN REMARK 500 16 ARG A 33 0.32 SIDE CHAIN REMARK 500 17 ARG A 7 0.27 SIDE CHAIN REMARK 500 17 ARG A 33 0.30 SIDE CHAIN REMARK 500 18 ARG A 33 0.32 SIDE CHAIN REMARK 500 19 ARG A 7 0.30 SIDE CHAIN REMARK 500 19 ARG A 33 0.25 SIDE CHAIN REMARK 500 20 ARG A 7 0.29 SIDE CHAIN REMARK 500 20 ARG A 33 0.31 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1SSL A 5 48 UNP P08581 MET_HUMAN 519 562 SEQADV 1SSL GLY A 1 UNP P08581 CLONING ARTIFACT SEQADV 1SSL SER A 2 UNP P08581 CLONING ARTIFACT SEQADV 1SSL ALA A 3 UNP P08581 CLONING ARTIFACT SEQADV 1SSL MET A 4 UNP P08581 CLONING ARTIFACT SEQRES 1 A 48 GLY SER ALA MET GLY CYS ARG HIS PHE GLN SER CYS SER SEQRES 2 A 48 GLN CYS LEU SER ALA PRO PRO PHE VAL GLN CYS GLY TRP SEQRES 3 A 48 CYS HIS ASP LYS CYS VAL ARG SER GLU GLU CYS LEU SER SEQRES 4 A 48 GLY THR TRP THR GLN GLN ILE CYS LEU HELIX 1 1 GLY A 5 PHE A 9 5 5 HELIX 2 2 CYS A 12 ALA A 18 1 7 SHEET 1 A 2 GLY A 25 CYS A 27 0 SHEET 2 A 2 LYS A 30 VAL A 32 -1 O LYS A 30 N CYS A 27 SSBOND 1 CYS A 6 CYS A 24 1555 1555 2.02 SSBOND 2 CYS A 12 CYS A 47 1555 1555 2.02 SSBOND 3 CYS A 15 CYS A 31 1555 1555 2.02 SSBOND 4 CYS A 27 CYS A 37 1555 1555 2.02 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 - r 2 2 Bytes