Header list of 1eh2.pdb file
Complete list - b 16 2 Bytes
HEADER CALCIUM BINDING 10-JUL-98 1EH2 TITLE STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 TITLE 2 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: EPS15; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: EPS15 HOMOLOGY (EH) DOMAIN 2, RESIDUES 121-218; COMPND 5 SYNONYM: EH2, EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: THIS DOMAIN CONTAINS A CALCIUM BINDING SITE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: EPS15; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834 (DE3) PLYSS AND BL21 (DE3) PLYSS; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSETA KEYWDS CALCIUM BINDING, SIGNALING DOMAIN, NPF BINDING, EF-HAND, EH DOMAIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.DE BEER,R.E.CARTER,K.E.LOBEL-RICE,A.SORKIN,M.OVERDUIN REVDAT 4 16-FEB-22 1EH2 1 REMARK LINK REVDAT 3 24-FEB-09 1EH2 1 VERSN REVDAT 2 01-APR-03 1EH2 1 JRNL REVDAT 1 22-JUL-99 1EH2 0 JRNL AUTH T.DE BEER,R.E.CARTER,K.E.LOBEL-RICE,A.SORKIN,M.OVERDUIN JRNL TITL STRUCTURE AND ASN-PRO-PHE BINDING POCKET OF THE EPS15 JRNL TITL 2 HOMOLOGY DOMAIN. JRNL REF SCIENCE V. 281 1357 1998 JRNL REFN ISSN 0036-8075 JRNL PMID 9721102 JRNL DOI 10.1126/SCIENCE.281.5381.1357 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE R-6 SUMMATION METHOD WAS USED REMARK 3 WITHIN A SIMULATED ANNEALING PROTOCOL. REMARK 4 REMARK 4 1EH2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000173051. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120 MILLIMOLAR REMARK 210 PRESSURE : ATMOSPHERIC ATM REMARK 210 SAMPLE CONTENTS : H2O AND D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-FILTERED TOCSY AND NOESY; REMARK 210 15N-1H HSQC-NOESY-HSQC; 1H-15N REMARK 210 HMQC-J; 3D AND 4D 13C/15N- REMARK 210 FILTERED NOESY'S; HNCO; CCC- REMARK 210 TOCSY-NNH; HCC-TOCSY-NNH; REMARK 210 HBCBCACONNH; HNCACB; HCCH-TOCSY; REMARK 210 HBCBCGCDHD; HBCBCGCDCEHE REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : 20 LOWEST NOE ENERGIES REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NMR EXPERIMENTS WERE PERFORMED ON UNLABELED, 15N-LABELED REMARK 210 AND 13C,15N-LABELED EH2 PROTEIN 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 ASN A 1 REMARK 465 ARG A 2 REMARK 465 TRP A 3 REMARK 465 GLY A 4 REMARK 465 SER A 5 REMARK 465 LYS A 101 REMARK 465 THR A 102 REMARK 465 TRP A 103 REMARK 465 LEU A 104 REMARK 465 GLU A 105 REMARK 465 ILE A 106 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 TRP A 54 H ASP A 58 1.47 REMARK 500 O SER A 32 H LYS A 35 1.48 REMARK 500 H ALA A 8 O ALA A 93 1.52 REMARK 500 O ASP A 66 H PHE A 70 1.56 REMARK 500 H VAL A 27 O PHE A 30 1.56 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 SER A 25 89.81 82.69 REMARK 500 1 LYS A 83 -23.70 177.95 REMARK 500 1 LEU A 90 107.10 -55.71 REMARK 500 2 SER A 25 