Header list of 1qjt.pdb file
Complete list - n 15 2 Bytes
HEADER GROWTH FACTOR 02-JUL-99 1QJT TITLE SOLUTION STRUCTURE OF THE APO EH1 DOMAIN OF MOUSE EPIDERMAL GROWTH TITLE 2 FACTOR RECEPTOR SUBSTRATE 15, EPS15 COMPND MOL_ID: 1; COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE SUBSTRATE 15, COMPND 3 EPS15; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: N-TERMINAL EH1 DOMAIN RESIDUES 1-120; COMPND 6 SYNONYM: EH1; COMPND 7 ENGINEERED: YES; COMPND 8 OTHER_DETAILS: STRUCTURED PART SELECTED FROM LARGER FRAGMENT SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: K10; SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PGEX-2T KEYWDS GROWTH FACTOR, EH DOMAIN, EPS15, EF-HAND, SOLUTION STRUCTURE, S100 KEYWDS 2 PROTEIN EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR B.WHITEHEAD,M.TESSARI,A.CAROTENUTO,P.M.VAN BERGEN EN HENEGOUWEN, AUTHOR 2 G.W.VUISTER REVDAT 5 15-JAN-20 1QJT 1 REMARK REVDAT 4 17-JAN-18 1QJT 1 SOURCE AUTHOR JRNL REVDAT 3 24-FEB-09 1QJT 1 VERSN REVDAT 2 11-SEP-02 1QJT 1 COMPND AUTHOR REMARK REVDAT 1 23-JAN-00 1QJT 0 JRNL AUTH B.WHITEHEAD,M.TESSARI,A.CAROTENUTO, JRNL AUTH 2 P.M.VAN BERGEN EN HENEGOUWEN,G.W.VUISTER JRNL TITL THE EH1 DOMAIN OF EPS15 IS STRUCTURALLY CLASSIFIED AS A JRNL TITL 2 MEMBER OF THE S100 SUBCLASS OF EF-HAND CONTAINING PROTEINS JRNL REF BIOCHEMISTRY V. 38 11271 1999 JRNL REFN ISSN 0006-2960 JRNL PMID 10471276 JRNL DOI 10.1021/BI990922I REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH B.WHITEHEAD,M.TESSARI,H.H.VERSTEEG,S.VAN DELFT, REMARK 1 AUTH 2 P.M.VAN BERGEN EN HENEGOUWEN,G.W.VUISTER REMARK 1 TITL SEQUENCE-SPECIFIC 1H, 13C AND 15N ASSIGNMENT OF THE EH1 REMARK 1 TITL 2 DOMAIN OF MOUSE EPS15 REMARK 1 REF J.BIOMOL.NMR V. 12 465 1998 REMARK 1 REFN ISSN 0925-2738 REMARK 1 PMID 9835057 REMARK 1 DOI 10.1023/A:1008382305918 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5 REMARK 3 AUTHORS : P.GUNTERT, C.MUMENTHALER, K.WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE CALCULATION DETAILS CAN BE REMARK 3 FOUND IN JRNL CITATION REMARK 4 REMARK 4 1QJT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-JUL-99. REMARK 100 THE DEPOSITION ID IS D_1290002108. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.2 REMARK 210 IONIC STRENGTH : 100 MM NACL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 90% H2O/10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE J.BIOMOL.NMR 12; 465-466 REMARK 210 (1998) REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; DRX REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE, XEASY, DYANA 1.5 REMARK 210 METHOD USED : TAD REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST OVERALL TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: STRUCTURE DETERMINED USING TRIPLE-RESONANCE HETERONUCLEAR REMARK 210 NMR SPECTROSCOPY 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 O LEU A 43 H SER A 46 1.57 