87.00 79.52 REMARK 500 2 LYS A 83 -25.53 177.41 REMARK 500 2 PRO A 85 -171.69 -69.59 REMARK 500 3 SER A 25 92.21 83.16 REMARK 500 3 ASN A 28 25.09 46.04 REMARK 500 3 LYS A 83 -28.76 178.44 REMARK 500 3 PRO A 85 -165.47 -75.38 REMARK 500 3 SER A 89 29.00 -177.74 REMARK 500 3 LEU A 90 120.49 57.65 REMARK 500 3 SER A 98 -32.45 80.70 REMARK 500 4 SER A 25 86.58 82.63 REMARK 500 4 ILE A 59 -29.87 -37.40 REMARK 500 4 LYS A 83 -37.87 177.94 REMARK 500 4 PRO A 85 -169.64 -74.77 REMARK 500 4 SER A 89 23.74 -161.14 REMARK 500 4 LEU A 90 118.48 61.70 REMARK 500 5 SER A 25 83.55 80.29 REMARK 500 5 LYS A 83 -28.33 178.90 REMARK 500 5 SER A 89 23.88 -165.89 REMARK 500 5 LEU A 90 123.17 62.09 REMARK 500 5 SER A 98 -45.20 76.47 REMARK 500 6 SER A 25 97.59 80.35 REMARK 500 6 LYS A 83 -89.38 -88.04 REMARK 500 6 PRO A 85 -179.19 -66.81 REMARK 500 7 SER A 25 93.56 79.70 REMARK 500 7 LYS A 83 -26.54 177.69 REMARK 500 7 PRO A 85 -167.44 -71.32 REMARK 500 7 LEU A 90 107.20 -56.88 REMARK 500 8 SER A 25 87.59 81.93 REMARK 500 8 ILE A 59 -30.98 -34.57 REMARK 500 8 VAL A 77 -62.74 -91.39 REMARK 500 8 LYS A 83 -23.34 177.92 REMARK 500 8 LEU A 90 106.49 -50.05 REMARK 500 8 LEU A 94 -11.34 -141.52 REMARK 500 8 SER A 98 -38.68 -143.18 REMARK 500 9 ALA A 8 -26.87 -39.39 REMARK 500 9 SER A 25 93.77 83.14 REMARK 500 9 LYS A 83 -69.46 -146.24 REMARK 500 9 LEU A 90 106.38 -51.74 REMARK 500 9 LEU A 94 34.36 -158.19 REMARK 500 9 SER A 98 -52.01 75.09 REMARK 500 10 SER A 25 95.07 82.17 REMARK 500 10 LYS A 83 79.51 176.89 REMARK 500 10 GLU A 84 116.36 -166.71 REMARK 500 10 LEU A 90 107.81 -54.66 REMARK 500 10 SER A 98 -52.74 73.99 REMARK 500 11 SER A 25 96.33 80.88 REMARK 500 REMARK 500 THIS ENTRY HAS 98 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 52 0.32 SIDE CHAIN REMARK 500 1 ARG A 67 0.27 SIDE CHAIN REMARK 500 1 ARG A 100 0.26 SIDE CHAIN REMARK 500 2 ARG A 52 0.18 SIDE CHAIN REMARK 500 2 ARG A 67 0.30 SIDE CHAIN REMARK 500 2 ARG A 100 0.31 SIDE CHAIN REMARK 500 3 ARG A 52 0.21 SIDE CHAIN REMARK 500 3 ARG A 67 0.31 SIDE CHAIN REMARK 500 3 ARG A 100 0.11 SIDE CHAIN REMARK 500 4 ARG A 52 0.21 SIDE CHAIN REMARK 500 4 ARG A 67 0.21 SIDE CHAIN REMARK 500 4 ARG A 100 0.32 SIDE CHAIN REMARK 500 5 ARG A 52 0.12 SIDE CHAIN REMARK 500 5 ARG A 67 0.30 SIDE CHAIN REMARK 500 5 ARG A 100 0.11 SIDE CHAIN REMARK 500 6 ARG A 52 0.28 SIDE CHAIN REMARK 500 6 ARG A 67 0.26 SIDE CHAIN REMARK 500 6 ARG A 100 0.20 SIDE CHAIN REMARK 500 7 ARG A 52 0.31 SIDE CHAIN REMARK 500 7 ARG A 67 0.29 SIDE CHAIN REMARK 500 7 ARG A 100 0.22 SIDE CHAIN REMARK 500 8 ARG A 52 0.30 SIDE CHAIN REMARK 500 8 ARG A 67 0.30 SIDE CHAIN REMARK 500 8 ARG A 100 0.18 SIDE CHAIN REMARK 500 9 ARG A 52 0.21 SIDE CHAIN REMARK 500 9 ARG A 67 0.30 SIDE CHAIN REMARK 500 9 ARG A 100 0.22 SIDE CHAIN REMARK 500 10 ARG A 52 0.32 SIDE CHAIN REMARK 500 10 ARG A 67 0.19 SIDE CHAIN REMARK 500 10 ARG A 100 0.28 SIDE CHAIN REMARK 500 11 ARG A 52 0.20 SIDE CHAIN REMARK 500 11 ARG A 67 0.15 SIDE CHAIN REMARK 500 11 ARG A 100 0.19 SIDE CHAIN REMARK 500 12 ARG A 52 0.29 SIDE CHAIN REMARK 500 12 ARG A 67 0.31 SIDE CHAIN REMARK 500 12 ARG A 100 0.30 SIDE CHAIN REMARK 500 13 ARG A 52 0.29 SIDE CHAIN REMARK 500 13 ARG A 67 0.15 SIDE CHAIN REMARK 500 13 ARG A 100 0.28 SIDE CHAIN REMARK 500 14 ARG A 52 0.25 SIDE CHAIN REMARK 500 14 ARG A 67 0.16 SIDE CHAIN REMARK 500 14 ARG A 100 0.31 SIDE CHAIN REMARK 500 15 ARG A 52 0.10 SIDE CHAIN REMARK 500 15 ARG A 67 0.18 SIDE CHAIN REMARK 500 15 ARG A 100 0.19 SIDE CHAIN REMARK 500 16 ARG A 52 0.31 SIDE CHAIN REMARK 500 16 ARG A 67 0.26 SIDE CHAIN REMARK 500 17 ARG A 52 0.31 SIDE CHAIN REMARK 500 17 ARG A 67 0.17 SIDE CHAIN REMARK 500 18 ARG A 52 0.29 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 57 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 107 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 58 OD1 REMARK 620 2 ASP A 60 OD1 56.8 REMARK 620 3 ASP A 60 OD2 98.8 42.3 REMARK 620 4 ASP A 62 OD1 79.1 51.1 50.1 REMARK 620 5 MET A 64 O 51.2 90.1 117.2 68.9 REMARK 620 6 GLU A 69 OE1 76.4 90.3 105.2 141.4 114.8 REMARK 620 7 GLU A 69 OE2 118.7 125.1 110.5 157.7 132.2 44.9 REMARK 620 N 1 2 3 4 5 6 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: NPF REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: TRP 54 IS POSITIONED WITHIN A BINDING SITE FOR REMARK 800 ASN-PRO-PHE PEPTIDES. REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 107 DBREF 1EH2 A 6 103 UNP P42566 EP15_HUMAN 121 218 SEQRES 1 A 106 ASN ARG TRP GLY SER PRO TRP ALA VAL LYS PRO GLU ASP SEQRES 2 A 106 LYS ALA LYS TYR ASP ALA ILE PHE ASP SER LEU SER PRO SEQRES 3 A 106 VAL ASN GLY PHE LEU SER GLY ASP LYS VAL LYS PRO VAL SEQRES 4 A 106 LEU LEU ASN SER LYS LEU PRO VAL ASP ILE LEU GLY ARG SEQRES 5 A 106 VAL TRP GLU LEU SER ASP ILE ASP HIS ASP GLY MET LEU SEQRES 6 A 106 ASP ARG ASP GLU PHE ALA VAL ALA MET PHE LEU VAL TYR SEQRES 7 A 106 CYS ALA LEU GLU LYS GLU PRO VAL PRO MET SER LEU PRO SEQRES 8 A 106 PRO ALA LEU VAL PRO PRO SER LYS ARG LYS THR TRP LEU SEQRES 9 A 106 GLU ILE HET CA A 107 1 HETNAM CA CALCIUM ION FORMUL 2 CA CA 2+ HELIX 1 1 PRO A 11 PHE A 21 1 11 HELIX 2 2 GLY A 33 LEU A 41 1 9 HELIX 3 3 VAL A 47 SER A 57 1 11 HELIX 4 4 GLU A 69 GLU A 82 1 14 LINK OD1 ASP A 58 CA CA A 107 1555 1555 2.80 LINK OD1 ASP A 60 CA CA A 107 1555 1555 2.53 LINK OD2 ASP A 60 CA CA A 107 1555 1555 3.19 LINK OD1 ASP A 62 CA CA A 107 1555 1555 2.81 LINK O MET A 64 CA CA A 107 1555 1555 2.70 LINK OE1 GLU A 69 CA CA A 107 1555 1555 2.83 LINK OE2 GLU A 69 CA CA A 107 1555 1555 2.82 SITE 1 NPF 1 TRP A 54 SITE 1 AC1 5 ASP A 58 ASP A 60 ASP A 62 MET A 64 SITE 2 AC1 5 GLU A 69 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 - b 16 2 Bytes