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 THR A 10 -70.85 -49.67 REMARK 500 1 SER A 13 61.89 -166.71 REMARK 500 1 SER A 14 28.20 41.67 REMARK 500 1 GLU A 27 137.18 -38.67 REMARK 500 1 ALA A 36 -54.18 84.73 REMARK 500 1 SER A 46 -71.93 -75.24 REMARK 500 1 ALA A 60 -70.71 -72.42 REMARK 500 1 ASP A 61 127.35 -38.26 REMARK 500 1 THR A 62 -43.19 -160.93 REMARK 500 1 VAL A 67 148.10 -39.73 REMARK 500 1 SER A 69 -150.19 -127.35 REMARK 500 1 LYS A 70 -94.14 -83.24 REMARK 500 1 LEU A 77 -77.50 -59.53 REMARK 500 1 SER A 95 35.46 72.89 REMARK 500 1 LEU A 96 -161.96 -116.50 REMARK 500 1 ALA A 97 57.83 -104.47 REMARK 500 1 PRO A 101 -163.66 -74.92 REMARK 500 1 PHE A 103 161.44 -39.35 REMARK 500 2 SER A 8 -179.83 179.36 REMARK 500 2 SER A 13 62.38 -167.61 REMARK 500 2 SER A 14 27.82 42.36 REMARK 500 2 GLU A 27 139.74 -39.03 REMARK 500 2 ALA A 36 -50.03 85.02 REMARK 500 2 SER A 46 -74.43 -97.38 REMARK 500 2 PRO A 49 -165.75 -74.94 REMARK 500 2 ASP A 61 126.98 -38.75 REMARK 500 2 THR A 62 -43.15 -161.78 REMARK 500 2 SER A 69 -149.28 -123.99 REMARK 500 2 LYS A 70 -90.62 -83.12 REMARK 500 2 GLU A 72 -72.92 -43.27 REMARK 500 2 VAL A 75 -60.95 -93.41 REMARK 500 2 SER A 95 31.73 74.80 REMARK 500 2 LEU A 96 -161.12 -115.79 REMARK 500 2 ALA A 97 68.01 -107.35 REMARK 500 2 PRO A 101 -163.52 -75.05 REMARK 500 2 PHE A 103 161.50 -39.04 REMARK 500 3 SER A 8 171.84 -46.00 REMARK 500 3 SER A 13 60.84 -170.17 REMARK 500 3 SER A 14 26.36 44.88 REMARK 500 3 ALA A 36 -56.76 85.20 REMARK 500 3 SER A 46 -74.02 -93.39 REMARK 500 3 ASP A 61 127.57 -38.98 REMARK 500 3 THR A 62 -45.68 -144.65 REMARK 500 3 LYS A 65 -42.70 168.32 REMARK 500 3 LYS A 70 -92.53 -49.14 REMARK 500 3 GLU A 72 -73.34 -41.03 REMARK 500 3 LEU A 77 -76.93 -61.08 REMARK 500 3 GLU A 88 164.29 -42.10 REMARK 500 3 SER A 95 2.64 82.19 REMARK 500 3 LEU A 96 -166.52 -113.06 REMARK 500 REMARK 500 THIS ENTRY HAS 515 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4491 RELATED DB: BMRB DBREF 1QJT A 7 105 UNP P42567 EP15_MOUSE 7 105 SEQRES 1 A 99 LEU SER LEU THR GLN LEU SER SER GLY ASN PRO VAL TYR SEQRES 2 A 99 GLU LYS TYR TYR ARG GLN VAL GLU ALA GLY ASN THR GLY SEQRES 3 A 99 ARG VAL LEU ALA LEU ASP ALA ALA ALA PHE LEU LYS LYS SEQRES 4 A 99 SER GLY LEU PRO ASP LEU ILE LEU GLY LYS ILE TRP ASP SEQRES 5 A 99 LEU ALA ASP THR ASP GLY LYS GLY VAL LEU SER LYS GLN SEQRES 6 A 99 GLU PHE PHE VAL ALA LEU ARG LEU VAL ALA CYS ALA GLN SEQRES 7 A 99 ASN GLY LEU GLU VAL SER LEU SER SER LEU SER LEU ALA SEQRES 8 A 99 VAL PRO PRO PRO ARG PHE HIS ASP HELIX 1 1 LEU A 9 SER A 14 1 6 HELIX 2 2 VAL A 18 VAL A 26 1 9 HELIX 3 3 ALA A 36 SER A 46 1 11 HELIX 4 4 ASP A 50 ALA A 60 1 11 HELIX 5 5 LYS A 70 GLN A 84 1 15 HELIX 6 6 SER A 90 LEU A 94 5 5 SHEET 1 A 2 ARG A 33 LEU A 35 0 SHEET 2 A 2 VAL A 67 SER A 69 -1 O VAL A 34 N LEU A 68 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 - n 15 2 Bytes